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  • Kinetics  (374)
  • American Association for the Advancement of Science (AAAS)  (374)
  • Annual Reviews
  • 2005-2009  (80)
  • 1985-1989  (158)
  • 1980-1984  (136)
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  • 1
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    Fidelity of HIV-1 reverse transcriptase (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-11-25
    Description: The human immunodeficiency virus type 1 (HIV-1) shows extensive genetic variation and undergoes rapid evolution. The fidelity of purified HIV-1 reverse transcriptase was measured during DNA polymerization in vitro by means of three different assays. Reverse transcriptase from HIV-1 introduced base-substitution errors in DNA from the bacteriophage phi X174 amber3 at estimated frequencies of 1/2000 to 1/4000. Analyses of misincorporation rates opposite a single template adenine residue showed that HIV-1 reverse transcriptase catalyzed nucleotide mismatches with a specificity of A:C much greater than A:G greater than A:A. The high error rate of HIV-1 reverse transcriptase in vitro translates to approximately five to ten errors per HIV-1 genome per round of replication in vivo. This high error rate suggests that misincorporation by HIV-1 reverse transcriptase is, at least in part, responsible for the hypermutability of the AIDS virus. The specificity of misincorporation may provide a basis for the systematic construction of antiviral nucleosides.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Preston, B D -- Poiesz, B J -- Loeb, L A -- CA-07263-03/CA/NCI NIH HHS/ -- N01AI72654/AI/NIAID NIH HHS/ -- R35-CA-39903/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1988 Nov 25;242(4882):1168-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, University of Washington, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2460924" target="_blank"〉PubMed〈/a〉
    Keywords: Avian Myeloblastosis Virus/enzymology ; Bacteriophage phi X 174/genetics ; DNA/*biosynthesis ; DNA Polymerase II/metabolism ; DNA, Viral/biosynthesis ; Electrophoresis, Polyacrylamide Gel ; HIV/*enzymology/genetics ; Kinetics ; Moloney murine leukemia virus/enzymology ; Mutation ; Nucleotides/metabolism ; RNA-Directed DNA Polymerase/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 2
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    Phosphatidylinositol-glycan anchors of membrane proteins: potential precursors of insulin mediators (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-04-22
    Description: BC3H1 myocytes release membrane-bound alkaline phosphatase to the incubation medium upon stimulation with insulin, following a time course that is consistent with the generation of dimyristoylglycerol and the appearance of a putative insulin mediator in the extracellular medium. The use of specific blocking agents shows, however, that alkaline phosphatase release and dimyristoylglycerol production are independent processes and that the blockade of either event inhibits the production of insulin mediator. These experiments suggest a new model of insulin action.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Romero, G -- Luttrell, L -- Rogol, A -- Zeller, K -- Hewlett, E -- Larner, J -- AI 18000/AI/NIAID NIH HHS/ -- AM 14334/AM/NIADDK NIH HHS/ -- AM 22125/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1988 Apr 22;240(4851):509-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Virginia School of Medicine, Charlottesville 22908.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3282305" target="_blank"〉PubMed〈/a〉
    Keywords: Alkaline Phosphatase/metabolism/secretion ; Animals ; Diglycerides/metabolism ; Enzyme Activation/drug effects ; Extracellular Space/enzymology ; Glycolipids/*physiology ; In Vitro Techniques ; Insulin/*pharmacology ; Kinetics ; Membrane Glycoproteins/*physiology ; Phosphatidylinositols/*physiology ; Pyruvate Dehydrogenase Complex/metabolism
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  • 3
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    Anticodon switching changes the identity of methionine and valine transfer RNAs (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-11-04
    Description: The anticodon has previously been shown to play a role in recognition of certain transfer RNAs by aminoacyl-tRNA synthetases; however, the extent to which this sequence dictates tRNA identity is generally unknown. To investigate the contribution of the anticodon to the identity of Escherichia coli methionine and valine tRNAs, in vitro transcripts of these tRNAs were prepared that contained normal and interchanged anticodon sequences. Transcripts containing wild-type tRNA sequences were excellent substrates for their respective cognate aminoacyl-tRNA synthetases and were effectively discriminated against by a variety of noncognate enzymes. The mutant tRNAs produced by switching the anticodon sequences lost their original tRNA identity and assumed an identity corresponding to the acquired anticodon sequence. These results indicate that the anticodon contains sufficient information to distinguish methionine and valine tRNAs with high fidelity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schulman, L H -- Pelka, H -- New York, N.Y. -- Science. 1988 Nov 4;242(4879):765-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Developmental Biology and Cancer, Albert Einstein College of Medicine, Bronx, New York 10461.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3055296" target="_blank"〉PubMed〈/a〉
    Keywords: *Anticodon ; Escherichia coli ; Kinetics ; Methionine-tRNA Ligase/metabolism ; *RNA, Transfer ; RNA, Transfer, Amino Acid-Specific/*physiology ; RNA, Transfer, Met/*physiology ; RNA, Transfer, Val/*physiology ; Substrate Specificity ; *Transfer RNA Aminoacylation ; Valine-tRNA Ligase/metabolism
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    A continuous cell-free translation system capable of producing polypeptides in high yield (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-11-25
    Description: A cell-free translation system has been constructed that uses a continuous flow of the feeding buffer [including amino acids, adenosine triphosphate (ATP), and guanosine triphosphate (GTP)] through the reaction mixture and a continuous removal of a polypeptide product. Both prokaryotic (Escherichia coli) and eukaryotic (wheat embryos, Triticum sp.) versions of the system have been tested. In both cases the system has proven active for long times, synthesizing polypeptides at a high constant rate for tens of hours. With the use of MS2 phage RNA or brome mosaic virus RNA 4 as templates, 100 copies of viral coat proteins per RNA were synthesized for 20 hours in the prokaryotic or eukaryotic system, respectively. With synthetic calcitonin messenger RNA, 150 to 300 copies of calcitonin polypeptide were produced per messenger RNA in both types of continuous translation systems for 40 hours.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Spirin, A S -- Baranov, V I -- Ryabova, L A -- Ovodov, S Y -- Alakhov, Y B -- New York, N.Y. -- Science. 1988 Nov 25;242(4882):1162-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Protein Research, Academy of Sciences, Moscow Region, USSR.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3055301" target="_blank"〉PubMed〈/a〉
    Keywords: Bacteriophages/genetics ; Calcitonin/biosynthesis/genetics ; Capsid/biosynthesis/genetics ; Electrophoresis ; Escherichia coli/*metabolism ; Kinetics ; Mosaic Viruses/genetics ; *Peptide Biosynthesis ; Plants/*metabolism ; *Protein Biosynthesis ; RNA, Messenger/metabolism ; RNA, Viral/genetics ; Ribosomes/metabolism ; Templates, Genetic ; Triticum
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  • 5
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    Role of the protein moiety of ribonuclease P, a ribonucleoprotein enzyme (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-01-08
    Description: The Bacillus subtilis ribonuclease P consists of a protein and an RNA. At high ionic strength the reaction is protein-independent; the RNA alone is capable of cleaving precursor transfer RNA, but the turnover is slow. Kinetic analyses show that high salt concentrations facilitate substrate binding in the absence of the protein, probably by decreasing the repulsion between the polyanionic enzyme and substrate RNAs, and also slow product release and enzyme turnover. It is proposed that the ribonuclease P protein, which is small and basic, provides a local pool of counter-ions that facilitates substrate binding without interfering with rapid product release.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reich, C -- Olsen, G J -- Pace, B -- Pace, N R -- GM34527/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Jan 8;239(4836):178-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Indiana University, Bloomington 47405.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3122322" target="_blank"〉PubMed〈/a〉
    Keywords: Bacillus subtilis/*enzymology ; Endoribonucleases/*physiology ; Kinetics ; Nucleic Acid Precursors/metabolism ; RNA, Transfer/metabolism ; Ribonuclease P ; Ribonucleoproteins/*physiology ; Structure-Activity Relationship
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  • 6
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    Accuracy of in vivo aminoacylation requires proper balance of tRNA and aminoacyl-tRNA synthetase (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-12-16
    Description: The fidelity of protein biosynthesis in any cell rests on the accuracy of aminoacylation of tRNA. The exquisite specificity of this reaction is critically dependent on the correct recognition of tRNA by aminoacyl-tRNA synthetases. It is shown here that the relative concentrations of a tRNA and its cognate aminoacyl-tRNA synthetase are normally well balanced and crucial for maintenance of accurate aminoacylation. When Escherichia coli Gln-tRNA synthetase is overproduced in vivo, it incorrectly acylates the supF amber suppressor tRNA(Tyr) with Gln. This effect is abolished when the intracellular concentration of the cognate tRNA(Gln2) is also elevate. These data indicate that the presence of aminoacyl-tRNA synthetase and the cognate tRNAs in complexed form, which requires the proper balance of the two macromolecules, is critical in maintaining the fidelity of protein biosynthesis. Thus, limits exist on the relative levels of tRNAs and aminoacyl-tRNA synthetases within a cell.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Swanson, R -- Hoben, P -- Sumner-Smith, M -- Uemura, H -- Watson, L -- Soll, D -- New York, N.Y. -- Science. 1988 Dec 16;242(4885):1548-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, CT 06511.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3144042" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acyl-tRNA Synthetases/genetics/*metabolism ; Escherichia coli/enzymology/*genetics ; Kinetics ; Plasmids ; RNA, Transfer, Amino Acid-Specific/*metabolism ; RNA, Transfer, Gln/*metabolism ; beta-Galactosidase/genetics/metabolism
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  • 7
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    Newly identified brain potassium channels gated by the guanine nucleotide binding protein Go (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-12-09
    Description: Potassium channels in neurons are linked by guanine nucleotide binding (G) proteins to numerous neurotransmitter receptors. The ability of Go, the predominant G protein in the brain, to stimulate potassium channels was tested in cell-free membrane patches of hippocampal pyramidal neurons. Four distinct types of potassium channels, which were otherwise quiescent, were activated by both isolated brain G0 and recombinant Go alpha. Hence brain Go can couple diverse brain potassium channels to neurotransmitter receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉VanDongen, A M -- Codina, J -- Olate, J -- Mattera, R -- Joho, R -- Birnbaumer, L -- Brown, A M -- DK-19318/DK/NIDDK NIH HHS/ -- HL-31154/HL/NHLBI NIH HHS/ -- HL-37044/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1988 Dec 9;242(4884):1433-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Molecular Biophysics, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3144040" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Imidodiphosphate/pharmacology ; Animals ; Cattle ; Electric Conductivity ; GTP-Binding Proteins/*pharmacology ; Hippocampus/*physiology ; In Vitro Techniques ; Kinetics ; Macromolecular Substances ; Membrane Potentials/drug effects ; Potassium Channels/drug effects/*physiology ; Pyramidal Tracts/physiology ; Rats ; Recombinant Proteins/*pharmacology
    Print ISSN: 0036-8075
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  • 8
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    Cachectin/TNF and IL-1 induced by glucose-modified proteins: role in normal tissue remodeling (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-06-10
    Description: Proteins undergo a series of nonenzymatic reactions with glucose over time to form advanced glycosylation end products (AGEs). Macrophages have a receptor that recognizes the AGE moiety and mediates the uptake and degradation of AGE proteins. This removal process is associated with the production and secretion of cachectin (tumor necrosis factor) and interleukin-1, two cytokines with diverse and seemingly paradoxical biological activities. The localized release and action of these cytokines could account for the coordinated removal and replacement of senescent extracellular matrix components in normal tissue homeostasis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vlassara, H -- Brownlee, M -- Manogue, K R -- Dinarello, C A -- Pasagian, A -- R01-AI15674/AI/NIAID NIH HHS/ -- R01-AM19655/AM/NIADDK NIH HHS/ -- R01-AM33861/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1988 Jun 10;240(4858):1546-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Medical Biochemistry, Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3259727" target="_blank"〉PubMed〈/a〉
    Keywords: Glycosylation ; Humans ; Interleukin-1/*biosynthesis/genetics ; Kinetics ; Membrane Glycoproteins/*physiology ; Monocytes/*metabolism ; Protein Biosynthesis ; RNA, Messenger/genetics ; Tumor Necrosis Factor-alpha/*biosynthesis/genetics
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  • 9
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    Modulation of acetylcholine receptor desensitization by forskolin is independent of cAMP (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-06-17
    Description: Biochemical and electrophysiological studies suggest that adenosine 3',5'-monophosphate (cAMP)-dependent phosphorylation of the nicotinic acetylcholine receptor channel is functionally significant because it modifies the receptor's rate of desensitization to acetylcholine. In studies that support this conclusion researchers have used forskolin to stimulate cAMP-dependent phosphorylation in intact muscle. It is now shown that although forskolin facilitated desensitization in voltage-clamped rat muscle, this effect was not correlated with the abilities of forskolin and forskolin analogs to activate adenylate cyclase or phosphorylate the receptor. Furthermore, elevation of intracellular cAMP or addition of the catalytic subunit of A-kinase failed to alter desensitization. Therefore, in intact skeletal muscle, cAMP-dependent phosphorylation does not modulate desensitization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wagoner, P K -- Pallotta, B S -- GM32211/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Jun 17;240(4859):1655-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Pharmacology, Glaxo Research Laboratories, Chapel Hill, NC 27599.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2454507" target="_blank"〉PubMed〈/a〉
    Keywords: 1-Methyl-3-isobutylxanthine/pharmacology ; Acetylcholine/pharmacology ; Adenylyl Cyclases/metabolism ; Animals ; Bucladesine/pharmacology ; Colforsin/*pharmacology ; Cyclic AMP/analogs & derivatives/*pharmacology ; Electric Conductivity ; Enzyme Activation/drug effects ; Kinetics ; Muscles/*metabolism ; Phosphorylation ; Rats ; Receptors, Cholinergic/drug effects/*physiology ; Torpedo/metabolism
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  • 10
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    Regulation of a heart potassium channel by protein kinase A and C (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-10-07
    Description: The enzymes adenosine 3',5'-monophosphate (cAMP)-dependent protein kinase (protein kinase A) and protein kinase C regulate the activity of a diverse group of cellular proteins including membrane ion channel proteins. When protein kinase A was stimulated in cardiac ventricular myocytes with the membrane-soluble cAMP analog 8-chlorphenylthio cAMP (8-CPT cAMP), the amplitude of the delayed-rectifier potassium current (IK) doubled when recorded at 32 degrees C but was not affected at 22 degrees C. In contrast, modulation of the calcium current (ICa) by 8-CPT cAMP was independent of temperature with similar increases in ICa occurring at both temperatures. Stimulation of protein kinase C by phorbol 12,13-dibutyrate also enhanced IK in a temperature-dependent manner but failed to increase ICa at either temperature. Thus, cardiac delayed-rectifier potassium but not calcium channels are regulated by two distinct protein kinases in a similar temperature-dependent fashion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Walsh, K B -- Kass, R S -- New York, N.Y. -- Science. 1988 Oct 7;242(4875):67-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of Rochester, School of Medicine and Dentistry, NY 14642.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2845575" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cyclic AMP/*analogs & derivatives/pharmacology ; Guinea Pigs ; Heart/*physiology ; Homeostasis ; In Vitro Techniques ; Kinetics ; Membrane Potentials ; Potassium Channels/*physiology ; Protein Kinase C/*metabolism ; Protein Kinases/*metabolism ; Thermodynamics ; Thionucleotides/*pharmacology ; Ventricular Function
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  • 11
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    AP1/jun function is differentially induced in promotion-sensitive and resistant JB6 cells (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-05-05
    Description: Tumor promoters may bring about events that lead to neoplastic transformation by inducing specific promotion-relevant effector genes. Functional activation of the transacting transcription factor AP-1 by the phorbol ester 12-O-tetradecanoylphorbol-13-acetate (TPA) may play an essential role in this process. Clonal genetic variants of mouse epidermal JB6 cells that are genetically susceptible (P+) or resistant (P-) to promotion of transformation by TPA were transfected with 3XTRE-CAT, a construct that has AP-1 cis-enhancer sequences attached to a reporter gene encoding chloramphenicol acetyltransferase (CAT). Transfected JB6 P+, but not P- variants, showed TPA-inducible CAT synthesis. Epidermal growth factor, another transformation promoter in JB6 cells, also caused P+ specific induction of CAT gene expression. These results demonstrate an association between induced AP-1 function and sensitivity to promotion of neoplastic transformation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bernstein, L R -- Colburn, N H -- New York, N.Y. -- Science. 1989 May 5;244(4904):566-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Johns Hopkins University, Department of Biology, Baltimore, MD 21218.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2541502" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; *Cell Transformation, Neoplastic ; Chloramphenicol O-Acetyltransferase/genetics ; Cloning, Molecular ; DNA-Binding Proteins/genetics/*physiology ; Epidermal Growth Factor/pharmacology ; Epidermis ; Gene Expression Regulation ; Genetic Variation ; Kinetics ; Mice ; Nucleic Acid Hybridization ; Plasmids ; Promoter Regions, Genetic ; Proto-Oncogene Proteins ; Proto-Oncogene Proteins c-jun ; Simplexvirus/genetics ; Tetradecanoylphorbol Acetate/*pharmacology ; Transcription Factors/genetics/*physiology ; Transfection
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  • 12
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    Catalytic antibodies with lipase activity and R or S substrate selectivity (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-04-28
    Description: The specific hydrolysis of unactivated esters bearing an R or S enantiomeric alcohol has been achieved by two separate classes of catalytic antibodies induced to bind either the R or S substrates. The antibodies exhibit rate accelerations (10(3) to 10(5] above background hydrolysis that, coupled with their antipodal specificity, provide a novel set of reagents for use in synthesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Janda, K D -- Benkovic, S J -- Lerner, R A -- New York, N.Y. -- Science. 1989 Apr 28;244(4903):437-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Research Institute of Scripps Clinic, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2717936" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antibodies, Monoclonal/immunology ; Antibody Specificity ; Antigens/immunology ; Benzyl Alcohols/metabolism ; *Catalysis ; Esters/metabolism ; Haptens ; Hemocyanin/immunology ; Hydrolysis ; Immunization ; Kinetics ; Lipase/*metabolism ; Mice ; Mice, Inbred A ; Molecular Structure ; Organophosphonates/immunology ; Stereoisomerism ; Substrate Specificity
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  • 13
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    Effect of antisense c-raf-1 on tumorigenicity and radiation sensitivity of a human squamous carcinoma (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-03-10
    Description: Antisense RNA-mediated inhibition of gene expression was used to investigate the biological function of the c-raf-1 gene in a radiation-resistant human squamous carcinoma cell line, SQ-20B. S1 nuclease protection assays revealed that transfection of full-length raf complementary DNA in the antisense orientation (AS) leads to a specific reduction (greater than tenfold) of steady-state levels of the endogenous c-raf-1 sense (S) transcript in SQ-20B cells. In nude mice, the malignant potential of SQ-20B cells transfected with raf (S) was significantly increased relative to that of SQ-20B cells transfected with raf (AS). SQ-20B cells containing transfected raf (S) maintained a radiation-resistant phenotype as compared to those cells harboring the AS version, which appeared to have enhanced radiation sensitivity. These data indicate that the reduced expression of endogenous c-raf-1 is sufficient to modulate the tumorigenicity and the radiation-resistant phenotype of SQ-20B cells, thus implicating c-raf-1 in a pathway important to the genesis of this type of cancer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kasid, U -- Pfeifer, A -- Brennan, T -- Beckett, M -- Weichselbaum, R R -- Dritschilo, A -- Mark, G E -- New York, N.Y. -- Science. 1989 Mar 10;243(4896):1354-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Radiation Medicine, Vincent T. Lombardi Comprehensive Cancer Research Center, Georgetown University Medical Center, Washington 20007.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2466340" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blotting, Southern ; Carcinoma, Squamous Cell/*genetics ; Cell Line ; Cell Survival/*radiation effects ; Clone Cells ; Dose-Response Relationship, Radiation ; *Gene Expression Regulation ; Humans ; Kinetics ; Mice ; Mice, Nude ; Neoplasm Transplantation ; Nucleic Acid Hybridization ; *Proto-Oncogenes ; RNA/*genetics ; RNA, Antisense ; RNA, Messenger/*antagonists & inhibitors ; Transcription, Genetic ; Transfection ; Transplantation, Heterologous ; Tumor Cells, Cultured/*radiation effects
