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  • Kinetics  (239)
  • Cloning, Molecular  (233)
  • American Association for the Advancement of Science (AAAS)  (457)
  • American Association for the Advancement of Science
  • American Association of Petroleum Geologists (AAPG)
  • American Physical Society
  • Elsevier
  • 1990-1994  (457)
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  • American Association for the Advancement of Science (AAAS)  (457)
  • American Association for the Advancement of Science
  • American Association of Petroleum Geologists (AAPG)
  • American Physical Society
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  • 101
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    Protein enhancement of hammerhead ribozyme catalysis (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-10-01
    Description: When the recognition sequence of a ribozyme is extended beyond a certain length, turnover is slowed and specificity is decreased. Here, it is shown that a protein can help a ribozyme overcome these general limitations on ribozyme activity. Cleavage of an RNA oligonucleotide by a hammerhead ribozyme is enhanced 10- to 20-fold upon addition of a protein derived from the p7 nucleocapsid (NC) protein of human immunodeficiency virus-type 1. The NC protein also enhances the ability of the ribozyme to discriminate between cleavage of RNA oligonucleotides with differing sequences. These catalytic improvements can be attributed to the strand exchange activity of this RNA binding protein. It is conceivable that endogenous or added proteins may provide analogous increases in ribozyme activity and specificity in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tsuchihashi, Z -- Khosla, M -- Herschlag, D -- New York, N.Y. -- Science. 1993 Oct 1;262(5130):99-102.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Stanford University, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7692597" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; *Capsid Proteins ; Catalysis ; DNA, Single-Stranded/metabolism ; Gene Products, gag/*metabolism ; Kinetics ; Molecular Sequence Data ; Oligoribonucleotides/*metabolism ; RNA/*metabolism ; RNA, Catalytic/chemistry/*metabolism ; Substrate Specificity ; *Viral Proteins ; Zinc Fingers ; gag Gene Products, Human Immunodeficiency Virus
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 102
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    Selection of bacterial virulence genes that are specifically induced in host tissues (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-01-29
    Description: A genetic system was devised that positively selects for bacterial genes that are specifically induced when bacteria infect their host. With the pathogen Salmonella typhimurium, the genes identified by this selection show a marked induction in bacteria recovered from mouse spleen. Mutations in all ivi (in vivo-induced) genes that were tested conferred a defect in virulence. This genetic system was designed to be of general use in a wide variety of bacterial-host systems and has several applications in both vaccine and antimicrobial drug development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mahan, M J -- Slauch, J M -- Mekalanos, J J -- AI08245/AI/NIAID NIH HHS/ -- AI26289/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1993 Jan 29;259(5095):686-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Molecular Genetics, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8430319" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromosomes, Bacterial ; Cloning, Molecular ; Genes, Bacterial ; Mice ; Mice, Inbred BALB C ; Mutagenesis ; Recombinant Fusion Proteins/metabolism ; Salmonella Infections, Animal/microbiology ; Salmonella typhimurium/*genetics/*pathogenicity ; Virulence/*genetics ; beta-Galactosidase/genetics/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 103
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    Role of the acylated amino terminus of recoverin in Ca(2+)-dependent membrane interaction (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-02-05
    Description: Recoverin, a calcium ion (Ca2+)-binding protein of vertebrate photoreceptors, binds to photoreceptor membranes when the Ca2+ concentration is greater than 1 micromolar. This interaction requires a fatty acyl residue covalently linked to the recoverin amino (NH2)-terminus. Removal of the acyl residue, either by proteolytic cleavage of the NH2-terminus or by production of nonacylated recoverin, prevented recoverin from binding to membranes. The acylated recoverin NH2-terminus could be cleaved by trypsin only when Ca2+ was bound to recoverin. These results suggest that the hydrophobic NH2-terminus is constrained in Ca(2+)-free recoverin and liberated by Ca2+ binding. The hydrophobic acyl moiety of recoverin may interact with the membrane only when recoverin binds Ca2+.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dizhoor, A M -- Chen, C K -- Olshevskaya, E -- Sinelnikova, V V -- Phillipov, P -- Hurley, J B -- EYO6641/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1993 Feb 5;259(5096):829-32.〈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/8430337" target="_blank"〉PubMed〈/a〉
    Keywords: 1,2-Dipalmitoylphosphatidylcholine ; Acylation ; Animals ; Antigens, Neoplasm/isolation & purification/*metabolism ; Calcium/*metabolism/pharmacology ; Calcium-Binding Proteins/isolation & purification/*metabolism ; Cattle ; Cell Membrane/metabolism ; Egtazic Acid/pharmacology ; Electrophoresis, Polyacrylamide Gel ; *Eye Proteins ; Hippocalcin ; Kinetics ; *Lipoproteins ; Liposomes ; Membrane Proteins/isolation & purification/*metabolism ; Molecular Weight ; Myristic Acid ; Myristic Acids/*metabolism ; *Nerve Tissue Proteins ; Peptide Fragments/isolation & purification ; Phosphatidylserines ; Protein Binding ; Recoverin ; Rod Cell Outer Segment/*metabolism
    Print ISSN: 0036-8075
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  • 104
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    Synthesis and degradation of cyclic ADP-ribose by NAD glycohydrolases (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-09-03
    Description: Cyclic adenosine diphosphoribose (cADPR), a recently discovered metabolite of nicotinamide adenine dinucleotide (NAD), is a potent calcium-releasing agent postulated to be a new second messenger. An enzyme that catalyzes the synthesis of cADPR from NAD and the hydrolysis of cADPR to ADP-ribose (ADPR) was purified to homogeneity from canine spleen microsomes. The net conversion of NAD to ADPR categorizes this enzyme as an NAD glycohydrolase. NAD glycohydrolases are ubiquitous membrane-bound enzymes that have been known for many years but whose function has not been identified. The results presented here suggest that these enzymes may function in the regulation of calcium homeostasis by the ability to synthesize and degrade cADPR.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, H -- Jacobson, E L -- Jacobson, M K -- CA43894/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 Sep 3;261(5126):1330-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, University of North Texas Health Science Center at Fort Worth 76107.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8395705" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Diphosphate Ribose/*analogs & derivatives/biosynthesis/metabolism ; Animals ; Calcium/metabolism ; Cyclic ADP-Ribose ; Dogs ; Hydrolysis ; Kinetics ; NAD/metabolism ; NAD+ Nucleosidase/isolation & purification/*metabolism ; Spleen/enzymology
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  • 105
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    The nonhelical structure of antifreeze protein type III (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-02-19
    Description: Antifreeze proteins (AFPs) are present in the blood of some marine fishes and inhibit the growth of ice crystals at subzero temperatures by adsorption to the ice lattice. The solution structure of a Type III AFP was determined by two-dimensional nuclear magnetic resonance spectroscopy. These measurements indicate that this 66-residue protein has an unusual fold in which eight beta strands form two sheets of three antiparallel strands and one sheet of two antiparallel strands, and the triple-stranded sheets are packed orthogonally into a beta sandwich. This structure is completely different from the amphipathic, helical structure observed for Type I AFPs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sonnichsen, F D -- Sykes, B D -- Chao, H -- Davies, P L -- New York, N.Y. -- Science. 1993 Feb 19;259(5098):1154-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Protein Engineering Network of Centres of Excellence, University of Alberta, Edmonton, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8438165" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antifreeze Proteins ; Cloning, Molecular ; Escherichia coli/genetics ; Fishes ; Freezing ; Genes, Synthetic ; Glycoproteins/*chemistry/genetics ; Magnetic Resonance Spectroscopy/methods ; Models, Molecular ; Molecular Sequence Data ; *Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Recombinant Proteins/chemistry
    Print ISSN: 0036-8075
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  • 106
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    Cloning of a type I TGF-beta receptor and its effect on TGF-beta binding to the type II receptor (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-05-28
    Description: Transforming growth factor-beta (TGF-beta) affects cellular proliferation, differentiation, and interaction with the extracellular matrix primarily through interaction with the type I and type II TGF-beta receptors. The type II receptors for TGF-beta and activin contain putative serine-threonine kinase domains. A murine serine-threonine kinase receptor, Tsk 7L, was cloned that shared a conserved extracellular domain with the type II TGF-beta receptor. Overexpression of Tsk 7L alone did not increase cell surface binding of TGF-beta, but coexpression with the type II TGF-beta receptor caused TGF-beta to bind to Tsk 7L, which had the size of the type I TGF-beta receptor. Overexpression of Tsk 7L inhibited binding of TGF-beta to the type II receptor in a dominant negative fashion. Combinatorial interactions and stoichiometric ratios between the type I and II receptors may therefore determine the extent of TGF-beta binding and the resulting biological activities.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ebner, R -- Chen, R H -- Shum, L -- Lawler, S -- Zioncheck, T F -- Lee, A -- Lopez, A R -- Derynck, R -- New York, N.Y. -- Science. 1993 May 28;260(5112):1344-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Growth and Development, University of California, San Francisco 94143-0640.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8388127" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Cercopithecus aethiops ; Cloning, Molecular ; Humans ; Mice ; Molecular Sequence Data ; Protein-Serine-Threonine Kinases ; Quail ; Receptors, Cell Surface/chemistry/genetics/*metabolism ; Receptors, Transforming Growth Factor beta ; Transfection ; Transforming Growth Factor beta/*metabolism
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  • 107
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    Release of excess amyloid beta protein from a mutant amyloid beta protein precursor (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-01-22
    Description: The 4-kilodalton amyloid beta protein (A beta), which forms fibrillar deposits in Alzheimer's disease (AD), is derived from a large protein referred to as the amyloid beta protein precursor (beta APP). Human neuroblastoma (M17) cells transfected with constructs expressing wild-type beta APP or a mutant, beta APP delta NL, recently linked to familial AD were compared. After continuous metabolic labeling for 8 hours, cells expressing beta APP delta NL had five times more of an A beta-bearing, carboxyl terminal, beta APP derivative than cells expressing wild-type beta APP and they released six times more A beta into the medium. Thus this mutant beta APP may cause AD because its processing is altered in a way that releases increased amounts of A beta.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cai, X D -- Golde, T E -- Younkin, S G -- AG06656/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 1993 Jan 22;259(5094):514-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Neuropathology, Case Western Reserve University, Cleveland, OH 44106.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8424174" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/genetics/metabolism ; Amino Acid Sequence ; Amyloid beta-Peptides/*biosynthesis/genetics ; Amyloid beta-Protein Precursor/*genetics/metabolism ; Base Sequence ; Cloning, Molecular ; Humans ; Molecular Sequence Data ; *Mutagenesis, Site-Directed ; Neuroblastoma ; Oligodeoxyribonucleotides ; Polymerase Chain Reaction/methods ; Transfection ; Tumor Cells, Cultured
    Print ISSN: 0036-8075
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  • 108
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    Activation of the sphingomyelin signaling pathway in intact EL4 cells and in a cell-free system by IL-1 beta (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-01-22
    Description: The mechanism of interleukin-1 (IL-1) signaling is unknown. Tumor necrosis factor-alpha uses a signal transduction pathway that involves sphingomyelin hydrolysis to ceramide and stimulation of a ceramide-activated protein kinase. In intact EL4 thymoma cells, IL-1 beta similarly stimulated a rapid decrease of sphingomyelin and an elevation of ceramide, and enhanced ceramide-activated protein kinase activity. This cascade was also activated by IL-1 beta in a cell-free system, demonstrating tight coupling to the receptor. Exogenous sphingomyelinase, but not phospholipases A2, C, or D, in combination with phorbol ester replaced IL-1 beta to stimulate IL-2 secretion. Thus, IL-1 beta signals through the sphingomyelin pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mathias, S -- Younes, A -- Kan, C C -- Orlow, I -- Joseph, C -- Kolesnick, R N -- R0-1-CA-42385/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 Jan 22;259(5094):519-22.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Signal Transduction, Sloan-Kettering Institute, Memorial Sloan-Kettering Cancer Center, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8424175" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell-Free System ; Ceramides/*metabolism ; Dose-Response Relationship, Drug ; Interleukin-1/*pharmacology ; Interleukin-2/biosynthesis ; Kinetics ; Mice ; Molecular Sequence Data ; Protein Kinases/metabolism ; Signal Transduction/*drug effects ; Sphingomyelin Phosphodiesterase/pharmacology ; Sphingomyelins/*metabolism ; Substrate Specificity ; Thymoma ; Thymus Neoplasms ; Tumor Cells, Cultured ; Type C Phospholipases/pharmacology
