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  • Kinetics  (49)
  • Protein Conformation  (37)
  • American Association for the Advancement of Science (AAAS)  (83)
  • American Meteorological Society
  • Elsevier
  • 1985-1989  (83)
  • 1988  (83)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (83)
  • American Meteorological Society
  • Elsevier
  • Springer  (4)
Years
  • 1985-1989  (83)
Year
  • 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
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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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    Zinc-dependent structure of a single-finger domain of yeast ADR1 (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-09-16
    Description: In the proposed "zinc finger" DNA-binding motif, each repeat unit binds a zinc metal ion through invariant Cys and His residues and this drives the folding of each 30-residue unit into an independent nucleic acid-binding domain. To obtain structural information, we synthesized single and double zinc finger peptides from the yeast transcription activator ADR1, and assessed the metal-binding and DNA-binding properties of these peptides, as well as the solution structure of the metal-stabilized domains, with the use of a variety of spectroscopic techniques. A single zinc finger can exist as an independent structure sufficient for zinc-dependent DNA binding. An experimentally determined model of the single finger is proposed that is consistent with circular dichroism, one- and two-dimensional nuclear magnetic resonance, and visual spectroscopy of the single-finger peptide reconstituted in the presence of zinc.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Parraga, G -- Horvath, S J -- Eisen, A -- Taylor, W E -- Hood, L -- Young, E T -- Klevit, R E -- New York, N.Y. -- Science. 1988 Sep 16;241(4872):1489-92.〈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/3047872" target="_blank"〉PubMed〈/a〉
    Keywords: Circular Dichroism ; DNA Mutational Analysis ; *DNA-Binding Proteins ; Magnetic Resonance Spectroscopy ; Metalloproteins ; Protein Conformation ; Saccharomyces cerevisiae ; Structure-Activity Relationship ; *Transcription Factors ; Zinc/*physiology
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  • 6
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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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  • 7
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    Combinatorial cassette mutagenesis as a probe of the informational content of protein sequences (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-07-01
    Description: A method of combinatorial cassette mutagenesis was designed to readily determine the informational content of individual residues in protein sequences. The technique consists of simultaneously randomizing two or three positions by oligonucleotide cassette mutagenesis, selecting for functional protein, and then sequencing to determine the spectrum of allowable substitutions at each position. Repeated application of this method to the dimer interface of the DNA-binding domain of lambda repressor reveals that the number and type of substitutions allowed at each position are extremely variable. At some positions only one or two residues are functionally acceptable; at other positions a wide range of residues and residue types are tolerated. The number of substitutions allowed at each position roughly correlates with the solvent accessibility of the wild-type side chain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reidhaar-Olson, J F -- Sauer, R T -- AI-15706/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1988 Jul 1;241(4861):53-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3388019" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Codon ; DNA/genetics/metabolism ; *DNA-Binding Proteins ; Macromolecular Substances ; Molecular Sequence Data ; Mutation ; Plasmids ; Protein Conformation ; Repressor Proteins/*genetics ; Structure-Activity Relationship ; Transcription Factors/*genetics ; Viral Proteins ; Viral Regulatory and Accessory Proteins
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  • 8
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    Three-dimensional solution structure of plastocyanin from the green alga Scenedesmus obliquus (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-04-15
    Description: The solution conformation of plastocyanin from the green alga Scenedesmus obliquus has been determined from distance and dihedral angle constraints derived by nuclear magnetic resonance (NMR) spectroscopy. Structures were generated with distance geometry and restrained molecular dynamics calculations. A novel molecular replacement method was also used with the same NMR constraints to generate solution structures of S. obliquus plastocyanin from the x-ray structure of the homologous poplar protein. Scenedesmus obliquus plastocyanin in solution adopts a beta-barrel structure. The backbone conformation is well defined and is similar overall to that of poplar plastocyanin in the crystalline state. The distinctive acidic region of the higher plant plastocyanins, which functions as a binding site for electron transfer proteins and inorganic complexes, differs in both shape and charge in S. obliquus plastocyanin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moore, J M -- Case, D A -- Chazin, W J -- Gippert, G P -- Havel, T F -- Powls, R -- Wright, P E -- GM36643/GM/NIGMS NIH HHS/ -- GM38221/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Apr 15;240(4850):314-7.〈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/3353725" target="_blank"〉PubMed〈/a〉
    Keywords: Calorimetry ; Chlorophyta/*metabolism ; Magnetic Resonance Spectroscopy/methods ; Models, Molecular ; *Plant Proteins ; *Plastocyanin ; Protein Conformation
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  • 9
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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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  • 10
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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
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  • 11
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    Sugar and signal-transducer binding sites of the Escherichia coli galactose chemoreceptor protein (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-12-02
    Description: D-galactose-binding (or chemoreceptor) protein of Escherichia coli serves as an initial component for both chemotaxis towards galactose and glucose and high-affinity active transport of the two sugars. Well-refined x-ray structures of the liganded forms of the wild-type and a mutant protein isolated from a strain defective in chemotaxis but fully competent in transport have provided a molecular view of the sugar-binding site and of a site for interacting with the Trg transmembrane signal transducer. The geometry of the sugar-binding site, located in the cleft between the two lobes of the bilobate protein, is novel in that it is designed for tight binding and sequestering of either the alpha or beta anomer of the D-stereoisomer of the 4-epimers galactose and glucose. Binding specificity and affinity are conferred primarily by polar planar side-chain residues that form intricate networks of cooperative and bidentate hydrogen bonds with the sugar substrates, and secondarily by aromatic residues that sandwich the pyranose ring. Each of the pairs of anomeric hydroxyls and epimeric hydroxyls is recognized by a distinct Asp residue. The site for interaction with the transducer is about 18 A from the sugar-binding site. Mutation of Gly74 to Asp at this site, concomitant with considerable changes in the local ordered water structures, contributes to the lack of productive interaction with the transmembrane signal transducer.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vyas, N K -- Vyas, M N -- Quiocho, F A -- New York, N.Y. -- Science. 1988 Dec 2;242(4883):1290-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Baylor College of Medicine, Houston, TX 77030.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3057628" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*ultrastructure ; Binding Sites ; *Calcium-Binding Proteins ; Carrier Proteins/*ultrastructure ; *Chemotaxis ; Computer Simulation ; DNA Mutational Analysis ; Escherichia coli ; Galactose/metabolism ; Glucose/metabolism ; Hydrogen Bonding ; Models, Molecular ; *Monosaccharide Transport Proteins ; *Periplasmic Binding Proteins ; Protein Conformation ; Structure-Activity Relationship ; X-Ray Diffraction
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  • 12
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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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  • 13
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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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  • 14
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    The gramicidin pore: crystal structure of a cesium complex (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-07-08
    Description: Gramicidin, a linear polypeptide composed of hydrophobic amino acids with alternating L- and D- configurations, forms transmembrane ion channels. The crystal structure of a gramicidin-cesium complex has been determined at 2.0 angstrom resolution. In this structure, gramicidin forms a 26 angstrom long tube comprised of two polypeptide chains arranged as antiparallel beta strands that are wrapped into a left-handed helical coil with 6.4 residues per turn. The polypeptide backbone forms the interior of the hydrophilic, solvent-filled pore and the side chains form a hydrophobic and relatively regular surface on the outside of the pore. This example of a crystal structure of a solvent-filled ion pore provides a basis for understanding the physical nature of ion translocation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wallace, B A -- Ravikumar, K -- New York, N.Y. -- Science. 1988 Jul 8;241(4862):182-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Center for Biophysics, Rensselaer Polytechnic Institute, Troy, NY 12180.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2455344" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Cesium ; Computer Simulation ; Crystallography ; *Gramicidin ; *Ion Channels ; Ligands ; Macromolecular Substances ; *Membrane Proteins ; Models, Molecular ; Protein Conformation
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  • 15
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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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  • 16
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    DNA binding by proteins (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-09-02
    Description: Study of proteins that recognize specific DNA sequences has yielded much information, but the field is still in its infancy. Already two major structural motifs have been discovered, the helix-turn-helix and zinc finger, and numerous examples of DNA-binding proteins containing either of them are known. The restriction enzyme Eco RI uses yet a different motif. Additional motifs are likely to be found as well. There is a growing understanding of some of the physical chemistry involved in protein-DNA binding, but much remains to be learned before it becomes possible to engineer a protein that binds to a specific DNA sequence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schleif, R -- New York, N.Y. -- Science. 1988 Sep 2;241(4870):1182-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Graduate Department of Biochemistry, Brandeis University, Waltham, MA 02254.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2842864" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acids/metabolism ; Binding Sites ; Chemical Phenomena ; Chemistry ; DNA/metabolism ; DNA Restriction Enzymes/metabolism ; DNA-Binding Proteins/*metabolism ; Deoxyribonuclease EcoRI ; Electrochemistry ; Nucleic Acids/metabolism ; Protein Conformation ; Zinc
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  • 17
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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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  • 18
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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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  • 19
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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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  • 20
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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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  • 21
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    What T cells see and how they see it (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-11-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1988 Nov 11;242(4880):863-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2460921" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/prevention & control ; Amino Acid Sequence ; Antigens/*immunology ; Epitopes/immunology ; Major Histocompatibility Complex ; Protein Conformation ; T-Lymphocytes/*immunology ; Viral Vaccines
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  • 22
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    First portrait of an oncogene product (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-02-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1988 Feb 19;239(4842):863.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3124269" target="_blank"〉PubMed〈/a〉
    Keywords: GTP-Binding Proteins/metabolism ; Guanosine Triphosphate/metabolism ; Humans ; Neoplasms/genetics ; Protein Conformation ; *Proto-Oncogene Proteins/genetics/metabolism ; Proto-Oncogene Proteins p21(ras)