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  • 14
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    Potassium channels in cardiac cells activated by arachidonic acid and phospholipids (1989)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1989-06-09
    Description: Two types of potassium-selective channels activated by intracellular arachidonic acid or phosphatidylcholine have been found in neonatal rat atrial cells. In inside-out patches, arachidonic acid and phosphatidylcholine each opened outwardly rectifying potassium-selective channels with conductances of 160 picosiemens (IK.AA) and 68 picosiemens (IK.PC), respectively. These potassium channels were not sensitive to internally applied adenosine triphosphate (ATP), magnesium, or calcium. Lowering the intracellular pH from 7.2 to 6.8 or 6.4 reversibly increased IK.AA channel activity three- or tenfold, respectively. A number of fatty acid derivatives were tested for their ability to activate IK.AA. These potassium-selective channels may help explain the increase in potassium conductance observed in ischemic cells and raise the possibility that fatty acid derivatives act as second messengers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, D -- Clapham, D E -- HL 34873/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1989 Jun 9;244(4909):1174-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Mayo Foundation, Rochester, MN 55905.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2727703" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Animals, Newborn ; Arachidonic Acids/*pharmacology ; Atrial Function ; Heart/*physiology ; Hydrogen-Ion Concentration ; In Vitro Techniques ; Kinetics ; Membrane Potentials ; Phosphatidylcholines/*pharmacology ; Potassium Channels/drug effects/*physiology ; Rats
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  • 15
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    Neutrophil Mac-1 and MEL-14 adhesion proteins inversely regulated by chemotactic factors (1989)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1989-09-15
    Description: The neutrophil Mac-1 and gp100MEL-14 adhesion proteins are involved in neutrophil extravasation during inflammation. Both the expression and activity of Mac-1 are greatly increased after neutrophil activation. In contrast, neutrophils shed gp100MEL-14 from the cell surface within 4 minutes after activation with chemotactic factors or phorbol esters, releasing a 96-kilodalton fragment of the antigen into the supernatant. Immunohistology showed that gp100MEL-14 was downregulated on neutrophils that had extravasated into inflamed tissue. The gp100MEL-14 adhesion protein may participate in the binding of unactivated neutrophils to the endothelium; rapid shedding of gp100MEL-14 may prevent extravasation into and damage of normal tissues by activated neutrophils.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kishimoto, T K -- Jutila, M A -- Berg, E L -- Butcher, E C -- AI 19957/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1989 Sep 15;245(4923):1238-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Stanford University, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2551036" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Differentiation/*immunology ; Antigens, Surface/*immunology ; Bone Marrow Cells ; Cell Adhesion ; Cell Adhesion Molecules ; Chemotactic Factors/*physiology ; Complement C5/physiology ; Complement C5a ; Fluorescent Antibody Technique ; Interleukin-1/physiology ; Interleukin-8 ; Kinetics ; Leukotriene B4/physiology ; Lipopolysaccharides/physiology ; Lymphocyte Activation ; Macrophage Activation ; Macrophage-1 Antigen ; Mice ; Mice, Inbred BALB C ; Neutrophils/cytology/*immunology ; Tetradecanoylphorbol Acetate ; Tumor Necrosis Factor-alpha/physiology
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  • 16
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    Enhanced activity and altered specificity of phospholipase A2 by deletion of a surface loop (1989)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1989-04-07
    Description: Protein engineering and x-ray crystallography have been used to study the role of a surface loop that is present in pancreatic phospholipases but is absent in snake venom phospholipases. Removal of residues 62 to 66 from porcine pancreatic phospholipase A2 does not change the binding constant for micelles significantly, but it improves catalytic activity up to 16 times on micellar (zwitterionic) lecithin substrates. In contrast, the decrease in activity on negatively charged substrates is greater than fourfold. A crystallographic study of the mutant enzyme shows that the region of the deletion has a well-defined structure that differs from the structure of the wild-type enzyme. No structural changes in the active site of the enzyme were detected.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kuipers, O P -- Thunnissen, M M -- de Geus, P -- Dijkstra, B W -- Drenth, J -- Verheij, H M -- de Haas, G H -- New York, N.Y. -- Science. 1989 Apr 7;244(4900):82-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Utrecht, The Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2704992" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Crystallography ; Enzyme Activation ; Kinetics ; Molecular Sequence Data ; Mutation ; Pancreas/enzymology ; Phospholipases/*metabolism ; Phospholipases A/genetics/*metabolism/physiology ; Phospholipases A2 ; *Protein Conformation ; Snake Venoms/analysis ; Structure-Activity Relationship ; Swine
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  • 17
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    Triggering of allostery in an enzyme by a point mutation: ornithine transcarbamoylase (1989)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1989-08-04
    Description: The origin of allostery is an unanswered question in the evolution of complex regulatory proteins. Anabolic ornithine transcarbamoylase, a trimer of identical subunits, is not an allosteric enzyme per se. However, when the active-site residue arginine-106 of the Escherichia coli enzyme is replaced with a glycine through site-directed mutagenesis, the resultant mutant enzyme manifests substrate cooperativity that is absent in the wild-type enzyme. Both homotropic and heterotropic interactions occur in the mutant enzyme. The initial velocity saturation curves of the substrates, carbamoyl phosphate and L-ornithine, conform to the Hill equation. The observed cooperativity depends on substrate but not enzyme concentration. The finding underscores the possibility that a single mutation of the enzyme in the cell could turn transcarbamoylation into a regulatory junction in the biosynthesis of L-arginine and urea.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kuo, L C -- Zambidis, I -- Caron, C -- DK01721/DK/NIDDK NIH HHS/ -- DK38089/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1989 Aug 4;245(4917):522-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Metcalf Center for Science and Engineering, Boston University, MA 02215.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2667139" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Binding Sites ; Carbamyl Phosphate/metabolism ; Escherichia coli/*enzymology ; Glycine ; Kinetics ; Macromolecular Substances ; *Mutation ; Ornithine/metabolism ; Ornithine Carbamoyltransferase/*genetics/metabolism ; Structure-Activity Relationship ; Zinc/pharmacology
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  • 18
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    Purification and complementary DNA cloning of a receptor for basic fibroblast growth factor (1989)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1989-07-07
    Description: Basic fibroblast growth factor (bFGF) participates in many processes including early developmental events, angiogenesis, wound healing, and maintenance of neuronal cell viability. A 130-kilodalton protein was isolated on the basis of its ability to specifically bind to bFGF. A complementary DNA clone was isolated with an oligonucleotide probe corresponding to determined amino acid sequences of tryptic peptide fragments of the purified protein. The putative bFGF receptor encoded by this complementary DNA is a transmembrane protein that contains three extracellular immunoglobulin-like domains, an unusual acidic region, and an intracellular tyrosine kinase domain. These domains are arranged in a pattern that is different from that of any growth factor receptor described.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, P L -- Johnson, D E -- Cousens, L S -- Fried, V A -- Williams, L T -- CA 21765/CA/NCI NIH HHS/ -- R01 HL32898/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1989 Jul 7;245(4913):57-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Medicine, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2544996" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cells, Cultured ; Chick Embryo ; *Cloning, Molecular ; DNA/*genetics ; Fibroblast Growth Factors/*genetics ; Kinetics ; Mice ; Molecular Sequence Data ; Peptide Fragments/analysis ; Receptors, Cell Surface/*genetics/metabolism ; Receptors, Fibroblast Growth Factor ; Recombinant Proteins/metabolism
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  • 19
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    Assembly of the native heterodimer of Rana esculenta tropomyosin by chain exchange (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-11-17
    Description: Rana esculenta tropomyosin assembles in vivo into a coiled-coil alpha helix from two different subunits, alpha and beta, which are present in about equal concentrations. Although the native composition is alpha beta, a mixture of equal amounts of alpha alpha and beta beta is produced by refolding dissociated alpha and beta at low temperature in vitro. Refolding kinetics showed that alpha alpha formed first and was relatively stable with regard to chain exchange below approximately 20 degrees C. Equilibration of the homodimer mixture at 30 degrees and 34 degrees C for long times, however, resulted in the formation of the native alpha beta molecule by chain exchange. Biosynthesis of alpha beta from separate alpha and beta genes is, therefore, favored thermodynamically over the formation of homodimers, and biological factors need not be invoked to explain the preferred native alpha beta composition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lehrer, S S -- Qian, Y D -- Hvidt, S -- HL22461/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1989 Nov 17;246(4932):926-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Muscle Research, Boston Biomedical Research Institute, MA 02114.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2814515" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Kinetics ; Macromolecular Substances ; Muscle, Smooth/metabolism ; Muscles/metabolism ; Myocardium/metabolism ; Protein Conformation ; Protein Denaturation ; Protein Processing, Post-Translational ; Rana esculenta ; Thermodynamics ; Tropomyosin/genetics/*metabolism
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  • 20
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    Correct folding of circularly permuted variants of a beta alpha barrel enzyme in vivo (1989)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1989-01-13
    Description: An important question in protein folding is whether the natural amino and carboxyl termini and the given order of secondary structure segments are critical to the stability and to the folding pathway of proteins. Here it is shown that two circularly permuted versions of the gene of a single-domain beta alpha barrel enzyme can be expressed in Escherichia coli. The variants are enzymically active and are practically indistinguishable from the original enzyme by several structural and spectroscopic criteria, despite the creation of new termini and the cleavage of a surface loop. This novel genetic approach should be useful for protein folding studies both in vitro and in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Luger, K -- Hommel, U -- Herold, M -- Hofsteenge, J -- Kirschner, K -- New York, N.Y. -- Science. 1989 Jan 13;243(4888):206-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Abteilung Biophysikalische Chemie, Universitat Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2643160" target="_blank"〉PubMed〈/a〉
    Keywords: *Aldose-Ketose Isomerases ; Amino Acid Sequence ; Base Sequence ; Carbohydrate Epimerases/*genetics/metabolism ; Circular Dichroism ; *Cloning, Molecular ; Enzyme Stability ; Escherichia coli/*enzymology/genetics ; *Genes ; Genetic Variation ; Kinetics ; Molecular Sequence Data ; *Protein Conformation ; Spectrometry, Fluorescence ; Spectrophotometry, Ultraviolet
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  • 21
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    Identification of an AUUUA-specific messenger RNA binding protein (1989)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1989-11-03
    Description: An important control point in gene expression is at the level of messenger RNA (mRNA) stability. The mRNAs of certain regulatory cellular proteins such as oncogenes, cytokines, lymphokines, and transcriptional activators are extremely labile. These messages share a common AUUUA pentamer in their 3' untranslated region, which confers cytoplasmic instability. A cytosolic protein was identified that binds specifically to RNA molecules containing four reiterations of the AUUUA structural element. This protein consists of three subunits and binds rapidly to AUUUA-containing RNA. Such protein-RNA complexes are resistant to the actions of denaturing and reducing agents, demonstrating very stable binding. The time course, stability, and specificity of the protein-AUUUA interaction suggests the possibility that the formation of this complex may target susceptible mRNA for rapid cytoplasmic degradation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Malter, J S -- CA01427-01/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1989 Nov 3;246(4930):664-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Tulane University School of Medicine, New Orleans, LA 70112.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2814487" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding, Competitive ; Carrier Proteins/isolation & purification/*metabolism ; Cell Line ; Humans ; Kinetics ; Macromolecular Substances ; Molecular Weight ; *Nucleocytoplasmic Transport Proteins ; RNA, Messenger/*metabolism ; *RNA-Binding Proteins ; Ribonuclease, Pancreatic
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  • 22
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    Arachidonic acid and other fatty acids directly activate potassium channels in smooth muscle cells (1989)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1989-06-09
    Description: Arachidonic acid, as well as fatty acids that are not substrates for cyclooxygenase and lipoxygenase enzymes, activated a specific type of potassium channel in freshly dissociated smooth muscle cells. Activation occurred in excised membrane patches in the absence of calcium and all nucleotides. Therefore signal transduction pathways that require such soluble factors, including the NADPH-dependent cytochrome P450 pathway, do not mediate the response. Thus, fatty acids directly activate potassium channels and so may constitute a class of signal molecules that regulate ion channels.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ordway, R W -- Walsh, J V Jr -- Singer, J J -- DK-31620/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1989 Jun 9;244(4909):1176-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of Massachusetts Medical School, Worcester 01655.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2471269" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arachidonic Acid ; Arachidonic Acids/*pharmacology ; Bufo marinus ; Fatty Acids, Nonesterified/*pharmacology ; In Vitro Techniques ; Ion Channels/drug effects/*physiology ; Kinetics ; Membrane Potentials/drug effects ; Muscle, Smooth/*physiology ; Stomach/physiology
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  • 23
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    The anticodon contains a major element of the identity of arginine transfer RNAs (1989)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1989-12-22
    Description: The contribution of the anticodon to the discrimination between cognate and noncognate tRNAs by Escherichia coli Arg-tRNA synthetase has been investigated by in vitro synthesis and aminoacylation of elongator methionine tRNA (tRNA(mMet) mutants. Substitution of the Arg anticodon CCG for the Met anticodon CAU leads to a dramatic increase in Arg acceptance by tRNA(mMet). A nucleotide (A20) previously identified by others in the dihydrouridine loop of tRNA(Arg)s makes a smaller contribution to the conversion of tRNA(mMet) identity from Met to Arg. The combined anticodon and dihydrouridine loop mutations yield a tRNA(mMet) derivative that is aminoacylated with near-normal kinetics by the Arg-tRNA synthetase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schulman, L H -- Pelka, H -- New York, N.Y. -- Science. 1989 Dec 22;246(4937):1595-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Developmental Biology and Cancer, Albert Einstein College of Medicine, Bronx, NY 10461.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2688091" target="_blank"〉PubMed〈/a〉
    Keywords: Anticodon/*genetics ; Arginine-tRNA Ligase/metabolism ; Base Sequence ; Escherichia coli/enzymology/genetics ; Kinetics ; Methionine-tRNA Ligase/metabolism ; Molecular Sequence Data ; Nucleic Acid Conformation ; RNA, Transfer/*genetics ; RNA, Transfer, Amino Acid-Specific/*genetics ; RNA, Transfer, Arg/*genetics ; Substrate Specificity ; T-Phages/genetics ; Transcription, Genetic
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  • 24
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    Catalytic hydrolysis of vasoactive intestinal peptide by human autoantibody (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-06-09
    Description: Vasoactive intestinal peptide (VIP) labeled with 125I, [Tyr10-125I]VIP, can be hydrolyzed by immunoglobulin G (IgG) purified from a human subject, as judged by trichloroacetic acid precipitation and reversed-phase high-performance liquid chromatography (HPLC). The hydrolytic activity was precipitated by antibody to human IgG, it was bound by immobilized protein G and showed a molecular mass close to 150 kilodaltons by gel filtration chromatography, properties similar to those of authentic IgG. The Fab fragment, prepared from IgG by papain treatment, retained the VIP hydrolytic activity of the IgG. Peptide fragments produced by treatment of VIP with the antibody fraction were purified by reversed-phase HPLC and identified by fast atom bombardment-mass spectrometry and peptide sequencing. The scissile bond in VIP deduced from these experiments was Gln16-Met17. The antibody concentration (73.4 fmol per milligram of IgG) and the Kd (0.4 nM) were computed from analysis of VIP binding under conditions that did not result in peptide hydrolysis. Analysis of the antibody-mediated VIP hydrolysis at varying concentrations of substrate suggested conformity with Michaelis-Menton kinetics (Km). The values for Km (37.9 X 10(-9) M) and the turnover number kcat (15.6 min-1) suggested relatively tight VIP binding and a moderate catalytic efficiency of the antibody.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Paul, S -- Volle, D J -- Beach, C M -- Johnson, D R -- Powell, M J -- Massey, R J -- HL 35506/HL/NHLBI NIH HHS/ -- HL 40348/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1989 Jun 9;244(4909):1158-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Nebraska Medical Center, Omaha 68105.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2727702" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Autoantibodies ; Catalysis ; Chromatography, High Pressure Liquid ; Humans ; Hydrolysis ; Immunoglobulin Fab Fragments ; *Immunoglobulin G ; Kinetics ; Molecular Sequence Data ; Peptide Fragments/isolation & purification ; Vasoactive Intestinal Peptide/*immunology
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  • 25
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    Inhibition of a class C beta-lactamase by a specific phosphonate monoester (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-11-17
    Description: A phosphonate monoester, m-carboxyphenyl phenylacetamidomethylphosphonate, has been found to be a specific inhibitor of the class C beta-lactamase of Enterobacter cloacae P99. Inactivation is rapid (10(3) per second per molar concentration) and reactivation very slow (2.2 X 10(-6) per second). Apparently concerted with the inactivation, one equivalent (with respect to the enzyme) of m-hydroxybenzoate is released. Reactivation is accelerated by hydroxylamine and benzohydroxamate. This suggests that the loss of enzyme activity is due to phosphonylation of an active site functional group. This discovery holds the promise of a new general class of beta-lactamase inhibitors and, perhaps, antibiotics.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pratt, R F -- New York, N.Y. -- Science. 1989 Nov 17;246(4932):917-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Chemistry Department, Wesleyan University, Middletown, CT 06457.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2814513" target="_blank"〉PubMed〈/a〉
    Keywords: Enterobacter/*enzymology ; Enterobacteriaceae/*enzymology ; Hydroxamic Acids/pharmacology ; Hydroxylamine ; Hydroxylamines/pharmacology ; Kinetics ; Organophosphorus Compounds/*pharmacology ; Protein Binding ; *beta-Lactamase Inhibitors
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  • 26
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    Role of Na+/H+ exchange by interferon-gamma in enhanced expression of JE and I-A beta genes (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-04-28