    Print ISSN: 0036-8075
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  • 109
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    Phosphorylation and modulation of a kainate receptor (GluR6) by cAMP-dependent protein kinase (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-02-19
    Description: Ligand-gated ion channels gated by glutamate constitute the major excitatory neurotransmitter system in the mammalian brain. The functional modulation of GluR6, a kainate-activated glutamate receptor, by adenosine 3',5'-monophosphate-dependent protein kinase A (PKA) was examined with receptors expressed in human embryonic kidney cells. Kainate-evoked currents underwent a rapid desensitization that was blocked by lectins. Kainate currents were potentiated by intracellular perfusion of PKA, and this potentiation was blocked by co-application of an inhibitory peptide. Site-directed mutagenesis was used to identify the site or sites of phosphorylation on GluR6. Although mutagenesis of two serine residues, Ser684 and Ser666, was required for complete abolition of the PKA-induced potentiation, Ser684 may be the preferred site of phosphorylation in native GluR6 receptor complexes. These results indicate that glutamate receptor function can be directly modulated by protein phosphorylation and suggest that a dynamic regulation of excitatory receptors could be associated with some forms of learning and memory in the mammalian brain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, L Y -- Taverna, F A -- Huang, X P -- MacDonald, J F -- Hampson, D R -- New York, N.Y. -- Science. 1993 Feb 19;259(5098):1173-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, University of Toronto, Ontario, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8382377" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding Sites ; Brain/*physiology ; Cells, Cultured ; Concanavalin A/pharmacology ; Evoked Potentials/drug effects ; Humans ; Kainic Acid/*pharmacology ; Kidney ; Kinetics ; Membrane Potentials/drug effects ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Oligodeoxyribonucleotides ; Protein Kinases/*metabolism ; Receptors, Glutamate/drug effects/genetics/*physiology ; Receptors, Kainic Acid ; Serine ; Wheat Germ Agglutinins/pharmacology
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 110
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    "MegaYAC" library (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-05-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Evans, G A -- New York, N.Y. -- Science. 1993 May 14;260(5110):877.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8493512" target="_blank"〉PubMed〈/a〉
    Keywords: *Chromosomes, Fungal ; Cloning, Molecular ; *Gene Library ; *Human Genome Project ; Humans
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  • 111
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    Substrate phage: selection of protease substrates by monovalent phage display (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-05-21
    Description: A method is described here for identifying good protease substrates among approximately 10(7) possible sequences. A library of fusion proteins was constructed containing an amino-terminal domain used to bind to an affinity support, followed by a randomized protease substrate sequence and the carboxyl-terminal domain of M13 gene III. Each fusion protein was displayed as a single copy on filamentous phagemid particles (substrate phage). Phage were then bound to an affinity support and treated with the protease of interest. Phage with good protease substrates were released, whereas phage with substrates that resisted proteolysis remained bound. After several rounds of binding, proteolysis, and phagemid propagation, sensitive and resistant substrate sequences were identified for two different proteases, a variant of subtilisin and factor Xa. The technique may also be useful for studying the sequence specificity of a variety of posttranslational modifications.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Matthews, D J -- Wells, J A -- New York, N.Y. -- Science. 1993 May 21;260(5111):1113-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Protein Engineering, Genentech, South San Francisco, CA 94080.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8493554" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Bacteriophages/*genetics ; Base Sequence ; Computer Simulation ; Factor Xa/chemistry/*metabolism ; Genetic Vectors ; Humans ; Kinetics ; Models, Molecular ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Oligopeptides/chemistry/*metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Substrate Specificity ; Subtilisins/chemistry/genetics/*metabolism
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  • 112
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    Arabidopsis ethylene-response gene ETR1: similarity of product to two-component regulators (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-10-22
    Description: Ethylene behaves as a hormone in plants, regulating such aspects of growth and development as fruit ripening, flower senescence, and abscission. Ethylene insensitivity is conferred by dominant mutations in the ETR1 gene early in the ethylene signal transduction pathway of Arabidopsis thaliana. The ETR1 gene was cloned by the method of chromosome walking. Each of the four known etr1 mutant alleles contains a missense mutation near the amino terminus of the predicted protein. Although the sequence of the amino-terminal half of the deduced ETR1 protein appears to be novel, the carboxyl-terminal half is similar in sequence to both components of the prokaryotic family of signal transducers known as the two-component systems. Thus, an early step in ethylene signal transduction in plants may involve transfer of phosphate as in prokaryotic two-component systems. The dominant etr1-1 mutant gene conferred ethylene insensitivity to wild-type Arabidopsis plants when introduced by transformation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chang, C -- Kwok, S F -- Bleecker, A B -- Meyerowitz, E M -- New York, N.Y. -- Science. 1993 Oct 22;262(5133):539-44.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology 156-29, California Institute of Technology, Pasadena 91125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8211181" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Arabidopsis/*genetics/metabolism ; Bacterial Proteins/chemistry/genetics ; Base Sequence ; Chromosome Walking ; Cloning, Molecular ; Ethylenes/*metabolism/pharmacology ; Genes, Dominant ; *Genes, Plant ; Molecular Sequence Data ; Plant Proteins/chemistry/*genetics/metabolism ; Protein Kinases/chemistry/genetics ; *Receptors, Cell Surface ; Sequence Alignment ; *Signal Transduction ; Transcription Factors/chemistry/genetics
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  • 113
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    Colicin E1 binding to membranes: time-resolved studies of spin-labeled mutants (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-02-12
    Description: To investigate the mechanism of interaction of the toxin colicin E1 with membranes, three cysteine substitution mutants and the wild type of the channel-forming fragment were spin labeled at the unique thiol. Time-resolved interaction of these labeled proteins with phospholipid vesicles was investigated with stopped-flow electron paramagnetic resonance spectroscopy. The fragment interacts with neutral bilayers at low pH, indicating that the interaction is hydrophobic rather than electrostatic. The interaction occurs in at least two distinct steps: (i) rapid adsorption to the surface; and (ii) slow, rate-limiting insertion of the hydrophobic central helices into the membrane interior.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shin, Y K -- Levinthal, C -- Levinthal, F -- Hubbell, W L -- EY05216/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1993 Feb 12;259(5097):960-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Jules Stein Eye Institute, University of California, Los Angeles 90024.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8382373" target="_blank"〉PubMed〈/a〉
    Keywords: Adsorption ; Binding Sites ; Cell Membrane/*metabolism ; Colicins/chemistry/genetics/*metabolism ; Cysteine/genetics ; Electron Spin Resonance Spectroscopy ; Hydrogen-Ion Concentration ; Kinetics ; Lipid Bilayers/metabolism ; *Mutagenesis ; Peptide Fragments/metabolism ; Protein Structure, Secondary ; *Spin Labels
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  • 114
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    Altered prevalence of gating modes in neurotransmitter inhibition of N-type calcium channels (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-02-12
    Description: G protein-mediated inhibition of voltage-activated calcium channels by neurotransmitters has important consequences for the control of synaptic strength. Single-channel recordings of N-type calcium channels in frog sympathetic neurons reveal at least three distinct patterns of gating, designated low-Po, medium-Po, and high-Po modes according to their probability of being open (Po) at -10 millivolts. The high-Po mode is responsible for the bulk of divalent cation entry in the absence of neurotransmitter. Norepinephrine greatly decreased the prevalence of high-Po gating and increased the proportion of time a channel exhibited low-Po behavior or no activity at all, which thereby reduced the overall current. Directly observed patterns of transition between the various modes suggest that activated G protein alters the balance between modal behaviors that freely interconvert even in the absence of modulatory signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Delcour, A H -- Tsien, R W -- HL13156/HL/NHLBI NIH HHS/ -- NS24607/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1993 Feb 12;259(5097):980-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Physiology, Beckman Center, Stanford University Medical Center, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8094902" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anura ; Calcium Channels/*drug effects/*physiology ; Cations, Divalent ; Electric Stimulation ; Electrophysiology ; GTP-Binding Proteins/physiology ; Ion Channel Gating/*physiology ; Kinetics ; Neurons/physiology ; Neurotransmitter Agents/*pharmacology ; Norepinephrine/pharmacology ; Sympathetic Nervous System/cytology/physiology ; Synapses/physiology
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    Betacellulin: a mitogen from pancreatic beta cell tumors (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-03-12
    Description: Betacellulin, a member of the epidermal growth factor family, has been identified in the conditioned medium of cell lines derived from mouse pancreatic beta cell tumors. Betacellulin is a 32-kilodalton glycoprotein that appears to be processed from a larger transmembrane precursor by proteolytic cleavage. The carboxyl-terminal domain of betacellulin has 50 percent sequence similarity with that of rat transforming growth factor alpha. Betacellulin is a potent mitogen for retinal pigment epithelial cells and vascular smooth muscle cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shing, Y -- Christofori, G -- Hanahan, D -- Ono, Y -- Sasada, R -- Igarashi, K -- Folkman, J -- CA 70118/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 Mar 12;259(5101):1604-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Surgery, Children's Hospital, Boston, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8456283" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Amino Acid Sequence ; Animals ; Base Sequence ; Betacellulin ; Cell Division/drug effects ; Cells, Cultured ; DNA Replication/drug effects ; Endothelium, Vascular/cytology/drug effects ; Epidermal Growth Factor/pharmacology ; Growth Substances/*genetics/isolation & purification/pharmacology ; Humans ; *Intercellular Signaling Peptides and Proteins ; Islets of Langerhans/physiopathology ; Kinetics ; Mice ; Molecular Sequence Data ; Muscle, Smooth, Vascular/cytology/drug effects ; Oligodeoxyribonucleotides ; Pancreatic Neoplasms/*physiopathology ; Pigment Epithelium of Eye/cytology/drug effects ; Polymerase Chain Reaction/methods ; Protein Precursors/genetics ; Rats ; Receptor, Epidermal Growth Factor/metabolism ; Recombinant Proteins/pharmacology ; Sequence Homology, Amino Acid ; Thymidine/metabolism ; Transforming Growth Factor alpha/genetics
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    Cyclin-dependent regulation of G1 in mammalian fibroblasts (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-03-26
    Description: Eukaryotic cells become committed to proliferate during the G1 phase of the cell cycle. In budding yeast, commitment occurs when the catalytic subunit of a protein kinase, encoded by the CDC28 gene (the homolog of the fission yeast cdc2+ gene), binds to a positively acting regulatory subunit, a cyclin. Related kinases are also required for progression through the G1 phase in higher eukaryotes. The role of cyclins in controlling G1 progression in mammalian cells was tested by construction of fibroblasts that constitutively overexpress human cyclin E. This was found to shorten the duration of G1, decrease cell size, and diminish the serum requirement for the transition from G1 to S phase. These observations show that cyclin levels can be rate-limiting for G1 progression in mammalian cells and suggest that cyclin synthesis may be the target of physiological signals that control cell proliferation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ohtsubo, M -- Roberts, J M -- New York, N.Y. -- Science. 1993 Mar 26;259(5103):1908-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Basic Sciences, Fred Hutchinson Cancer Research Center, Seattle, WA 98104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8384376" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Division/physiology ; Cell Line ; Cloning, Molecular ; Cyclins/genetics/*physiology ; Fibroblasts/*cytology/metabolism ; Flow Cytometry ; G1 Phase/*physiology ; Gene Expression ; Genetic Vectors ; Humans ; Kanamycin Kinase ; Male ; Phosphotransferases/genetics ; Rats ; Recombinant Fusion Proteins/metabolism ; Retroviridae/genetics ; S Phase/physiology ; Time Factors ; Transfection