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  • 23
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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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  • 24
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    Modulation of folding pathways of exported proteins by the leader sequence (1988)
    American Association for the Advancement of Science (AAAS)
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    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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  • 25
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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)
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    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
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  • 26
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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
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  • 27
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    A chemically synthesized Antennapedia homeo domain binds to a specific DNA sequence (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-11-11
    Description: A peptide 60 residues in length that corresponds to the homeo domain of Antennapedia (Antp), a protein governing development in Drosophila, was synthesized by segment condensation with protected peptide segments prepared on an oxime resin. A footprinting assay showed that the homeo domain binds specifically to a TAA repeat DNA sequence in the Antp gene. Thus the Antp homeo domain has a sequence-specific DNA binding property. The circular dichroism spectra of the homeo domain peptide showed the presence of a significant amount of alpha-helical structure in aqueous solution and in 50 percent trifluoroethanol. The alpha helicity measured in water appears to depend on the peptide concentration, which suggests that the peptide aggregates. These results support the hypothesis that the homeo domain binds to DNA through a helix-turn-helix motif.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mihara, H -- Kaiser, E T -- RR 862/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1988 Nov 11;242(4880):925-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Bioorganic Chemistry and Biochemistry, Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2903553" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Chromatography, High Pressure Liquid ; Circular Dichroism ; DNA/*metabolism ; Drosophila/*growth & development ; Electrophoresis, Polyacrylamide Gel ; *Genes, Homeobox ; Insect Hormones/*chemical synthesis/genetics/metabolism ; Molecular Sequence Data ; Peptide Fragments/*chemical synthesis/genetics ; Protein Conformation ; Repetitive Sequences, Nucleic Acid
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    Probing the mechanisms of macromolecular recognition: the cytochrome b5-cytochrome c complex (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-06-17
    Description: The specificity of complex formation between cytochrome b5 (cyt b5) and cytochrome c (cyt c) is believed to involve the formation of salt linkages between specific carboxylic acid residues of cyt b5 with lysine residues on cyt c. Site-directed mutagenesis was used to alter the specified acidic residues of cyt b5 to the corresponding amide analogues, which resulted in a lower affinity for complex formation with cyt c. The dissociation of the complex under high pressure resulted in specific volume changes, the magnitude of which reflected the degree of solvation of the acidic residues in the proposed protein-protein interface.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rodgers, K K -- Pochapsky, T C -- Sligar, S G -- GM 31756/GM/NIGMS NIH HHS/ -- GM 33775/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Jun 17;240(4859):1657-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Illinois, Urbana 61801.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2837825" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cytochrome b Group/genetics/*metabolism ; Cytochrome c Group/*metabolism ; Cytochromes b5 ; Hydrogen Bonding ; Hydrogen-Ion Concentration ; Hydrostatic Pressure ; Macromolecular Substances ; Mutation ; Protein Conformation ; Rats ; Solubility ; Thermodynamics
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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
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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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    A specific, highly active malate dehydrogenase by redesign of a lactate dehydrogenase framework (1988)
    American Association for the Advancement of Science (AAAS)
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    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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    Putative melatonin receptors in a human biological clock (1988)
    American Association for the Advancement of Science (AAAS)
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    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
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    Three-dimensional structure of cholera toxin penetrating a lipid membrane (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-03-11
    Description: Two-dimensional crystals of cholera toxin bound to receptors in a lipid membrane give diffraction extending to 15 A resolution. Three-dimensional structure determination reveals a ring of five B subunits on the membrane surface, with one-third of the A subunit occupying the center of the ring. The remaining mass of the A subunit appears to penetrate the hydrophobic interior of the membrane. Cleavage of a disulfide bond in the A subunit, which activates the toxin, causes a major conformational change, with the A subunit mostly exiting from the B ring.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ribi, H O -- Ludwig, D S -- Mercer, K L -- Schoolnik, G K -- Kornberg, R D -- AI21144/AI/NIAID NIH HHS/ -- GM07276-12/GM/NIGMS NIH HHS/ -- GM07365/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1988 Mar 11;239(4845):1272-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Howard Hughes Medical Institute, Stanford University School of Medicine, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3344432" target="_blank"〉PubMed〈/a〉
    Keywords: *Cholera Toxin ; G(M1) Ganglioside ; *Liposomes ; Macromolecular Substances ; Microscopy, Electron ; Models, Molecular ; Phosphatidylethanolamines ; Protein Conformation
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    Inactivation and block of calcium channels by photo-released Ca2+ in dorsal root ganglion neurons (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-08-12
    Description: Calcium channels are inactivated by voltage and intracellular calcium. To study the kinetics and the mechanism of calcium-induced inactivation of calcium channels, a "caged" calcium compound, dimethoxy-nitrophen was used to photo-release about 50 microM calcium ion within 0.2 millisecond in dorsal root ganglion neurons. When divalent cations were the charge carriers, intracellular photo-release of calcium inactivated the calcium channel with an invariant rate [time constant (tau) approximately equal to 7 milliseconds]. When the monovalent cation sodium was the charge carrier, photorelease of calcium inside or outside of the cell blocked the channel rapidly (tau approximately equal to 0.4 millisecond), but the block was greater from the external side. Thus the kinetics of calcium-induced calcium channel inactivation depends on the valency of the permeant cation. The data imply that calcium channels exist in either of two conformational states, the calcium- and sodium-permeant forms, or, alternatively, calcium-induced inactivation occurs at a site closely associated with the internal permeating site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Morad, M -- Davies, N W -- Kaplan, J H -- Lux, H D -- R01 HL-16152/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1988 Aug 12;241(4867):842-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of Pennsylvania, Department of Physiology, Philadelphia 19104-6085.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2457253" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/*physiology/radiation effects ; Cells, Cultured ; Chickens ; Ganglia, Spinal/*physiology/radiation effects ; Ion Channels/*physiology ; Kinetics ; Neurons/*physiology/radiation effects ; Photolysis ; Sodium/metabolism ; *Ultraviolet Rays
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    Coding of two sphingolipid activator proteins (SAP-1 and SAP-2) by same genetic locus (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-08-26
    Description: Several complementary DNAs (cDNAs) coding for sphingolipid activator protein-2 (SAP-2) were isolated from a lambda gt-11 human hepatoma library by means of polyclonal antibodies. The nucleotide sequence of the largest cDNA was colinear with the derived amino acid sequence of SAP-2 and with the nucleotide sequence of the cDNA coding for the 70-kilodalton precursor of SAP-1 (SAP precursor cDNA). The coding sequence for mature SAP-2 was located 3' to that coding for SAP-1 in the SAP precursor cDNA. Both SAP-1 and SAP-2 appeared to be derived by proteolytic processing from a common precursor that is coded by a genetic locus on human chromosome 10. Two other domains similar to SAP-1 and SAP-2 were also identified in SAP precursor protein. Each of the four domains was approximately 80 amino acid residues long, had nearly identical placement of cysteine residues, potential glycosylation sites, and proline residues. Each domain also contained internal amino acid sequences capable of forming amphipathic helices separated by helix breakers to give a cylindrical hydrophobic domain that is probably stabilized by disulfide bridges. Protein immunoblotting experiments indicated that SAP precursor protein (70 kilodaltons) as well as immunoreactive SAP-like proteins of intermediate sizes (65, 50, and 31 kilodaltons) are present in most human tissues.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Brien, J S -- Kretz, K A -- Dewji, N -- Wenger, D A -- Esch, F -- Fluharty, A L -- DK 38795/DK/NIDDK NIH HHS/ -- HD 18983/HD/NICHD NIH HHS/ -- NS 08682/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1988 Aug 26;241(4869):1098-101.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurosciences, University of California, San Diego, La Jolla 92093.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2842863" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Carcinoma, Hepatocellular/analysis ; Chromosome Mapping ; Chromosomes, Human, Pair 10 ; DNA/genetics/isolation & purification ; Glycoproteins/analysis/*genetics ; Humans ; Liver Neoplasms/analysis ; Male ; Mice ; Mice, Nude ; Molecular Sequence Data ; Nucleic Acid Hybridization ; Protein Conformation ; Protein Precursors/analysis/genetics ; Protein Processing, Post-Translational ; Rats ; Saposins ; Sphingolipid Activator Proteins ; Tissue Distribution
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    Induction of manganous superoxide dismutase by tumor necrosis factor: possible protective mechanism (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-11-11
    Description: Manganous superoxide dismutase (MnSOD) scavenges potentially toxic superoxide radicals produced in the mitochondria. Tumor necrosis factor-alpha (TNF-alpha) was found to induce the messenger RNA for MnSOD, but not the mRNAs for other antioxidant or mitochondrial enzymes tested. The increase in MnSOD mRNA occurred rapidly and was blocked by actinomycin D, but not by cycloheximide. Induction of MnSOD mRNA was also observed with TNF-beta, interleukin-1 alpha (IL-1 alpha), and IL-1 beta but not with other cytokines or agents tested. TNF-alpha induced MnSOD mRNA in all cell lines and normal cells examined in vitro and in various organs of mice in vivo. These effects of TNF-alpha and IL-1 on target cells may contribute to their reported protective activity against radiation as well as their ability to induce resistance to cell killing induced by the combination of TNF-alpha and cycloheximide.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wong, G H -- Goeddel, D V -- New York, N.Y. -- Science. 1988 Nov 11;242(4880):941-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Genentech, San Francisco, CA 94080.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3263703" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Catalase/metabolism ; Cell Line ; Cycloheximide/pharmacology ; Dactinomycin/pharmacology ; Enzyme Induction/drug effects ; Humans ; Interleukin-1/pharmacology ; Kinetics ; Mice ; Mitochondria/enzymology ; RNA, Messenger/biosynthesis ; Rats ; Superoxide Dismutase/*biosynthesis/genetics/metabolism ; Tissue Distribution ; Tumor Necrosis Factor-alpha/*pharmacology
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  • 37
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    Replacements of Pro86 in phage T4 lysozyme extend an alpha-helix but do not alter protein stability (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-02-05