    Description: The rapid transductional sequences initiated by interferon-gamma (IFN-gamma) on binding to its receptor regulate functional and genomic responses in many cells but are not well defined. Induction of macrophage activation is an example of such functional and genomic changes in response to IFN-gamma. Addition of IFN-gamma to murine macrophages, at activating concentrations, produced rapid (within 60 seconds) alkalinization of the cytosol and a concomitant, rapid influx of 22Na+. Amiloride inhibited the ion fluxes and the accumulation of specific messenger RNA for two genes induced by IFN-gamma (the early gene JE and the beta chain of the class II major histocompatibility complex gene I-A). The data indicate that IFN-gamma initiates rapid exchange of Na+ and H+ by means of the Na+/H+ antiporter and that these amiloride-sensitive ion fluxes are important to some of the genomic effects of IFN-gamma.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Prpic, V -- Yu, S F -- Figueiredo, F -- Hollenbach, P W -- Gawdi, G -- Herman, B -- Uhing, R J -- Adams, D O -- New York, N.Y. -- Science. 1989 Apr 28;244(4903):469-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Duke University Medical Center, Durham, NC 27710.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2541500" target="_blank"〉PubMed〈/a〉
    Keywords: Amiloride/pharmacology ; Animals ; Carrier Proteins/antagonists & inhibitors/metabolism ; Cells, Cultured ; Cytosol/metabolism ; *Gene Expression Regulation ; Histocompatibility Antigens Class II/*genetics ; Hydrogen-Ion Concentration ; Interferon-gamma/*physiology ; Kinetics ; Macrophage Activation ; Macrophages/drug effects/metabolism ; Mice ; *Protons ; RNA, Messenger/biosynthesis ; Sodium/*metabolism ; Sodium-Hydrogen Antiporter
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    The product of the mos proto-oncogene as a candidate "initiator" for oocyte maturation (1989)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1989-08-11
    Description: The endogenous c-mos product, pp39mos, is required for progesterone-induced meiotic maturation in Xenopus oocytes. Treatment of oocytes with progesterone induced a rapid increase in pp39mos that preceded both the activation of maturation promoting factor (MPF) and germinal vesicle breakdown (GVBD). Microinjection of synthetic mos RNA into oocytes activated MPF and induced GVBD in the absence of progesterone. Thus, the mos proto-oncogene product may qualify as a candidate "initiator" protein of MPF and is at least one of the "triggers" for G2 to M transition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sagata, N -- Daar, I -- Oskarsson, M -- Showalter, S D -- Vande Woude, G F -- N01-CO-74101/CO/NCI NIH HHS/ -- New York, N.Y. -- Science. 1989 Aug 11;245(4918):643-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉BRI-Basic Research Program, National Cancer Institute, Frederick Cancer Research Facility, MD 21701.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2474853" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cycloheximide/pharmacology ; Female ; Growth Substances/physiology ; Kinetics ; Maturation-Promoting Factor ; Meiosis/drug effects ; Microinjections ; Oocytes/*physiology ; Progesterone/pharmacology ; Protein Biosynthesis ; Proto-Oncogene Proteins/genetics/*physiology ; Proto-Oncogene Proteins c-mos ; RNA/genetics ; Transcription, Genetic ; Transfection ; Xenopus
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    Epithelial cell surfaces induce Salmonella proteins required for bacterial adherence and invasion (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-02-17
    Description: Salmonella bacteria are capable of entering (invading) and multiplying within eukaryotic cells. Stable adherence to and invasion of epithelial cells by S. choleraesuis and S. typhimurium were found to require de novo synthesis of several new bacterial proteins. This inducible event appears to be a coordinately regulated system dependent on trypsin- and neuraminidase-sensitive structures present on the epithelial cell surface. Mutants of S. choleraesuis and S. typhimurium were unable to synthesize these proteins and did not stably adhere to nor invade eukaryotic cells. Two such S. typhimurium mutants were avirulent in mice, an indication that these proteins are required for Salmonella virulence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Finlay, B B -- Heffron, F -- Falkow, S -- AI26195/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1989 Feb 17;243(4893):940-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medical Microbiology, Stanford University School of Medicine, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2919285" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Bacterial Adhesion ; Bacterial Proteins/*biosynthesis ; Cell Line ; Epithelium/physiology ; Kinetics ; Methionine/metabolism ; Salmonella/pathogenicity/*physiology ; Sulfur Radioisotopes
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    Specific interactions in RNA enzyme-substrate complexes (1989)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1989-12-22
    Description: Analysis of crosslinked complexes of M1 RNA, the catalytic RNA subunit of ribonuclease P from Escherichia coli, and transfer RNA precursor substrates has led to the identification of regions in the enzyme and in the substrate that are in close physical proximity to each other. The nucleotide in M1 RNA, residue C92, which participates in a crosslink with the substrate was deleted and the resulting mutant M1 RNA was shown to cleave substrates lacking the 3' terminal CCAUCA sequence at sites several nucleotides away from the normal site of cleavage. The presence or absence of the 3' terminal CCAUCA sequence in transfer RNA precursor substrates markedly affects the way in which these substrates interact with the catalytic RNA in the enzyme-substrate complex. The contacts between wild-type M1 RNA and its substrate are in a region that resembles part of the transfer RNA "E" (exit) site in 23S ribosomal RNA. These data demonstrate that in RNA's with very different cellular functions, there are domains with similar structural and functional properties and that there is a nucleotide in M1 RNA that affects the site of cleavage by the enzyme.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Guerrier-Takada, C -- Lumelsky, N -- Altman, S -- New York, N.Y. -- Science. 1989 Dec 22;246(4937):1578-84.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Yale University, New Haven, CT 06520.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2480641" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Endoribonucleases/genetics/*metabolism ; Escherichia coli/enzymology/*genetics ; *Escherichia coli Proteins ; Kinetics ; Molecular Sequence Data ; Nucleic Acid Conformation ; RNA Precursors/genetics ; RNA, Bacterial/*genetics/metabolism ; RNA, Transfer/genetics ; Ribonuclease P ; Substrate Specificity
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    Stereochemistry of RNA cleavage by the Tetrahymena ribozyme and evidence that the chemical step is not rate-limiting (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-05-12
    Description: The intervening sequence of the ribosomal RNA precursor of Tetrahymena is a catalytic RNA molecule, or ribozyme. Acting as a sequence-specific endoribonuclease, it cleaves single-stranded RNA substrates with concomitant addition of guanosine. The chemistry of the reaction has now been studied by introduction of a single phosphorothioate in the substrate RNA at the cleavage site. Kinetic studies show no significant effect of this substitution on kcat (rate constant) or Km (Michaelis constant), providing evidence that some step other than the chemical step is rate-limiting. Product analysis reveals that the reaction proceeds with inversion of configuration at phosphorus, consistent with an in-line, SN2 (P) mechanism. Thus, the ribozyme reaction is in the same mechanistic category as the individual displacement reactions catalyzed by protein nucleotidyltransferases, phosphotransferases, and nucleases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McSwiggen, J A -- Cech, T R -- GM28039/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1989 May 12;244(4905):679-83.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309-0215.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2470150" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Guanosine/metabolism ; Hydrolysis ; Kinetics ; Molecular Conformation ; Phosphates/metabolism ; Phosphorus ; RNA/*metabolism ; RNA Precursors/*metabolism ; RNA Splicing ; RNA, Catalytic ; RNA, Ribosomal/*metabolism ; Tetrahymena/*genetics ; Thionucleotides/metabolism
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    Double-stranded ribonuclease coinduced with interferon (1989)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1989-06-02
    Description: Double-stranded (ds) RNA and many viruses are inducers of interferon (IFN), the latter presumably because they contain, or can form, dsRNA. Concomitant with the induction of IFN in chicken embryo cells was the induction of a novel double-stranded ribonuclease (dsRNase), which was released into the medium and continued to accumulate long after IFN production ceased. Only avian cells (chicken, quail, turkey, or duck) expressed high levels of this dsRNase; mammalian, turtle, or fish cells did not. Production of the nuclease was inducer dose-dependent. Optimum pH and cation requirements distinguished it from other dsRNase activities. Degradation of dsRNA was endonucleolytic. Activity resided in a molecule of an Mr of approximately 34,500. Low levels of a single-stranded (ss) RNase activity were inseparable from the dsRNase. The role for a dsRNA-inducible dsRNase released from cells is unknown.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meegan, J M -- Marcus, P I -- AI18381/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1989 Jun 2;244(4908):1089-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, The University of Connecticut, Storrs 06269.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2471268" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Birds/embryology/*metabolism ; Cations ; Chick Embryo ; Ducks/embryology ; Endoribonucleases/*biosynthesis ; Enzyme Induction ; Hydrogen-Ion Concentration ; Interferon Inducers/pharmacology ; Interferons/*metabolism ; Kinetics ; Newcastle disease virus/physiology/radiation effects ; Poly I-C/pharmacology ; Quail/embryology ; RNA, Double-Stranded/metabolism ; Species Specificity ; Substrate Specificity ; Turkeys/embryology ; Ultraviolet Rays
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    Receptor-mediated drug delivery to macrophages in chemotherapy of leishmaniasis (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-05-12
    Description: Methotrexate coupled to maleylated bovine serum albumin was taken up efficiently through the "scavenger" receptors present on macrophages and led to selective killing of intracellular Leishmania mexicana amazonensis amastigotes in cultured hamster peritoneal macrophages. The drug conjugate was nearly 100 times as effective as free methotrexate in eliminating the intracellular parasites. Furthermore, in a model of experimental cutaneous leishmaniasis in hamsters, the drug conjugate brought about more than 90% reduction in the size of footpad lesions within 11 days. In contrast, the free drug at a similar concentration did not significantly affect lesion size. These studies demonstrate the potential of receptor-mediated drug delivery in the therapy of macrophage-associated diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mukhopadhyay, A -- Chaudhuri, G -- Arora, S K -- Sehgal, S -- Basu, S K -- New York, N.Y. -- Science. 1989 May 12;244(4905):705-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Microbial Technology, Chandigarh, India.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2717947" target="_blank"〉PubMed〈/a〉
    Keywords: Albumins/*administration & dosage/metabolism ; Animals ; Cells, Cultured ; Cricetinae ; Female ; Kinetics ; Leishmania mexicana/*drug effects ; Leishmaniasis/*drug therapy ; Macrophages/metabolism/*parasitology ; Male ; *Membrane Proteins ; Mesocricetus ; Methotrexate/*administration & dosage/pharmacology/therapeutic use ; *Receptors, Immunologic/metabolism ; *Receptors, Lipoprotein ; Receptors, Scavenger ; Scavenger Receptors, Class B ; Serum Albumin, Bovine
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    Steroid binding at sigma-"opioid" receptors (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-12-22
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schwarz, S -- Pohl, P -- Zhou, G Z -- New York, N.Y. -- Science. 1989 Dec 22;246(4937):1635-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2556797" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding, Competitive ; Brain/metabolism ; Kinetics ; Ligands ; Lymphocytes/metabolism ; Progesterone/blood/cerebrospinal fluid/metabolism ; Receptors, Opioid/*metabolism ; Receptors, sigma ; Steroids/*metabolism/pharmacology
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    Dispersed polaron simulations of electron transfer in photosynthetic reaction centers (1989)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1989-10-06
    Description: A microscopic method for simulating quantum mechanical, nuclear tunneling effects in biological electron transfer reactions is presented and applied to several electron transfer steps in photosynthetic bacterial reaction centers. In this "dispersed polaron" method the fluctuations of the protein and the electron carriers are projected as effective normal modes onto an appropriate reaction coordinate and used to evaluate the quantum mechanical rate constant. The simulations, based on the crystallographic structure of the reaction center from Rhodopseudomonas viridis, focus on electron transfer from a bacteriopheophytin to a quinone and the subsequent back-reaction. The rates of both of these reactions are almost independent of temperature or even increase with decreasing temperature. The simulations reproduce this unusual temperature dependence in a qualitative way, without the use of adjustable parameters for the protein's Franck-Condon factors. The observed dependence of the back-reaction on the free energy of the reaction also is reproduced, including the special behavior in the "inverted region."〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Warshel, A -- Chu, Z T -- Parson, W W -- GM-40283/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1989 Oct 6;246(4926):112-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of Southern California, Los Angeles 90007.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2675313" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*metabolism ; *Electron Transport ; Kinetics ; Models, Chemical ; *Photosynthesis ; Photosynthetic Reaction Center Complex Proteins ; Rhodopseudomonas/metabolism ; Thermodynamics
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    Direct Bronsted analysis of the restoration of activity to a mutant enzyme by exogenous amines (1989)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1989-03-17
    Description: A true Bronsted analysis of proton transfer in an enzyme mechanism is made possible by the chemical rescue of an inactive mutant of aspartate aminotransferase, where the endogenous general base, Lys258, is replaced with Ala by site-directed mutagenesis. Catalytic activity is restored to this inactive mutant by exogenous amines. The eleven amines studied generate a Bronsted correlation with beta of 0.4 for the transamination of cysteine sulfinate, when steric effects are included in the regression analysis. Localized mutagenesis thus allows the classical Bronsted analysis of transition-state structure to be applied to enzyme-catalyzed reactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Toney, M D -- Kirsch, J F -- GM07232/GM/NIGMS NIH HHS/ -- GM35393/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1989 Mar 17;243(4897):1485-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2538921" target="_blank"〉PubMed〈/a〉
    Keywords: Amines ; Aspartate Aminotransferases/*metabolism ; Binding Sites ; Catalysis ; Escherichia coli/enzymology ; Kinetics ; Lysine ; Mutation ; Protons
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    Block of stretch-activated ion channels in Xenopus oocytes by gadolinium and calcium ions (1989)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1989-02-24
    Description: Gadolinium ions produce three distinct kinds of block of the stretch-activated (SA) ion channels in Xenopus oocytes: a concentration-dependent reduction in channel open time, a concentration-dependent reduction in open channel current, and a unique, steeply concentration-dependent, reversible inhibition of channel opening. This last effect reduces the probability of a channel being open from about 10(-1) at 5 microM to less than 10(-5) at 10 microM gadolinium. Calcium has effects on open time and current similar to that of gadolinium, but this channel is permeable to calcium and calcium does not completely inhibit channel activity. The availability of a blocker for SA ion channels may help to define their physiological function, and will simplify the use of oocytes as an expression system for ion channels.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yang, X C -- Sachs, F -- DK-37792/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1989 Feb 24;243(4894 Pt 1):1068-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉State University of New York, Buffalo 14214.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2466333" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding, Competitive ; Calcium/*pharmacology ; Cations ; Electric Conductivity ; Female ; Gadolinium/*pharmacology ; Ion Channels/drug effects/*physiology ; Kinetics ; Oocytes/*physiology ; Xenopus
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    Rapid beta-adrenergic modulation of cardiac calcium channel currents by a fast G protein pathway (1989)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1989-07-07
    Description: beta-Adrenergic agonists activate the G protein, Gs, which stimulates cardiac calcium currents by both cytoplasmic, indirect and membrane-delimited, direct pathways. To test whether beta-adrenergic agonists might use both pathways in the heart, isoproterenol was rapidly applied to cardiac myocytes, resulting in a biphasic increase in cardiac calcium channel currents that had time constants of 150 milliseconds and 36 seconds. beta-Adrenergic antagonists of a G protein inhibitor blocked both the fast and slow responses, whereas the adenylyl cyclase activator forskolin produced only the slow response. The presence of a fast pathway in the heart can explain what the slow pathway cannot account for: the ability of cardiac sympathetic nerves to change heart rate within a single beat.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yatani, A -- Brown, A M -- HL36930/HL/NHLBI NIH HHS/ -- HL37044/HL/NHLBI NIH HHS/ -- NS23877/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1989 Jul 7;245(4913):71-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Physiology and Biophysics, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2544999" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Atrial Function ; Calcium Channels/drug effects/*physiology ; Carbachol/pharmacology ; Cells, Cultured ; Colforsin/pharmacology ; GTP-Binding Proteins/*physiology ; Guinea Pigs ; Heart/*physiology ; Isoproterenol/*pharmacology ; Kinetics ; Membrane Potentials/drug effects ; *Signal Transduction
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    Proton motive force involved in protein transport across the outer membrane of Aeromonas salmonicida (1989)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1989-11-03
    Description: Many Gram-negative bacteria export proteins to the exterior. Some of these proteins are first secreted into the periplasm and then cross the outer membrane in a separate step. The source of energy required for the translocation is unknown. Export of the extracellular protein proaerolysin from the periplasm through the outer membrane of Aeromonas salmonicida is inhibited by a proton ionophore and by low extracellular pH. One possible explanation of these results is that a proton gradient across the outer membrane is required for export.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wong, K R -- Buckley, J T -- New York, N.Y. -- Science. 1989 Nov 3;246(4930):654-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Microbiology, University of Victoria, BC, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2814486" target="_blank"〉PubMed〈/a〉
    Keywords: Aeromonas/drug effects/*metabolism ; Bacterial Toxins/*metabolism ; Carbonyl Cyanide m-Chlorophenyl Hydrazone/pharmacology ; Cell Membrane/metabolism ; Culture Media ; Hemolysin Proteins/*metabolism ; Hydrogen-Ion Concentration ; Kinetics ; Pore Forming Cytotoxic Proteins
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    Coherent control of retinal isomerization in bacteriorhodopsin (2006)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2006-09-02
    Description: Optical control of the primary step of photoisomerization of the retinal molecule in bacteriorhodopsin from the all-trans to the 13-cis state was demonstrated under weak field conditions (where only 1 of 300 retinal molecules absorbs a photon during the excitation cycle) that are relevant to understanding biological processes. By modulating the phases and amplitudes of the spectral components in the photoexcitation pulse, we showed that the absolute quantity of 13-cis retinal formed upon excitation can be enhanced or suppressed by +/-20% of the yield observed using a short transform-limited pulse having the same actinic energy. The shaped pulses were shown to be phase-sensitive at intensities too low to access different higher electronic states, and so these pulses apparently steer the isomerization through constructive and destructive interference effects, a mechanism supported by observed signatures of vibrational coherence. These results show that the wave properties of matter can be observed and even manipulated in a system as large and complex as a protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Prokhorenko, Valentyn I -- Nagy, Andrea M -- Waschuk, Stephen A -- Brown, Leonid S -- Birge, Robert R -- Miller, R J Dwayne -- R01 GM034548/GM/NIGMS NIH HHS/ -- R01 GM034548-17/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Sep 1;313(5791):1257-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Optical Sciences, Departments of Chemistry and Physics, University of Toronto, 80 St. George Street, M5S3H6, Toronto, Ontario, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16946063" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Bacteriorhodopsins/*chemistry ; Halobacterium salinarum/chemistry ; Isomerism ; Kinetics ; Lasers ; *Light ; Photochemistry ; Photons ; Quantum Theory ; Retinaldehyde/*chemistry ; Thermodynamics
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    Transcript-assisted transcriptional proofreading (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-07-29