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    Characterization of a presynaptic glutamate receptor (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-10-15
    Description: Glutamate receptors mediate excitatory neurotransmission in the brain and are important in the formation of memory and in some neurodegenerative disorders. A complementary DNA clone that encoded a 33-kilodalton protein (GR33) was obtained by screening a library with an antibody generated against glutamate binding proteins. The sequence of GR33 is identical to that of the recently reported presynaptic protein syntaxin. When GR33 was expressed in Xenopus oocytes, it formed glutamate-activated ion channels that are pharmacologically similar to those of N-methyl-D-aspartate receptors but with different electrophysiological properties. Mutation of the leucine 278 residue in the single putative transmembrane segment of GR33 affects the properties of the channel. Thus, in vivo GR33 may be a presynaptic glutamate receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smirnova, T -- Stinnakre, J -- Mallet, J -- New York, N.Y. -- Science. 1993 Oct 15;262(5132):430-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire de genetique moleculaire de la neurotransmission et des processus neurodegeneratifs, Centre National de la Recherche Scientifique (CNRS), Gif sur Yvette, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8105537" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Surface/chemistry ; Brain/embryology ; Brain Chemistry ; Calcium/metabolism ; Cells, Cultured ; Cloning, Molecular ; Glutamates/pharmacology ; Glutamic Acid ; Humans ; Membrane Potentials ; Mutagenesis, Site-Directed ; N-Methylaspartate/pharmacology ; Nerve Tissue Proteins/chemistry ; Neurons/chemistry ; Oocytes ; Rats ; Rats, Wistar ; Receptors, Glutamate/chemistry/genetics/*metabolism ; Receptors, N-Methyl-D-Aspartate/metabolism ; Receptors, Presynaptic/chemistry/genetics/*metabolism ; Syntaxin 1 ; Xenopus
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    Structure and functional expression of a member of the low voltage-activated calcium channel family (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-05-21
    Description: Oscillatory firing patterns are an intrinsic property of some neurons and have an important function in information processing. In some cells, low voltage-activated calcium channels have been proposed to underlie a depolarizing potential that regulates bursting. The sequence of a rat brain calcium channel alpha 1 subunit (rbE-II) was deduced. Although it is structurally related to high voltage-activated calcium channels, the rbE-II channel transiently activated at negative membrane potentials, required a strong hyperpolarization to deinactivate, and was highly sensitive to block by nickel. In situ hybridization showed that rbE-II messenger RNA is expressed in regions throughout the central nervous system. The electrophysiological properties of the rbE-II current are consistent with a type of low voltage-activated calcium channel that requires membrane hyperpolarization for maximal activity, which suggests that rbE-II may be involved in the modulation of firing patterns.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Soong, T W -- Stea, A -- Hodson, C D -- Dubel, S J -- Vincent, S R -- Snutch, T P -- New York, N.Y. -- Science. 1993 May 21;260(5111):1133-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biotechnology Laboratory, University of British Columbia, Vancouver, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8388125" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Brain Chemistry ; Calcium Channels/*chemistry/genetics/physiology ; Calcium Channels, R-Type ; Cation Transport Proteins ; Cloning, Molecular ; Electric Conductivity ; Hippocampus/chemistry ; In Situ Hybridization ; Membrane Potentials ; Membrane Proteins/*chemistry/genetics/physiology ; Molecular Sequence Data ; Nerve Tissue Proteins/*chemistry/genetics/physiology ; RNA, Messenger/analysis/genetics ; Rats ; Sequence Alignment
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    A first step toward gene therapy for hemophilia B? (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-10-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J -- New York, N.Y. -- Science. 1993 Oct 1;262(5130):29-30.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8211125" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; Dogs ; Factor IX/biosynthesis/*genetics ; Gene Transfer Techniques ; *Genetic Therapy ; Genetic Vectors ; Hemophilia A/genetics/therapy ; Hemophilia B/genetics/*therapy ; Hepatectomy ; Humans ; Liver/metabolism ; Liver Regeneration ; Retroviridae/genetics
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    Phosphorodithioate DNA as a potential therapeutic drug (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-03-12
    Description: This article summarizes methods for the synthesis of phosphorodithioate-linked deoxyoligonucleotides and details an analysis of one of the distinctive properties of phosphorodithioate DNA oligomers, their ability to strongly inhibit human immunodeficiency virus type-1 reverse transcriptase (HIV-1 RT). Mechanistic studies indicate that oligomers of this type interfere with enzyme function by binding tightly to the active site for primer-template, which results in low or subnanomolar inhibitory constants. Although many of these studies have used deoxyoligocytidine analogs, a rationally designed approach has led to the discovery of a very active phosphorodithioate deoxyoligonucleotide inhibitor. This type of inhibitor, which binds strongly to the primer-template active site of HIV-1 RT, provides another type of potential therapeutic agent against HIV-1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marshall, W S -- Caruthers, M H -- GM21120/GM/NIGMS NIH HHS/ -- GM25680/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Mar 12;259(5101):1564-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7681216" target="_blank"〉PubMed〈/a〉
    Keywords: Antiviral Agents/*chemical synthesis/pharmacology ; Base Sequence ; HIV Reverse Transcriptase ; HIV-1/drug effects/*enzymology ; Kinetics ; Molecular Sequence Data ; Oligodeoxyribonucleotides/*chemical synthesis/pharmacology ; Organothiophosphates/*chemical synthesis/pharmacology ; *Reverse Transcriptase Inhibitors ; Structure-Activity Relationship
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    Multiple RNA polymerase conformations and GreA: control of the fidelity of transcription (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-11-05
    Description: Pre-steady state kinetics of misincorporation were used to investigate the addition of single nucleotides to nascent RNA by Escherichia coli RNA polymerase during transcription elongation. The results were fit with a branched kinetic mechanism that permits conformational switching, at each template position, between an activated and an unactivated enzyme complex, both of which can bind nucleotide triphosphates (NTPs) from solution. The complex exists most often in the long-lived activated state, and only becomes unactivated when transcription is slowed. This model permits multiple levels of nucleotide discrimination in transcription, since the complex can be "kinetically trapped" in the unactivated state in the absence of the correct NTP or if the 3' terminal residue is incorrectly matched. The transcription cleavage factor GreA (or an activity enhanced by GreA) increased the fidelity of transcription by preferential cleavage of transcripts containing misincorporated residues in the unactivated state of the elongation complex. This cleavage mechanism by GreA may prevent the formation of "dead-end" transcription complexes in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Erie, D A -- Hajiseyedjavadi, O -- Young, M C -- von Hippel, P H -- GM-12915/GM/NIGMS NIH HHS/ -- GM-15792/GM/NIGMS NIH HHS/ -- GM-29158/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Nov 5;262(5135):867-73.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Biology, University of Oregon, Eugene 97403.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8235608" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; DNA-Directed RNA Polymerases/*chemistry/metabolism ; Endoribonucleases/metabolism ; Escherichia coli/enzymology ; *Escherichia coli Proteins ; Kinetics ; Models, Genetic ; Molecular Sequence Data ; Nucleotides/metabolism ; Peptide Elongation Factors/*metabolism ; Protein Conformation ; RNA, Messenger/*biosynthesis/metabolism ; Templates, Genetic ; Transcription Factors/*metabolism ; *Transcription, Genetic ; Uridine Triphosphate/metabolism
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    A role for the transcription factors Mbp1 and Swi4 in progression from G1 to S phase (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-09-17
    Description: In budding yeast genes that encode G1 cyclins and proteins involved in DNA synthesis are transcriptionally activated in late G1. A transcription factor, called SBF, is composed of Swi4 and Swi6 proteins and activates transcription of G1 cyclin genes. A different, but related, complex called MBF binds to MCB elements (Mlu I cell cycle box) found in the promoter of most DNA synthesis genes. MBF contains Swi6 and a 120-kilodalton protein (p120). MBF was purified and the gene encoding p120 (termed MBP1) was cloned. A deletion of MBP1 was not lethal but led to deregulated expression of DNA synthesis genes, indicating a direct regulatory role for MBF in MCB-driven transcription. Mbp1 is related to Swi4. Strains deleted for both MBP1 and SWI4 were inviable, demonstrating that transcriptional activation by MBF and SBF has an important role in the transition from G1 to S phase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koch, C -- Moll, T -- Neuberg, M -- Ahorn, H -- Nasmyth, K -- New York, N.Y. -- Science. 1993 Sep 17;261(5128):1551-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Pathology, Vienna, Austria.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8372350" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; CDC28 Protein Kinase, S cerevisiae/genetics/metabolism ; Cloning, Molecular ; Cyclins/genetics ; DNA, Fungal/biosynthesis ; DNA-Binding Proteins ; Fungal Proteins/chemistry/*genetics/metabolism ; *G1 Phase ; Gene Expression Regulation, Fungal ; Genes, Fungal ; Molecular Sequence Data ; Mutation ; Promoter Regions, Genetic ; *S Phase ; Saccharomyces cerevisiae/cytology/*genetics ; *Saccharomyces cerevisiae Proteins ; Sequence Alignment ; Transcription Factors/chemistry/*genetics/metabolism
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    SH2-containing phosphotyrosine phosphatase as a target of protein-tyrosine kinases (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-03-12
    Description: A mouse phosphotyrosine phosphatase containing two Src homology 2 (SH2) domains, Syp, was identified. Syp bound to autophosphorylated epidermal growth factor (EGF) and platelet-derived growth factor (PDGF) receptors through its SH2 domains and was rapidly phosphorylated on tyrosine in PDGF- and EGF-stimulated cells. Furthermore, Syp was constitutively phosphorylated on tyrosine in cells transformed by v-src. This mammalian phosphatase is most closely related, especially in its SH2 domains, to the corkscrew (csw) gene product of Drosophila, which is required for signal transduction downstream of the Torso receptor tyrosine kinase. The Syp gene is widely expressed throughout embryonic mouse development and in adult tissues. Thus, Syp may function in mammalian embryonic development and as a common target of both receptor and nonreceptor tyrosine kinases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Feng, G S -- Hui, C C -- Pawson, T -- New York, N.Y. -- Science. 1993 Mar 12;259(5101):1607-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular and Developmental Biology, Samuel Lunenfeld Research Institute, Mount Sinai Hospital, Toronto, Ontario, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8096088" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line, Transformed ; Cell Transformation, Neoplastic ; Embryo, Mammalian ; Embryonic and Fetal Development ; Epidermal Growth Factor/pharmacology ; *Genes, src ; Humans ; Intracellular Signaling Peptides and Proteins ; Kinetics ; Mice ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; Phosphorylation ; Platelet-Derived Growth Factor/pharmacology ; Poly A/isolation & purification/metabolism ; Polymerase Chain Reaction ; Protein Tyrosine Phosphatase, Non-Receptor Type 11 ; Protein Tyrosine Phosphatase, Non-Receptor Type 6 ; Protein Tyrosine Phosphatases/genetics/*metabolism ; Protein-Tyrosine Kinases/*metabolism ; RNA, Messenger/isolation & purification/metabolism ; Rats ; Receptor, Epidermal Growth Factor/metabolism ; Receptors, Platelet-Derived Growth Factor/genetics/metabolism ; Sequence Homology, Amino Acid ; Transfection
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    A functional role for GTP-binding proteins in synaptic vesicle cycling (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-02-19
    Description: The squid giant synapse was used to test the hypothesis that guanosine-5'-triphosphate (GTP)-binding proteins regulate the local distribution of synaptic vesicles within nerve terminals. Presynaptic injection of the nonhydrolyzable GTP analog GTP gamma S irreversibly inhibited neurotransmitter release without changing either the size of the calcium signals produced by presynaptic action potentials or the number of synaptic vesicles docked at presynaptic active zones. Neurotransmitter release was also inhibited by injection of the nonhydrolyzable guanosine diphosphate (GDP) analog GDP beta S but not by injection of AIF4-. These results suggest that a small molecular weight GTP-binding protein directs the docking of synaptic vesicles that occurs before calcium-dependent neurotransmitter release. Depletion of undocked synaptic vesicles by GTP gamma S indicates that additional GTP-binding proteins function in the terminal at other steps responsible for synaptic vesicle replenishment.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hess, S D -- Doroshenko, P A -- Augustine, G J -- NS-21624/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1993 Feb 19;259(5098):1169-72.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, University of Southern California.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8438167" target="_blank"〉PubMed〈/a〉