    Description: To investigate the relation between protein stability and the predicted stabilities of individual secondary structural elements, residue Pro86 in an alpha-helix in phage T4 lysozyme was replaced by ten different amino acids. The x-ray crystal structures of seven of the mutant lysozymes were determined at high resolution. In each case, replacement of the proline resulted in the formation of an extended alpha-helix. This involves a large conformational change in residues 81 to 83 and smaller shifts that extend 20 angstroms across the protein surface. Unexpectedly, all ten amino acid substitutions marginally reduce protein thermostability. This insensitivity of stability to the amino acid at position 86 is not simply explained by statistical and thermodynamic criteria for helical propensity. The observed conformational changes illustrate a general mechanism by which proteins can tolerate mutations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Alber, T -- Bell, J A -- Sun, D P -- Nicholson, H -- Wozniak, J A -- Cook, S -- Matthews, B W -- GM 20066/GM/NIGMS NIH HHS/ -- GM 21967/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Feb 5;239(4840):631-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics, University of Oregon, Eugene 97403.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3277275" target="_blank"〉PubMed〈/a〉
    Keywords: Enzyme Stability ; Escherichia coli/enzymology ; Models, Molecular ; Muramidase/*genetics/metabolism ; Mutation ; *Proline ; Protein Conformation ; T-Phages/*enzymology/genetics ; X-Ray Diffraction
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    Insights into enzyme function from studies on mutants of dihydrofolate reductase (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-03-04
    Description: Kinetic analysis and protein mutagenesis allow the importance of individual amino acids in ligand binding and catalysis to be assessed. A kinetic analysis has shown that the reaction catalyzed by dihydrofolate reductase is optimized with respect to product flux, which in turn is predetermined by the active-site hydrophobic surface. Protein mutagenesis has revealed that specific hydrophobic residues contribute 2 to 5 kilocalories per mole to ligand binding and catalysis. The extent to which perturbations within this active-site ensemble may affect catalysis is discussed in terms of the constraints imposed by the energy surface for the reaction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Benkovic, S J -- Fierke, C A -- Naylor, A M -- GM24129/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Mar 4;239(4844):1105-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Pennsylvania State University, University Park 16802.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3125607" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Catalysis ; Chemical Phenomena ; Chemistry ; Escherichia coli/enzymology ; Kinetics ; Lactobacillus casei/enzymology ; *Mutation ; Structure-Activity Relationship ; Tetrahydrofolate Dehydrogenase/genetics/*metabolism ; Thermodynamics
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  • 39
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    Repair of the secretion defect in the Z form of alpha 1-antitrypsin by addition of a second mutation (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-12-23
    Description: Homozygous inheritance of the Z-type mutant form of the alpha 1-antitrypsin (alpha 1AT) gene results in the most common form of alpha 1AT deficiency, a human hereditary disease associated with a high risk for the development of emphysema and an increased incidence of neonatal hepatitis. The alpha 1AT-synthesizing cells of individuals with the Z gene have normal alpha 1AT messenger RNA levels, but alpha 1AT secretion is markedly reduced secondary to accumulation of newly synthesized alpha 1AT in the rough endoplasmic reticulum. Crystallographic analysis of alpha 1AT predicts that in normal alpha 1AT, a negatively charged Glu342 is adjacent to positively charged Lys290. Thus the Glu342----Lys342 Z mutation caused the loss of a normal salt bridge, resulting in the intracellular aggregation of the Z molecule. The prediction was made that a second mutation in the alpha 1AT genet that changed the positively charged Lys290 to a negatively charged Glu290 would correct the secretion defect. When the second mutation was added to the Z-type complementary DNA, the resulting gene directed the synthesis and secretion of amounts of alpha 1AT similar to that directed by the normal alpha 1AT complementary DNA in an in vitro eukaryotic expression system. This suggests the possibility that a human hereditary disease can be corrected by inserting an additional mutation in the same gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brantly, M -- Courtney, M -- Crystal, R G -- New York, N.Y. -- Science. 1988 Dec 23;242(4886):1700-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Pulmonary Branch, National Heart, Lung, and Blood Institute, Bethesda, MD.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2904702" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Codon ; DNA/genetics ; Electrochemistry ; Endoplasmic Reticulum/metabolism ; Glutamates ; Glutamic Acid ; Humans ; Lysine ; *Mutation ; Protein Conformation ; RNA, Messenger/metabolism ; Structure-Activity Relationship ; Transfection ; alpha 1-Antitrypsin/*genetics/secretion ; alpha 1-Antitrypsin Deficiency
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    Site of G protein binding to rhodopsin mapped with synthetic peptides from the alpha subunit (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-08-12
    Description: The interaction between receptors and guanine nucleotide binding (G) proteins leads to G protein activation and subsequent regulation of effector enzymes. The molecular basis of receptor-G protein interaction has been examined by using the ability of the G protein from rods (transducin) to cause a conformational change in rhodopsin as an assay. Synthetic peptides corresponding to two regions near the carboxyl terminus of the G protein alpha subunit, Glu311-Val328 and Ile340-Phe350, compete with G protein for interaction with rhodopsin. Amino acid substitution studies show that Cys321 is required for this effect. Ile340-Phe350 and a modified peptide, acetyl-Glu311-Lys329-amide, mimic G protein effects on rhodopsin conformation, showing that these peptides bind to and stabilize the activated conformation of rhodopsin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hamm, H E -- Deretic, D -- Arendt, A -- Hargrave, P A -- Koenig, B -- Hofmann, K P -- EY06062/EY/NEI NIH HHS/ -- EY06225/EY/NEI NIH HHS/ -- RP05369/PHS HHS/ -- etc. -- New York, N.Y. -- Science. 1988 Aug 12;241(4867):832-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Biophysics, University of Illinois College of Medicine, Chicago 60680.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3136547" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antibodies, Monoclonal ; Antigen-Antibody Complex ; Binding Sites ; GTP-Binding Proteins/*metabolism ; Kinetics ; Macromolecular Substances ; Membrane Proteins/*metabolism ; Peptides/metabolism ; Protein Binding ; Protein Conformation ; Retinal Pigments/*metabolism ; Rhodopsin/analogs & derivatives/*metabolism ; Transducin
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    Induction of an antibody that catalyzes the hydrolysis of an amide bond (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-09-02
    Description: Catalysis of amide bond hydrolysis is of singular importance in enzymology. An antibody was induced to an analog of a high-energy intermediate anticipated along the reaction coordinate of amide hydrolysis. This antibody is an amidase with high specificity and a large rate enhancement (250,000) relative to the uncatalyzed reaction. This reaction represents the kinetically most difficult hydrolysis reaction yet catalyzed by an antibody.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Janda, K D -- Schloeder, D -- Benkovic, S J -- Lerner, R A -- New York, N.Y. -- Science. 1988 Sep 2;241(4870):1188-91.〈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/3413482" target="_blank"〉PubMed〈/a〉
    Keywords: Amidohydrolases/metabolism ; Animals ; Antibodies, Monoclonal/biosynthesis/*physiology ; Antibody Specificity ; Antigens/immunology ; *Catalysis ; Chemical Phenomena ; Chemistry ; Hemocyanin/analogs & derivatives/immunology ; Hydrolysis ; Immunization ; Kinetics ; Mice ; Organophosphorus Compounds/immunology ; Substrate Specificity
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    Location and chemical synthesis of a binding site for HIV-1 on the CD4 protein (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-06-03
    Description: The human immunodeficiency virus type 1 (HIV-1) uses the CD4 protein as a receptor for infection of susceptible cells. A candidate structure for the HIV-1 binding site on the CD4 protein was identified by epitope mapping with a family of eight functionally distinct CD4-specific monoclonal antibodies in conjunction with a panel of large CD4-derived synthetic peptides. All of the seven epitopes that were located reside within two immunoglobulin-like disulfide loops situated between residues 1 and 168 of the CD4 protein. The CD4-specific monoclonal antibody OKT4A, a potent inhibitor of HIV-1 binding, recognized a site between residues 32 and 47 on the CD4 protein. By analogy to other members of the immunoglobulin superfamily of proteins, this particular region has been predicted to exist as a protruding loop. A synthetic analog of this loop (residues 25 to 58) showed a concentration-dependent inhibition of HIV-1-induced cell fusion. It is proposed that a loop extending from residues 37 to 53 of the CD4 protein is a binding site for the AIDS virus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jameson, B A -- Rao, P E -- Kong, L I -- Hahn, B H -- Shaw, G M -- Hood, L E -- Kent, S B -- AI25784/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1988 Jun 3;240(4857):1335-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, California Institute of Technology, Pasadena 91125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2453925" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Monoclonal/immunology ; Binding, Competitive ; Cell Fusion ; Disulfides/metabolism ; Epitopes/immunology ; Fluorescent Antibody Technique ; HIV/immunology/*metabolism ; HIV Envelope Protein gp120 ; Humans ; Immunoglobulins ; Peptide Fragments/chemical synthesis/immunology ; Protein Conformation ; Radioimmunoassay ; Receptors, HIV ; Receptors, Virus/*immunology ; Retroviridae Proteins/immunology ; T-Lymphocytes, Helper-Inducer/immunology/*microbiology
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    A chemoattractant receptor controls development in Dictyostelium discoideum (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-09-16
    Description: During the early stages of its developmental program, Dictyostelium discoideum expresses cell surface cyclic adenosine monophosphate (cyclic AMP) receptors. It has been suggested that these receptors coordinate the aggregation of individual cells into a multicellular organism and regulate the expression of a large number of developmentally regulated genes. The complementary DNA (cDNA) for the cyclic AMP receptor has now been cloned from lambda gt-11 libraries by screening with specific antiserum. The 2-kilobase messenger RNA (mRNA) that encodes the receptor is undetectable in growing cells, rises to a maximum at 3 to 4 hours of development, and then declines. In vitro transcribed complementary RNA, when hybridized to cellular mRNA, specifically arrests in vitro translation of the receptor polypeptide. When the cDNA is expressed in Dictyostelium cells, the undifferentiated cells specifically bind cyclic AMP. Cell lines transformed with a vector that expresses complementary mRNA (antisense) do not express the cyclic AMP receptor protein. These cells fail to enter the aggregation stage of development during starvation, whereas control and wild-type cells aggregate and complete the developmental program within 24 hours. The phenotype of the antisense transformants suggests that the cyclic AMP receptor is essential for development. The deduced amino acid sequence of the receptor reveals a high percentage of hydrophobic residues grouped in seven domains, similar to the rhodopsins and other receptors believed to interact with G proteins. It shares amino acid sequence identity and is immunologically cross-reactive with bovine rhodopsin. A model is proposed in which the cyclic AMP receptor crosses the bilayer seven times with a serine-rich cytoplasmic carboxyl terminus, the proposed site of ligand-induced receptor phosphorylation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Klein, P S -- Sun, T J -- Saxe, C L 3rd -- Kimmel, A R -- Johnson, R L -- Devreotes, P N -- GM 34933/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Sep 16;241(4872):1467-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, 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/3047871" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Cloning, Molecular ; Dictyostelium/*growth & development/physiology ; Membrane Proteins/physiology ; Molecular Sequence Data ; Protein Conformation ; Receptors, Cyclic AMP/*physiology ; Solubility
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    Requirement for glycine in activation of NMDA-receptors expressed in Xenopus oocytes (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-08-12
    Description: Receptors for N-methyl-D-aspartate (NMDA) are involved in many plastic and pathological processes in the brain. Glycine has been reported to potentiate NMDA responses in neurons and in Xenopus oocytes injected with rat brain messenger RNA. Glycine is now shown to be absolutely required for activation of NMDA receptors in oocytes. In voltage-clamped oocytes, neither perfusion nor rapid pressure application of NMDA onto messenger RNA-injected oocytes caused a distinct ionic current without added glycine. When glycine was added, however, NMDA evoked large inward currents. The concentration of glycine required to produce a half-maximal response was 670 nanomolar, and the glycine dose-response curve extrapolated to zero in the absence of glycine. Several analogs of glycine could substitute for glycine, among which D-serine and D-alanine were the most effective. The observation that D-amino acids are effective will be important in developing drugs targeted at the glycine site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kleckner, N W -- Dingledine, R -- NS17771/NS/NINDS NIH HHS/ -- NS22249/NS/NINDS NIH HHS/ -- NS23804/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1988 Aug 12;241(4867):835-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of North Carolina, Chapel Hill 27599-7365.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2841759" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acids/pharmacology ; Animals ; Brain/metabolism ; Female ; Glycine/*analogs & derivatives/*pharmacology ; Kinetics ; Oocytes/drug effects/*metabolism ; RNA, Messenger/genetics ; Rats ; Receptors, N-Methyl-D-Aspartate ; Receptors, Neurotransmitter/drug effects/genetics/*metabolism ; Xenopus