    Description: Fidelity of template-dependent nucleic acid synthesis is the main determinant of stable heredity and error-free gene expression. The mechanism (or mechanisms) ensuring fidelity of transcription by DNA-dependent RNA polymerases (RNAPs) is not fully understood. Here, we show that the 3' end-proximal nucleotide of the nascent transcript stimulates hydrolysis of the penultimate phosphodiester bond by providing active groups and coordination bonds to the RNAP active center. This stimulation is much higher in the case of misincorporated nucleotide. We show that during transcription elongation, the hydrolytic reaction stimulated by misincorporated nucleotides proofreads most of the misincorporation events and thus serves as an intrinsic mechanism of transcription fidelity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zenkin, Nikolay -- Yuzenkova, Yulia -- Severinov, Konstantin -- New York, N.Y. -- Science. 2006 Jul 28;313(5786):518-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Waksman Institute, Rutgers University, Piscataway, NJ 08854, USA. nicserzen@mail.ru〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16873663" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Monophosphate/metabolism ; Base Pairing ; Binding Sites ; Catalysis ; Cytidine Monophosphate/metabolism ; DNA/metabolism ; DNA-Directed RNA Polymerases/*metabolism ; Hydrogen Bonding ; Hydrolysis ; Kinetics ; Magnesium/metabolism ; Models, Genetic ; Nucleotides/metabolism ; RNA, Messenger/*metabolism ; Templates, Genetic ; Thermus/enzymology ; *Transcription, Genetic
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    Atomic description of an enzyme reaction dominated by proton tunneling (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-04-15
    Description: We present an atomic-level description of the reaction chemistry of an enzyme-catalyzed reaction dominated by proton tunneling. By solving structures of reaction intermediates at near-atomic resolution, we have identified the reaction pathway for tryptamine oxidation by aromatic amine dehydrogenase. Combining experiment and computer simulation, we show proton transfer occurs predominantly to oxygen O2 of Asp(128)beta in a reaction dominated by tunneling over approximately 0.6 angstroms. The role of long-range coupled motions in promoting tunneling is controversial. We show that, in this enzyme system, tunneling is promoted by a short-range motion modulating proton-acceptor distance and no long-range coupled motion is required.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Masgrau, Laura -- Roujeinikova, Anna -- Johannissen, Linus O -- Hothi, Parvinder -- Basran, Jaswir -- Ranaghan, Kara E -- Mulholland, Adrian J -- Sutcliffe, Michael J -- Scrutton, Nigel S -- Leys, David -- New York, N.Y. -- Science. 2006 Apr 14;312(5771):237-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Manchester Interdisciplinary Biocentre, University of Manchester, Jackson's Mill, Post Office Box 88, Manchester M60 1QD, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16614214" target="_blank"〉PubMed〈/a〉
    Keywords: Alcaligenes faecalis/*enzymology ; Aspartic Acid/chemistry ; Binding Sites ; Catalysis ; Chemistry, Physical ; Computer Simulation ; Crystallography, X-Ray ; Kinetics ; Models, Chemical ; Motion ; Oxidation-Reduction ; Oxidoreductases Acting on CH-NH Group Donors/*chemistry/*metabolism ; Oxygen/chemistry ; Physicochemical Phenomena ; *Protons ; Temperature ; Thermodynamics ; Tryptamines/*metabolism ; Water/chemistry
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Protein dynamics control the kinetics of initial electron transfer in photosynthesis (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2007-05-05
    Description: The initial electron transfer dynamics during photosynthesis have been studied in Rhodobacter sphaeroides reaction centers from wild type and 14 mutants in which the driving force and the kinetics of charge separation vary over a broad range. Surprisingly, the protein relaxation kinetics, as measured by tryptophan absorbance changes, are invariant in these mutants. By applying a reaction-diffusion model, we can fit the complex electron transfer kinetics of each mutant quantitatively, varying only the driving force. These results indicate that initial photosynthetic charge separation is limited by protein dynamics rather than by a static electron transfer barrier.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Haiyu -- Lin, Su -- Allen, James P -- Williams, Joann C -- Blankert, Sean -- Laser, Christa -- Woodbury, Neal W -- New York, N.Y. -- Science. 2007 May 4;316(5825):747-50.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biodesign Institute, Arizona State University, 1001 South McAllister Avenue, Tempe, AZ 85287-5201, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17478721" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*chemistry/genetics/*metabolism ; Bacteriochlorophylls/metabolism ; *Electron Transport ; Kinetics ; Light ; Models, Chemical ; Mutation ; *Photosynthesis ; Photosynthetic Reaction Center Complex Proteins/*chemistry/genetics/*metabolism ; Rhodobacter sphaeroides/genetics/*metabolism ; Spectrum Analysis ; Temperature ; Thermodynamics ; Tryptophan/chemistry
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    Biochemistry. Enzyme motions inside and out (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-04-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Benkovic, Stephen J -- Hammes-Schiffer, Sharon -- GM24129/GM/NIGMS NIH HHS/ -- GM56207/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Apr 14;312(5771):208-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Pennsylvania State University, University Park, PA 16802, USA. sjb1@psu.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16614206" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Catalysis ; Chemistry, Physical ; Computer Simulation ; Hydrogen/chemistry ; Kinetics ; Models, Chemical ; Motion ; Oxidation-Reduction ; Oxidoreductases Acting on CH-NH Group Donors/*chemistry/*metabolism ; Physicochemical Phenomena ; Protein Conformation ; *Protons ; Thermodynamics ; Tryptamines/*metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Biochemistry. Photosynthesis from the protein's perspective (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2007-05-05
    Description: 〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3984475/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3984475/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Skourtis, Spiros S -- Beratan, David N -- R01 GM048043/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 May 4;316(5825):703-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics, University of Cyprus, Nicosia 1678, Cyprus. skourtis@ucy.ac.cy〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17478711" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*chemistry/*metabolism ; Bacteriochlorophylls/metabolism ; *Electron Transport ; Kinetics ; Light ; Models, Chemical ; *Photosynthesis ; Photosynthetic Reaction Center Complex Proteins/*chemistry/*metabolism ; Rhodobacter sphaeroides/genetics/*metabolism ; Spectrum Analysis ; Temperature ; Thermodynamics ; Tryptophan/chemistry
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    A 3-hydroxypropionate/4-hydroxybutyrate autotrophic carbon dioxide assimilation pathway in Archaea (2007)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2007-12-15
    Description: The assimilation of carbon dioxide (CO2) into organic material is quantitatively the most important biosynthetic process. We discovered that an autotrophic member of the archaeal order Sulfolobales, Metallosphaera sedula, fixed CO2 with acetyl-coenzyme A (acetyl-CoA)/propionyl-CoA carboxylase as the key carboxylating enzyme. In this system, one acetyl-CoA and two bicarbonate molecules were reductively converted via 3-hydroxypropionate to succinyl-CoA. This intermediate was reduced to 4-hydroxybutyrate and converted into two acetyl-CoA molecules via 4-hydroxybutyryl-CoA dehydratase. The key genes of this pathway were found not only in Metallosphaera but also in Sulfolobus, Archaeoglobus, and Cenarchaeum species. Moreover, the Global Ocean Sampling database contains half as many 4-hydroxybutyryl-CoA dehydratase sequences as compared with those found for another key photosynthetic CO2-fixing enzyme, ribulose-1,5-bisphosphate carboxylase-oxygenase. This indicates the importance of this enzyme in global carbon cycling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berg, Ivan A -- Kockelkorn, Daniel -- Buckel, Wolfgang -- Fuchs, Georg -- New York, N.Y. -- Science. 2007 Dec 14;318(5857):1782-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Mikrobiologie, Fakultat Biologie, Universitat Freiburg, Schanzlestrasse 1, D-79104 Freiburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18079405" target="_blank"〉PubMed〈/a〉
    Keywords: Acetyl Coenzyme A/metabolism ; Acetyl-CoA Carboxylase/metabolism ; Acyl Coenzyme A/metabolism ; Amino Acid Sequence ; Anaerobiosis ; Archaea/genetics/metabolism ; Autotrophic Processes ; Bicarbonates/metabolism ; Carbon Dioxide/*metabolism ; Genes, Archaeal ; Hydro-Lyases/genetics/metabolism ; Hydroxybutyrates/*metabolism ; Kinetics ; Lactic Acid/*analogs & derivatives/metabolism ; Metabolic Networks and Pathways ; Molecular Sequence Data ; Oxidation-Reduction ; Photosynthesis ; Phylogeny ; Sulfolobaceae/genetics/*metabolism
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    Live-cell imaging of enzyme-substrate interaction reveals spatial regulation of PTP1B (2007)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2007-01-06
    Description: Endoplasmic reticulum-localized protein-tyrosine phosphatase PTP1B terminates growth factor signal transduction by dephosphorylation of receptor tyrosine kinases (RTKs). But how PTP1B allows for RTK signaling in the cytoplasm is unclear. In order to test whether PTP1B activity is spatially regulated, we developed a method based on Forster resonant energy transfer for imaging enzyme-substrate (ES) intermediates in live cells. We observed the establishment of a steady-state ES gradient across the cell. This gradient exhibited robustness to cell-to-cell variability, growth factor activation, and RTK localization, which demonstrated spatial regulation of PTP1B activity. Such regulation may be important for generating distinct cellular environments that permit RTK signal transduction and that mediate its eventual termination.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yudushkin, Ivan A -- Schleifenbaum, Andreas -- Kinkhabwala, Ali -- Neel, Benjamin G -- Schultz, Carsten -- Bastiaens, Philippe I H -- R01 DK60838/DK/NIDDK NIH HHS/ -- R37 49152/PHS HHS/ -- New York, N.Y. -- Science. 2007 Jan 5;315(5808):115-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉European Molecular Biology Laboratory (EMBL), Meyerhofstrasse 1, D-69117 Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17204654" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; COS Cells ; Catalysis ; Cell Line, Tumor ; Cercopithecus aethiops ; Epidermal Growth Factor/metabolism/pharmacology ; Fluorescence Resonance Energy Transfer ; Humans ; Kinetics ; Mathematics ; Microscopy, Fluorescence ; Models, Biological ; Phosphorylation ; Protein Tyrosine Phosphatase, Non-Receptor Type 1 ; Protein Tyrosine Phosphatases/*metabolism ; Receptor Protein-Tyrosine Kinases/*metabolism ; Receptor, Epidermal Growth Factor/*metabolism ; Recombinant Fusion Proteins/metabolism
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    Physical model for the decay and preservation of marine organic carbon (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2007-06-02
    Description: Degradation of marine organic carbon provides a major source of atmospheric carbon dioxide, whereas preservation in sediments results in accumulation of oxygen. These processes involve the slow decay of chemically recalcitrant compounds and physical protection. To assess the importance of physical protection, we constructed a reaction-diffusion model in which organic matter differs only in its accessibility to microbial degradation but not its intrinsic reactivity. The model predicts that organic matter decays logarithmically with time t and that decay rates decrease approximately as 0.2 x t(-1) until burial. Analyses of sediment-core data are consistent with these predictions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rothman, Daniel H -- Forney, David C -- New York, N.Y. -- Science. 2007 Jun 1;316(5829):1325-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Earth, Atmospheric, and Planetary Sciences, Massachusetts Institute of Technology, Cambridge, MA 02139, USA. dhr@mit.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17540901" target="_blank"〉PubMed〈/a〉
    Keywords: Aluminum Silicates ; Bacteria/*metabolism ; *Biodegradation, Environmental ; *Carbon/metabolism ; Databases, Factual ; Diffusion ; Enzymes/metabolism ; *Geologic Sediments/chemistry/microbiology ; Hydrolysis ; Kinetics ; Mathematics ; *Models, Theoretical ; Oceans and Seas ; *Organic Chemicals/chemistry/metabolism ; Oxygen/analysis ; *Seawater
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    Chimeras of two isoprenoid synthases catalyze all four coupling reactions in isoprenoid biosynthesis (2007)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2007-04-07
    Description: The carbon skeletons of over 55,000 naturally occurring isoprenoid compounds are constructed from four fundamental coupling reactions: chain elongation, cyclopropanation, branching, and cyclobutanation. Enzymes that catalyze chain elongation and cyclopropanation are well studied, whereas those that catalyze branching and cyclobutanation are unknown. We have catalyzed the four reactions with chimeric proteins generated by replacing segments of a chain-elongation enzyme with corresponding sequences from a cyclopropanation enzyme. Stereochemical and mechanistic considerations suggest that the four coupling enzymes could have evolved from a common ancestor through relatively small changes in the catalytic site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thulasiram, Hirekodathakallu V -- Erickson, Hans K -- Poulter, C Dale -- GM 21328/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2007 Apr 6;316(5821):73-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of Utah, 315 South 1400 East, Room 2020, Salt Lake City, UT 84112, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17412950" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Artemisia/enzymology ; Catalysis ; Catalytic Domain ; Chrysanthemum cinerariifolium/enzymology ; Cyclopropanes/chemistry ; Evolution, Molecular ; Geranyltranstransferase/chemistry/genetics/*metabolism ; Kinetics ; Molecular Conformation ; Molecular Sequence Data ; Molecular Structure ; Mutagenesis, Site-Directed ; Recombinant Fusion Proteins/chemistry/metabolism ; Stereoisomerism ; Terpenes/chemistry/*metabolism
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    In situ imaging of the endogenous CD8 T cell response to infection (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2007-10-06
    Description: Mounting a protective immune response is critically dependent on the orchestrated movement of cells within lymphoid organs. We report here the visualization, using major histocompatability complex class I tetramers, of the CD8-positive (CD8) T cell response in the spleens of mice to Listeria monocytogenes infection. A multistage pathway was revealed that included initial activation at the borders of the B and T cell zones followed by cluster formation with antigenpresenting cells leading to CD8 T cell exit to the red pulp via bridging channels. Strikingly, many memory CD8 T cells localized to the B cell zones and, when challenged, underwent rapid migration to the T cell zones where proliferation occurred, followed by egress via bridging channels in parallel with the primary response. Thus, the ability to track endogenous immune responses has uncovered both distinct and overlapping mechanisms and anatomical locations driving primary and secondary immune responses.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2846662/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2846662/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Khanna, Kamal M -- McNamara, Jeffery T -- Lefrancois, Leo -- AI41576/AI/NIAID NIH HHS/ -- AI56172/AI/NIAID NIH HHS/ -- DRG-1886-05/PHS HHS/ -- P01 AI056172/AI/NIAID NIH HHS/ -- P01 AI056172-05/AI/NIAID NIH HHS/ -- R01 AI041576/AI/NIAID NIH HHS/ -- R01 AI041576-06/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2007 Oct 5;318(5847):116-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, University of Connecticut, Farmington, CT 06030, U.S.A.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17916739" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigen-Presenting Cells/immunology ; Antigens, CD/analysis ; Antigens, CD8/analysis ; B-Lymphocytes/immunology ; CD8-Positive T-Lymphocytes/cytology/*immunology/physiology ; Cell Movement ; Dendritic Cells/immunology/physiology ; Fluorescent Dyes ; Histocompatibility Antigens Class I ; *Immunologic Memory ; Kinetics ; Listeria monocytogenes/*immunology ; Listeriosis/*immunology ; Lymphocyte Activation ; Mice ; Mice, Inbred C57BL ; Microscopy, Confocal ; Receptors, Antigen, T-Cell/analysis ; Spleen/cytology/*immunology ; Staining and Labeling ; T-Lymphocyte Subsets/cytology/immunology/physiology
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    Methyl salicylate is a critical mobile signal for plant systemic acquired resistance (2007)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2007-10-06
    Description: In plants, the mobile signal for systemic acquired resistance (SAR), an organism-wide state of enhanced defense to subsequent infections, has been elusive. By stimulating immune responses in mosaic tobacco plants created by grafting different genetic backgrounds, we showed that the methyl salicylate (MeSA) esterase activity of salicylic acid-binding protein 2 (SABP2), which converts MeSA into salicylic acid (SA), is required for SAR signal perception in systemic tissue, the tissue that does not receive the primary (initial) infection. Moreover, in plants expressing mutant SABP2 with unregulated MeSA esterase activity in SAR signal-generating, primary infected leaves, SAR was compromised and the associated increase in MeSA levels was suppressed in primary infected leaves, their phloem exudates, and systemic leaves. SAR was also blocked when SA methyl transferase (which converts SA to MeSA) was silenced in primary infected leaves, and MeSA treatment of lower leaves induced SAR in upper untreated leaves. Therefore, we conclude that MeSA is a SAR signal in tobacco.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Park, Sang-Wook -- Kaimoyo, Evans -- Kumar, Dhirendra -- Mosher, Stephen -- Klessig, Daniel F -- New York, N.Y. -- Science. 2007 Oct 5;318(5847):113-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Boyce Thompson Institute for Plant Research, Tower Road, Ithaca, NY 14853, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17916738" target="_blank"〉PubMed〈/a〉
    Keywords: Esterases/genetics/metabolism ; Feedback, Physiological ; Kinetics ; Mixed Function Oxygenases/genetics/metabolism ; Mutation ; Phloem/metabolism ; Plant Diseases/*immunology/virology ; Plant Leaves/metabolism/virology ; Plant Proteins/genetics/metabolism ; Plants, Genetically Modified ; Salicylates/*metabolism ; Salicylic Acid/metabolism ; *Signal Transduction ; Tobacco/immunology/*metabolism/virology ; Tobacco Mosaic Virus/*physiology ; Virus Replication
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    Complex riboswitches (2008)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2008-03-29
    Description: Using simple biochemical tricks, metabolite-binding riboswitches take on gene control functions that have long been thought to be the work of protein factors. Although modern riboswitches might be the last holdouts of primitive genetic elements, some are capable of sensory and regulatory feats that are competitive with their protein counterparts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Breaker, Ronald R -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2008 Mar 28;319(5871):1795-7. doi: 10.1126/science.1152621.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular, Cellular and Developmental Biology and Howard Hughes Medical Institute, Yale University, New Haven, CT 06520, USA. ronald.breaker@yale.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18369140" target="_blank"〉PubMed〈/a〉
    Keywords: Alternative Splicing ; Aptamers, Nucleotide/*metabolism ; Bacteria/genetics ; Fungi/genetics ; *Gene Expression Regulation ; Kinetics ; Ligands ; Nucleic Acid Conformation ; Plants/genetics ; RNA, Messenger/chemistry/*genetics/metabolism ; Regulatory Sequences, Ribonucleic Acid/*genetics ; Thermodynamics ; Untranslated Regions/chemistry/*genetics/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Mechanism of threading a polymer through a macrocyclic ring (2008)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2008-12-17
    Description: The translocation of biopolymers through pores and channels plays a fundamental role in numerous biological processes. We describe here the mechanism of the threading of a series of polymer chains through a synthetic macrocycle, which mimics these natural processes. The threading of polymers involves a kinetically favorable "entron" effect, which is associated with the initial filling of the cavity by the end of the polymer. A preassociation between the outside of the macrocycle and the polymer induces a process in which the polymer end loops back into the cavity of the macrocycle. This looping mechanism results in accelerated threading rates and unidirectional motion and is reminiscent of the protein translocation through membrane pores.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Deutman, Alexander B C -- Monnereau, Cyrille -- Elemans, Johannes A A W -- Ercolani, Gianfranco -- Nolte, Roeland J M -- Rowan, Alan E -- New York, N.Y. -- Science. 2008 Dec 12;322(5908):1668-71. doi: 10.1126/science.1164647.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Molecules and Materials, Radboud University Nijmegen, Toernooiveld 1, 6525ED Nijmegen, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19074344" target="_blank"〉PubMed〈/a〉
    Keywords: Biological Transport ; Cell Membrane/metabolism ; Kinetics ; Macrocyclic Compounds/*chemistry ; Magnetic Resonance Spectroscopy ; Molecular Structure ; Polymers/*chemistry ; Porphyrins/*chemistry ; Proteins/chemistry/metabolism ; Thermodynamics ; Viologens/chemistry
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Biochemistry. Zooming into live cells (2008)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2008-04-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pinaud, Fabien -- Dahan, Maxime -- New York, N.Y. -- Science. 2008 Apr 11;320(5873):187-8. doi: 10.1126/science.1156510.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire Kastler Brossel, CNRS UMR8552; Physics and Biology Department, Ecole Normale Superieure, Universite Pierre et Marie Curie-Paris 6, 46 rue d'Ulm, 75005 Paris, France. maxime.dahan@lkb.ens.fr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18403700" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Fluorescent Dyes ; Imaging, Three-Dimensional/methods ; Kinetics ; Microscopy, Fluorescence/*methods ; Movement ; Neurons/ultrastructure ; Optics and Photonics ; Synaptic Vesicles/*physiology/*ultrastructure ; Video Recording