    Keywords: Aluminum/pharmacology ; *Aluminum Compounds ; Animals ; Calcium/metabolism ; Decapodiformes ; *Fluorides ; Fluorine/pharmacology ; GTP-Binding Proteins/*physiology ; Ganglia/physiology ; Guanosine 5'-O-(3-Thiotriphosphate)/pharmacology ; Guanosine Diphosphate/analogs & derivatives/metabolism/pharmacology ; Guanosine Triphosphate/metabolism ; In Vitro Techniques ; Kinetics ; Models, Neurological ; Nerve Endings/physiology/ultrastructure ; Signal Transduction/drug effects ; Synaptic Vesicles/drug effects/*physiology/ultrastructure ; Thionucleotides/pharmacology ; Time Factors
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    An inhibitor of p34CDC28 protein kinase activity from Saccharomyces cerevisiae (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-01-08
    Description: The p34CDC28 protein from Saccharomyces cerevisiae is a homolog of the p34cdc2 protein kinase, a fundamental regulator of cell division in all eukaryotic cells. Once activated it initiates the visible events of mitosis (chromosome condensation, nuclear envelope breakdown, and spindle formation). The p34CDC28 protein also has a critical role in the initiation of DNA synthesis. The protein kinase activity is regulated by cycles of phosphorylation and dephosphorylation and by periodic association with cyclins. An endogenous 40-kilodalton protein (p40) originally identified as a substrate of the p34CDC28 protein kinase was purified. The p40 protein bound tightly to p34CDC28 and inhibited the activity of the kinase. The p40 protein may provide another mechanism to regulate p34CDC28 protein kinase activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mendenhall, M D -- New York, N.Y. -- Science. 1993 Jan 8;259(5092):216-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Kentucky, Lexington 40536.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8421781" target="_blank"〉PubMed〈/a〉
    Keywords: CDC28 Protein Kinase, S cerevisiae ; Cyclins/metabolism ; Histones/metabolism ; Kinetics ; Molecular Weight ; Phosphorylation ; Phosphothreonine/metabolism ; *Protein Kinase Inhibitors ; Protein Kinases/metabolism ; Saccharomyces cerevisiae/*enzymology
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    TH1 and TH2 cell antigen receptors in experimental leishmaniasis (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-03-05
    Description: The complexity and chronicity of parasitic infections have obscured the identification of biologically relevant antigens. Analysis of the T cell receptor repertoire used by mice infected with Leishmania major revealed the expansion of a restricted population of CD4+ cells. These cells expressed the V alpha 8-J alpha TA72, V beta 4 heterodimer in both progressive infection and protective immunity and across several major histocompatibility haplotypes. Thus, the same immunodominant parasite epitope drives the disparate outcomes of this infectious process, suggesting that candidate vaccine antigens selected by screening of immune individuals may be capable of exacerbating disease in genetically susceptible individuals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reiner, S L -- Wang, Z E -- Hatam, F -- Scott, P -- Locksley, R M -- AI30663/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1993 Mar 5;259(5100):1457-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8451641" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD4/analysis ; Base Sequence ; Cloning, Molecular ; *Leishmania tropica ; Leishmaniasis, Cutaneous/*immunology ; Mice ; Mice, Inbred BALB C ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; Polymerase Chain Reaction/methods ; RNA, Messenger/genetics/isolation & purification ; Receptors, Antigen, T-Cell/analysis/genetics/*metabolism ; Receptors, Antigen, T-Cell, alpha-beta/analysis/genetics/*metabolism ; Reference Values ; T-Lymphocyte Subsets/immunology
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    Identification of a ten-amino acid proline-rich SH3 binding site (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-02-19
    Description: The Src homology 3 (SH3) region is a small protein domain present in a very large group of proteins, including cytoskeletal elements and signaling proteins. It is believed that SH3 domains serve as modules that mediate protein-protein associations and, along with Src homology 2 (SH2) domains, regulate cytoplasmic signaling. The SH3 binding sites of two SH3 binding proteins were localized to a nine- or ten-amino acid stretch very rich in proline residues. Similar SH3 binding motifs exist in the formins, proteins that function in pattern formation in embryonic limbs of the mouse, and one subtype of the muscarinic acetylcholine receptor. Identification of the SH3 binding site provides a basis for understanding the interaction between the SH3 domains and their targets.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ren, R -- Mayer, B J -- Cicchetti, P -- Baltimore, D -- CA 08875/CA/NCI NIH HHS/ -- CA 09673/CA/NCI NIH HHS/ -- CA 51462/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 Feb 19;259(5098):1157-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8438166" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Cytoskeletal Proteins/genetics/*metabolism ; DNA/genetics/metabolism ; Genes, abl ; Glutathione Transferase/genetics/metabolism ; Kinetics ; Mice ; Molecular Sequence Data ; *Proline ; Proto-Oncogene Proteins c-abl/genetics/*metabolism ; Rats ; Receptors, Muscarinic/metabolism ; Recombinant Fusion Proteins/metabolism ; Sequence Homology, Amino Acid ; Signal Transduction
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    NF-kappa B controls expression of inhibitor I kappa B alpha: evidence for an inducible autoregulatory pathway (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-03-26
    Description: The eukaryotic transcription factor nuclear factor-kappa B (NF-kappa B) participates in many parts of the genetic program mediating T lymphocyte activation and growth. Nuclear expression of NF-kappa B occurs after its induced dissociation from its cytoplasmic inhibitor I kappa B alpha. Phorbol ester and tumor necrosis factor-alpha induction of nuclear NF-kappa B is associated with both the degradation of performed I kappa B alpha and the activation of I kappa B alpha gene expression. Transfection studies indicate that the I kappa B alpha gene is specifically induced by the 65-kilodalton transactivating subunit of NF-kappa B. Association of the newly synthesized I kappa B alpha with p65 restores intracellular inhibition of NF-kappa B DNA binding activity and prolongs the survival of this labile inhibitor. Together, these results show that NF-kappa B controls the expression of I kappa B alpha by means of an inducible autoregulatory pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sun, S C -- Ganchi, P A -- Ballard, D W -- Greene, W C -- 5T32CA09111/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1993 Mar 26;259(5103):1912-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Gladstone Institute of Virology and Immunology, University of California, San Francisco.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8096091" target="_blank"〉PubMed〈/a〉
    Keywords: CD4-Positive T-Lymphocytes/metabolism ; Cell Line ; Cell Nucleus/metabolism ; Cycloheximide/pharmacology ; Cytoplasm/metabolism ; DNA/metabolism ; DNA-Binding Proteins/*genetics ; *Gene Expression Regulation ; Humans ; *I-kappa B Proteins ; Immunoblotting ; Kinetics ; Molecular Weight ; Mutagenesis ; NF-kappa B/*antagonists & inhibitors/genetics/*physiology ; RNA, Messenger/biosynthesis ; Tetradecanoylphorbol Acetate/pharmacology ; Trans-Activators/pharmacology ; Transfection ; Tumor Necrosis Factor-alpha/pharmacology
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    Rad: a member of the Ras family overexpressed in muscle of type II diabetic humans (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-11-26
    Description: To identify the gene or genes associated with insulin resistance in Type II (non-insulin-dependent) diabetes mellitus, subtraction libraries were prepared from skeletal muscle of normal and diabetic humans and screened with subtracted probes. Only one clone out of 4000 was selectively overexpressed in Type II diabetic muscle as compared to muscle of non-diabetic or Type I diabetic individuals. This clone encoded a new 29-kilodalton member of the Ras-guanosine triphosphatase superfamily and was termed Rad (Ras associated with diabetes). Messenger ribonucleic acid of Rad was expressed primarily in skeletal and cardiac muscle and was increased an average of 8.6-fold in the muscle of Type II diabetics as compared to normal individuals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reynet, C -- Kahn, C R -- DK 36836/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1993 Nov 26;262(5138):1441-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Research Division, Joslin Diabetes Center, Boston, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8248782" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Blotting, Northern ; Blotting, Southern ; Chromosome Aberrations ; Cloning, Molecular ; Diabetes Mellitus, Type 2/*genetics/metabolism ; GTP Phosphohydrolases/biosynthesis/chemistry/genetics ; GTP-Binding Proteins/biosynthesis/chemistry/*genetics ; Gene Amplification ; *Genes ; Humans ; Insulin Resistance/*genetics ; Molecular Sequence Data ; Muscles/*metabolism ; RNA, Messenger/analysis/genetics ; *ras Proteins
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    The effect of posttranslational modifications on the interaction of Ras2 with adenylyl cyclase (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-01-29
    Description: Ras proteins undergo a series of posttranslational modifications that are critical for their cellular function. These modifications are necessary to anchor Ras proteins to the membrane. Yeast Ras2 proteins were purified with various degrees of modification and examined for their ability to activate their effector, adenylyl cyclase. The farnesylated intermediate form of Ras2 had more than 100 times higher affinity for adenylyl cyclase than for the unprocessed form. The subsequent palmitoylation reaction had little effect. In contrast, palmitoylation was required for efficient membrane localization of the Ras2 protein. These results indicate the importance of farnesylation in the interaction of Ras2 with its effector.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kuroda, Y -- Suzuki, N -- Kataoka, T -- New York, N.Y. -- Science. 1993 Jan 29;259(5095):683-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, Kobe University School of Medicine, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8430318" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/genetics/isolation & purification/*metabolism ; Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Cell Membrane/enzymology ; Electrophoresis, Polyacrylamide Gel ; Enzyme Activation ; Fungal Proteins/genetics/isolation & purification/*metabolism ; GTP-Binding Proteins/genetics/*metabolism ; Genes, Fungal ; Guanosine 5'-O-(3-Thiotriphosphate)/metabolism ; Insects ; Kinetics ; Molecular Sequence Data ; Molecular Weight ; Oligodeoxyribonucleotides ; Palmitic Acid ; Palmitic Acids/metabolism ; Protein Binding ; *Protein Processing, Post-Translational ; Recombinant Fusion Proteins/isolation & purification/metabolism ; Saccharomyces cerevisiae/genetics/*metabolism ; *Saccharomyces cerevisiae Proteins ; Transfection ; *ras Proteins
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    Inhibition of neural crest cell attachment by integrin antisense oligonucleotides (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-01-29
    Description: Neural crest cell interactions with extracellular matrix molecules were analyzed with the use of antisense oligonucleotides to block synthesis of integrin subunits. When added to the culture medium of quail neural crest cells, selected antisense phosphorothiol oligonucleotides reduced the amounts of cell surface alpha 1 or beta 1 integrin subunits by up to 95 percent and inhibited neural crest cell attachment to laminin or fibronectin substrata. Differential effects on specific alpha integrins were noted after treatment with alpha-specific oligonucleotides. Cells recovered the ability to bind to substrata 8 to 16 hours after treatment with inhibitory oligonucleotides. The operation of at least three distinct alpha integrin subunits is indicated by substratum-selective inhibition of cell attachment.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lallier, T -- Bronner-Fraser, M -- 15527/PHS HHS/ -- New York, N.Y. -- Science. 1993 Jan 29;259(5095):692-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Developmental Biology Center, University of California, Irvine 92717.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8430321" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Cell Adhesion/*drug effects ; Chickens ; Dose-Response Relationship, Drug ; Humans ; Integrins/biosynthesis/*genetics/isolation & purification ; Kinetics ; Macromolecular Substances ; Molecular Sequence Data ; Neural Crest/cytology/drug effects/*physiology ; Oligonucleotides, Antisense/*pharmacology ; Rats ; Structure-Activity Relationship
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    Detection of transient protein folding populations by mass spectrometry (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-11-05
    Description: Hydrogen-deuterium exchange measurements are becoming increasingly important in studies of the dynamics of protein molecules and, particularly, of their folding behavior. Electrospray ionization mass spectrometry (ESI-MS) has been used to obtain the distribution of masses within a population of protein molecules that had undergone hydrogen exchange in solution. This information is complementary to that from nuclear magnetic resonance spectroscopy (NMR) experiments, which measure the average occupancy of individual sites over the distribution of protein molecules. In experiments with hen lysozyme, a combination of ESI-MS and NMR was used to distinguish between alternative mechanisms of hydrogen exchange, providing insight into the nature and populations of transient folding intermediates. These results have helped to detail the pathways available to a protein during refolding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miranker, A -- Robinson, C V -- Radford, S E -- Aplin, R T -- Dobson, C M -- New York, N.Y. -- Science. 1993 Nov 5;262(5135):896-900.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Oxford Centre for Molecular Sciences, Oxford University, United Kingdom.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8235611" target="_blank"〉PubMed〈/a〉
    Keywords: Hydrogen/chemistry ; Hydrogen-Ion Concentration ; Kinetics ; Magnetic Resonance Spectroscopy ; Mass Spectrometry ; Models, Chemical ; Muramidase/*chemistry ; *Protein Folding ; Temperature