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    West African HIV-2-related human retrovirus with attenuated cytopathicity (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-06-10
    Description: Clinical and seroepidemiological studies in West Africa indicate that human immunodeficiency virus type 2 (HIV-2) is widespread and associated with immunodeficiency states of variable degree. In this study, an isolate of HIV-2 from a patient in Senegal was molecularly cloned and characterized. This isolate (HIV-2ST) was shown by hybridization and restriction enzyme analysis to be more related to the prototype HIV-2ROD than to other human or primate retroviruses. Cultures of HIV-2ST showed genotypic polymorphism, and clones of the virus had transmembrane envelope glycoproteins of 30 and 42 kilodaltons. Unlike other immunodeficiency viruses, HIV-2ST did not cause cell death or induce cell fusion in peripheral blood lymphocytes or in any of four CD4+ cell lines tested. Although HIV-2ST entered cells by a CD4-dependent mechanism and replicated actively, cell-free transmission of the virus was retarded at the level of cell entry. These findings suggest that immunodeficiency viruses prevalent in West African populations are members of the HIV-2 virus group and that certain strains of this virus have attenuated virulence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kong, L I -- Lee, S W -- Kappes, J C -- Parkin, J S -- Decker, D -- Hoxie, J A -- Hahn, B H -- Shaw, G M -- New York, N.Y. -- Science. 1988 Jun 10;240(4858):1525-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Internal Medicine, University of Alabama, Birmingham 35294.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3375832" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; Cell Survival ; DNA, Viral/genetics ; Genes, Viral ; HIV/classification/*isolation & purification/pathogenicity ; Humans ; Kinetics ; Lymphocytes/microbiology ; Senegal ; Species Specificity
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    The leucine zipper: a hypothetical structure common to a new class of DNA binding proteins (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-06-24
    Description: A 30-amino-acid segment of C/EBP, a newly discovered enhancer binding protein, shares notable sequence similarity with a segment of the cellular Myc transforming protein. Display of these respective amino acid sequences on an idealized alpha helix revealed a periodic repetition of leucine residues at every seventh position over a distance covering eight helical turns. The periodic array of at least four leucines was also noted in the sequences of the Fos and Jun transforming proteins, as well as that of the yeast gene regulatory protein, GCN4. The polypeptide segments containing these periodic arrays of leucine residues are proposed to exist in an alpha-helical conformation, and the leucine side chains extending from one alpha helix interdigitate with those displayed from a similar alpha helix of a second polypeptide, facilitating dimerization. This hypothetical structure is referred to as the "leucine zipper," and it may represent a characteristic property of a new category of DNA binding proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Landschulz, W H -- Johnson, P F -- McKnight, S L -- New York, N.Y. -- Science. 1988 Jun 24;240(4860):1759-64.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Embryology, Carnegie Institution of Washington, Baltimore, MD 21210.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3289117" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Computer Simulation ; *DNA-Binding Proteins ; *Enhancer Elements, Genetic ; *Leucine ; Models, Molecular ; Protein Conformation ; Proto-Oncogene Proteins ; Structure-Activity Relationship
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    Three-dimensional structure at 0.86 A of the uncomplexed form of the transmembrane ion channel peptide gramicidin A (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-07-08
    Description: The crystal structure of the uncomplexed orthorhombic form of gramicidin A has been determined at 120 K and at 0.86 angstrom resolution. The pentadecapeptide crystallizes as a left-handed antiparallel double-stranded helical dimer with 5.6 amino acid residues per turn. The helix has an overall length of 31 angstroms and an average inner channel diameter of 4.80 angstroms. The channel of this crystalline form is void of ions or solvent molecules. The channel diameter varies from a minimum of 3.85 angstroms to a maximum of 5.47 angstroms and contains three pockets where the cross-channel contacts are 5.25 angstroms or greater. The range of variation seen for the phi and psi torsion angles of the backbone of the helix suggests that these potential ion binding sites can be induced to travel the length of the channel in a peristaltic manner by cooperatively varying these angles. The indole rings of the eight tryptophan residues of the dimer are overlapped in three separate regions on the outer surface of the helix when viewed down the barrel of the channel. This arrangement would permit long-chained lipid molecules to nest parallel to the outer channel surface between these protruding tryptophan regions and act like molecular splines to constrain helical twist deformations of the channel.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Langs, D A -- GM32812/GM/NIGMS NIH HHS/ -- HL32303/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1988 Jul 8;241(4862):188-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Foundation of Buffalo, NY 14203.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2455345" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Crystallography ; *Gramicidin ; *Ion Channels ; *Membrane Proteins ; Models, Molecular ; Protein Conformation
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    The primary structure and heterogeneity of tau protein from mouse brain (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-01-15
    Description: Tau protein is a family of microtubule binding proteins, heterogeneous in molecular weight, that are induced during neurite outgrowth and are found prominently in neurofibrillary tangles in Alzheimer's disease. The predicted amino acid sequences of two forms of tau protein from mouse brain were determined from complementary DNA clones. These forms are identical in their amino-terminal sequences but differ in their carboxyl-terminal domains. Both proteins contain repeated sequences that may be tubulin binding sites. The sequence suggests that tau is an elongated molecule with no extensive alpha-helical or beta-sheet domains. These complementary DNAs should enable the study of various functional domains of tau and the study of tau expression in normal and pathological states.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, G -- Cowan, N -- Kirschner, M -- GM32099/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Jan 15;239(4837):285-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3122323" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; *Brain Chemistry ; Codon ; DNA/genetics ; DNA, Recombinant ; Mice ; Microtubule-Associated Proteins/*genetics ; Molecular Sequence Data ; Molecular Weight ; Nerve Tissue Proteins/genetics ; Protein Conformation ; RNA, Messenger/genetics ; Repetitive Sequences, Nucleic Acid ; tau Proteins
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    Evidence that the M2 membrane-spanning region lines the ion channel pore of the nicotinic receptor (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-12-16
    Description: Site-directed mutagenesis and expression in Xenopus oocytes were used to study acetylcholine receptors in which serine residues (i) were replaced by alanines (alpha, delta subunits) or (ii) replaced a phenylalanine (beta subunit) at a postulated polar site within the M2 transmembrane helix. As the number of serines decreased, there were decreases in the residence time and consequently the equilibrium binding affinity of QX-222, a quaternary ammonium anesthetic derivative thought to bind within the open channel. Receptors with three serine-to-alanine mutations also displayed a selective decrease in outward single-channel currents. Both the direction of this rectification and the voltage dependence of QX-222 blockade suggest that the residues mutated are within the aqueous pore of the receptor and near its cytoplasmic (inner) surface.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Leonard, R J -- Labarca, C G -- Charnet, P -- Davidson, N -- Lester, H A -- NS-11756/NS/NINDS NIH HHS/ -- NS-8083/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1988 Dec 16;242(4885):1578-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, California Institute of Technology, Pasadena 91125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2462281" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Membrane/*physiology ; Cloning, Molecular ; Electric Conductivity ; Female ; Ion Channels/*physiology ; Kinetics ; Membrane Potentials ; Mutation ; Oocytes/physiology ; RNA, Messenger/genetics ; Receptors, Nicotinic/genetics/*physiology ; Transcription, Genetic ; Xenopus
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    A mutation in the catalytic subunit of cAMP-dependent protein kinase that disrupts regulation (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-04-01
    Description: A mutant catalytic subunit of adenosine 3',5'-monophosphate (cAMP)-dependent protein kinase has been isolated from Saccharomyces cerevisiae that is no longer subject to regulation yet retains its catalytic activity. Biochemical analysis of the mutant subunit indicates a 100-fold decreased affinity for the regulatory subunit. The mutant catalytic subunit exhibits approximately a threefold increase in Michaelis constant for adenosine triphosphate and peptide cosubstrates, and is essentially unchanged in its catalytic rate. The nucleotide sequence of the mutant gene contains a single nucleotide change resulting in a threonine-to-alanine substitution at amino acid 241. This residue is conserved in other serine-threonine protein kinases. These results identify this threonine as an important contact between catalytic and regulatory subunits but only a minor contact in substrate recognition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Levin, L R -- Kuret, J -- Johnson, K E -- Powers, S -- Cameron, S -- Michaeli, T -- Wigler, M -- Zoller, M J -- GM33986/GM/NIGMS NIH HHS/ -- R35 CA39829-02/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1988 Apr 1;240(4848):68-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cold Spring Harbor Laboratory, NY 11724.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2832943" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Catalysis ; Cyclic AMP/*pharmacology ; Genes, Fungal ; Kinetics ; Macromolecular Substances ; Molecular Sequence Data ; Mutation ; Phosphorylation ; Protein Kinases/*genetics/metabolism ; Saccharomyces cerevisiae/enzymology/*genetics ; Structure-Activity Relationship ; Threonine
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    Effect of neuropeptides on production of inflammatory cytokines by human monocytes (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-09-02
    Description: Two groups of mediators, the neuropeptides substance P and K and the monocyte-derived cytokines, interact in the neural regulation of immunological and inflammatory responses. Substance P, substance K, and the carboxyl-terminal peptide SP(4-11) induce the release of interleukin-1, tumor necrosis factor-alpha, and interleukin-6 from human blood monocytes. The neuropeptide effects occur at low doses, are specific as shown by inhibition studies with a substance P antagonist, and require de novo protein synthesis. Since monocyte-derived cytokines regulate multiple cellular functions in inflammation and immunity and since neuropeptides can be released from peripheral nerve endings into surrounding tissues, these findings identify a potent mechanism for nervous system regulation of host defense responses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lotz, M -- Vaughan, J H -- Carson, D A -- AI10386/AI/NIAID NIH HHS/ -- AR21175/AR/NIAMS NIH HHS/ -- AR25443/AR/NIAMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1988 Sep 2;241(4870):1218-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Basic and Clinical Research, 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/2457950" target="_blank"〉PubMed〈/a〉
    Keywords: Cells, Cultured ; Humans ; Interleukin-1/biosynthesis ; Interleukin-6 ; Interleukins/*biosynthesis ; Kinetics ; Monocytes/drug effects/immunology/*metabolism ; Neurokinin A ; Neuropeptides/*pharmacology ; Protein Biosynthesis ; Substance P/pharmacology ; Tumor Necrosis Factor-alpha/*biosynthesis
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    Regulation of interprotein electron transfer by residue 82 of yeast cytochrome c (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-04-15