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    Myosin I can act as a molecular force sensor (2008)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2008-07-05
    Description: The ability to sense molecular tension is crucial for a wide array of cellular processes, including the detection of auditory stimuli, control of cell shape, and internalization and transport of membranes. We show that myosin I, a motor protein that has been implicated in powering key steps in these processes, dramatically alters its motile properties in response to tension. We measured the displacement generated by single myosin I molecules, and we determined the actin-attachment kinetics with varying tensions using an optical trap. The rate of myosin I detachment from actin decreases 〉75-fold under tension of 2 piconewtons or less, resulting in myosin I transitioning from a low (〈0.2) to a high (〉0.9) duty-ratio motor. This impressive tension sensitivity supports a role for myosin I as a molecular force sensor.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2493443/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2493443/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Laakso, Joseph M -- Lewis, John H -- Shuman, Henry -- Ostap, E Michael -- AR051174/AR/NIAMS NIH HHS/ -- GM057247/GM/NIGMS NIH HHS/ -- P01 AR051174/AR/NIAMS NIH HHS/ -- P01 AR051174-050003/AR/NIAMS NIH HHS/ -- R01 GM057247-10/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2008 Jul 4;321(5885):133-6. doi: 10.1126/science.1159419.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Pennsylvania Muscle Institute and Department of Physiology, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18599791" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/*metabolism ; Actomyosin/physiology ; Adenosine Diphosphate/metabolism ; Adenosine Triphosphate/metabolism ; Amino Acid Motifs ; Animals ; Biophysical Phenomena ; Biophysics ; Kinetics ; Likelihood Functions ; Models, Biological ; Molecular Motor Proteins/metabolism/*physiology ; Monte Carlo Method ; Myosin Type I/chemistry/metabolism/*physiology ; Optical Tweezers ; Protein Structure, Tertiary ; Rabbits ; Stress, Mechanical
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    Four-jointed is a Golgi kinase that phosphorylates a subset of cadherin domains (2008)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2008-07-19
    Description: The atypical cadherin Fat acts as a receptor for a signaling pathway that regulates growth, gene expression, and planar cell polarity. Genetic studies in Drosophila identified the four-jointed gene as a regulator of Fat signaling. We show that four-jointed encodes a protein kinase that phosphorylates serine or threonine residues within extracellular cadherin domains of Fat and its transmembrane ligand, Dachsous. Four-jointed functions in the Golgi and is the first molecularly defined kinase that phosphorylates protein domains destined to be extracellular. An acidic sequence motif (Asp-Asn-Glu) within Four-jointed was essential for its kinase activity in vitro and for its biological activity in vivo. Our results indicate that Four-jointed regulates Fat signaling by phosphorylating cadherin domains of Fat and Dachsous as they transit through the Golgi.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2562711/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2562711/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ishikawa, Hiroyuki O -- Takeuchi, Hideyuki -- Haltiwanger, Robert S -- Irvine, Kenneth D -- CA123071/CA/NCI NIH HHS/ -- GM061126/GM/NIGMS NIH HHS/ -- GM078620/GM/NIGMS NIH HHS/ -- R01 CA123071/CA/NCI NIH HHS/ -- R01 CA123071-02/CA/NCI NIH HHS/ -- R01 GM061126/GM/NIGMS NIH HHS/ -- R01 GM061126-08/GM/NIGMS NIH HHS/ -- R01 GM078620/GM/NIGMS NIH HHS/ -- R01 GM078620-02/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2008 Jul 18;321(5887):401-4. doi: 10.1126/science.1158159.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Waksman Institute and Department of Molecular Biology and Biochemistry, Rutgers University, Piscataway, NJ 08854, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18635802" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Cadherins/chemistry/*metabolism ; Cell Adhesion Molecules/chemistry/*metabolism ; Cell Line ; Drosophila Proteins/chemistry/genetics/*metabolism ; Drosophila melanogaster ; Electrophoretic Mobility Shift Assay ; Glycosylation ; Golgi Apparatus/enzymology/*metabolism ; Kinetics ; Membrane Glycoproteins/chemistry/genetics/*metabolism ; Molecular Sequence Data ; Mutant Proteins/chemistry/metabolism ; Phosphorylation ; Protein Kinases/chemistry/genetics/*metabolism ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/metabolism ; Serine/metabolism ; Signal Transduction ; Threonine/metabolism
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    De novo computational design of retro-aldol enzymes (2008)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2008-03-08
    Description: The creation of enzymes capable of catalyzing any desired chemical reaction is a grand challenge for computational protein design. Using new algorithms that rely on hashing techniques to construct active sites for multistep reactions, we designed retro-aldolases that use four different catalytic motifs to catalyze the breaking of a carbon-carbon bond in a nonnatural substrate. Of the 72 designs that were experimentally characterized, 32, spanning a range of protein folds, had detectable retro-aldolase activity. Designs that used an explicit water molecule to mediate proton shuffling were significantly more successful, with rate accelerations of up to four orders of magnitude and multiple turnovers, than those involving charged side-chain networks. The atomic accuracy of the design process was confirmed by the x-ray crystal structure of active designs embedded in two protein scaffolds, both of which were nearly superimposable on the design model.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3431203/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3431203/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jiang, Lin -- Althoff, Eric A -- Clemente, Fernando R -- Doyle, Lindsey -- Rothlisberger, Daniela -- Zanghellini, Alexandre -- Gallaher, Jasmine L -- Betker, Jamie L -- Tanaka, Fujie -- Barbas, Carlos F 3rd -- Hilvert, Donald -- Houk, Kendall N -- Stoddard, Barry L -- Baker, David -- R01 CA097328/CA/NCI NIH HHS/ -- R01 GM049857/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2008 Mar 7;319(5868):1387-91. doi: 10.1126/science.1152692.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Washington, Seattle, WA 98195, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18323453" target="_blank"〉PubMed〈/a〉
    Keywords: Aldehyde-Lyases/*chemistry/metabolism ; *Algorithms ; Binding Sites ; Catalysis ; Catalytic Domain ; Computer Simulation ; Crystallography, X-Ray ; Hydrogen Bonding ; Hydrophobic and Hydrophilic Interactions ; Kinetics ; Models, Molecular ; Protein Conformation ; Protein Engineering
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    Surface sites for engineering allosteric control in proteins (2008)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2008-10-18
    Description: Statistical analyses of protein families reveal networks of coevolving amino acids that functionally link distantly positioned functional surfaces. Such linkages suggest a concept for engineering allosteric control into proteins: The intramolecular networks of two proteins could be joined across their surface sites such that the activity of one protein might control the activity of the other. We tested this idea by creating PAS-DHFR, a designed chimeric protein that connects a light-sensing signaling domain from a plant member of the Per/Arnt/Sim (PAS) family of proteins with Escherichia coli dihydrofolate reductase (DHFR). With no optimization, PAS-DHFR exhibited light-dependent catalytic activity that depended on the site of connection and on known signaling mechanisms in both proteins. PAS-DHFR serves as a proof of concept for engineering regulatory activities into proteins through interface design at conserved allosteric sites.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3071530/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3071530/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, Jeeyeon -- Natarajan, Madhusudan -- Nashine, Vishal C -- Socolich, Michael -- Vo, Tina -- Russ, William P -- Benkovic, Stephen J -- Ranganathan, Rama -- R01 EY018720/EY/NEI NIH HHS/ -- R01 EY018720-01/EY/NEI NIH HHS/ -- R01 EY018720-02/EY/NEI NIH HHS/ -- R01 EY018720-03/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 2008 Oct 17;322(5900):438-42. doi: 10.1126/science.1159052.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Pennsylvania State University, University Park, PA 16802, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/18927392" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Allosteric Site ; Binding Sites ; Catalysis ; Cryptochromes ; Escherichia coli/enzymology ; Flavoproteins/*chemistry/metabolism ; Kinetics ; Ligands ; Light ; Models, Molecular ; NADP/metabolism ; Protein Conformation ; *Protein Engineering ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Recombinant Fusion Proteins/*chemistry/*metabolism ; Tetrahydrofolate Dehydrogenase/*chemistry/metabolism
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    An analytical solution to the kinetics of breakable filament assembly (2009)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2009-12-17
    Description: We present an analytical treatment of a set of coupled kinetic equations that governs the self-assembly of filamentous molecular structures. Application to the case of protein aggregation demonstrates that the kinetics of amyloid growth can often be dominated by secondary rather than by primary nucleation events. Our results further reveal a range of general features of the growth kinetics of fragmenting filamentous structures, including the existence of generic scaling laws that provide mechanistic information in contexts ranging from in vitro amyloid growth to the in vivo development of mammalian prion diseases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Knowles, Tuomas P J -- Waudby, Christopher A -- Devlin, Glyn L -- Cohen, Samuel I A -- Aguzzi, Adriano -- Vendruscolo, Michele -- Terentjev, Eugene M -- Welland, Mark E -- Dobson, Christopher M -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2009 Dec 11;326(5959):1533-7. doi: 10.1126/science.1178250.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cavendish Laboratory, University of Cambridge, J. J. Thomson Avenue, Cambridge CB3 0HE, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/20007899" target="_blank"〉PubMed〈/a〉
    Keywords: Amyloid/*chemistry ; Biochemical Processes ; Glutathione Peroxidase/chemistry ; Insulin/chemistry ; Kinetics ; Lactoglobulins/chemistry ; Mathematical Concepts ; Multiprotein Complexes/*chemistry ; Peptide Termination Factors/chemistry ; Peptides/chemistry ; Prions/chemistry ; *Protein Multimerization ; Saccharomyces cerevisiae Proteins/chemistry
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    Orc1 controls centriole and centrosome copy number in human cells (2009)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2009-02-07
    Description: Centrosomes, each containing a pair of centrioles, organize microtubules in animal cells, particularly during mitosis. DNA and centrosomes are normally duplicated once before cell division to maintain optimal genome integrity. We report a new role for the Orc1 protein, a subunit of the origin recognition complex (ORC) that is a key component of the DNA replication licensing machinery, in controlling centriole and centrosome copy number in human cells, independent of its role in DNA replication. Cyclin A promotes Orc1 localization to centrosomes where Orc1 prevents Cyclin E-dependent reduplication of both centrioles and centrosomes in a single cell division cycle. The data suggest that Orc1 is a regulator of centriole and centrosome reduplication as well as the initiation of DNA replication.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2653626/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2653626/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hemerly, Adriana S -- Prasanth, Supriya G -- Siddiqui, Khalid -- Stillman, Bruce -- CA13106/CA/NCI NIH HHS/ -- P01 CA013106/CA/NCI NIH HHS/ -- P01 CA013106-310025/CA/NCI NIH HHS/ -- P01 CA013106-36/CA/NCI NIH HHS/ -- P01 CA013106-370025/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2009 Feb 6;323(5915):789-93. doi: 10.1126/science.1166745.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cold Spring Harbor Laboratory, 1 Bungtown Road, Cold Spring Harbor 11724, NY, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19197067" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Cycle ; Cell Line, Tumor ; Centrioles/*physiology ; Centrosome/*physiology ; Cyclin A/metabolism ; Cyclin E/metabolism ; Cyclin-Dependent Kinase 2/metabolism ; DNA Replication ; HeLa Cells ; Humans ; Kinetics ; Mutant Proteins/metabolism ; Origin Recognition Complex/genetics/*metabolism ; RNA Interference ; RNA, Small Interfering ; Transfection
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    Real-time DNA sequencing from single polymerase molecules (2008)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2008-11-22
    Description: We present single-molecule, real-time sequencing data obtained from a DNA polymerase performing uninterrupted template-directed synthesis using four distinguishable fluorescently labeled deoxyribonucleoside triphosphates (dNTPs). We detected the temporal order of their enzymatic incorporation into a growing DNA strand with zero-mode waveguide nanostructure arrays, which provide optical observation volume confinement and enable parallel, simultaneous detection of thousands of single-molecule sequencing reactions. Conjugation of fluorophores to the terminal phosphate moiety of the dNTPs allows continuous observation of DNA synthesis over thousands of bases without steric hindrance. The data report directly on polymerase dynamics, revealing distinct polymerization states and pause sites corresponding to DNA secondary structure. Sequence data were aligned with the known reference sequence to assay biophysical parameters of polymerization for each template position. Consensus sequences were generated from the single-molecule reads at 15-fold coverage, showing a median accuracy of 99.3%, with no systematic error beyond fluorophore-dependent error rates.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Eid, John -- Fehr, Adrian -- Gray, Jeremy -- Luong, Khai -- Lyle, John -- Otto, Geoff -- Peluso, Paul -- Rank, David -- Baybayan, Primo -- Bettman, Brad -- Bibillo, Arkadiusz -- Bjornson, Keith -- Chaudhuri, Bidhan -- Christians, Frederick -- Cicero, Ronald -- Clark, Sonya -- Dalal, Ravindra -- Dewinter, Alex -- Dixon, John -- Foquet, Mathieu -- Gaertner, Alfred -- Hardenbol, Paul -- Heiner, Cheryl -- Hester, Kevin -- Holden, David -- Kearns, Gregory -- Kong, Xiangxu -- Kuse, Ronald -- Lacroix, Yves -- Lin, Steven -- Lundquist, Paul -- Ma, Congcong -- Marks, Patrick -- Maxham, Mark -- Murphy, Devon -- Park, Insil -- Pham, Thang -- Phillips, Michael -- Roy, Joy -- Sebra, Robert -- Shen, Gene -- Sorenson, Jon -- Tomaney, Austin -- Travers, Kevin -- Trulson, Mark -- Vieceli, John -- Wegener, Jeffrey -- Wu, Dawn -- Yang, Alicia -- Zaccarin, Denis -- Zhao, Peter -- Zhong, Frank -- Korlach, Jonas -- Turner, Stephen -- R01HG003710/HG/NHGRI NIH HHS/ -- New York, N.Y. -- Science. 2009 Jan 2;323(5910):133-8. doi: 10.1126/science.1162986. Epub 2008 Nov 20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Pacific Biosciences, 1505 Adams Drive, Menlo Park, CA 94025, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19023044" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Consensus Sequence ; DNA/biosynthesis ; DNA, Circular/chemistry ; DNA, Single-Stranded/chemistry ; DNA-Directed DNA Polymerase/*metabolism ; Deoxyribonucleotides/metabolism ; Enzymes, Immobilized ; Fluorescent Dyes ; Kinetics ; Nanostructures ; Sequence Analysis, DNA/*methods ; Spectrometry, Fluorescence
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    Structural plasticity in actin and tubulin polymer dynamics (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-08-22
    Description: Actin filaments and microtubules polymerize and depolymerize by adding and removing subunits at polymer ends, and these dynamics drive cytoplasmic organization, cell division, and cell motility. Since Wegner proposed the treadmilling theory for actin in 1976, it has largely been assumed that the chemical state of the bound nucleotide determines the rates of subunit addition and removal. This chemical kinetics view is difficult to reconcile with observations revealing multiple structural states of the polymer that influence polymerization dynamics but that are not strictly coupled to the bound nucleotide state. We refer to these phenomena as "structural plasticity" and discuss emerging evidence that they play a central role in polymer dynamics and function.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2864651/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2864651/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kueh, Hao Yuan -- Mitchison, Timothy J -- GM 23928/GM/NIGMS NIH HHS/ -- R01 GM023928/GM/NIGMS NIH HHS/ -- R01 GM023928-31/GM/NIGMS NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2009 Aug 21;325(5943):960-3. doi: 10.1126/science.1168823.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Systems Biology, Harvard Medical School, Boston, MA 02215, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19696342" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Cytoskeleton/*chemistry/metabolism/ultrastructure ; Actin Depolymerizing Factors/metabolism ; Actins/*chemistry/metabolism ; Adenosine Triphosphate/metabolism ; Guanosine Diphosphate/metabolism ; Guanosine Triphosphate/metabolism ; Kinetics ; Microfilament Proteins/metabolism ; Microtubules/*chemistry/metabolism/ultrastructure ; Models, Biological ; Tubulin/*chemistry/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Mechanistic analysis of a dynamin effector (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-08-15
    Description: Dynamin-related proteins (DRPs) can generate forces to remodel membranes. In cells, DRPs require additional proteins [DRP-associated proteins (DAPs)] to conduct their functions. To dissect the mechanistic role of a DAP, we used the yeast mitochondrial division machine as a model, which requires the DRP Dnm1, and two other proteins, Mdv1 and Fis1. Mdv1 played a postmitochondrial targeting role in division by specifically interacting and coassembling with the guanosine triphosphate-bound form of Dnm1. This regulated interaction nucleated and promoted the self-assembly of Dnm1 into helical structures, which drive membrane scission. The nucleation of DRP assembly probably represents a general regulatory strategy for this family of filament-forming proteins, similar to F-actin regulation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lackner, Laura L -- Horner, Jennifer S -- Nunnari, Jodi -- 1F32GM078749/GM/NIGMS NIH HHS/ -- R01 GM062942/GM/NIGMS NIH HHS/ -- R01GM062942/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2009 Aug 14;325(5942):874-7. doi: 10.1126/science.1176921.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, University of California, Davis, CA 95616, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19679814" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing/*metabolism ; GTP Phosphohydrolases/chemistry/genetics/*metabolism ; Guanosine Triphosphate/analogs & derivatives/metabolism ; Intracellular Membranes/physiology ; Kinetics ; Liposomes/metabolism ; Mitochondria/*physiology ; Mitochondrial Proteins/chemistry/genetics/*metabolism ; Models, Biological ; Protein Binding ; Protein Conformation ; Protein Structure, Secondary ; Saccharomyces cerevisiae Proteins/chemistry/genetics/*metabolism
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    Meropenem-clavulanate is effective against extensively drug-resistant Mycobacterium tuberculosis (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-03-03
    Description: beta-lactam antibiotics are ineffective against Mycobacterium tuberculosis, being rapidly hydrolyzed by the chromosomally encoded blaC gene product. The carbapenem class of beta-lactams are very poor substrates for BlaC, allowing us to determine the three-dimensional structure of the covalent BlaC-meropenem covalent complex at 1.8 angstrom resolution. When meropenem was combined with the beta-lactamase inhibitor clavulanate, potent activity against laboratory strains of M. tuberculosis was observed [minimum inhibitory concentration (MIC(meropenem)) less than 1 microgram per milliliter], and sterilization of aerobically grown cultures was observed within 14 days. In addition, this combination exhibited inhibitory activity against anaerobically grown cultures that mimic the "persistent" state and inhibited the growth of 13 extensively drug-resistant strains of M. tuberculosis at the same levels seen for drug-susceptible strains. Meropenem and clavulanate are Food and Drug Administration-approved drugs and could potentially be used to treat patients with currently untreatable disease.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2679150/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2679150/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hugonnet, Jean-Emmanuel -- Tremblay, Lee W -- Boshoff, Helena I -- Barry, Clifton E 3rd -- Blanchard, John S -- AI33696/AI/NIAID NIH HHS/ -- Z01 AI000693-15/Intramural NIH HHS/ -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 2009 Feb 27;323(5918):1215-8. doi: 10.1126/science.1167498.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Albert Einstein College of Medicine, 1300 Morris Park Avenue, Bronx, NY 10461, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19251630" target="_blank"〉PubMed〈/a〉
    Keywords: Acylation ; Antibiotics, Antitubercular/*pharmacology ; Catalytic Domain ; Clavulanic Acid/*pharmacology ; Crystallography, X-Ray ; Drug Combinations ; *Drug Resistance, Multiple, Bacterial ; Enzyme Inhibitors/pharmacology ; Extensively Drug-Resistant Tuberculosis/*microbiology ; Humans ; Kinetics ; Mass Spectrometry ; Microbial Sensitivity Tests ; Mycobacterium tuberculosis/*drug effects/enzymology/growth & development ; Thienamycins/metabolism/*pharmacology ; beta-Lactamase Inhibitors ; beta-Lactamases/*chemistry/metabolism
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    Small-molecule activators of a proenzyme (2009)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2009-11-07