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    Database contamination (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-04-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mistry, A -- Greenlee, R -- Fong, K -- New York, N.Y. -- Science. 1993 Apr 30;260(5108):605-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8480169" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cloning, Molecular ; *Dna ; DNA Probes ; Databases, Factual ; *Gene Library ; Quality Control ; RNA, Fungal/genetics ; RNA, Transfer/genetics
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    Tyrosine phosphorylation of actin in Dictyostelium associated with cell-shape changes (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-01-08
    Description: When Dictyostelium cells that have initiated their developmental program upon starvation are returned to growth medium, there is a rapid and transient de novo tyrosine phosphorylation of a 43-kilodalton protein. This protein was found to be actin. Most of the phosphorylation occurred in a single, minor acidic isoform of actin. Developing cells that had been returned to growth medium lost their pseudopod extensions, became round, and had reduced adhesion to the substratum. These effects occurred with kinetics that matched the increase in tyrosine phosphorylation of actin. In mutant cell lines in which the gene for the phosphotyrosine phosphatase PTP1 had been disrupted, tyrosine phosphorylation of actin was rapid and more prolonged. These cells responded with proportionally accelerated kinetics of cell rounding. Cell lines overexpressing PTP1 had diminished amplitude and duration of actin tyrosine phosphorylation and exhibited diminished cell-shape change and an accelerated return to the extended cell-shape morphology seen in starved cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Howard, P K -- Sefton, B M -- Firtel, R A -- New York, N.Y. -- Science. 1993 Jan 8;259(5092):241-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, 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/7678470" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/*metabolism ; Animals ; Cell Adhesion ; Cell Membrane/metabolism ; Dictyostelium/*cytology/growth & development/*metabolism ; Immunoblotting ; Immunosorbent Techniques ; Kinetics ; Phosphotyrosine ; Tyrosine/*analogs & derivatives/metabolism
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    Phosphatidylinositol 4-kinase: gene structure and requirement for yeast cell viability (1993)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1993-11-26
    Description: Phosphatidylinositol (PtdIns) 4-kinase catalyzes the first step in the biosynthesis of PtdIns-4,5-bisphosphate (PtdIns[4,5]P2). Hydrolysis of PtdIns[4,5]P2 in response to extracellular stimuli is thought to initiate intracellular signaling cascades that modulate cell proliferation and differentiation. The PIK1 gene encoding a PtdIns 4-kinase from the yeast Saccharomyces cerevisiae was isolated by polymerase chain reaction (PCR) with oligonucleotides based on the sequence of peptides derived from the purified enzyme. The sequence of the PIK1 gene product bears similarities to that of PtdIns 3-kinases from mammals (p110) and yeast (Vps34p). Expression of PIK1 from a multicopy plasmid elevated PtdIns 4-kinase activity and enhanced the response to mating pheromone. A pik1 null mutant was inviable, indicating that PtdIns4P and presumably PtdIns[4,5]P2 are indispensable phospholipids.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Flanagan, C A -- Schnieders, E A -- Emerick, A W -- Kunisawa, R -- Admon, A -- Thorner, J -- CA09041/CA/NCI NIH HHS/ -- GM07232/GM/NIGMS NIH HHS/ -- GM21841/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1993 Nov 26;262(5138):1444-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8248783" target="_blank"〉PubMed〈/a〉
    Keywords: 1-Phosphatidylinositol 4-Kinase ; Amino Acid Sequence ; Cloning, Molecular ; Gene Expression ; *Genes, Fungal ; Molecular Sequence Data ; Molecular Weight ; Mutation ; Phosphatidylinositol 4,5-Diphosphate ; Phosphatidylinositol Phosphates/metabolism ; Phosphotransferases (Alcohol Group Acceptor)/biosynthesis/chemistry/*genetics ; Polymerase Chain Reaction ; Saccharomyces cerevisiae/enzymology/*genetics/growth & development ; *Saccharomyces cerevisiae Proteins
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    The cloning of PIG-A, a component in the early step of GPI-anchor biosynthesis (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-02-26
    Description: The glycosylphosphatidylinositol (GPI) anchor is a membrane attachment structure of many proteins and occurs in a wide variety of eukaryotes from yeasts to mammals. The structure of the core of the GPI anchor is conserved in protozoa and mammals and so is its biosynthetic pathway. A complementary DNA encoding a human protein termed PIG-A (phosphatidylinositol glycan-class A) was cloned. PIG-A was necessary for synthesis of N-acetylglucosaminyl-phosphatidylinositol, the very early intermediate in GPI-anchor biosynthesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miyata, T -- Takeda, J -- Iida, Y -- Yamada, N -- Inoue, N -- Takahashi, M -- Maeda, K -- Kitani, T -- Kinoshita, T -- New York, N.Y. -- Science. 1993 Feb 26;259(5099):1318-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunoregulation, Osaka University, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7680492" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD/metabolism ; Antigens, CD55 ; Antigens, CD59 ; Antigens, Surface/metabolism ; Antigens, Thy-1 ; Cloning, Molecular ; DNA/genetics ; Genetic Complementation Test ; Glycosylphosphatidylinositols/*biosynthesis ; HeLa Cells ; Humans ; In Vitro Techniques ; Membrane Glycoproteins/metabolism ; Membrane Proteins/*genetics/metabolism ; Mice ; Molecular Sequence Data ; Solubility ; Species Specificity
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    Controlling chemical reactivity with antibodies (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-04-16
    Description: The remarkable specificity of an antibody molecule has been used to accomplish highly selective functional group transformations not attainable by current chemical methods. An antibody raised against an amine-oxide hapten catalyzes the reduction of a diketone to a hydroxyketone with greater than 75:1 regioselectivity for one of two nearly equivalent ketone moieties. The antibody-catalyzed reaction is highly stereoselective, affording the hydroxyketone in high enantiomeric excess. Similarly, the reduction of ketones containing branched and aryl substituents, including the highly symmetrical 1-nitrophenyl-3-phenyl-2-propanone, was enantioselective. The simple strategy presented herein may find general applicability to the regio- and stereoselective reduction of a broad range of compounds.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hsieh, L C -- Yonkovich, S -- Kochersperger, L -- Schultz, P G -- New York, N.Y. -- Science. 1993 Apr 16;260(5106):337-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10049109" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Catalytic/*chemistry ; Antibodies, Monoclonal/chemistry ; Haptens ; Ketones/*chemistry ; Kinetics ; Oxidation-Reduction ; Propiophenones/chemistry ; Stereoisomerism
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    Inhibition of an in vivo antigen-specific IgE response by antibodies to CD23 (1993)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1993-08-20
    Description: Immunoglobulin E (IgE) mediates many allergic responses. CD23 is a 45-kilodalton type II transmembrane glycoprotein expressed in many cell types. It is a low-affinity IgE receptor and interacts specifically with CD21, thereby modulating IgE production by B lymphocytes in vitro. In an in vivo model of an allergen-specific IgE response, administration of a rabbit polyclonal antibody to recombinant human truncated CD23 resulted in up to 90 percent inhibition of ovalbumin-specific IgE synthesis. Both Fabs and intact IgG inhibited IgE production in vitro and in vivo. Thus, CD23 participates in the regulation of IgE synthesis in vivo and so could be important in allergic disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Flores-Romo, L -- Shields, J -- Humbert, Y -- Graber, P -- Aubry, J P -- Gauchat, J F -- Ayala, G -- Allet, B -- Chavez, M -- Bazin, H -- New York, N.Y. -- Science. 1993 Aug 20;261(5124):1038-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Glaxo Institute for Molecular Biology, Geneva, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8351517" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies/*immunology ; B-Lymphocytes/immunology ; Cloning, Molecular ; Humans ; Immunization ; Immunoglobulin E/*biosynthesis ; Molecular Sequence Data ; Ovalbumin/immunology ; Rabbits ; Rats ; Receptors, Complement 3d/immunology ; Receptors, IgE/analysis/*immunology ; Recombinant Proteins/immunology ; Virulence Factors, Bordetella/immunology
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    Diverse migratory pathways in the developing cerebral cortex (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-10-09
    Description: During early development of the mammalian cerebral cortex, young neurons migrate outward from the site of their final mitosis in the ventricular zone into the cortical plate, where they form the adult cortex. Time-lapse confocal microscopy was used to observe directly the dynamic behaviors of migrating cells in living slices of developing cortex. The majority of cells migrated along a radial pathway, consistent with the view that cortical neurons migrate along radial glial fibers. A fraction of cells, however, turned within the intermediate zone and migrated orthogonal to the radial fibers. This orthogonal migration may contribute to the tangential dispersion of clonally related cortical neurons.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉O'Rourke, N A -- Dailey, M E -- Smith, S J -- McConnell, S K -- EY06314/EY/NEI NIH HHS/ -- NS09027/NS/NINDS NIH HHS/ -- NS28587/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1992 Oct 9;258(5080):299-302.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Stanford University, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1411527" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal ; Carbocyanines ; Cell Movement ; Cerebral Cortex/cytology/*growth & development ; Culture Techniques ; Ferrets ; Fluorescent Dyes ; Immunohistochemistry ; Kinetics ; Lasers ; Microscopy ; Neurons/*physiology ; Vimentin/immunology
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  • 140
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    Cooperativity induced by a single mutation at the subunit interface of a dimeric enzyme: glutathione reductase (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-11-13
    Description: When glycine418 of Escherichia coli glutathione reductase, which is in a closely packed region of the dimer interface, is replaced with a bulky tryptophan residue, the enzyme becomes highly cooperative (Hill coefficient 1.76) for glutathione binding. The cooperativity is lost when the mutant subunit is hybridized with a wild-type subunit to create a heterodimer. The mutation appears to disrupt atomic packing at the dimer interface, which induces a change of kinetic mechanism. A single mutation in a region of the protein remote from the active site can thus act as a molecular switch to confer cooperativity on an enzyme.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scrutton, N S -- Deonarain, M P -- Berry, A -- Perham, R N -- New York, N.Y. -- Science. 1992 Nov 13;258(5085):1140-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Cambridge, United Kingdom.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1439821" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Escherichia coli/*enzymology/genetics ; Genes, Bacterial ; Glutathione/metabolism ; Glutathione Reductase/*chemistry/genetics/metabolism ; Glycine/chemistry ; Kinetics ; Macromolecular Substances ; Models, Molecular ; Molecular Sequence Data ; Molecular Structure ; *Mutagenesis, Site-Directed ; NADP/metabolism ; Plasmids ; Protein Multimerization ; Tryptophan/chemistry
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  • 141
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    Reductase activity encoded by the HM1 disease resistance gene in maize (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-11-06
    Description: The HM1 gene in maize controls both race-specific resistance to the fungus Cochliobolus carbonum race 1 and expression of the NADPH (reduced form of nicotinamide adenine dinucleotide phosphate)-dependent HC toxin reductase (HCTR), which inactivates HC toxin, a cyclic tetrapeptide produced by the fungus to permit infection. Several HM1 alleles were generated and cloned by transposon-induced mutagenesis. The sequence of wild-type HM1 shares homology with dihydroflavonol-4-reductase genes from maize, petunia, and snap-dragon. Sequence homology is greatest in the beta alpha beta-dinucleotide binding fold that is conserved among NADPH- and NADH (reduced form of nicotinamide adenine dinucleotide)-dependent reductases and dehydrogenases. This indicates that HM1 encodes HCTR.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Johal, G S -- Briggs, S P -- New York, N.Y. -- Science. 1992 Nov 6;258(5084):985-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biotechnology Research, Pioneer Hi-Bred International, Inc., Johnston, IA 50131.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1359642" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Blotting, Southern ; Cloning, Molecular ; DNA/chemistry/genetics ; *Genes, Plant ; *Helminthosporium ; Introns ; Molecular Sequence Data ; NADP/pharmacology ; Nucleic Acid Hybridization ; Oxidoreductases/chemistry/*genetics ; Peptides, Cyclic/antagonists & inhibitors ; *Plant Diseases ; *Plant Proteins ; Polymorphism, Restriction Fragment Length ; RNA Splicing ; RNA, Messenger/genetics ; Zea mays/enzymology/*genetics
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  • 142
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    Diacylglycerol-stimulated formation of actin nucleation sites at plasma membranes (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-04-10