    Description: Yeast iso-1-cytochrome c (Cc) mutants have been constructed with Phe, Tyr, Gly, Ser, Leu, and Ile at position 82, each with Thr substituted for Cys at position 102. Their long-range electron transfer with zinc-substituted cytochrome c peroxidase (ZnCcP) has been studied by two kinetic techniques. The charge-separated complex, [(ZnCcP)+,FeIICc] converts to [ZnCcP,FeIIICc] by a single, intracomplex electron transfer step that is not governed by "gating" through possible rapid dissociation of the complex or isomerization (for example, heme-ligand) by FeIICc subsequent to its formation from FeIIICc. In every variant with an aliphatic residue at position 82 of Cc, the rate of this electron transfer process is approximately 10(4) slower at approximately 0 degrees C than for the two variants with aromatic residues.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Liang, N -- Mauk, A G -- Pielak, G J -- Johnson, J A -- Smith, M -- Hoffman, B M -- GM-33804/GM/NIGMS NIH HHS/ -- HL-13531/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1988 Apr 15;240(4850):311-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Northwestern University, Evanston, IL 60208.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2832950" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acids ; Cytochrome c Group/*metabolism ; Cytochrome-c Peroxidase/*metabolism ; *Cytochromes c ; Electron Transport ; Genetic Variation ; Kinetics ; Peroxidases/*metabolism ; Photolysis ; Saccharomyces cerevisiae/metabolism ; *Saccharomyces cerevisiae Proteins
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    Ryanodine receptor of skeletal muscle is a gap junction-type channel (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-10-07
    Description: In the sarcoplasmic reticulum membrane of skeletal muscle, the ryanodine receptor forms an aqueous pore identified as the calcium-release pathway that operates during excitation-contraction coupling. The purified ryanodine receptor channel has now been shown to have four properties usually associated with gap junction channels: (i) a large nonspecific voltage-dependent conductance consisting of several open states; (ii) an inhibition of open probability by low pH; (iii) an inhibition of open probability by calcium; and (iv) a sensitivity to blockade by heptanol and octanol but not other alcohols. This functional homology may provide an insight into the mechanism of how muscle cells transduce depolarization into an intracellular release of calcium.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ma, J -- Fill, M -- Knudson, C M -- Campbell, K P -- Coronado, R -- GM 36852/GM/NIGMS NIH HHS/ -- HL 37044/HL/NHLBI NIH HHS/ -- HL 39262/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1988 Oct 7;242(4875):99-102.〈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/2459777" target="_blank"〉PubMed〈/a〉
    Keywords: Alcohols/pharmacology ; Animals ; Electric Conductivity ; Intercellular Junctions/*physiology ; Ion Channels/drug effects/*physiology ; Kinetics ; Membrane Potentials ; Muscles/*physiology ; Receptors, Cholinergic/drug effects/isolation & purification/*physiology ; Ryanodine/metabolism/pharmacology ; Ryanodine Receptor Calcium Release Channel ; Sarcoplasmic Reticulum/physiology
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    Apolipoprotein E: cholesterol transport protein with expanding role in cell biology (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-04-29
    Description: Apolipoprotein E is a plasma protein that serves as a ligand for low density lipoprotein receptors and, through its interaction with these receptors, participates in the transport of cholesterol and other lipids among various cells of the body. A mutant form of apolipoprotein E that is defective in binding to low density lipoprotein receptors is associated with familial type III hyperlipoproteinemia, a genetic disorder characterized by elevated plasma cholesterol levels and accelerated coronary artery disease. Apolipoprotein E is synthesized in various organs, including liver, brain, spleen, and kidney, and is present in high concentrations in interstitial fluid, where it appears to participate in cholesterol redistribution from cells with excess cholesterol to those requiring cholesterol. Apolipo-protein E also appears to be involved in the repair response to tissue injury; for example, markedly increased amounts of apolipoprotein E are found at sites of peripheral nerve injury and regeneration. Other functions of apolipoprotein E, unrelated to lipid transport, are becoming known, including immunoregulation and modulation of cell growth and differentiation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mahley, R W -- New York, N.Y. -- Science. 1988 Apr 29;240(4852):622-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Gladstone Foundation Laboratories for Cardiovascular Disease, University of California, San Francisco 94140-0608.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3283935" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Apolipoproteins E/genetics/*physiology ; Biological Transport ; Cholesterol/*metabolism ; Gene Expression Regulation ; Humans ; Hyperlipoproteinemia Type III/genetics/metabolism ; Immunity ; Lipid Metabolism ; Molecular Sequence Data ; Polymorphism, Genetic ; Protein Conformation ; Receptors, LDL/metabolism
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    Postsynaptic calcium is sufficient for potentiation of hippocampal synaptic transmission (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-10-07
    Description: Brief repetitive activation of excitatory synapses in the hippocampus leads to an increase in synaptic strength that lasts for many hours. This long-term potentiation (LTP) of synaptic transmission is the most compelling cellular model in the vertebrate brain for learning and memory. The critical role of postsynaptic calcium in triggering LTP has been directly examined using three types of experiment. First, nitr-5, a photolabile nitrobenzhydrol tetracarboxylate calcium chelator, which releases calcium in response to ultraviolet light, was used. Photolysis of nitr-5 injected into hippocampal CA1 pyramidal cells resulted in a large enhancement of synaptic transmission. Second, in agreement with previous results, buffering intracellular calcium at low concentrations blocked LTP. Third, depolarization of the postsynaptic membrane so that calcium entry is suppressed prevented LTP. Taken together, these results demonstrate that an increase in postsynaptic calcium is necessary to induce LTP and sufficient to potentiate synaptic transmission.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Malenka, R C -- Kauer, J A -- Zucker, R S -- Nicoll, R A -- MH00437/MH/NIMH NIH HHS/ -- MH38256/MH/NIMH NIH HHS/ -- NS24205/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1988 Oct 7;242(4875):81-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, School 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/2845577" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/*physiology ; Chelating Agents/pharmacology ; Egtazic Acid/analogs & derivatives/pharmacology ; Evoked Potentials/drug effects ; Hippocampus/*physiology ; In Vitro Techniques ; Kinetics ; Photolysis ; Pyramidal Tracts/physiology ; Rats ; Synapses/*physiology ; *Synaptic Transmission
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    Recognition of a DNA operator by the repressor of phage 434: a view at high resolution (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-11-11
    Description: The repressors of temperate bacteriophages such as 434 and lambda control transcription by binding to a set of DNA operator sites. The different affinity of repressor for each of these sites ensures efficient regulation. High-resolution x-ray crystallography was used to study the DNA-binding domain of phage 434 repressor in complex with a synthetic DNA operator. The structure shows recognition of the operator by direct interactions with base pairs in the major groove, combined with the sequence-dependent ability of DNA to adopt the required conformation on binding repressor. In particular, a network of three-centered bifurcated hydrogen bonds among base pairs in the operator helps explain why 434 repressor prefers certain sites over others. These bonds, which stabilize the conformation of the bound DNA, can form only with certain sequences.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Aggarwal, A K -- Rodgers, D W -- Drottar, M -- Ptashne, M -- Harrison, S C -- GMS-29109/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Nov 11;242(4880):899-907.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, MA 02138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3187531" target="_blank"〉PubMed〈/a〉
    Keywords: Base Composition ; Base Sequence ; Binding Sites ; DNA/*metabolism ; *DNA-Binding Proteins ; Hydrogen Bonding ; Molecular Structure ; Nucleic Acid Conformation ; *Operator Regions, Genetic ; Protein Binding ; Protein Conformation ; Repressor Proteins/*metabolism ; Software ; Transcription Factors/*metabolism ; Viral Proteins/*metabolism ; Viral Regulatory and Accessory Proteins ; X-Ray Diffraction
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    I kappa B: a specific inhibitor of the NF-kappa B transcription factor (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-10-28
    Description: In cells that do not express immunoglobulin kappa light chain genes, the kappa enhancer binding protein NF-kappa B is found in cytosolic fractions and exhibits DNA binding activity only in the presence of a dissociating agent such as sodium deoxycholate. The dependence on deoxycholate is shown to result from association of NF-kappa B with a 60- to 70-kilodalton inhibitory protein (I kappa B). The fractionated inhibitor can inactivate NF-kappa B from various sources--including the nuclei of phorbol ester-treated cells--in a specific, saturable, and reversible manner. The cytoplasmic localization of the complex of NF-kappa B and I kappa B was supported by enucleation experiments. An active phorbol ester must therefore, presumably by activation of protein kinase C, cause dissociation of a cytoplasmic complex of NF-kappa B and I kappa B by modifying I kappa B. this releases active NF-kappa B which can translocate into the nucleus to activate target enhancers. The data show the existence of a phorbol ester-responsive regulatory protein that acts by controlling the DNA binding activity and subcellular localization of a transcription factor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Baeuerle, P A -- Baltimore, D -- New York, N.Y. -- Science. 1988 Oct 28;242(4878):540-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Whitehead Institute for Biomedical Research, MA 02142.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3140380" target="_blank"〉PubMed〈/a〉
    Keywords: B-Lymphocytes/physiology ; Cytoplasm/physiology ; DNA-Binding Proteins/physiology ; Enhancer Elements, Genetic ; *Gene Expression Regulation/drug effects ; Humans ; Immunoglobulin kappa-Chains/*genetics ; Kinetics ; Molecular Structure ; Molecular Weight ; Protein Binding ; Regulatory Sequences, Nucleic Acid ; Tetradecanoylphorbol Acetate/pharmacology ; Transcription Factors/*antagonists & inhibitors/physiology
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    Mutant Trp repressors with new DNA-binding specificities (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-10-14
    Description: Oligonucleotide-directed mutagenesis of the codons for glutamine-68 (Gln68), lysine-72 (Lys72), isoleucine-79 (Ile79), alanine-80 (Ala80), and threonine-81 (Thr81) of the Escherichia coli trpR (tryptophan aporepressor) gene was used to make mutant repressors with each of 36 different amino acid changes. Mutant repressors were tested for binding to each member of a set of 28 different operators closely related to the consensus trp operator. Of the 36 mutant repressors, 11 bind a subset of the 28 operators; 5 of these have new binding specificities. These new specificities indicate that the hydroxyl group of Thr81 makes a specific contact with one of the four critical base pairs in a trp operator half-site, and the methyl group of Thr81 determines specificity at a second, critical base pair. The Trp repressor does not use the first two amino acids of its "recognition alpha-helix," Ile79 and Ala80, to make sequence-specific DNA contacts, and interacts with its operator in vivo in a way fundamentally different from the way that phage lambda repressor, lambda Cro protein, and coliphage 434 repressor contact their respective binding sites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bass, S -- Sorrells, V -- Youderian, P -- GM34150/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Oct 14;242(4876):240-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, University of Southern California, Los Angeles 90089-1481.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3140377" target="_blank"〉PubMed〈/a〉
    Keywords: Alanine/genetics ; Amino Acid Sequence ; Apoproteins/*genetics/metabolism ; Bacterial Proteins ; Base Sequence ; Binding Sites ; Codon ; DNA, Bacterial/*metabolism ; Escherichia coli/*genetics ; *Escherichia coli Proteins ; Glutamine/genetics ; Isoleucine/genetics ; Lysine/genetics ; Mutation ; Operator Regions, Genetic ; Protein Conformation ; Repressor Proteins/*genetics/metabolism ; Threonine/genetics ; Transcription Factors/*genetics
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    Aldolase activity of a Plasmodium falciparum protein with protective properties (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-05-20
    Description: Immunization with a 41-kilodalton blood stage antigen (p41) of Plasmodium falciparum induces immunity to malaria in monkeys. However, antigenic polymorphism and repetitive amino acids commonly found in protective antigens complicate vaccine development. The gene encoding p41 has now been cloned and analyzed. Sequencing and hybridization studies revealed that the gene structure is highly conserved in 14 parasite isolates from three continents. This finding and the lack of repetitive amino acids in the translated DNA sequence may indicate that p41 has an essential function. In this study the protein was found to be 60 percent homologous to the key glycolytic enzyme aldolase from vertebrates, and the affinity-purified p41 protein from parasites showed aldolase activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Certa, U -- Ghersa, P -- Dobeli, H -- Matile, H -- Kocher, H P -- Shrivastava, I K -- Shaw, A R -- Perrin, L H -- New York, N.Y. -- Science. 1988 May 20;240(4855):1036-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Central Research Units, F. Hoffmann-La Roche and Co., Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3285469" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Protozoan/immunology ; Antigen-Antibody Complex/analysis ; Antigens, Protozoan/genetics/*immunology ; Fructose-Bisphosphate Aldolase/genetics/immunology/*metabolism ; Kinetics ; Plasmodium falciparum/enzymology/*immunology ; Polymorphism, Genetic