    Description: Virtually all of the 560 human proteases are stored as inactive proenyzmes and are strictly regulated. We report the identification and characterization of the first small molecules that directly activate proenzymes, the apoptotic procaspases-3 and -6. It is surprising that these compounds induce autoproteolytic activation by stabilizing a conformation that is both more active and more susceptible to intermolecular proteolysis. These procaspase activators bypass the normal upstream proapoptotic signaling cascades and induce rapid apoptosis in a variety of cell lines. Systematic biochemical and biophysical analyses identified a cluster of mutations in procaspase-3 that resist small-molecule activation both in vitro and in cells. Compounds that induce gain of function are rare, and the activators reported here will enable direct control of the executioner caspases in apoptosis and in cellular differentiation. More generally, these studies presage the discovery of other proenzyme activators to explore fundamental processes of proenzyme activation and their fate-determining roles in biology.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2886848/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2886848/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wolan, Dennis W -- Zorn, Julie A -- Gray, Daniel C -- Wells, James A -- F32 CA119641/CA/NCI NIH HHS/ -- F32 CA119641-03/CA/NCI NIH HHS/ -- R01 CA136779/CA/NCI NIH HHS/ -- R21 N5057022/PHS HHS/ -- New York, N.Y. -- Science. 2009 Nov 6;326(5954):853-8. doi: 10.1126/science.1177585.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmaceutical Chemistry, University of California, San Francisco, Byers Hall, 1700 4th Street, San Francisco, CA 94158, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19892984" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis ; Benzopyrans/chemistry/*metabolism/pharmacology ; Biocatalysis ; Caspase 3/chemistry/genetics/*metabolism ; Caspase 6/chemistry/genetics/*metabolism ; Caspase Inhibitors ; Catalytic Domain ; Cell Line, Transformed ; Cell Line, Tumor ; Cells, Cultured ; Enzyme Activation ; Enzyme Activators/chemistry/*metabolism/pharmacology ; Enzyme Inhibitors/metabolism/pharmacology ; Enzyme Precursors/antagonists & inhibitors/chemistry/genetics/*metabolism ; Granzymes/metabolism ; Humans ; Imidazoles/chemistry/*metabolism/pharmacology ; Kinetics ; Mice ; Molecular Structure ; Mutagenesis ; Pyridines/chemistry/*metabolism/pharmacology ; Signal Transduction ; Small Molecule Libraries/chemistry/metabolism
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    Epicontinental seas versus open-ocean settings: the kinetics of mass extinction and origination (2009)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2009-12-08
    Description: Environmental perturbations during mass extinctions were likely manifested differently in epicontinental seas than in open-ocean-facing habitats of comparable depth. Here, we present a dissection of origination and extinction in epicontinental seas versus open-ocean-facing coastal regions in the Permian through Cretaceous periods, an interval through which both settings are well represented in the fossil record. Results demonstrate that extinction rates were significantly higher in open-ocean settings than in epicontinental seas during major mass extinctions but not at other times and that origination rates were significantly higher in open-ocean settings for a protracted interval from the Late Jurassic through the Late Cretaceous. These patterns are manifested even when other paleogeographic and environmental variables are held fixed, indicating that epicontinental seas and open-ocean-facing coastlines carry distinct macroevolutionary signatures.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, Arnold I -- Foote, Michael -- New York, N.Y. -- Science. 2009 Nov 20;326(5956):1106-9. doi: 10.1126/science.1180061.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Geology, University of Cincinnati, Post Office Box 210013, Cincinnati, OH 45221, USA. arnold.miller@uc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19965428" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Evolution ; Bivalvia ; *Ecosystem ; Environment ; *Extinction, Biological ; Geologic Sediments ; Geological Phenomena ; Kinetics ; Oceans and Seas
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    Self-sustained replication of an RNA enzyme (2009)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2009-01-10
    Description: An RNA enzyme that catalyzes the RNA-templated joining of RNA was converted to a format whereby two enzymes catalyze each other's synthesis from a total of four oligonucleotide substrates. These cross-replicating RNA enzymes undergo self-sustained exponential amplification in the absence of proteins or other biological materials. Amplification occurs with a doubling time of about 1 hour and can be continued indefinitely. Populations of various cross-replicating enzymes were constructed and allowed to compete for a common pool of substrates, during which recombinant replicators arose and grew to dominate the population. These replicating RNA enzymes can serve as an experimental model of a genetic system. Many such model systems could be constructed, allowing different selective outcomes to be related to the underlying properties of the genetic system.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2652413/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2652413/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lincoln, Tracey A -- Joyce, Gerald F -- R01 GM065130/GM/NIGMS NIH HHS/ -- R01 GM065130-07/GM/NIGMS NIH HHS/ -- R01GM065130/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2009 Feb 27;323(5918):1229-32. doi: 10.1126/science.1167856. Epub 2009 Jan 8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Skaggs Institute for Chemical Biology, Scripps Research Institute, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19131595" target="_blank"〉PubMed〈/a〉
    Keywords: Base Pairing ; Biocatalysis ; Directed Molecular Evolution ; Kinetics ; Nucleic Acid Conformation ; Oligonucleotides/*metabolism ; Polynucleotide Ligases/*chemistry/metabolism ; RNA, Catalytic/chemistry/*metabolism
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    Achieving stability of lipopolysaccharide-induced NF-kappaB activation (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-09-17
    Description: The activation dynamics of the transcription factor NF-kappaB exhibit damped oscillatory behavior when cells are stimulated by tumor necrosis factor-alpha (TNFalpha) but stable behavior when stimulated by lipopolysaccharide (LPS). LPS binding to Toll-like receptor 4 (TLR4) causes activation of NF-kappaB that requires two downstream pathways, each of which when isolated exhibits damped oscillatory behavior. Computational modeling of the two TLR4-dependent signaling pathways suggests that one pathway requires a time delay to establish early anti-phase activation of NF-kappaB by the two pathways. The MyD88-independent pathway required Inferon regulatory factor 3-dependent expression of TNFalpha to activate NF-kappaB, and the time required for TNFalpha synthesis established the delay.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Covert, Markus W -- Leung, Thomas H -- Gaston, Jahlionais E -- Baltimore, David -- GM039458-21/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Sep 16;309(5742):1854-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, California Institute of Technology, Pasadena, CA 91125, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16166516" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; Adaptor Proteins, Vesicular Transport/deficiency/physiology ; Animals ; Antigens, Differentiation/physiology ; Cell Line ; Cells, Cultured ; Computer Simulation ; Cycloheximide/pharmacology ; DNA-Binding Proteins/genetics/physiology ; Gene Expression Profiling ; Gene Expression Regulation ; I-kappa B Kinase ; I-kappa B Proteins/biosynthesis/genetics/metabolism ; Interferon Regulatory Factor-3 ; Kinetics ; Lipopolysaccharides/*immunology/metabolism ; Mice ; Models, Biological ; Myeloid Differentiation Factor 88 ; NF-kappa B/*metabolism ; Oligonucleotide Array Sequence Analysis ; Protein Synthesis Inhibitors/pharmacology ; Protein-Serine-Threonine Kinases/metabolism ; Receptors, Immunologic/deficiency/metabolism/physiology ; Signal Transduction ; Time Factors ; Toll-Like Receptor 4 ; Transcription Factors/genetics/physiology ; Tumor Necrosis Factor-alpha/biosynthesis/metabolism
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    Distinct kinetic changes in neurotransmitter release after SNARE protein cleavage (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-07-16
    Description: Neurotransmitter release is triggered by calcium ions and depends critically on the correct function of three types of SNARE [soluble N-ethylmaleimide-sensitive factor attachment protein (SNAP) receptor] proteins. With use of the large calyx of Held presynaptic terminal from rats, we found that cleavage of different SNARE proteins by clostridial neurotoxins caused distinct kinetic changes in neurotransmitter release. When elevating calcium ion concentration directly at the presynaptic terminal with the use of caged calcium, cleavage of SNAP-25 by botulinum toxin A (BoNT/A) produced a strong reduction in the calcium sensitivity for release, whereas cleavage of syntaxin using BoNT/C1 and synaptobrevin using tetanus toxin (TeNT) produced an all-or-nothing block without changing the kinetics of remaining vesicles. When stimulating release by calcium influx through channels, a difference between BoNT/C1 and TeNT emerged, which suggests that cleavage of synaptobrevin modifies the coupling between channels and release-competent vesicles.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sakaba, Takeshi -- Stein, Alexander -- Jahn, Reinhard -- Neher, Erwin -- New York, N.Y. -- Science. 2005 Jul 15;309(5733):491-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology and Department of Membrane Biophysics, Max Planck Institute for Biophysical Chemistry, Gottingen 37077, Germany. tsakaba@gwdg.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16020741" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Animals ; Botulinum Toxins/metabolism/pharmacology ; Botulinum Toxins, Type A/metabolism/pharmacology ; Calcium/metabolism ; Calcium Channels/metabolism ; Excitatory Postsynaptic Potentials ; In Vitro Techniques ; Kinetics ; Membrane Proteins/*metabolism ; Nerve Tissue Proteins/*metabolism ; Neurotransmitter Agents/*metabolism ; Patch-Clamp Techniques ; Presynaptic Terminals/*metabolism ; Qa-SNARE Proteins ; R-SNARE Proteins ; Rats ; Synaptic Vesicles/metabolism ; Synaptosomal-Associated Protein 25 ; Tetanus Toxin/metabolism/pharmacology
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    Sequence-directed DNA translocation by purified FtsK (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-02-01
    Description: DNA translocases are molecular motors that move rapidly along DNA using adenosine triphosphate as the source of energy. We directly observed the movement of purified FtsK, an Escherichia coli translocase, on single DNA molecules. The protein moves at 5 kilobases per second and against forces up to 60 piconewtons, and locally reverses direction without dissociation. On three natural substrates, independent of its initial binding position, FtsK efficiently translocates over long distances to the terminal region of the E. coli chromosome, as it does in vivo. Our results imply that FtsK is a bidirectional motor that changes direction in response to short, asymmetric directing DNA sequences.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pease, Paul J -- Levy, Oren -- Cost, Gregory J -- Gore, Jeff -- Ptacin, Jerod L -- Sherratt, David -- Bustamante, Carlos -- Cozzarelli, Nicholas R -- GM07232-27/GM/NIGMS NIH HHS/ -- GM08295-15/GM/NIGMS NIH HHS/ -- GM31657/GM/NIGMS NIH HHS/ -- GM32543/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Jan 28;307(5709):586-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720-3204, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15681387" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Bacteriophage lambda ; Base Sequence ; Chromosomes, Bacterial ; DNA, Bacterial/chemistry/*metabolism ; DNA, Superhelical/chemistry/metabolism ; DNA, Viral/chemistry/*metabolism ; Escherichia coli/*metabolism ; Escherichia coli Proteins/isolation & purification/*metabolism ; Kinetics ; Membrane Proteins/isolation & purification/*metabolism ; Models, Biological ; Molecular Motor Proteins/isolation & purification/*metabolism ; Nucleic Acid Conformation
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    Computational thermostabilization of an enzyme (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-05-10
    Description: Thermostabilizing an enzyme while maintaining its activity for industrial or biomedical applications can be difficult with traditional selection methods. We describe a rapid computational approach that identified three mutations within a model enzyme that produced a 10 degrees C increase in apparent melting temperature T(m) and a 30-fold increase in half-life at 50 degrees C, with no reduction in catalytic efficiency. The effects of the mutations were synergistic, giving an increase in excess of the sum of their individual effects. The redesigned enzyme induced an increased, temperature-dependent bacterial growth rate under conditions that required its activity, thereby coupling molecular and metabolic engineering.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3412875/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3412875/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Korkegian, Aaron -- Black, Margaret E -- Baker, David -- Stoddard, Barry L -- CA85939/CA/NCI NIH HHS/ -- CA97328/CA/NCI NIH HHS/ -- GM49857/GM/NIGMS NIH HHS/ -- GM59224/GM/NIGMS NIH HHS/ -- R01 CA097328/CA/NCI NIH HHS/ -- R01 GM049857/GM/NIGMS NIH HHS/ -- T32-GM08268/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 May 6;308(5723):857-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Basic Sciences, Fred Hutchinson Cancer Research Center (FHCRC), 1100 Fairview Avenue North, Seattle, WA 98109, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15879217" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Catalysis ; Circular Dichroism ; *Computer Simulation ; Crystallography, X-Ray ; Cytosine Deaminase/*chemistry/*metabolism ; Enzyme Stability ; Escherichia coli/genetics/metabolism ; Kinetics ; Models, Molecular ; Molecular Sequence Data ; Monte Carlo Method ; Mutagenesis, Site-Directed ; Point Mutation ; Protein Conformation ; Protein Denaturation ; *Protein Engineering ; Protein Folding ; Protein Structure, Secondary ; Software ; Temperature ; Thermodynamics ; Transformation, Genetic ; Yeasts/enzymology
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    Photosynthetic O2 formation tracked by time-resolved x-ray experiments (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-11-15
    Description: Plants and cyanobacteria produce atmospheric dioxygen from water, powered by sunlight and catalyzed by a manganese complex in photosystem II. A classic S-cycle model for oxygen evolution involves five states, but only four have been identified. The missing S4 state is particularly important because it is directly involved in dioxygen formation. Now progress comes from an x-ray technique that can monitor redox and structural changes in metal centers in real time with 10-microsecond resolution. We show that in the O2-formation step, an intermediate is formed--the enigmatic S4 state. Its creation is identified with a deprotonation process rather than the expected electron-transfer mechanism. Subsequent electron transfer would give an additional S4' state, thus extending the fundamental S-state cycle of dioxygen formation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Haumann, M -- Liebisch, P -- Muller, C -- Barra, M -- Grabolle, M -- Dau, H -- New York, N.Y. -- Science. 2005 Nov 11;310(5750):1019-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Freie Universitat Berlin, FB Physik, Arnimallee 14, D-14195 Berlin, Germany. haumann@physik.fu-berlin.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16284178" target="_blank"〉PubMed〈/a〉
    Keywords: Chemistry, Physical ; Electrons ; Entropy ; Kinetics ; Lasers ; Manganese/chemistry ; Models, Biological ; Models, Chemical ; Oxidation-Reduction ; Oxygen/chemistry/*metabolism ; *Photosynthesis ; Photosystem II Protein Complex/chemistry/*metabolism ; Physicochemical Phenomena ; Protons ; Spectrum Analysis ; Spinacia oleracea ; Water/metabolism ; X-Rays
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    The nature of aqueous tunneling pathways between electron-transfer proteins (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-11-29
    Description: Structured water molecules near redox cofactors were found recently to accelerate electron-transfer (ET) kinetics in several systems. Theoretical study of interprotein electron transfer across an aqueous interface reveals three distinctive electronic coupling mechanisms that we describe here: (i) a protein-mediated regime when the two proteins are in van der Waals contact; (ii) a structured water-mediated regime featuring anomalously weak distance decay at relatively close protein-protein contact distances; and (iii) a bulk water-mediated regime at large distances. Our analysis explains a range of otherwise puzzling biological ET kinetic data and provides a framework for including explicit water-mediated tunneling effects on ET kinetics.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3613566/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3613566/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lin, Jianping -- Balabin, Ilya A -- Beratan, David N -- GM-048043/GM/NIGMS NIH HHS/ -- R01 GM048043/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Nov 25;310(5752):1311-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departments of Chemistry and Biochemistry, Duke University, Durham, NC 27708, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16311331" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cattle ; Chemistry, Physical ; Cytochromes b5/chemistry/*metabolism ; *Electron Transport ; Kinetics ; Models, Chemical ; Physicochemical Phenomena ; Porphyrins/chemistry ; Protein Conformation ; Thermodynamics ; Water/*chemistry
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    Small-molecule inhibition of TNF-alpha (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-11-15
    Description: We have identified a small-molecule inhibitor of tumor necrosis factor alpha (TNF-alpha) that promotes subunit disassembly of this trimeric cytokine family member. The compound inhibits TNF-alpha activity in biochemical and cell-based assays with median inhibitory concentrations of 22 and 4.6 micromolar, respectively. Formation of an intermediate complex between the compound and the intact trimer results in a 600-fold accelerated subunit dissociation rate that leads to trimer dissociation. A structure solved by x-ray crystallography reveals that a single compound molecule displaces a subunit of the trimer to form a complex with a dimer of TNF-alpha subunits.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉He, Molly M -- Smith, Annemarie Stroustrup -- Oslob, Johan D -- Flanagan, William M -- Braisted, Andrew C -- Whitty, Adrian -- Cancilla, Mark T -- Wang, Jun -- Lugovskoy, Alexey A -- Yoburn, Josh C -- Fung, Amy D -- Farrington, Graham -- Eldredge, John K -- Day, Eric S -- Cruz, Leslie A -- Cachero, Teresa G -- Miller, Stephan K -- Friedman, Jessica E -- Choong, Ingrid C -- Cunningham, Brian C -- New York, N.Y. -- Science. 2005 Nov 11;310(5750):1022-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Sunesis Pharmaceuticals, Incorporated, 341 Oyster Point Boulevard, South San Francisco, CA 94080, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16284179" target="_blank"〉PubMed〈/a〉
    Keywords: Biotinylation ; Chemistry, Physical ; Crystallography, X-Ray ; Dimerization ; Fluorescence ; Hydrogen/chemistry ; Hydrophobic and Hydrophilic Interactions ; Indoles/chemical synthesis/*chemistry/*pharmacology ; Kinetics ; Mass Spectrometry ; Models, Chemical ; Models, Molecular ; Molecular Conformation ; Molecular Structure ; Physicochemical Phenomena ; Protein Conformation ; Protein Subunits/chemistry ; Receptors, Tumor Necrosis Factor, Type I/metabolism ; Tumor Necrosis Factor-alpha/*antagonists & inhibitors/*chemistry/metabolism
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    The biochemical architecture of an ancient adaptive landscape (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-10-22
    Description: Molecular evolution is moving from statistical descriptions of adaptive molecular changes toward predicting the fitness effects of mutations. Here, we characterize the fitness landscape of the six amino acids controlling coenzyme use in isopropylmalate dehydrogenase (IMDH). Although all natural IMDHs use nicotinamide adenine dinucleotide (NAD) as a coenzyme, they can be engineered to use nicotinamide adenine dinucleotide phosphate (NADP) instead. Intermediates between these two phenotypic extremes show that each amino acid contributes additively to enzyme function, with epistatic contributions confined to fitness. The genotype-phenotype-fitness map shows that NAD use is a global optimum.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lunzer, Mark -- Miller, Stephen P -- Felsheim, Roderick -- Dean, Antony M -- GM060611/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Oct 21;310(5747):499-501.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉BioTechnology Institute, Evolution and Behavior, University of Minnesota, St. Paul, MN 55108, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16239478" target="_blank"〉PubMed〈/a〉
    Keywords: 3-Isopropylmalate Dehydrogenase/*chemistry/genetics/*metabolism ; Amino Acid Substitution ; Analysis of Variance ; Catalysis ; Epistasis, Genetic ; Escherichia coli/enzymology ; *Evolution, Molecular ; Genotype ; Kinetics ; Leucine/biosynthesis ; Mathematics ; Models, Chemical ; Mutation ; NAD/*metabolism ; NADP/*metabolism ; Oxidation-Reduction ; Phenotype ; Protein Engineering ; Selection, Genetic ; Thermodynamics
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    Equivalent effects of snake PLA2 neurotoxins and lysophospholipid-fatty acid mixtures (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-12-13