    Description: Diacylglycerols, which are generated during phospholipase-catalyzed hydrolysis of phospholipids, stimulated actin polymerization in the presence of highly purified plasma membranes from the cellular slime mold Dictyostelium discoideum. The increased rate of actin polymerization apparently resulted from de novo formation of actin nucleation sites rather than uncapping of existing filament ends, because the membranes lacked detectable endogenous actin. The increased actin nucleation was mediated by a peripheral membrane component other than protein kinase C, the classical target of diacylglycerol action. These results indicate that diacylglycerols increase actin nucleation at plasma membranes and suggest a mechanism whereby signal transduction pathways may control cytoskeletal assembly.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shariff, A -- Luna, E J -- GM-33048/GM/NIGMS NIH HHS/ -- R01 GM033048/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Apr 10;256(5054):245-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology Group, Worcester Foundation for Experimental Biology, Shresbury, MA 01545.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1373523" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/*metabolism ; Alkaloids/pharmacology ; Animals ; Calcium/pharmacology ; Cell Membrane/drug effects/*metabolism ; Dictyostelium/*metabolism ; Diglycerides/*pharmacology ; Kinetics ; Macromolecular Substances ; *Naphthalenes ; Polycyclic Compounds/pharmacology ; Protein Kinase C/antagonists & inhibitors ; Staurosporine ; Tetradecanoylphorbol Acetate/pharmacology ; Time Factors
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  • 143
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    DNA hydrolyzing autoantibodies (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-05-01
    Description: A DNA-nicking activity was detected in the sera of patients with various autoimmune pathologies and was shown to be a property of autoantibodies. The DNA hydrolyzing activity, which was purified by affinity and high-performance liquid chromatography, corresponded in size to immunoglobulin M (IgM) and IgG and had a positive response to antibodies to human IgG. The DNA hydrolyzing autoantibodies were stable to acid shock and yielded a DNA degradation pattern that was different from that of deoxyribonuclease (DNase) I and blood DNase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shuster, A M -- Gololobov, G V -- Kvashuk, O A -- Bogomolova, A E -- Smirnov, I V -- Gabibov, A G -- New York, N.Y. -- Science. 1992 May 1;256(5057):665-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉V.A. Engelhardt Institute of Molecular Biology, Academy of Sciences of Russia, Moscow.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1585181" target="_blank"〉PubMed〈/a〉
    Keywords: Acetates/pharmacology ; Acetic Acid ; Autoantibodies/isolation & purification/*metabolism ; Autoimmune Diseases/*metabolism ; Chromatography, High Pressure Liquid ; DNA/*metabolism ; DNA Polymerase I/metabolism ; Deoxyribonuclease I/metabolism ; Electrophoresis, Agar Gel ; Humans ; Immunoglobulin G/isolation & purification/metabolism ; Immunoglobulin M/isolation & purification/metabolism ; Kinetics ; Lupus Erythematosus, Systemic/immunology ; Plasmids
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    The fms-like tyrosine kinase, a receptor for vascular endothelial growth factor (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-02-21
    Description: The fms-like tyrosine kinase (Flt) is a transmembrane receptor in the tyrosine kinase family. Expression of flt complementary DNA in COS cells conferred specific, high-affinity binding of vascular endothelial growth factor, also known as vascular permeability factor (VEGF-VPF), a factor that induces vascular permeability when injected in the guinea pig skin and stimulates endothelial cell proliferation. Expression of Flt in Xenopus laevis oocytes caused the oocytes to release calcium in response to VEGF-VPF. These findings show that flt encodes a receptor for VEGF-VPF.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉de Vries, C -- Escobedo, J A -- Ueno, H -- Houck, K -- Ferrara, N -- Williams, L T -- P01 HL-43821/HL/NHLBI NIH HHS/ -- R01 HL-32898/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1992 Feb 21;255(5047):989-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1312256" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; Cross-Linking Reagents ; Endothelial Growth Factors/*physiology ; Enzyme Activation ; Humans ; In Vitro Techniques ; Lymphokines/*physiology ; Proto-Oncogene Proteins/genetics/*physiology ; Receptors, Cell Surface/*genetics ; Signal Transduction ; Transfection ; Vascular Endothelial Growth Factor A ; Vascular Endothelial Growth Factor Receptor-1 ; Vascular Endothelial Growth Factors ; Xenopus laevis
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    Cloning and expression in yeast of a plant potassium ion transport system (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-05-01
    Description: A membrane polypeptide involved in K+ transport in a higher plant was cloned by complementation of a yeast mutant defective in K+ uptake with a complementary DNA library from Arabidopsis thaliana. A 2.65-kilobase complementary DNA conferred ability to grow on media with K+ concentration in the micromolar range and to absorb K+ (or 86Rb+) at rates similar to those in wild-type yeast. The predicted amino acid sequence (838 amino acids) has three domains: a channel-forming region homologous to animal K+ channels, a cyclic nucleotide-binding site, and an ankyrin-like region.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sentenac, H -- Bonneaud, N -- Minet, M -- Lacroute, F -- Salmon, J M -- Gaymard, F -- Grignon, C -- New York, N.Y. -- Science. 1992 May 1;256(5057):663-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Biochimie et Physiologie Vegetales, ENSA-M/INRA/CNRS URA 573, Montpellier, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1585180" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Arabidopsis Proteins ; Biological Transport ; Blotting, Southern ; Carrier Proteins/chemistry/genetics ; *Cloning, Molecular ; DNA/genetics ; Deoxyribonuclease EcoRI ; Gene Expression ; Kinetics ; Molecular Sequence Data ; Plant Proteins/chemistry/*genetics ; Plants/*genetics ; Potassium/*metabolism ; Potassium Channels/chemistry/*genetics ; Saccharomyces cerevisiae/*genetics ; Sequence Homology, Nucleic Acid
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  • 146
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    Pseudo--half-knot formation with RNA (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-08-14
    Description: A pseudo--half-knot can be formed by binding an oligonucleotide asymmetrically to an RNA hairpin loop. This binding motif was used to target the human immunodeficiency virus TAR element, an important viral RNA structure that is the receptor for Tat, the major viral transactivator protein. Oligonucleotides complementary to different halves of the TAR structure bound with greater affinity than molecules designed to bind symmetrically around the hairpin. The pseudo--half-knot--forming oligonucleotides altered the TAR structure so that specific recognition and binding of a Tat-derived peptide was disrupted. This general binding motif may be used to disrupt the structure of regulatory RNA hairpins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ecker, D J -- Vickers, T A -- Bruice, T W -- Freier, S M -- Jenison, R D -- Manoharan, M -- Zounes, M -- New York, N.Y. -- Science. 1992 Aug 14;257(5072):958-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉ISIS Pharmaceuticals, Carlsbad, CA 92008.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1502560" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; DNA, Viral/metabolism ; Gene Products, tat/metabolism ; HIV/*genetics ; Kinetics ; Molecular Sequence Data ; *Nucleic Acid Conformation ; Oligoribonucleotides/*chemistry ; RNA, Viral/*chemistry/genetics/metabolism ; tat Gene Products, Human Immunodeficiency Virus
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  • 147
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    G protein activation of a hormone-stimulated phosphatase in human tumor cells (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-05-22
    Description: The growth-inhibiting peptide hormone somatostatin stimulates phosphotyrosine phosphatase activity in the human pancreatic cell line MIA PaCa-2. This hormonal activation was mediated by a pertussis toxin-sensitive guanosine 5'-triphosphate-binding protein (G protein) in the membranes of these cells. Activation of this G protein by somatostatin stimulated the dephosphorylation of exogenous epidermal growth factor receptor prepared from A-431 cells in vitro. This pathway may mediate the antineoplastic action of somatostatin in these cells and in human tumors and could represent a general mechanism of G protein coupling that is utilized by normal cells in the hormonal control of cell growth.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pan, M G -- Florio, T -- Stork, P J -- New York, N.Y. -- Science. 1992 May 22;256(5060):1215-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vollum Institute for Advanced Biomedical Research, Oregon Health Sciences University, Portland 97201.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1350382" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Carcinoma, Squamous Cell ; Cell Line ; Cell Membrane/metabolism ; Dose-Response Relationship, Drug ; Enzyme Activation ; GTP-Binding Proteins/*metabolism ; Guanosine 5'-O-(3-Thiotriphosphate)/pharmacology ; Guanosine Diphosphate/analogs & derivatives/pharmacology ; Humans ; Kinetics ; Pancreatic Neoplasms ; Peptides/metabolism ; Pertussis Toxin ; Phosphorylation ; Protein Kinases/metabolism ; Protein Tyrosine Phosphatases/*metabolism ; Receptor, Epidermal Growth Factor/metabolism ; Somatostatin/*pharmacology ; Thionucleotides/pharmacology ; Virulence Factors, Bordetella/pharmacology
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  • 148
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    Spatial control of the gap gene knirps in the Drosophila embryo by posterior morphogen system (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-02-21
    Description: The gap genes of Drosophila are the first zygotic genes to respond to the maternal positional signals and establish the body pattern along the anterior-posterior axis. The gap gene knirps, required for patterning in the posterior region of the embryo, can be activated throughout the wild-type embryo and is normally repressed from the anterior and posterior sides. These results provide direct molecular evidence that the posterior morphogen system interacts in a fundamentally different manner than do hunchback and bicoid, which are responsible for anterior pattern formation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pankratz, M J -- Busch, M -- Hoch, M -- Seifert, E -- Jackle, H -- New York, N.Y. -- Science. 1992 Feb 21;255(5047):986-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max-Planck Institut fur Biophysikalische Chemie, Abteilung Molekulare Entwicklungsbiologie, Gottingen, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1546296" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites ; Cloning, Molecular ; Drosophila melanogaster/embryology/*genetics ; Gene Expression Regulation ; Genes ; Molecular Sequence Data ; Morphogenesis ; Regulatory Sequences, Nucleic Acid
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    Dimerization of a specific DNA-binding protein on the DNA (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-01-10
    Description: Many specific DNA-binding proteins bind to sites with dyad symmetry, and the bound form of the protein is a dimer. For some proteins, dimers form in solution and bind to DNA. LexA repressor of Escherichia coli has been used to test an alternative binding model in which two monomers bind sequentially. This model predicts that a repressor monomer should bind with high specificity to an isolated operator half-site. Monomer binding to a half-site was observed. A second monomer bound to an intact operator far more tightly than the first monomer; this cooperativity arose from protein-protein contacts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kim, B -- Little, J W -- GM24178/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Jan 10;255(5041):203-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Arizona, Tucson 85721.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1553548" target="_blank"〉PubMed〈/a〉
    Keywords: Bacterial Proteins/*metabolism ; Base Sequence ; Binding Sites ; DNA, Bacterial/*metabolism ; DNA-Binding Proteins/*metabolism ; Deoxyribonucleases ; Escherichia coli/*metabolism ; Kinetics ; Macromolecular Substances ; Models, Structural ; Molecular Sequence Data ; Oligodeoxyribonucleotides/metabolism ; Operon ; Rec A Recombinases/genetics ; Repressor Proteins/metabolism ; *Serine Endopeptidases
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    Isolation of two genes that encode subunits of the yeast transcription factor IIA (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-02-28
    Description: The yeast transcription factor IIA (TFIIA), a component of the basal transcription machinery of RNA polymerase II and implicated in vitro in regulation of basal transcription, is composed of two subunits of 32 and 13.5 kilodaltons. The genes that encode these subunits, termed TOA1 and TOA2, respectively, were cloned. Neither gene shares obvious sequence similarity with the other or with any other previously identified genes. The recombinant factor bound to a TATA binding protein-DNA complex and complemented yeast and mammalian in vitro transcription systems depleted of TFIIA. Both the TOA1 and TOA2 genes are essential for growth of yeast.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ranish, J A -- Lane, W S -- Hahn, S -- New York, N.Y. -- Science. 1992 Feb 28;255(5048):1127-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Fred Hutchinson Cancer Research Center, Seattle, WA 98104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1546313" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Cloning, Molecular ; DNA Mutational Analysis ; DNA-Binding Proteins/genetics ; *Genes, Fungal ; Molecular Sequence Data ; Recombinant Proteins/metabolism ; Saccharomyces cerevisiae/*genetics ; *Saccharomyces cerevisiae Proteins ; Transcription Factor TFIIA ; Transcription Factors/*genetics ; Transcription, Genetic
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    Identification of a protein that binds to the SH3 region of Abl and is similar to Bcr and GAP-rho (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-07