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    Phase determination by multiple-wavelength x-ray diffraction: crystal structure of a basic "blue" copper protein from cucumbers (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-08-12
    Description: A novel x-ray diffraction technique, multiple-wavelength anomalous dispersion (MAD) phasing, has been applied to the de novo determination of an unknown protein structure, that of the "blue" copper protein isolated from cucumber seedlings. This method makes use of crystallographic phases determined from measurements made at several wavelengths and has recently been made technically feasible through the use of intense, polychromatic synchrotron radiation together with accurate data collection from multiwire electronic area detectors. In contrast with all of the conventional methods of solving protein structures, which require either multiple isomorphous derivatives or coordinates of a similar structure for molecular replacement, this technique allows direct solution of the classical "phase problem" in x-ray crystallography. MAD phase assignment should be particularly useful for determining structures of small to medium-sized metalloproteins for which isomorphous derivatives are difficult or impossible to make. The structure of this particular protein provides new insights into the spectroscopic and redox properties of blue copper proteins, an important class of metalloproteins widely distributed in nature.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Guss, J M -- Merritt, E A -- Phizackerley, R P -- Hedman, B -- Murata, M -- Hodgson, K O -- Freeman, H C -- New York, N.Y. -- Science. 1988 Aug 12;241(4867):806-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Inorganic Chemistry, University of Sydney, New South Wales, Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3406739" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Bacterial Proteins ; *Metalloproteins/metabolism ; Models, Molecular ; Plants/*metabolism ; Protein Conformation ; X-Ray Diffraction/methods
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    Single-chain antigen-binding proteins (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-10-21
    Description: Single-chain antigen-binding proteins are novel recombinant polypeptides, composed of an antibody variable light-chain amino acid sequence (VL) tethered to a variable heavy-chain sequence (VH) by a designed peptide that links the carboxyl terminus of the VL sequence to the amino terminus of the VH sequence. These proteins have the same specificities and affinities for their antigens as the monoclonal antibodies whose VL and VH sequences were used to construct the recombinant genes that were expressed in Escherichia coli. Three of these proteins, one derived from the sequence for a monoclonal antibody to growth hormone and two derived from the sequences of two different monoclonal antibodies to fluorescein, were designed, constructed, synthesized, purified, and assayed. These proteins are expected to have significant advantages over monoclonal antibodies in a number of applications.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bird, R E -- Hardman, K D -- Jacobson, J W -- Johnson, S -- Kaufman, B M -- Lee, S M -- Lee, T -- Pope, S H -- Riordan, G S -- Whitlow, M -- 1-R43-GM39646-01/GM/NIGMS NIH HHS/ -- 1-R43-GM39662-01/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Oct 21;242(4877):423-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Genex Corporation, Gaithersburg, MD 20877.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3140379" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Escherichia coli/genetics ; Genes ; Genetic Vectors ; Humans ; *Immunoglobulin Heavy Chains/genetics ; *Immunoglobulin Light Chains/genetics ; *Immunoglobulin Variable Region/genetics ; Models, Molecular ; Molecular Sequence Data ; Protein Conformation ; *Recombinant Proteins ; X-Ray Diffraction
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    Three-dimensional structure of an oncogene protein: catalytic domain of human c-H-ras p21 (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-02-19
    Description: The crystal structure at 2.7 A resolution of the normal human c-H-ras oncogene protein lacking a flexible carboxyl-terminal 18 residue reveals that the protein consists of a six-stranded beta sheet, four alpha helices, and nine connecting loops. Four loops are involved in interactions with bound guanosine diphosphate: one with the phosphates, another with the ribose, and two with the guanine base. Most of the transforming proteins (in vivo and in vitro) have single amino acid substitutions at one of a few key positions in three of these four loops plus one additional loop. The biological functions of the remaining five loops and other exposed regions are at present unknown. However, one loop corresponds to the binding site for a neutralizing monoclonal antibody and another to a putative "effector region"; mutations in the latter region do not alter guanine nucleotide binding or guanosine triphosphatase activity but they do reduce the transforming activity of activated proteins. The data provide a structural basis for understanding the known biochemical properties of normal as well as activated ras oncogene proteins and indicate additional regions in the molecule that may possibly participate in other cellular functions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉de Vos, A M -- Tong, L -- Milburn, M V -- Matias, P M -- Jancarik, J -- Noguchi, S -- Nishimura, S -- Miura, K -- Ohtsuka, E -- Kim, S H -- CA 45593/CA/NCI NIH HHS/ -- GM 29287/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Feb 19;239(4842):888-93.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of California, Berkely 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2448879" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antibodies, Monoclonal/immunology ; Binding Sites ; Catalysis ; Crystallization ; Epitopes/immunology ; Escherichia coli/genetics ; GTP Phosphohydrolases ; Guanosine Diphosphate/metabolism ; Guanosine Triphosphate/metabolism ; Neoplasms/genetics ; Phosphates/metabolism ; Protein Conformation ; Proto-Oncogene Proteins/genetics/immunology/*metabolism ; Proto-Oncogene Proteins p21(ras) ; Recombinant Proteins/metabolism ; X-Ray Diffraction
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    Voltage-sensitive calcium channels in normal and transformed 3T3 fibroblasts (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-02-26
    Description: Patch clamp recordings of whole-cell and single channel currents revealed the presence of two voltage-sensitive calcium channel types in the membrane of 3T3 fibroblasts. The two calcium channel types were identified by their unitary properties and pharmacological sensitivities. Both calcium channel types were present in all control 3T3 cells, but one type was selectively suppressed in 3T3 cells that had been transformed by activated c-H-ras, EJ-ras, v-fms, or polyoma middle T oncogenes. The presence of voltage-sensitive calcium channels in these nonexcitable cells and the control of their functional expression by transforming oncogenes raises questions about their role in the control of calcium-sensitive processes such as cell motility, cytoskeletal organization, and cell growth.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, C F -- Corbley, M J -- Roberts, T M -- Hess, P -- CA21082/CA/NCI NIH HHS/ -- HL37124/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1988 Feb 26;239(4843):1024-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2449730" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/*metabolism ; Calcium Channel Agonists ; Cell Division ; Cell Line ; Cell Line, Transformed ; *Cell Transformation, Neoplastic ; Electric Conductivity ; Fibroblasts/*physiology ; Ion Channels/drug effects/*physiology ; Kinetics ; Membrane Potentials ; Mice ; Nicotinic Acids/pharmacology ; Oncogenes ; *Oxadiazoles
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Endothelial adhesiveness for blood neutrophils is inhibited by transforming growth factor-beta (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-10-07
    Description: Adhesion of blood cells to endothelial cells is an essential component of all inflammatory responses. The capacity of the endothelium to support adhesion of neutrophils is increased by cytokines such as tumor necrosis factor-alpha, interleukin-1, and endotoxin. Another cytokine, transforming growth factor-beta (TGF-beta), was a strong inhibitor of basalneutrophil adhesion and also decreased the adhesive response of endothelial cells to tumor necrosis factor-alpha (TNF-alpha). The ability of cells to respond to TGF-beta was related to the duration of culture of endothelial cells after explantation from umbilical veins. TGF-beta is likely to serve an anti-inflammatory role at sites of blood vessel injury undergoing active endothelial regeneration.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gamble, J R -- Vadas, M A -- New York, N.Y. -- Science. 1988 Oct 7;242(4875):97-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Human Immunology, Institute of Medical and Veterinary Science, Adelaide, South Australia.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3175638" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Adhesion/drug effects ; Cells, Cultured ; Endothelium, Vascular/cytology/drug effects/*physiology ; Humans ; Kinetics ; Neutrophils/cytology/drug effects/*physiology ; Transforming Growth Factors/*pharmacology ; Umbilical Veins
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    Evidence from cassette mutagenesis for a structure-function motif in a protein of unknown structure (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-04-22
    Description: The three-dimensional structure of most enzymes is unknown; however, many enzymes may have structural motifs similar to those in the known structures of functionally related enzymes. Evidence is presented that an enzyme of unknown structure [Ile-transfer RNA (tRNA) synthetase] may share a functionally important structural motif with an enzyme of related function (Tyr-tRNA synthetase). This approach involves (i) identifying segments of Ile-tRNA synthetase that have been unusually conserved during evolution, (ii) predicting the function of one such segment by assuming a structural relation between Ile-tRNA synthetase and Tyr-tRNA synthetase, and (iii) testing the predicted function by mutagenesis and subsequent biochemical analysis. Random mutations were introduced by cassette mutagenesis into a ten-amino-acid segment of Ile-tRNA synthetase that was predicted to be involved in the formation of the binding site for isoleucine. Few amino acid substitutions appear to be tolerated in this region. However, one substitution (independently isolated twice) increased the Michaelis constant Km for isoleucine in the adenylate synthesis reaction by greater than 6000-fold, but had little effect on the Km for adenosine triphosphate, the apparent Km for tRNA, or the rate constant kcat.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Clarke, N D -- Lien, D C -- Schimmel, P -- GM15539/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Apr 22;240(4851):521-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3282306" target="_blank"〉PubMed〈/a〉
    Keywords: *Amino Acyl-tRNA Synthetases ; Binding Sites ; DNA Mutational Analysis ; Escherichia coli/enzymology ; *Isoleucine-tRNA Ligase ; Kinetics ; Protein Conformation ; Saccharomyces cerevisiae/enzymology ; Structure-Activity Relationship
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    Genetic and crystallographic studies of the 3',5'-exonucleolytic site of DNA polymerase I (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-04-08
    Description: Site-directed mutagenesis of the large fragment of DNA polymerase I (Klenow fragment) yielded two mutant proteins lacking 3',5'-exonuclease activity but having normal polymerase activity. Crystallographic analysis of the mutant proteins showed that neither had any alteration in protein structure other than the expected changes at the mutation sites. These results confirmed the presumed location of the exonuclease active site on the small domain of Klenow fragment and its physical separation from the polymerase active site. An anomalous scattering difference Fourier of a complex of the wild-type enzyme with divalent manganese ion and deoxythymidine monophosphate showed that the exonuclease active site has binding sites for two divalent metal ions. The properties of the mutant proteins suggest that one metal ion plays a role in substrate binding while the other is involved in catalysis of the exonuclease reaction.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Derbyshire, V -- Freemont, P S -- Sanderson, M R -- Beese, L -- Friedman, J M -- Joyce, C M -- Steitz, T A -- GM-22778/GM/NIGMS NIH HHS/ -- GM-28550/GM/NIGMS NIH HHS/ -- RR-01644/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1988 Apr 8;240(4849):199-201.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biophysics and Biochemistry, Yale University Medical School, New Haven, CT 06510.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2832946" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Catalysis ; Computer Graphics ; Crystallography ; DNA Mutational Analysis ; *DNA Polymerase I/genetics ; Escherichia coli/enzymology ; Exonucleases ; Metals ; Models, Molecular ; Protein Conformation ; Structure-Activity Relationship