    Description: Snake presynaptic phospholipase A2 neurotoxins (SPANs) paralyze the neuromuscular junction (NMJ). Upon intoxication, the NMJ enlarges and has a reduced content of synaptic vesicles, and primary neuronal cultures show synaptic swelling with surface exposure of the lumenal domain of the synaptic vesicle protein synaptotagmin I. Concomitantly, these neurotoxins induce exocytosis of neurotransmitters. We found that an equimolar mixture of lysophospholipids and fatty acids closely mimics all of the biological effects of SPANs. These results draw attention to the possible role of local lipid changes in synaptic vesicle release and provide new tools for the study of exocytosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rigoni, Michela -- Caccin, Paola -- Gschmeissner, Steve -- Koster, Grielof -- Postle, Anthony D -- Rossetto, Ornella -- Schiavo, Giampietro -- Montecucco, Cesare -- GP0272Y01/Telethon/Italy -- New York, N.Y. -- Science. 2005 Dec 9;310(5754):1678-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biomedical Sciences and Consiglio Nazionale Ricerche Institute of Neuroscience, University of Padova, Italy.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16339444" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cells, Cultured ; Elapid Venoms/toxicity ; Esterification ; Exocytosis ; Fatty Acids/*metabolism/toxicity ; Glutamic Acid/metabolism ; Hydrolysis ; Kinetics ; Lipid Bilayers ; Lysophospholipids/*metabolism/toxicity ; Male ; Mass Spectrometry ; Membrane Fusion ; Membrane Lipids/metabolism ; Mice ; Neuromuscular Junction/drug effects/metabolism/physiology ; Neurons/drug effects/metabolism/ultrastructure ; Neurotoxins/*metabolism/toxicity ; Neurotransmitter Agents/metabolism ; Phospholipases A/*metabolism/toxicity ; Phospholipases A2 ; Synapses/drug effects/ultrastructure ; Synaptic Membranes/metabolism/*physiology ; Synaptic Vesicles/drug effects/physiology/ultrastructure
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    An acylation cycle regulates localization and activity of palmitoylated Ras isoforms (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-02-12
    Description: We show that the specific subcellular distribution of H- and Nras guanosine triphosphate-binding proteins is generated by a constitutive de/reacylation cycle that operates on palmitoylated proteins, driving their rapid exchange between the plasma membrane (PM) and the Golgi apparatus. Depalmitoylation redistributes farnesylated Ras in all membranes, followed by repalmitoylation and trapping of Ras at the Golgi, from where it is redirected to the PM via the secretory pathway. This continuous cycle prevents Ras from nonspecific residence on endomembranes, thereby maintaining the specific intracellular compartmentalization. The de/reacylation cycle also initiates Ras activation at the Golgi by transport of PM-localized Ras guanosine triphosphate. Different de/repalmitoylation kinetics account for isoform-specific activation responses to growth factors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rocks, Oliver -- Peyker, Anna -- Kahms, Martin -- Verveer, Peter J -- Koerner, Carolin -- Lumbierres, Maria -- Kuhlmann, Jurgen -- Waldmann, Herbert -- Wittinghofer, Alfred -- Bastiaens, Philippe I H -- New York, N.Y. -- Science. 2005 Mar 18;307(5716):1746-52. Epub 2005 Feb 10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Structural Biology, Max Planck Institute for Molecular Physiology, Otto-Hahn-Strasse 11, 44227 Dortmund, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15705808" target="_blank"〉PubMed〈/a〉
    Keywords: Acylation ; Amino Acid Sequence ; Animals ; COS Cells ; Cell Line ; Cell Membrane/*metabolism ; Cercopithecus aethiops ; Dogs ; Golgi Apparatus/*metabolism ; Guanosine Triphosphate/metabolism ; Kinetics ; Models, Biological ; Molecular Sequence Data ; Palmitic Acid/*metabolism ; Protein Isoforms/chemistry/metabolism ; Protein Processing, Post-Translational ; Protein Structure, Tertiary ; Protein Transport ; Proto-Oncogene Proteins p21(ras)/chemistry/*metabolism ; Recombinant Fusion Proteins/metabolism ; Transfection
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    The selective cause of an ancient adaptation (2005)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2005-01-18
    Description: Phylogenetic analysis reveals that the use of nicotinamide adenine dinucleotide phosphate (NADP) by prokaryotic isocitrate dehydrogenase (IDH) arose around the time eukaryotic mitochondria first appeared, about 3.5 billion years ago. We replaced the wild-type gene that encodes the NADP-dependent IDH of Escherichia coli with an engineered gene that possesses the ancestral NAD-dependent phenotype. The engineered enzyme is disfavored during competition for acetate. The selection intensifies in genetic backgrounds where other sources of reduced NADP have been removed. A survey of sequenced prokaryotic genomes reveals that those genomes that encode isocitrate lyase, which is essential for growth on acetate, always have an NADP-dependent IDH. Those with only an NAD-dependent IDH never have isocitrate lyase. Hence, the NADP dependence of prokaryotic IDH is an ancient adaptation to anabolic demand for reduced NADP during growth on acetate.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhu, Guoping -- Golding, G Brian -- Dean, Antony M -- GM060611/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 Feb 25;307(5713):1279-82. Epub 2005 Jan 13.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉BioTechnology Institute, University of Minnesota, St. Paul, MN 55108, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15653464" target="_blank"〉PubMed〈/a〉
    Keywords: 3-Isopropylmalate Dehydrogenase ; Acetates/metabolism ; *Adaptation, Physiological ; Alcohol Oxidoreductases/chemistry/metabolism ; Bacteria/*genetics/growth & development/*metabolism ; Binding Sites ; Biological Evolution ; Escherichia coli/enzymology/genetics/metabolism ; Isocitrate Dehydrogenase/chemistry/genetics/*metabolism ; Isocitrate Lyase/genetics/metabolism ; Kinetics ; NAD/*metabolism ; NADP/*metabolism ; Oxidation-Reduction ; Phylogeny ; Protein Engineering ; *Selection, Genetic
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    An active role for tRNA in decoding beyond codon:anticodon pairing (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-05-21
    Description: During transfer RNA (tRNA) selection, a cognate codon:anticodon interaction triggers a series of events that ultimately results in the acceptance of that tRNA into the ribosome for peptide-bond formation. High-fidelity discrimination between the cognate tRNA and near- and noncognate ones depends both on their differential dissociation rates from the ribosome and on specific acceleration of forward rate constants by cognate species. Here we show that a mutant tRNA(Trp) carrying a single substitution in its D-arm achieves elevated levels of miscoding by accelerating these forward rate constants independent of codon:anticodon pairing in the decoding center. These data provide evidence for a direct role for tRNA in signaling its own acceptance during decoding and support its fundamental role during the evolution of protein synthesis.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1687177/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1687177/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cochella, Luisa -- Green, Rachel -- R01 GM059425/GM/NIGMS NIH HHS/ -- R01GM059425/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2005 May 20;308(5725):1178-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Molecular Biology and Genetics, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15905403" target="_blank"〉PubMed〈/a〉
    Keywords: Anticodon ; Base Pairing ; Codon ; Codon, Terminator ; Dipeptides/biosynthesis ; GTP Phosphohydrolases/metabolism ; Guanosine Triphosphate/metabolism ; Hydrolysis ; Kinetics ; Mutation ; Nucleic Acid Conformation ; Peptide Elongation Factor Tu/metabolism ; *Protein Biosynthesis ; RNA, Messenger/metabolism ; RNA, Transfer, Trp/*chemistry/genetics/*metabolism ; Ribosomes/*metabolism
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    The intracellular fate of Salmonella depends on the recruitment of kinesin (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-05-21
    Description: Salmonella enterica causes a variety of diseases, including gastroenteritis and typhoid fever. The success of this pathogen depends on its capacity to proliferate within host cells in a membrane-bound compartment. We found that the Salmonella-containing vacuole recruited the plus-end-directed motor kinesin. Bacterial effector proteins translocated into the host cell by a type III secretion system antagonistically regulated this event. Among these effectors, SifA targeted SKIP, a host protein that down-regulated the recruitment of kinesin on the bacterial vacuole and, in turn, controlled vacuolar membrane dynamics.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boucrot, Emmanuel -- Henry, Thomas -- Borg, Jean-Paul -- Gorvel, Jean-Pierre -- Meresse, Stephane -- New York, N.Y. -- Science. 2005 May 20;308(5725):1174-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre d'Immunologie de Marseille-Luminy, CNRS-INSERM-Universite de la Mediterranee, Parc Scientifique de Luminy, Case 906-13288 Marseille Cedex 9, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15905402" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing/*chemistry/*metabolism ; Amino Acid Motifs ; Animals ; Bacterial Proteins/genetics/*metabolism ; Cell Line, Tumor ; Cytosol/metabolism ; Dyneins/metabolism ; Glycoproteins/genetics/*metabolism ; Golgi Apparatus/metabolism ; HeLa Cells ; Humans ; Immunoprecipitation ; Intracellular Membranes/metabolism ; Kinesin/*metabolism ; Kinetics ; Macrophages/metabolism/microbiology ; Mice ; RNA Interference ; Recombinant Fusion Proteins/metabolism ; Salmonella typhimurium/genetics/growth & development/*metabolism/*pathogenicity ; Vacuoles/metabolism/*microbiology ; Virulence
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    Elementary response of olfactory receptor neurons to odorants (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-06-25
    Description: Signaling by heterotrimeric GTP-binding proteins (G proteins) drives numerous cellular processes. The number of G protein molecules activated by a single membrane receptor is a determinant of signal amplification, although in most cases this parameter remains unknown. In retinal rod photoreceptors, a long-lived photoisomerized rhodopsin molecule activates many G protein molecules (transducins), yielding substantial amplification and a large elementary (single-photon) response, before rhodopsin activity is terminated. Here we report that the elementary response in olfactory transduction is extremely small. A ligand-bound odorant receptor has a low probability of activating even one G protein molecule because the odorant dwell-time is very brief. Thus, signal amplification in olfactory transduction appears fundamentally different from that of phototransduction.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2957801/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2957801/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bhandawat, Vikas -- Reisert, Johannes -- Yau, King-Wai -- DC06904/DC/NIDCD NIH HHS/ -- R01 DC006904/DC/NIDCD NIH HHS/ -- R01 DC006904-01/DC/NIDCD NIH HHS/ -- R01 EY006837/EY/NEI NIH HHS/ -- R01 EY006837-16A1/EY/NEI NIH HHS/ -- R01 EY006837-17/EY/NEI NIH HHS/ -- R01 EY006837-18/EY/NEI NIH HHS/ -- R01 EY014596/EY/NEI NIH HHS/ -- R01 EY014596-01/EY/NEI NIH HHS/ -- R01 EY014596-02/EY/NEI NIH HHS/ -- R01 EY014596-03/EY/NEI NIH HHS/ -- R37 EY006837/EY/NEI NIH HHS/ -- R37 EY006837-15/EY/NEI NIH HHS/ -- R37 EY006837-15S1/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 2005 Jun 24;308(5730):1931-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. vbhanda@mail.jhmi.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15976304" target="_blank"〉PubMed〈/a〉
    Keywords: Acetophenones/*metabolism/pharmacology ; Action Potentials ; Adenylyl Cyclases/metabolism ; Animals ; Calcium/metabolism/pharmacology ; Cell Separation ; Cyclohexanols/*metabolism/pharmacology ; Dose-Response Relationship, Drug ; Heterotrimeric GTP-Binding Proteins/metabolism ; In Vitro Techniques ; Kinetics ; Ligands ; Monoterpenes/*metabolism/pharmacology ; *Odors ; Olfactory Receptor Neurons/cytology/*physiology ; Phosphorylation ; Rana pipiens ; Receptors, Odorant/*metabolism ; Signal Transduction ; Smell/physiology
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    Biochemistry. The photosynthesis "oxygen clock" gets a new number (2005)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2005-11-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Penner-Hahn, James E -- Yocum, Charles F -- New York, N.Y. -- Science. 2005 Nov 11;310(5750):982-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of Michigan, 930 North University Avenue, Ann Arbor, MI 48109-1055, USA. jeph@umich.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16284168" target="_blank"〉PubMed〈/a〉
    Keywords: Chemistry, Physical ; Electrons ; Entropy ; Kinetics ; Manganese/chemistry ; Models, Biological ; Models, Chemical ; Oxidation-Reduction ; Oxygen/chemistry/*metabolism ; *Photosynthesis ; Photosystem II Protein Complex/*chemistry/*metabolism ; Physicochemical Phenomena ; Protons ; Spectrum Analysis ; Water/metabolism ; X-Rays
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    PIN proteins perform a rate-limiting function in cellular auxin efflux (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-04-08
    Description: Intercellular flow of the phytohormone auxin underpins multiple developmental processes in plants. Plant-specific pin-formed (PIN) proteins and several phosphoglycoprotein (PGP) transporters are crucial factors in auxin transport-related development, yet the molecular function of PINs remains unknown. Here, we show that PINs mediate auxin efflux from mammalian and yeast cells without needing additional plant-specific factors. Conditional gain-of-function alleles and quantitative measurements of auxin accumulation in Arabidopsis and tobacco cultured cells revealed that the action of PINs in auxin efflux is distinct from PGP, rate-limiting, specific to auxins, and sensitive to auxin transport inhibitors. This suggests a direct involvement of PINs in catalyzing cellular auxin efflux.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Petrasek, Jan -- Mravec, Jozef -- Bouchard, Rodolphe -- Blakeslee, Joshua J -- Abas, Melinda -- Seifertova, Daniela -- Wisniewska, Justyna -- Tadele, Zerihun -- Kubes, Martin -- Covanova, Milada -- Dhonukshe, Pankaj -- Skupa, Petr -- Benkova, Eva -- Perry, Lucie -- Krecek, Pavel -- Lee, Ok Ran -- Fink, Gerald R -- Geisler, Markus -- Murphy, Angus S -- Luschnig, Christian -- Zazimalova, Eva -- Friml, Jiri -- New York, N.Y. -- Science. 2006 May 12;312(5775):914-8. Epub 2006 Apr 6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Experimental Botany, the Academy of Sciences of the Czech Republic, 165 02 Prague 6, Czech Republic.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16601150" target="_blank"〉PubMed〈/a〉
    Keywords: ATP-Binding Cassette Transporters/genetics/metabolism ; Arabidopsis/cytology/growth & development/*metabolism/physiology ; Arabidopsis Proteins/genetics/*metabolism ; Biological Transport ; Cell Membrane/metabolism ; Cells, Cultured ; Gravitropism ; HeLa Cells ; Humans ; Indoleacetic Acids/*metabolism ; Kinetics ; Membrane Transport Proteins/genetics/*metabolism ; Mutation ; Naphthaleneacetic Acids/metabolism ; Phthalimides/pharmacology ; Plant Roots/physiology ; Saccharomyces cerevisiae/genetics ; Tobacco ; Transfection ; Transformation, Genetic
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    Direct demonstration of an adaptive constraint (2006)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2006-10-21
    Description: The role of constraint in adaptive evolution is an open question. Directed evolution of an engineered beta-isopropylmalate dehydrogenase (IMDH), with coenzyme specificity switched from nicotinamide adenine dinucleotide (NAD) to nicotinamide adenine dinucleotide phosphate (NADP), always produces mutants with lower affinities for NADP. This result is the correlated response to selection for relief from inhibition by NADPH (the reduced form of NADP) expected of an adaptive landscape subject to three enzymatic constraints: an upper limit to the rate of maximum turnover (kcat), a correlation in NADP and NADPH affinities, and a trade-off between NAD and NADP usage. Two additional constraints, high intracellular NADPH abundance and the cost of compensatory protein synthesis, have ensured the conserved use of NAD by IMDH throughout evolution. Our results show that selective mechanisms and evolutionary constraints are to be understood in terms of underlying adaptive landscapes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, Stephen P -- Lunzer, Mark -- Dean, Antony M -- GM060611/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Oct 20;314(5798):458-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉BioTechnology Institute, University of Minnesota, St. Paul, MN 55108, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17053145" target="_blank"〉PubMed〈/a〉
    Keywords: 3-Isopropylmalate Dehydrogenase/antagonists & ; inhibitors/chemistry/genetics/*metabolism ; *Adaptation, Physiological ; Amino Acid Substitution ; Binding Sites ; Codon ; *Directed Molecular Evolution ; Escherichia coli/*enzymology/growth & development/physiology ; *Evolution, Molecular ; Kinetics ; Mutation ; NAD/metabolism ; NADP/metabolism ; Phenotype ; Selection, Genetic
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  • 84
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    The dynamic energy landscape of dihydrofolate reductase catalysis (2006)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2006-09-16
    Description: We used nuclear magnetic resonance relaxation dispersion to characterize higher energy conformational substates of Escherichia coli dihydrofolate reductase. Each intermediate in the catalytic cycle samples low-lying excited states whose conformations resemble the ground-state structures of preceding and following intermediates. Substrate and cofactor exchange occurs through these excited substates. The maximum hydride transfer and steady-state turnover rates are governed by the dynamics of transitions between ground and excited states of the intermediates. Thus, the modulation of the energy landscape by the bound ligands funnels the enzyme through its reaction cycle along a preferred kinetic path.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boehr, David D -- McElheny, Dan -- Dyson, H Jane -- Wright, Peter E -- GM56879/GM/NIGMS NIH HHS/ -- GM75995/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Sep 15;313(5793):1638-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Skaggs Institute for Chemical Biology, Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16973882" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Catalysis ; Escherichia coli/*enzymology ; Kinetics ; Ligands ; Models, Molecular ; NADP/metabolism ; Nuclear Magnetic Resonance, Biomolecular ; Protein Binding ; *Protein Conformation ; Tetrahydrofolate Dehydrogenase/*chemistry/*metabolism ; Tetrahydrofolates/metabolism ; Thermodynamics
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  • 85
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    Chemical rescue of a mutant enzyme in living cells (2006)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2006-03-04
    Description: The restoration of catalytic activity to mutant enzymes by small molecules is well established for in vitro systems. Here, we show that the protein tyrosine kinase Src arginine-388--〉alanine (R388A) mutant can be rescued in live cells with the use of the small molecule imidazole. Cellular rescue of a viral Src homolog was rapid and reversible and conferred predicted oncogenic properties. Using chemical rescue in combination with mass spectrometry, we confirmed six known Src kinase substrates and identified several new protein targets. Chemical rescue data suggest that cellular Src is active under basal conditions. Rescue of R388A cellular Src provided insights into the mitogen-activated protein kinase pathway. This chemical rescue approach will likely have many applications in cell signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Qiao, Yingfeng -- Molina, Henrik -- Pandey, Akhilesh -- Zhang, Jin -- Cole, Philip A -- New York, N.Y. -- Science. 2006 Mar 3;311(5765):1293-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology and Molecular Sciences, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16513984" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing/metabolism ; Animals ; Cell Line ; Cell Transformation, Neoplastic ; Fluorescence Resonance Energy Transfer ; Gene Expression Profiling ; Gene Expression Regulation ; Growth Substances/metabolism/pharmacology ; Humans ; Imidazoles/*metabolism/pharmacology ; Kinetics ; Mice ; Mitogen-Activated Protein Kinases/metabolism ; Mutation ; Nuclear Proteins/metabolism ; Oligonucleotide Array Sequence Analysis ; Phenotype ; Phosphorylation ; Phosphotyrosine/metabolism ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins pp60(c-src)/*genetics/*metabolism ; Recombinant Proteins/metabolism ; Transfection ; src Homology Domains
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  • 86
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    Unexpectedly high levels of HIV-1 RNA and protein synthesis in a cytocidal infection (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-12-16
    Description: The expression of a laboratory strain of HIV-1 (HTLV-IIIB) has been studied in mitogen-stimulated peripheral blood lymphocytes (PBLs) and in two lymphoid cell lines (CEM cells and C8166 cells). HIV-expressing cells contained from 300,000 to 2,500,000 copies of viral RNA per cell. Near-synchronous expression of an active infection could be achieved in C8166 cells. In these cells, the high copy numbers of viral RNA used as much as 40% of total protein synthesis for the production of viral gag protein, with high levels of viral RNA and protein synthesis preceding cell death by 2 to 4 days.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Somasundaran, M -- Robinson, H L -- AI 24474/AI/NIAID NIH HHS/ -- N01-HB-6-7022/HB/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1988 Dec 16;242(4885):1554-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, University of Massachusetts Medical Center, Worcester 01655.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3201245" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; *Cell Transformation, Viral ; HIV-1/*genetics/growth & development/metabolism ; Humans ; Kinetics ; Lymphocytes/*microbiology ; RNA, Viral/*biosynthesis ; Viral Proteins/*biosynthesis
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  • 87
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    Lithium blocks a phosphoinositide-mediated cholinergic response in hippocampal slices (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-03-18