    Description: A Src homology 3 (SH3) region is a sequence of approximately 50 amino acids found in many nonreceptor tyrosine kinases and other proteins. Deletion of the SH3 region from the protein encoded by the c-abl proto-oncogene activates the protein's transforming capacity, thereby suggesting the participation of the SH3 region in the negative regulation of transformation. A complementary DNA was isolated that encoded a protein, 3BP-1, to which the SH3 region of Abl bound with high specificity and to which SH3 regions from other proteins bound differentially. The sequence of the 3BP-1 protein is similar to that of a COOH-terminal segment of Bcr and to guanosine triphosphatase-activating protein (GAP)-rho, which suggests that it might have GAP activity for Ras-related proteins. The 3BP-1 protein may therefore be a mediator of SH3 function in transformation inhibition and may link tyrosine kinases to Ras-related proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cicchetti, P -- Mayer, B J -- Thiel, G -- Baltimore, D -- A107233/PHS HHS/ -- CA 08875/CA/NCI NIH HHS/ -- CA51462/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 Aug 7;257(5071):803-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Rockefeller University, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1379745" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Amino Acid Sequence ; Animals ; Binding Sites ; Chimera ; Cloning, Molecular ; GTPase-Activating Proteins ; Gene Library ; *Genes, abl ; *Genes, src ; Glutathione Transferase/genetics/metabolism ; Mice ; Molecular Sequence Data ; Oncogene Proteins/genetics/*metabolism ; Plasmids ; Polymerase Chain Reaction/methods ; Prosencephalon/physiology ; Protein-Tyrosine Kinases/*metabolism ; Proteins/*metabolism ; *Proto-Oncogene Proteins ; Proto-Oncogene Proteins c-abl/genetics/*metabolism ; Proto-Oncogene Proteins c-bcr ; Proto-Oncogene Proteins pp60(c-src)/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Restriction Mapping ; Rho Factor/*metabolism ; Sequence Homology, Nucleic Acid ; ras GTPase-Activating Proteins
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    Converting trypsin to chymotrypsin: the role of surface loops (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-03-06
    Description: Trypsin (Tr) and chymotrypsin (Ch) have similar tertiary structures, yet Tr cleaves peptides at arginine and lysine residues and Ch prefers large hydrophobic residues. Although replacement of the S1 binding site of Tr with the analogous residues of Ch is sufficient to transfer Ch specificity for ester hydrolysis, specificity for amide hydrolysis is not transferred. Trypsin is converted to a Ch-like protease when the binding pocket alterations are further modified by exchange of the Ch surface loops 185 through 188 and 221 through 225 for the analogous Tr loops. These loops are not structural components of either the S1 binding site or the extended substrate binding sites. This mutant enzyme is equivalent to Ch in its catalytic rate, but its substrate binding is impaired. Like Ch, this mutant utilizes extended substrate binding to accelerate catalysis, and substrate discrimination occurs during the acylation step rather than in substrate binding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hedstrom, L -- Szilagyi, L -- Rutter, W J -- DK21344/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1992 Mar 6;255(5049):1249-53.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Hormone Research Institute, University of California, San Francisco 94143-0534.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1546324" target="_blank"〉PubMed〈/a〉
    Keywords: Acylation ; Amino Acid Sequence ; Base Sequence ; Binding Sites ; Chymotrypsin/*chemistry/metabolism ; Hydrolysis ; Kinetics ; Models, Molecular ; Molecular Sequence Data ; Molecular Structure ; Mutagenesis, Site-Directed ; Protein Conformation ; Substrate Specificity ; Trypsin/*chemistry/genetics/metabolism
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    Removal of nonhomologous DNA ends in double-strand break recombination: the role of the yeast ultraviolet repair gene RAD1 (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-10-16
    Description: Double-strand breaks (DSBs) in Saccharomyces cerevisiae can be repaired by gene conversions or by deletions resulting from single-strand annealing between direct repeats of homologous sequences. Although rad1 mutants are resistant to x-rays and can complete DSB-mediated mating-type switching, they could not complete recombination when the ends of the break contained approximately 60 base pairs of nonhomology. Recombination was restored when the ends of the break were made homologous to donor sequences. Additionally, the absence of RAD1 led to the frequent appearance of a previously unobserved type of recombination product. These data suggest RAD1 is required to remove nonhomologous DNA from the 3' ends of recombining DNA, a process analogous to the excision of photodimers during repair of ultraviolet-damaged DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fishman-Lobell, J -- Haber, J E -- GM01722/GM/NIGMS NIH HHS/ -- GM20056/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Oct 16;258(5081):480-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Rosenstiel Basic Medical Sciences Research Center, Brandeis University, Waltham, MA 02254.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1411547" target="_blank"〉PubMed〈/a〉
    Keywords: *DNA Repair ; DNA, Fungal/genetics ; Deoxyribonucleases, Type II Site-Specific/*metabolism ; Gene Conversion ; Kinetics ; *Recombination, Genetic ; Saccharomyces cerevisiae/*genetics ; Saccharomyces cerevisiae Proteins ; Sequence Deletion ; Ultraviolet Rays
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  • 154
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    Molecular cloning of the interleukin-1 beta converting enzyme (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-04-03
    Description: Interleukin-1 beta (IL-1 beta) mediates a wide range of immune and inflammatory responses. The active cytokine is generated by proteolytic cleavage of an inactive precursor. A complementary DNA encoding a protease that carries out this cleavage has been cloned. Recombinant expression in COS-7 cells enabled the cells to process precursor IL-1 beta to the mature form. Sequence analysis indicated that the enzyme itself may undergo proteolytic processing. The gene encoding the protease was mapped to chromosomal band 11q23, a site frequently involved in rearrangement in human cancers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cerretti, D P -- Kozlosky, C J -- Mosley, B -- Nelson, N -- Van Ness, K -- Greenstreet, T A -- March, C J -- Kronheim, S R -- Druck, T -- Cannizzaro, L A -- New York, N.Y. -- Science. 1992 Apr 3;256(5053):97-100.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Immunex Corporation, Seattle, WA 98101.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1373520" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Caspase 1 ; Cell Line ; Chromosome Banding ; *Chromosomes, Human, Pair 11 ; Cloning, Molecular ; Enzyme Precursors/biosynthesis/*genetics/isolation & purification ; Humans ; Metalloendopeptidases/biosynthesis/*genetics/isolation & purification ; Molecular Sequence Data ; Neutrophils/enzymology ; Oligodeoxyribonucleotides ; Poly A/genetics/isolation & purification ; Polymerase Chain Reaction/methods ; RNA/genetics/isolation & purification ; RNA, Messenger/genetics ; Recombinant Proteins/biosynthesis/isolation & purification ; Transfection
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 155
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    Regulatory elements that control the lineage-specific expression of myoD (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-05-04
    Description: The molecular basis of skeletal muscle lineage determination was investigated by analyzing DNA control elements that regulate the myogenic determination gene myoD. A distal enhancer was identified that positively regulates expression of the human myoD gene. The myoD enhancer and promoter were active in myogenic and several nonmyogenic cell lines. In transgenic mouse embryos, however, the myoD enhancer and promoter together directed expression of a lacZ transgene specifically to the skeletal muscle lineage. These data suggest that during development myoD is regulated by mechanisms that restrict accessibility of myoD control elements to positive trans-acting factors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goldhamer, D J -- Faerman, A -- Shani, M -- Emerson, C P Jr -- CA-06927/CA/NCI NIH HHS/ -- HD-07796/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1992 Apr 24;256(5056):538-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Cancer Research, Fox Chase Cancer Center, Philadelphia, PA 19111.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1315077" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation ; Cell Line ; Chloramphenicol O-Acetyltransferase/genetics ; Cloning, Molecular ; Enhancer Elements, Genetic ; *Gene Expression Regulation ; Humans ; Mice ; Mice, Transgenic ; Muscle Proteins/*genetics ; Muscles/embryology/metabolism ; MyoD Protein ; Promoter Regions, Genetic ; Transcription, Genetic ; Transfection ; Tumor Cells, Cultured ; beta-Galactosidase/genetics
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  • 156
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    Antibody-catalyzed rearrangement of the peptide bond (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-10-30
    Description: The generation of antibodies from a bifunctional cyclic phosphinate transition-state analog provided agents capable of efficiently catalyzing both steps of the overall conversion of a substrate containing an asparaginyl-glycyl sequence through a succinimide intermediate to the products aspartyl-glycyl and the rearranged isoaspartyl-glycyl sequence. This reaction provides a potential means in addition to amide cleavage for the deactivation of protein or peptide biological functions in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gibbs, R A -- Taylor, S -- Benkovic, S J -- New York, N.Y. -- Science. 1992 Oct 30;258(5083):803-5.〈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/1439788" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Catalytic/*metabolism ; Asparagine/metabolism ; Aspartic Acid/metabolism ; Chromatography, High Pressure Liquid ; Dipeptides/metabolism ; Glycine/metabolism ; Hydrogen-Ion Concentration ; Kinetics ; Peptides/chemistry/*metabolism ; Stereoisomerism ; Succinimides/metabolism
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    Awakenings ... UV light and HIV gene activation (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wallace, B M -- Lasker, J S -- New York, N.Y. -- Science. 1992 Aug 28;257(5074):1211-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1519057" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; DNA/radiation effects ; DNA Damage ; Gene Expression/*radiation effects ; Genes, Viral/*radiation effects ; HIV/*genetics ; HIV Long Terminal Repeat ; Humans ; Mice ; PUVA Therapy/adverse effects ; Sunlight/adverse effects ; Ultraviolet Rays/*adverse effects
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 158
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    Tertiary structure around the guanosine-binding site of the Tetrahymena ribozyme (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-04-24
    Description: A cleavage reagent directed to the active site of the Tetrahymena catalytic RNA was synthesized by derivatization of the guanosine substrate with a metal chelator. When complexed with iron(II), this reagent cleaved the RNA in five regions. Cleavage at adenosine 207, which is far from the guanosine-binding site in the primary and secondary structure, provides a constraint for the higher order folding of the RNA. This cleavage site constitutes physical evidence for a key feature of the Michel-Westhof model. Targeting a reactive entity to a specific site should be generally useful for determining proximity within folded RNA molecules or ribonucleoprotein complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, J F -- Cech, T R -- New York, N.Y. -- Science. 1992 Apr 24;256(5056):526-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309-0215.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1315076" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites ; Edetic Acid/metabolism ; Free Radicals ; Guanosine/*metabolism ; Guanosine Monophosphate/metabolism ; Iron/metabolism ; Iron Chelating Agents/metabolism ; Kinetics ; Models, Molecular ; Molecular Sequence Data ; Molecular Structure ; Nucleic Acid Conformation ; Pentetic Acid/metabolism ; RNA, Catalytic/*chemistry/metabolism ; Tetrahymena/*chemistry
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  • 159
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    GAP domains responsible for ras p21-dependent inhibition of muscarinic atrial K+ channel currents (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-01-10
    Description: The interaction between the low molecular weight G protein ras p21 and a guanosine triphosphatase activating protein (GAP) uncouples a heterotrimeric G protein (Gk) from muscarinic receptors. Through the use of isolated atrial cell membranes and genetically engineered GAP deletion mutants, the src homology regions (SH2-SH3) at the amino terminus of GAP have been identified as the domains responsible for this effect. Deletion of the domain required to stimulate the guanosine triphosphatase activity of ras p21 relieves the requirement for ras p21 in this system. A model is presented that suggests that ras p21 induces a conformational change in GAP, which allows the SH2-SH3 regions of GAP to function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Martin, G A -- Yatani, A -- Clark, R -- Conroy, L -- Polakis, P -- Brown, A M -- McCormick, F -- CA51992-01/CA/NCI NIH HHS/ -- HL36930/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1992 Jan 10;255(5041):192-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Cetus Corporation, Emeryville, CA 94608.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1553544" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Baculoviridae ; Cell Membrane/metabolism ; Cells, Cultured ; Cloning, Molecular ; GTP-Binding Proteins/*physiology ; GTPase-Activating Proteins ; Genetic Engineering ; Genetic Vectors ; Guanosine 5'-O-(3-Thiotriphosphate)/pharmacology ; Guanosine Triphosphate/pharmacology ; Guinea Pigs ; Heart/*physiology ; Heart Atria ; Models, Biological ; Polymerase Chain Reaction ; Potassium Channels/drug effects/*physiology ; Proteins/genetics/*physiology ; Proto-Oncogene Proteins p21(ras)/*metabolism ; Receptors, Muscarinic/drug effects/*physiology ; ras GTPase-Activating Proteins
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  • 160