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    Overexpression of low density lipoprotein (LDL) receptor eliminates LDL from plasma in transgenic mice (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-03-11
    Description: A complementary DNA encoding the human low density lipoprotein (LDL) receptor under control of the mouse metallothionein-I promoter was injected into fertilized mouse eggs, and a strain of mice expressing high levels of LDL receptors was established. After administration of cadmium, these mice cleared intravenously injected 125I-labeled LDL from blood eight to ten times more rapidly than did normal mice. The plasma concentrations of apoproteins B-100 and E, the two ligands for the LDL receptor, declined by more than 90 percent after cadmium treatment, but the concentration of another apoprotein, A-I, was unaffected. Therefore, overexpression of an endocytotic receptor can dramatically lower the ambient concentration of its ligand in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hofmann, S L -- Russell, D W -- Brown, M S -- Goldstein, J L -- Hammer, R E -- HL 01287/HL/NHLBI NIH HHS/ -- HL 20948/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1988 Mar 11;239(4845):1277-81.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics, University of Texas Southwestern Medical Center, Dallas 75235.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3344433" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; DNA/genetics ; Female ; *Genes ; Humans ; Kinetics ; Lipoproteins, LDL/*blood ; Mice ; Mice, Transgenic ; Plasmids ; Receptors, LDL/*genetics/metabolism ; Reference Values ; Transcription, Genetic
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    Exploiting the insights from protein structure (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-05-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jasny, B -- New York, N.Y. -- Science. 1988 May 6;240(4853):722-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3363357" target="_blank"〉PubMed〈/a〉
    Keywords: *Information Systems ; Magnetic Resonance Spectroscopy ; Protein Conformation ; *Proteins ; X-Ray Diffraction
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    Inhibition of cellular proliferation by antisense oligodeoxynucleotides to PCNA cyclin (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-06-10
    Description: The proliferating cell nuclear antigen (PCNA or cyclin) is a nuclear protein recently identified as a cofactor of DNA polymerase delta. When exponentially growing Balb/c3T3 cells are exposed to antisense oligodeoxynucleotides to PCNA, both DNA synthesis and mitosis are completely suppressed. A corresponding sense oligodeoxynucleotide has no inhibitory effects. These experiments indicate that PCNA (cyclin) is important in cellular DNA synthesis and in cell cycle progression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jaskulski, D -- deRiel, J K -- Mercer, W E -- Calabretta, B -- Baserga, R -- CA 42866/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1988 Jun 10;240(4858):1544-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Temple University Medical School, Philadelphia, PA 19140.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2897717" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Autoantigens/*genetics ; Base Sequence ; Cell Division/drug effects ; Cells, Cultured ; Codon ; DNA Replication/*drug effects ; Kinetics ; Mice ; Mice, Inbred BALB C ; Mitosis/*drug effects ; Molecular Sequence Data ; Nuclear Proteins/*genetics ; Oligodeoxyribonucleotides/*pharmacology ; Proliferating Cell Nuclear Antigen
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    Escherichia coli aspartate transcarbamylase: the relation between structure and function (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-08-05
    Description: The x-ray structures of the allosteric enzyme aspartate transcarbamylase from Escherichia coli have been solved and refined for both allosteric forms. The T form was determined in the presence of the heterotropic inhibitor cytidine triphosphate, CTP, while the R form was determined in the presence of the bisubstrate analog N-phosphonacetyl-L-aspartate. These two x-ray structures provide the starting point for an understanding of how allosteric enzymes are able to control the rates of metabolic pathways. Insights into the mechanisms of both catalysis and homotropic cooperativity have been obtained by using site-directed mutagenesis to probe residues thought to be critical to the function of the enzyme based on these x-ray structures.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kantrowitz, E R -- Lipscomb, W N -- GM 06920/GM/NIGMS NIH HHS/ -- GM26237/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Aug 5;241(4866):669-74.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Boston College, MA 02167.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3041592" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Allosteric Site ; Aspartate Carbamoyltransferase/*physiology ; Binding Sites ; Chemical Phenomena ; Chemistry ; Escherichia coli/*enzymology ; Macromolecular Substances ; Protein Conformation ; Structure-Activity Relationship
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    Aminoacylation of synthetic DNAs corresponding to Escherichia coli phenylalanine and lysine tRNAs (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-07-01
    Description: Synthetic DNA oligomers (tDNAs) corresponding to Escherichia coli tRNA(Phe) or tRNA(Lys) have been synthesized with either deoxythymidine (dT) or deoxyuridine (dU) substituted in the positions occupied by ribouridine or its derivatives. The tDNAs inhibited the aminoacylation of their respective tRNAs with their cognate amino acids, but not the aminoacylation of tRNA(Leu) with Leu. In the presence of aminoacyl-tRNA synthetase, species of both a tDNA(Phe) synthesized with a 3' terminal riboadenosine and a tDNA(Lys) containing only deoxynucleotides could be aminoacylated with the appropriate amino acids, although the Michaelis constant Km and observed maximal rate Vmax values for aminoacylation were increased by three- to fourfold and decreased by two- to threefold, respectively. The aminoacylation of synthetic tDNAs demonstrates that the ribose backbone of a tRNA is not absolutely required for tRNA aminoacylation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Khan, A S -- Roe, B A -- GM-30400/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Jul 1;241(4861):74-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of Oklahoma, Norman 73019.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2455342" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA/genetics/*metabolism ; Deoxyuridine/metabolism ; Dimethyl Sulfoxide/pharmacology ; Escherichia coli/*genetics ; Hydrogen-Ion Concentration ; Kinetics ; Lysine-tRNA Ligase/metabolism ; Molecular Sequence Data ; Phenylalanine-tRNA Ligase/metabolism ; RNA, Bacterial/*genetics ; RNA, Transfer, Amino Acyl/*genetics ; Spermidine/pharmacology ; Structure-Activity Relationship ; Thymidine/metabolism
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    Recognition and transport of adenine derivatives with synthetic receptors (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-10-14
    Description: Several new synthetic agents show high affinity for binding adenine derivatives. The structures feature complementary hydrogen bonds that cause the molecular chelation of the purine nucleus. The high lipophilicity of the new agents permits the transport of adenosine and deoxyadenosine across organic liquid membranes. The use of synthetic receptors for small biological targets may have application in drug delivery.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Benzing, T -- Tjivikua, T -- Wolfe, J -- Rebek, J Jr -- New York, N.Y. -- Science. 1988 Oct 14;242(4876):266-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of Pittsburgh, PA 15260.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3262924" target="_blank"〉PubMed〈/a〉
    Keywords: Adenine/analogs & derivatives/*metabolism ; Biological Transport ; Chloroform ; Deoxyadenosines/metabolism ; *Drug Carriers ; Hydrogen Bonding ; Kinetics ; Membranes, Artificial ; Molecular Structure
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    Structure and function of voltage-sensitive ion channels (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-10-07
    Description: Voltage-sensitive ion channels mediate action potentials in electrically excitable cells and play important roles in signal transduction in other cell types. In the past several years, their protein components have been identified, isolated, and restored to functional form in the purified state. Na+ and Ca2+ channels consist of a principal transmembrane subunit, which forms the ion-conducting pore and is expressed with a variable number of associated subunits in different cell types. The principal subunits of voltage-sensitive Na+, Ca2+, and K+ channels are homologous members of a gene family. Models relating the primary structures of these principal subunits to their functional properties have been proposed, and experimental results have begun to define a functional map of these proteins. Coordinated application of biochemical, biophysical, and molecular genetic methods should lead to a clear understanding of the molecular basis of electrical excitability.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Catterall, W A -- New York, N.Y. -- Science. 1988 Oct 7;242(4875):50-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, School of Medicine, University of Washington, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2459775" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Electric Conductivity ; Ion Channels/*physiology ; Membrane Glycoproteins/*genetics ; Models, Molecular ; Neurotoxins/metabolism ; Protein Conformation ; Receptors, Cholinergic/physiology
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    Tertiary structure of plant RuBisCO: domains and their contacts (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-07-01
    Description: The three-dimensional structure of ribulose-1,5-biphosphate carboxylase-oxygenase (RuBisCO), has been determined at 2.6 A resolution. This enzyme initiates photosynthesis by combining carbon dioxide with ribulose bisphosphate to form two molecules of 3-phosphoglycerate. In plants, RuBisCO is built from eight large (L) and eight small (S) polypeptide chains, or subunits. Both S chains and the NH2-terminal domain (N) of L are antiparallel beta, "open-face-sandwich" domains with four-stranded beta sheets and flanking alpha helices. The main domain (B) of L is an alpha/beta barrel containing most of the catalytic residues. The active site is in a pocket at the opening of the barrel that is partly covered by the N domain of a neighboring L chain. The domain contacts of the molecule and its conserved residues are discussed in terms of this structure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chapman, M S -- Suh, S W -- Curmi, P M -- Cascio, D -- Smith, W W -- Eisenberg, D S -- New York, N.Y. -- Science. 1988 Jul 1;241(4861):71-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biology Institute, University of California, Los Angeles 90024.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3133767" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Macromolecular Substances ; Molecular Sequence Data ; Plants/*enzymology ; Protein Conformation ; Rhodospirillum rubrum/enzymology ; *Ribulose-Bisphosphate Carboxylase ; X-Ray Diffraction
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    A common PDGF receptor is activated by homodimeric A and B forms of PDGF (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-06-10
    Description: The human platelet-derived growth factor (PDGF) receptor complementary DNA was cloned and expressed by transfection of Chinese hamster ovary (CHO) fibroblasts. The ability of CHO cells expressing the human receptor complementary DNA (CHO-HR5) to interact with different recombinant forms of PDGF (AA and BB homodimers) was tested. Both forms of PDGF bind to the transfected receptor, stimulate the receptor tyrosine kinase activity, and elicit a mitogenic response in a manner that was indistinguishable from the responses of Balb/c 3T3 cells to AA and BB forms of PDGF can be attributed to a single type of receptor and show that the AA form, like the BB form, is a true mitogen.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Escobedo, J A -- Navankasatussas, S -- Cousens, L S -- Coughlin, S R -- Bell, G I -- Williams, L T -- HL-32898/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1988 Jun 10;240(4858):1532-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of California, San Francisco.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2836953" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Division/drug effects ; Cell Line ; Cells, Cultured ; DNA Replication/drug effects ; Enzyme Activation ; Humans ; Kinetics ; Macromolecular Substances ; Mice ; Phosphorylation ; Platelet-Derived Growth Factor/genetics/*metabolism/pharmacology ; Protein-Tyrosine Kinases/*metabolism ; Receptors, Cell Surface/genetics/*metabolism ; Receptors, Platelet-Derived Growth Factor ; Recombinant Proteins/pharmacology ; Transfection
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    Tat protein from human immunodeficiency virus forms a metal-linked dimer (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-04-01