    Description: The effects of lithium on inositol phosphate metabolism may account for the therapeutic actions of lithium in affective disorder. Muscarinic stimulation of the phosphoinositide system blocks synaptic inhibitory actions of adenosine in the hippocampal slice. At therapeutic concentrations, lithium diminished this muscarinic response, whereas rubidium, which does not affect phosphoinositide metabolism, had no effect. A dampening of phosphoinositide-mediated neurotransmission may explain the normalizing effects of lithium in treating both mania and depression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Worley, P F -- Heller, W A -- Snyder, S H -- Baraban, J M -- DA-00266/DA/NIDA NIH HHS/ -- MH-18501/MH/NIMH NIH HHS/ -- MH-42323/MH/NIMH NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1988 Mar 18;239(4846):1428-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2831626" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine/pharmacology ; Carbachol/pharmacology ; Enzyme Activation/drug effects ; Hippocampus/drug effects/*physiology ; Inositol Phosphates/metabolism ; Kinetics ; Lithium/*pharmacology ; Oxotremorine/analogs & derivatives/pharmacology ; Phorbol Esters/pharmacology ; Phosphatidylinositols/*metabolism ; Protein Kinase C/metabolism ; Receptors, Muscarinic/drug effects/*physiology ; Synapses/physiology ; Synaptic Transmission/drug effects
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  • 88
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    A specific amino acid binding site composed of RNA (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-06-24
    Description: A specific, reversible binding site for a free amino acid is detectable on the intron of the Tetrahymena self-splicing ribosomal precursor RNA. The site selects arginine among the natural amino acids, and prefers the L- to the D-amino acid. The dissociation constant is in the millimolar range, and amino acid binding is at or in the catalytic rG splicing substrate site. Occupation of the G site by L-arginine therefore inhibits splicing by inhibiting the binding of rG, without inhibition of later reactions in the splicing reaction sequence. Arginine binding specificity seems to be directed at the side chain and the guanidino radical, and the alpha-amino and carboxyl groups are dispensable for binding. The arginine site can be placed within the G site by structural homology, with consequent implications for RNA-amino acid interaction, for the origin of the genetic code, for control of RNA activities, and for further catalytic capabilities for RNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yarus, M -- R37 GM30881/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Jun 24;240(4860):1751-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular, Cellular, and Developmental Biology, University of Colorado, Boulder 80309.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3381099" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arginine/*metabolism ; Binding Sites ; Catalysis ; Genetic Code ; Guanosine Triphosphate/metabolism ; Kinetics ; Magnesium/metabolism ; Models, Molecular ; *RNA Splicing ; RNA, Ribosomal/*physiology ; Structure-Activity Relationship ; Tetrahymena
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  • 89
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    Elevated D2 dopamine receptors in drug-naive schizophrenics (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-02-12
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zeeberg, B R -- Gibson, R E -- Reba, R C -- MH42821-01/MH/NIMH NIH HHS/ -- NS-15080/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1988 Feb 12;239(4841 Pt 1):789-91.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2963379" target="_blank"〉PubMed〈/a〉
    Keywords: Brain/*metabolism ; Haloperidol/therapeutic use ; Humans ; Kinetics ; Receptors, Dopamine/drug effects/*metabolism ; Receptors, Dopamine D2 ; Schizophrenia/*metabolism
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  • 90
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    Membranes as the energy source in the endergonic transformation of vitamin A to 11-cis-retinol (1989)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1989-05-26
    Description: The eye needs to biosynthesize 11-cis-retinoids because the chromophore of rhodopsin is 11-cis-retinal. The critical metabolic step is the endergonic isomerization of free all-trans-retinol (vitamin A) into 11-cis-retinol. This isomerization process can take place in isolated membranes from the retinal pigment epithelium in the absence of added energy sources. Specific binding proteins probably do not serve as an energy source, and since all of the reactions in the visual cycle are shown here to be reversible, trapping reactions also do not participate in the isomerization reaction. One previously unexplored possibility is that the chemical energy in the bonds of the membrane itself may drive the isomerization reaction. A group transfer reaction is proposed that forms a retinyl ester from a lipid acyl donor and vitamin A. This transfer can drive the isomerization reaction because the all-trans-retinyl ester is isomerized directly to 11-cis-retinol. Thus, the free energy of hydrolysis of the ester is coupled to the thermodynamically uphill trans to cis isomerization. The prediction of an obligate C-O bond cleavage in the vitamin A moiety during isomerization is borne out. Although the natural substrate for isomerization is not known, all-trans-retinyl palmitate is processed in vitro to 11-cis-retinol by pigment epithelial membranes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Deigner, P S -- Law, W C -- Canada, F J -- Rando, R R -- EY04096/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1989 May 26;244(4907):968-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2727688" target="_blank"〉PubMed〈/a〉
    Keywords: Amphibians ; Animals ; Cattle ; Cell Membrane/*metabolism ; *Energy Metabolism ; Isomerases/metabolism ; Isomerism ; Kinetics ; Molecular Structure ; Pigment Epithelium of Eye/*metabolism/radiation effects ; Ultraviolet Rays ; Vitamin A/analogs & derivatives/*metabolism ; *cis-trans-Isomerases
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  • 91
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    Analysis of ligand binding specificity of receptor chimeras (1989)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1989-01-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Catterall, W A -- New York, N.Y. -- Science. 1989 Jan 13;243(4888):236-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2536189" target="_blank"〉PubMed〈/a〉
    Keywords: Kinetics ; Ligands ; Receptors, Adrenergic, alpha/*metabolism ; Receptors, Adrenergic, beta/*metabolism ; Thermodynamics
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  • 92
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    Hydrogen tunneling in enzyme reactions (1989)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1989-03-10
    Description: Primary and secondary protium-to-tritium (H/T) and deuterium-to-tritium (D/T) kinetic isotope effects for the catalytic oxidation of benzyl alcohol to benzaldehyde by yeast alcohol dehydrogenase (YADH) at 25 degrees Celsius have been determined. Previous studies showed that this reaction is nearly or fully rate limited by the hydrogen-transfer step. Semiclassical mass considerations that do not include tunneling effects would predict that kH/kT = (kD/kT)3.26, where kH, kD, and kT are the rate constants for the reaction of protium, deuterium, and tritium derivatives, respectively. Significant deviations from this relation have now been observed for both primary and especially secondary effects, such that experimental H/T ratios are much greater than those calculated from the above expression. These deviations also hold in the temperature range from 0 to 40 degrees Celsius. Such deviations were previously predicted to result from a reaction coordinate containing a significant contribution from hydrogen tunneling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cha, Y -- Murray, C J -- Klinman, J P -- New York, N.Y. -- Science. 1989 Mar 10;243(4896):1325-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2646716" target="_blank"〉PubMed〈/a〉
    Keywords: Alcohol Dehydrogenase/*metabolism ; Benzyl Alcohols ; *Hydrogen ; Kinetics ; Mathematics ; Models, Theoretical ; Oxidation-Reduction ; Saccharomyces cerevisiae/enzymology ; Thermodynamics ; Tritium
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  • 93
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    Mitogenesis in response to PDGF and bombesin abolished by microinjection of antibody to PIP2 (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-02-05
    Description: The turnover of phosphatidylinositol 4,5-bisphosphate (PIP2) is believed to constitute a crucial step in the signaling pathways for stimulation of cells by a variety of bioactive substances, including mitogens, but decisive evidence for the idea has not been obtained. In the present study, a monoclonal antibody to PIP2 was microinjected into the cytoplasm of NIH 3T3 cells before or after exposure to mitogens. The antibody completely abolished nuclear labeling with [3H]thymidine induced by platelet-derived growth factor and bombesin, but not by fibroblast growth factor, epidermal growth factor, insulin, or serum. The findings strongly suggest that PIP2 breakdown is crucial in the elicitation and sustaining of cell proliferation induced by some types of mitogens such as platelet-derived growth factor and bombesin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Matuoka, K -- Fukami, K -- Nakanishi, O -- Kawai, S -- Takenawa, T -- New York, N.Y. -- Science. 1988 Feb 5;239(4840):640-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, Tokyo Metropolitan Institute of Gerontology, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2829356" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antibodies, Monoclonal ; Antigen-Antibody Complex ; Bombesin/*pharmacology ; Cell Division/*drug effects ; Cells, Cultured ; Insulin/pharmacology ; Kinetics ; Mice ; Mice, Inbred Strains ; Phosphatidylinositol 4,5-Diphosphate ; Phosphatidylinositols/immunology/*physiology ; Platelet-Derived Growth Factor/*pharmacology
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  • 94
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    Modulation of folding pathways of exported proteins by the leader sequence (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-02-26
    Description: Leader peptides that function to direct export of proteins through membranes have some common features but exhibit a remarkable sequence diversity. Thus there is some question whether leader peptides exert their function through conventional stereospecific protein-protein interaction. Here it is shown that the leader peptides retarded the folding of precursor maltose-binding protein and ribose-binding protein from Escherichia coli. This kinetic effect may be crucial in allowing precursors to enter the export pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Park, S -- Liu, G -- Topping, T B -- Cover, W H -- Randall, L L -- GM29798/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Feb 26;239(4843):1033-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biochemistry/Biophysics Program, Washington State University, Pullman 99164.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3278378" target="_blank"〉PubMed〈/a〉
    Keywords: *ATP-Binding Cassette Transporters ; Bacterial Proteins/*metabolism ; Biological Transport ; Carrier Proteins/metabolism ; Endopeptidase K ; Escherichia coli/*metabolism ; *Escherichia coli Proteins ; Guanidine ; Guanidines/pharmacology ; Kinetics ; Maltose-Binding Proteins ; *Monosaccharide Transport Proteins ; Peptide Hydrolases ; *Periplasmic Binding Proteins ; *Protein Conformation/drug effects ; Protein Denaturation ; Protein Precursors/*metabolism ; Protein Sorting Signals/pharmacology/*physiology ; Serine Endopeptidases/pharmacology ; Spectrometry, Fluorescence
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  • 95
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    2,3,7,8-Tetrachlorodibenzo-p-dioxin kills immature thymocytes by Ca2+-mediated endonuclease activation (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-10-14
    Description: Suspensions of thymocytes from young rats were incubated with 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD), which resulted in a sustained increase in cytosolic free Ca2+ concentration followed by DNA fragmentation and loss of cell viability. Both the Ca2+ increase and DNA fragmentation were prevented in cells treated with the inhibitor of protein synthesis, cycloheximide, and DNA fragmentation and cell killing were not detected when cells were incubated in a "Ca2+-free" medium or pretreated with high concentrations of the calcium probe, quin-2 tetraacetoxymethyl ester. These results indicate that TCDD can kill immature thymocytes by initiating a suicide process similar to that previously described for glucocorticoid hormones.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉McConkey, D J -- Hartzell, P -- Duddy, S K -- Hakansson, H -- Orrenius, S -- New York, N.Y. -- Science. 1988 Oct 14;242(4876):256-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Toxicology, Karolinska Institutet, Stockholm, Sweden.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3262923" target="_blank"〉PubMed〈/a〉
    Keywords: Aminoquinolines ; Animals ; Calcium/metabolism/*pharmacology ; Cell Survival/drug effects ; Cycloheximide/pharmacology ; Cytosol/metabolism ; DNA/metabolism ; Deoxyribonuclease I/*metabolism ; Dioxins/*pharmacology ; Enzyme Activation/drug effects ; Fluorescent Dyes ; Glucocorticoids/pharmacology ; Kinetics ; Rats ; T-Lymphocytes/drug effects ; Tetrachlorodibenzodioxin/*pharmacology ; Thymus Gland/*drug effects/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 96
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    Highly cooperative opening of calcium channels by inositol 1,4,5-trisphosphate (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-04-29
    Description: The kinetics of calcium release by inositol 1,4,5-trisphosphate (IP3) in permeabilized rat basophilic leukemia cells were studied to obtain insight into the molecular mechanism of action of this intracellular messenger of the phosphoinositide cascade. Calcium release from intracellular storage sites was monitored with fura-2, a fluorescent indicator. The dependence of the rate of calcium release on the concentration of added IP3 in the 4 to 40 nM range showed that channel opening requires the binding of at least three molecules of IP3. Channel opening occurred in the absence of added adenosine triphosphate, indicating that IP3 acts directly on the channel or on a protein that gates it. The channels were opened by IP3 in less than 4 seconds. The highly cooperative opening of calcium channels by nanomolar concentrations of IP3 enables cells to detect and amplify very small changes in the concentration of this messenger in response to hormonal, sensory, and growth control stimuli.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meyer, T -- Holowka, D -- Stryer, L -- AI22449/AI/NIAID NIH HHS/ -- GM24032/GM/NIGMS NIH HHS/ -- GM30387/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Apr 29;240(4852):653-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Sherman Fairchild Center, Stanford University School of Medicine, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2452482" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Basophils ; Benzofurans ; Calcimycin/pharmacology ; Calcium/*metabolism ; Cell Membrane Permeability ; Cytoplasm/metabolism ; Fluorescent Dyes ; Fura-2 ; Inositol 1,4,5-Trisphosphate ; Inositol Phosphates/metabolism/*pharmacology ; Ion Channels/drug effects/*metabolism ; Kinetics ; Leukemia, Experimental/metabolism ; Rats ; Spectrometry, Fluorescence ; Sugar Phosphates/*pharmacology ; Tumor Cells, Cultured
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 97
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    Kaposi's sarcoma cells: long-term culture with growth factor from retrovirus-infected CD4+ T cells (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-10-21
    Description: Studies of the biology and pathogenesis of Kaposi's sarcoma (KS) have been hampered by the inability to maintain long-term cultures of KS cells in vitro. In this study AIDS-KS-derived cells with characteristic spindle-like morphology were cultured with a growth factor (or factors) released by CD4+ T lymphocytes infected with human T-lymphotropic virus type I or II (HTLV-I or HTLV-II) or with human immunodeficiency virus type 1 or 2 (HIV-1 or HIV-2). Medium conditioned by HTLV-II-infected, transformed lines of T cells (HTLV-II CM) contained large amounts of this growth activity and also supported the temporary growth of normal vascular endothelial cells, but not fibroblasts. Interleukin-1 and tumor necrosis factor-alpha stimulated the growth of the KS-derived cells, but the growth was only transient and these could be distinguished from that in HTLV-II CM. Other known endothelial cell growth promoting factors, such as acidic and basic fibroblast growth factors and epidermal growth factor, did not support the long-term growth of the AIDS-KS cells. The factor released by CD4+ T cells infected with human retroviruses should prove useful in studies of the pathogenesis of KS.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nakamura, S -- Salahuddin, S Z -- Biberfeld, P -- Ensoli, B -- Markham, P D -- Wong-Staal, F -- Gallo, R C -- New York, N.Y. -- Science. 1988 Oct 21;242(4877):426-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Tumor Cell Biology, National Cancer Institute, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3262925" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/immunology/*pathology ; Antigens, Differentiation, T-Lymphocyte/analysis ; Cell Division ; *Cell Transformation, Viral ; Growth Substances/*isolation & purification/physiology ; Human T-lymphotropic virus 1/*genetics ; Human T-lymphotropic virus 2/*genetics ; Humans ; Kinetics ; Sarcoma, Kaposi/*pathology ; T-Lymphocytes/*immunology ; Tumor Cells, Cultured
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 98
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    Ovothiol replaces glutathione peroxidase as a hydrogen peroxide scavenger in sea urchin eggs (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-11-11
    Description: Despite its potential toxicity, H2O2 is used as an extracellular oxidant by Stronglylocentrotus purpuratus eggs to cross-link their fertilization envelopes. These eggs contain 5 mM 1-methyl-N alpha,N alpha-dimethyl-4-mercaptohistidine (ovothiol C), which reacts with H2O2. In consuming H2O2 and being reduced by glutathione, ovothiol acts as a glutathione peroxidase and replaces the function of the enzyme in eggs. The ovothiol system is more effective than egg catalase in destroying H2O2 at concentrations produced during fertilization and constitutes a principal mechanism for preventing oxidative damage at fertilization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Turner, E -- Hager, L J -- Shapiro, B M -- GM23910/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Nov 11;242(4880):939-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Washington, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3187533" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acids, Sulfur/*metabolism ; Animals ; Catalase/metabolism ; Disulfides/metabolism ; Female ; Fertilization ; Glutathione/metabolism ; Glutathione Peroxidase/*metabolism ; Kinetics ; *Methylhistidines ; NADP/metabolism ; Ovum/*metabolism ; Oxidation-Reduction ; Sea Urchins
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 99
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    A specific, highly active malate dehydrogenase by redesign of a lactate dehydrogenase framework (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-12-16
    Description: Three variations to the structure of the nicotinamide adenine dinucleotide (NAD)-dependent L-lactate dehydrogenase from Bacillus stearothermophilus were made to try to change the substrate specificity from lactate to malate: Asp197----Asn, Thr246----Gly, and Gln102----Arg). Each modification shifts the specificity from lactate to malate, although only the last (Gln102----Arg) provides an effective and highly specific catalyst for the new substrate. This synthetic enzyme has a ratio of catalytic rate (kcat) to Michaelis constant (Km) for oxaloacetate of 4.2 x 10(6)M-1 s-1, equal to that of native lactate dehydrogenase for its natural substrate, pyruvate, and a maximum velocity (250 s-1), which is double that reported for a natural malate dehydrogenase from B. stearothermophilus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilks, H M -- Hart, K W -- Feeney, R -- Dunn, C R -- Muirhead, H -- Chia, W N -- Barstow, D A -- Atkinson, T -- Clarke, A R -- Holbrook, J J -- New York, N.Y. -- Science. 1988 Dec 16;242(4885):1541-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Bristol, United Kingdom.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3201242" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Geobacillus stearothermophilus/*enzymology/genetics ; Kinetics ; L-Lactate Dehydrogenase/*genetics/metabolism ; Malate Dehydrogenase/*metabolism ; Models, Molecular ; Protein Conformation ; Substrate Specificity
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 100
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    Putative melatonin receptors in a human biological clock (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-10-07
    Description: In vitro autoradiography with 125I-labeled melatonin was used to examine melatonin binding sites in human hypothalamus. Specific 125I-labeled melatonin binding was localized to the suprachiasmatic nuclei, the site of a putative biological clock, and was not apparent in other hypothalamic regions. Specific 125I-labeled melatonin binding was consistently found in the suprachiasmatic nuclei of hypothalami from adults and fetuses. Densitometric analysis of competition experiments with varying concentrations of melatonin showed monophasic competition curves, with comparable half-maximal inhibition values for the suprachiasmatic nuclei of adults (150 picomolar) and fetuses (110 picomolar). Micromolar concentrations of the melatonin agonist 6-chloromelatonin completely inhibited specific 125I-labeled melatonin binding, whereas the same concentrations of serotonin and norepinephrine caused only a partial reduction in specific binding. The results suggest that putative melatonin receptors are located in a human biological clock.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reppert, S M -- Weaver, D R -- Rivkees, S A -- Stopa, E G -- HD06976/HD/NICHD NIH HHS/ -- HD14427/HD/NICHD NIH HHS/ -- U10-HD22297/HD/NICHD NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1988 Oct 7;242(4875):78-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Developmental Chronobiology, Boston.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2845576" target="_blank"〉PubMed〈/a〉
    Keywords: Autoradiography ; Binding, Competitive ; *Biological Clocks ; Humans ; Hypothalamus/*metabolism ; Iodine Radioisotopes ; Kinetics ; Melatonin/*metabolism ; Optic Chiasm/metabolism ; Receptors, Melatonin ; Receptors, Neurotransmitter/*physiology ; Suprachiasmatic Nucleus/metabolism ; Supraoptic Nucleus/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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