    Description: Tat, the transactivating protein from HIV, forms a metal-linked dimer with metal ions bridging cysteine-rich regions from each monomer. This novel arrangement is distinct from the "zinc finger" domain observed in other eukaryotic regulatory proteins. Ultraviolet absorption spectra show that Tat binds two Zn2+ or two Cd2+ ions per monomer, and electrophoresis of the Tat-metal complexes demonstrates that the protein forms metal-linked dimers. Partial proteolysis and circular dichroism spectra suggest that metal binding has its primary effects in the cysteine-rich region and relatively little effect on the folding of other regions. These results suggest new directions for biological studies and new approaches to drug design.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Frankel, A D -- Bredt, D S -- Pabo, C O -- GM31471/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Apr 1;240(4848):70-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Genetics, 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/2832944" target="_blank"〉PubMed〈/a〉
    Keywords: Cadmium/*metabolism ; Circular Dichroism ; Cobalt/metabolism ; Cysteine ; Electrophoresis, Polyacrylamide Gel ; Gene Products, tat ; HIV/*analysis ; Macromolecular Substances ; Metals/metabolism ; Oncogene Proteins, Viral ; Oxidation-Reduction ; Peptide Fragments/metabolism ; Peptide Hydrolases/metabolism ; Protein Conformation ; Spectrophotometry ; Sulfhydryl Compounds/metabolism ; Transcription Factors/*metabolism ; Zinc/*metabolism ; tat Gene Products, Human Immunodeficiency Virus
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    Two classes of PDGF receptor recognize different isoforms of PDGF (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-06-10
    Description: Previous studies involving platelet-derived growth factor (PDGF) have been based on the premise that a single cell-surface receptor binds all three isoforms of PDGF (AA, BB, and AB). It is now shown that two populations of PDGF receptor exist and can be distinguished by their ligand binding specificity. The B receptor binds only the BB dimer, whereas the A/B receptor binds AA, BB, and AB dimers. Human dermal fibroblasts appear to express seven times as much B receptor as A/B receptor. The B receptor is responsible for most PDGF receptor phosphorylation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hart, C E -- Forstrom, J W -- Kelly, J D -- Seifert, R A -- Smith, R A -- Ross, R -- Murray, M J -- Bowen-Pope, D F -- DE07063-11/DE/NIDCR NIH HHS/ -- GM35501/GM/NIGMS NIH HHS/ -- HL18645/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1988 Jun 10;240(4858):1529-31.〈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/2836952" target="_blank"〉PubMed〈/a〉
    Keywords: Binding, Competitive ; Cell Membrane/metabolism ; Cells, Cultured ; Fibroblasts/metabolism ; Humans ; Kinetics ; Platelet-Derived Growth Factor/*metabolism ; Receptors, Cell Surface/*metabolism ; Receptors, Platelet-Derived Growth Factor ; Skin/*metabolism ; Structure-Activity Relationship
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 78
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    Effect of forskolin on voltage-gated K+ channels is independent of adenylate cyclase activation (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-06-17
    Description: Forskolin is commonly used to stimulate adenylate cyclase in the study of modulation of ion channels and other proteins by adenosine 3',5'-monophosphate (cAMP)-dependent second messenger systems. In addition to its action on adenylate cyclase, forskolin directly alters the gating of a single class of voltage-dependent potassium channels from a clonal pheochromocytoma (PC12) cell line. This alteration occurred in isolated cell-free patches independent of soluble cytoplasmic enzymes. The effect of forskolin was distinct from those of other agents that raise intracellular cAMP levels. The 1,9-dideoxy derivative of forskolin, which is unable to activate the cyclase, was also effective in altering the potassium channel activity. This direct action of forskolin can lead to misinterpretation of results in experiments in which forskolin is assumed to selectively activate adenylate cyclase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hoshi, T -- Garber, S S -- Aldrich, R W -- NS07158/NS/NINDS NIH HHS/ -- NS23294/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1988 Jun 17;240(4859):1652-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Stanford University, School of Medicine, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2454506" target="_blank"〉PubMed〈/a〉
    Keywords: 1-Methyl-3-isobutylxanthine/pharmacology ; Adenylyl Cyclases/*metabolism ; Adrenal Gland Neoplasms/metabolism ; Colforsin/analogs & derivatives/*pharmacology ; Cyclic AMP/metabolism ; Electric Conductivity ; Enzyme Activation/drug effects ; Ion Channels/drug effects/*physiology ; Kinetics ; Pheochromocytoma/metabolism ; Potassium/*metabolism ; Theophylline/pharmacology ; Tumor Cells, Cultured
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 79
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    Structure of the lambda complex at 2.5 A resolution: details of the repressor-operator interactions (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-11-11
    Description: The crystal structure of a complex containing the DNA-binding domain of lambda repressor and a lambda operator site was determined at 2.5 A resolution and refined to a crystallographic R factor of 24.2 percent. The complex is stabilized by an extensive network of hydrogen bonds between the protein and the sugar-phosphate backbone. Several side chains form hydrogen bonds with sites in the major groove, and hydrophobic contacts also contribute to the specificity of binding. The overall arrangement of the complex is quite similar to that predicted from earlier modeling studies, which fit the protein dimer against linear B-form DNA. However, the cocrystal structure reveals important side chain-side chain interactions that were not predicted from the modeling or from previous genetic and biochemical studies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jordan, S R -- Pabo, C O -- GM-31471/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1988 Nov 11;242(4880):893-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biophysics, Howard Hughes Medical Institute, 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/3187530" target="_blank"〉PubMed〈/a〉
    Keywords: Base Composition ; Base Sequence ; Binding Sites ; Chemical Phenomena ; Chemistry ; Crystallization ; DNA/*metabolism ; *DNA-Binding Proteins ; Glutamine/metabolism ; Hydrogen Bonding ; Molecular Sequence Data ; Molecular Structure ; Nucleic Acid Conformation ; *Operator Regions, Genetic ; Protein Binding ; Protein Conformation ; Repressor Proteins/genetics/*metabolism ; Sugar Phosphates/metabolism ; Transcription Factors/*metabolism ; Viral Proteins ; Viral Regulatory and Accessory Proteins
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 80
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    Dynamic instability of sheared microtubules observed by quasi-elastic light scattering (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-09-23
    Description: The kinetics of microtubule reassembly was studied in vitro by quasi-elastic light scattering (QELS). When microtubules assembled in the absence of microtubule-associated proteins (MAPs) were sheared, they rapidly depolymerized, recovered, and reassembled. The mean length of the recovered microtubules was the same as that observed just before shearing, implying that on average one fragment per original microtubule survived the fragmentation and recovery. When microtubules that contained 25 percent brain MAP were sheared, the fragments did not depolymerize extensively and the average length of the fragments decreased by a factor of 3 relative to the unsheared sample. The results support the dynamic instability model, which predicts that cellular microtubules are latently unstable structures protected on their ends by stabilizing caps.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Keates, R A -- Hallett, F R -- New York, N.Y. -- Science. 1988 Sep 23;241(4873):1642-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of Guelph, Ontario, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3420415" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Guanosine Diphosphate/physiology ; Guanosine Triphosphate/physiology ; In Vitro Techniques ; Kinetics ; Light ; Microtubule-Associated Proteins/metabolism ; Microtubules/*metabolism ; Scattering, Radiation ; Tubulin/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 81
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    Chimeric alpha 2-,beta 2-adrenergic receptors: delineation of domains involved in effector coupling and ligand binding specificity (1988)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1988-06-03
    Description: The alpha 2 and beta 2 adrenergic receptors, both of which are activated by epinephrine, but which can be differentiated by selective drugs, have opposite effects (inhibitory and stimulatory) on the adenylyl cyclase system. The two receptors are homologous with each other, rhodopsin, and other receptors coupled to guanine nucleotide regulatory proteins and they contain seven hydrophobic domains, which may represent transmembrane spanning segments. The function of specific structural domains of these receptors was determined after construction and expression of a series of chimeric alpha 2-,beta 2-adrenergic receptor genes. The specificity for coupling to the stimulatory guanine nucleotide regulatory protein lies within a region extending from the amino terminus of the fifth hydrophobic domain to the carboxyl terminus of the sixth. Major determinants of alpha 2- and beta 2-adrenergic receptor agonist and antagonist ligand binding specificity are contained within the seventh membrane spanning domain. Chimeric receptors should prove useful for elucidating the structural basis of receptor function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kobilka, B K -- Kobilka, T S -- Daniel, K -- Regan, J W -- Caron, M G -- Lefkowitz, R J -- HL 16037/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1988 Jun 3;240(4857):1310-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Medicine, Duke University Medical Center, Durham, NC 27710.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2836950" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Chimera ; Cloning, Molecular ; GTP-Binding Proteins/metabolism ; Humans ; Molecular Sequence Data ; Pindolol/analogs & derivatives/metabolism ; Protein Conformation ; Receptors, Adrenergic, alpha/*genetics ; Receptors, Adrenergic, beta/*genetics ; Yohimbine/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 82
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    Cytokines alter production of HIV-1 from primary mononuclear phagocytes (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-09-23
    Description: Some strains of human immunodeficiency virus type 1 (HIV-1) can infect primary monocytes and monocyte-derived macrophages in vitro. In this report, the effect of cytokines on the production of one of these strains that shows a tropism for mononuclear phagocytes, designated HIV-1JR-FL, was studied. Primary peripheral blood mononuclear phagocytes infected with HIV-1JR-FL were treated with the hematopoietic factors: granulocyte colony-stimulating factor (G-CSF), granulocyte-macrophage colony-stimulating factor (GM-CSF), interleukin-3 (IL-3), macrophage colony-stimulating factor (M-CSF), and gamma-interferon (gamma-IFN). The M-CSF, GM-CSF, IL-3, and gamma-IFN were able to alter HIV-1 production under different conditions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koyanagi, Y -- O'Brien, W A -- Zhao, J Q -- Golde, D W -- Gasson, J C -- Chen, I S -- New York, N.Y. -- Science. 1988 Sep 23;241(4873):1673-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, UCLA School of Medicine 90024.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3047875" target="_blank"〉PubMed〈/a〉
    Keywords: Biological Products/*pharmacology ; Colony-Stimulating Factors/pharmacology ; Cytokines ; Granulocyte-Macrophage Colony-Stimulating Factor ; Growth Substances/pharmacology ; HIV/*physiology ; Humans ; Interleukin-3/pharmacology ; Kinetics ; Macrophages ; Monocytes/*microbiology ; *Virus Replication
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 83
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    How do enzymes work? (1988)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1988-10-28
    Description: The principle of transition-state stabilization asserts that the occurrence of enzymic catalysis is equivalent to saying that an enzyme binds the transition state much more strongly than it binds the ground-state reactants. An outline of the origin and gradual acceptance of this idea is presented, and elementary transition-state theory is reviewed. It is pointed out that a misconception about the theory has led to oversimplification of the accepted expression relating catalysis and binding, and an amended expression is given. Some implications of the transition-state binding principle are then explored. The amended expression suggests that internal molecular dynamics may also play a role in enzymic catalysis. Although such effects probably do not make a major contribution, their magnitude is completely unknown. Two examples of recent advances due to application of the transition-state binding principle are reviewed, one pertaining to the zinc protease mechanism and the other to the generation of catalytic antibodies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kraut, J -- New York, N.Y. -- Science. 1988 Oct 28;242(4878):533-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of California, San Diego, La Jolla 92093.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3051385" target="_blank"〉PubMed〈/a〉
    Keywords: *Catalysis ; Chemistry, Physical ; DNA Mutational Analysis ; Enzymes/*physiology ; Physicochemical Phenomena ; Protein Conformation ; Structure-Activity Relationship
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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