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    Calcium-dependent transmitter secretion reconstituted in Xenopus oocytes: requirement for synaptophysin (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-07-31
    Description: Calcium-dependent glutamate secretion was reconstituted in Xenopus oocytes by injecting the oocyte with total rat cerebellar messenger RNA (mRNA). Co-injection of total mRNA with antisense oligonucleotides to synaptophysin message decreased the expression of synaptophysin in the oocyte and reduced the calcium-dependent secretion. A similar effect on secretion was observed for oocytes injected with total mRNA together with an antibody to rat synaptophysin. These results indicate that synaptophysin is necessary for transmitter secretion and that the oocyte expression system may be useful for dissecting the molecular events associated with the secretory process.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Alder, J -- Lu, B -- Valtorta, F -- Greengard, P -- Poo, M M -- MH 39327/MH/NIMH NIH HHS/ -- NS 22764/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1992 Jul 31;257(5070):657-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Columbia University, New York, NY 10027.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1353905" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Blotting, Western ; Calcimycin/pharmacology ; Calcium/*pharmacology ; Cerebellum/chemistry ; Fluorescent Antibody Technique ; Gene Expression ; Glutamates/*secretion ; Glutamic Acid ; Kinetics ; Liver/chemistry ; Microscopy, Immunoelectron ; Molecular Sequence Data ; Oligonucleotides, Antisense/pharmacology ; Oocytes/*physiology ; RNA, Messenger/genetics ; Rats ; Synaptophysin/genetics/*physiology ; Transfection ; Xenopus
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  • 161
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    Regulation of dynein-driven microtubule sliding by the radial spokes in flagella (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-09-11
    Description: The regulation of microtubule sliding in flagellar axonemes was studied with the use of Chlamydomonas mutants and in vitro assays. Microtubule sliding velocities were diminished in axonemes from mutant cells missing radial spoke structures but could be restored upon reconstitution with dynein from axonemes with wild-type radial spokes. These experiments demonstrate that the radial spokes activate dynein's microtubule sliding activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, E F -- Sale, W S -- GM 08367/GM/NIGMS NIH HHS/ -- HD 20497/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1992 Sep 11;257(5076):1557-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy and Cell Biology, Emory University School of Medicine, Atlanta, GA 30322.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1387971" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Movement ; Chlamydomonas/genetics/*physiology/ultrastructure ; Dyneins/genetics/*metabolism ; Flagella/*physiology/ultrastructure ; Kinetics ; Microscopy, Electron ; Microtubules/*physiology/ultrastructure
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    How technique is changing science (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-07-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hall, S S -- New York, N.Y. -- Science. 1992 Jul 17;257(5068):344-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1631556" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; DNA/analysis ; Drosophila/genetics ; Fiber Optic Technology ; Microscopy/methods ; Polymerase Chain Reaction ; Radioimmunoassay ; Research/instrumentation ; *Research Design
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    Participation of non-zinc finger residues in DNA binding by two nuclear orphan receptors (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-04-03
    Description: Steroid-thyroid hormone receptors typically bind as dimers to DNA sequences that contain repeated elements termed half-sites. NGFI-B, an early response protein and orphan member of this receptor superfamily, binds to a DNA sequence that contains only one half-site (5'-AAAGGTCA-3'). A domain separate from the NGFI-B zinc fingers, termed the A box, was identified and is required for recognition of the two adenine-thymidine (A-T) base pairs at the 5' end of the NGFI-B DNA binding element. In addition, a domain downstream of the zinc fingers of the orphan receptor H-2 region II binding protein, termed the T box, determined binding to tandem repeats of the estrogen receptor half-site (5'-AGGTCA-3').〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilson, T E -- Paulsen, R E -- Padgett, K A -- Milbrandt, J -- NS01018/NS/NINDS NIH HHS/ -- P01 CA49712/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 Apr 3;256(5053):107-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1314418" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; CHO Cells ; Cell Nucleus/*physiology ; Cricetinae ; DNA/*metabolism ; DNA-Binding Proteins/genetics/*metabolism ; Kinetics ; Mice ; Molecular Sequence Data ; Nuclear Receptor Subfamily 4, Group A, Member 1 ; Oligodeoxyribonucleotides/metabolism ; Polymerase Chain Reaction ; Receptors, Cell Surface/*metabolism ; Receptors, Cytoplasmic and Nuclear ; Receptors, Steroid ; Recombinant Fusion Proteins/metabolism ; Sequence Homology, Nucleic Acid ; Substrate Specificity ; Transcription Factors/genetics/*metabolism ; Transfection ; Zinc Fingers/genetics
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  • 164
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    Mechanism of DNA strand transfer reactions catalyzed by HIV-1 reverse transcriptase (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-11-13
    Description: Two DNA strand transfer reactions occur during retroviral reverse transcription. The mechanism of the first, minus strand strong-stop DNA, transfer has been studied in vitro with human immunodeficiency virus 1 reverse transcriptase (HIV-1 RT) and a model template-primer system derived from the HIV-1 genome. The results reveal that HIV-1 RT alone can catalyze DNA strand transfer reactions. Two kinetically distinct ribonuclease (RNase) H activities associated with HIV-1 RT are required for removal of RNA fragments annealed to the nascent DNA strand. Examination of the binding of DNA.RNA duplex and single-stranded RNA to HIV-1 RT during strand transfer supports a model where the enzyme accommodates both the acceptor RNA template and the nascent DNA strand before the transfer event is completed. The polymerase activity incorporated additional bases beyond the 5' end of the RNA template, resulting in a base misincorporation upon DNA strand transfer. Such a process occurring in vivo during retroviral homologous recombination could contribute to the hypermutability of the HIV-1 genome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Peliska, J A -- Benkovic, S J -- AI08275/AI/NIAID NIH HHS/ -- GM13306/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Nov 13;258(5085):1112-8.〈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/1279806" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Catalysis ; DNA, Viral/biosynthesis/chemistry/*metabolism ; Deoxyribonucleotides ; HIV Reverse Transcriptase ; HIV-1/*enzymology/genetics ; Kinetics ; Molecular Sequence Data ; Mutation ; Nucleic Acid Hybridization ; RNA, Transfer/metabolism ; RNA, Viral/chemistry/metabolism ; RNA-Directed DNA Polymerase/genetics/*metabolism ; Ribonuclease H/metabolism ; Templates, Genetic
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  • 165
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    High-efficiency expression and solubilization of functional T cell antigen receptor heterodimers (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-05-29
    Description: The T cell receptor (TCR) zeta chain was attached to the TCR alpha and beta extracellular domains to induce efficient expression of alpha beta heterodimers that can recognize complexes of antigen with major histocompatibility complex (MHC) molecules. Chimeric constructs expressed in RBL-2H3 cells were efficiently transported to the cell surface uniquely as disulfide-linked heterodimers. Transfectants were activated by specific antigen-MHC complexes, which demonstrated that the expressed alpha beta was functional and that CD3 was not required for antigen-MHC binding. Constructs with thrombin cleavage sites were efficiently cleaved to soluble disulfide-linked heterodimers. Thus, attachment of TCR zeta domains and protease cleavage sites to TCR alpha and beta induces expression of demonstrably functional heterodimers that can be solubilized.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Engel, I -- Ottenhoff, T H -- Klausner, R D -- New York, N.Y. -- Science. 1992 May 29;256(5061):1318-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1598575" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Cell Membrane/immunology ; Disulfides ; Flow Cytometry ; Histocompatibility Antigens/metabolism ; Kinetics ; Macromolecular Substances ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; Polymerase Chain Reaction ; Receptors, Antigen, T-Cell/genetics/isolation & purification/*metabolism ; Solubility ; Transfection
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  • 166
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    A surface protease and the invasive character of plague (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-11-06
    Description: A 9.5-kilobase plasmid of Yersinia pestis, the causative agent of plague, is required for high virulence when mice are inoculated with the bacterium by subcutaneous injection. Inactivation of the plasmid gene pla, which encodes a surface protease, increased the median lethal dose of the bacteria for mice by a millionfold. Moreover, cloned pla was sufficient to restore segregants lacking the entire pla-bearing plasmid to full virulence. Both pla+ strains injected subcutaneously and pla- mutants injected intravenously reached high titers in liver and spleen of infected mice, whereas pla- mutants injected subcutaneously failed to do so even though they establish a sustained local infection at the injection site. More inflammatory cells accumulated in lesions caused by the pla- mutants than in lesions produced by the pla+ parent. The Pla protease was shown to be a plasminogen activator with unusual kinetic properties. It can also cleave complement C3 at a specific site.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sodeinde, O A -- Subrahmanyam, Y V -- Stark, K -- Quan, T -- Bao, Y -- Goguen, J D -- AI22176/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1992 Nov 6;258(5084):1004-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics and Microbiology, University of Massachusetts Medical School, Worcester 01655.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1439793" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Bacterial Proteins ; Colony Count, Microbial ; Escherichia coli/enzymology ; Fibrinolysin/chemistry/metabolism ; Injections, Intravenous ; Kinetics ; Liver/microbiology ; Mice ; Molecular Sequence Data ; Mutation ; Plague/microbiology ; Plasmids ; Plasminogen Activators/genetics/*physiology ; Recombinant Proteins/metabolism ; Spleen/microbiology ; Tissue Plasminogen Activator/metabolism ; Urokinase-Type Plasminogen Activator/metabolism ; Yersinia pestis/*enzymology/isolation & purification/*pathogenicity
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  • 167
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    Aminoacyl esterase activity of the Tetrahymena ribozyme (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-06-05
    Description: Several classes of ribozymes (catalytic RNA's) catalyze reactions at phosphorus centers, but apparently no reaction at a carbon center has been demonstrated. The active site of the Tetrahymena ribozyme was engineered to bind an oligonucleotide derived from the 3' end of N-formyl-methionyl-tRNA(fMet). This ribozyme catalyzes the hydrolysis of the aminoacyl ester bond to a modest extent, 5 to 15 times greater than the uncatalyzed rate. Catalysis involves binding of the oligonucleotide to the internal guide sequence of the ribozyme and requires Mg2+ and sequence elements of the catalytic core. The ability of RNA to catalyze reactions with aminoacyl esters expands the catalytic versatility of RNA and suggests that the first aminoacyl tRNA synthetase could have been an RNA molecule.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Piccirilli, J A -- McConnell, T S -- Zaug, A J -- Noller, H F -- Cech, T R -- New York, N.Y. -- Science. 1992 Jun 5;256(5062):1420-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Chemistry and Biochemistry, University of Colorado, Boulder 80309.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1604316" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites ; Carboxylic Ester Hydrolases/*metabolism ; Kinetics ; Models, Structural ; Molecular Sequence Data ; Nucleic Acid Conformation ; Oligoribonucleotides ; RNA, Catalytic/genetics/*metabolism ; RNA, Transfer, Amino Acyl/metabolism ; *RNA, Transfer, Met ; Substrate Specificity ; Tetrahymena/*enzymology
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  • 168
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    Cloning of a delta opioid receptor by functional expression (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-12-28
    Description: Opiate drugs have potent analgesic and addictive properties. These drugs interact with receptors that also mediate the response to endogenous opioid peptide ligands. However, the receptors for opioids have eluded definitive molecular characterization. By transient expression in COS cells and screening with an iodinated analog of the opioid peptide enkephalin, a complementary DNA clone encoding a functional delta opioid receptor has been identified. The sequence shows homology to G protein-coupled receptors, in particular the receptors for somatostatin, angiotensin, and interleukin-8.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Evans, C J -- Keith, D E Jr -- Morrison, H -- Magendzo, K -- Edwards, R H -- DA05010/DA/NIDA NIH HHS/ -- P50 DA005010/DA/NIDA NIH HHS/ -- New York, N.Y. -- Science. 1992 Dec 18;258(5090):1952-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychiatry, University of California, School of Medicine, Los Angeles 90024-1759.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1335167" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding, Competitive ; Blotting, Northern ; Blotting, Southern ; Cell Line ; Cyclic AMP/metabolism ; Diprenorphine/metabolism ; Enkephalin, D-Penicillamine (2,5)- ; Enkephalins/pharmacology ; Etorphine/pharmacology ; Gene Expression ; Humans ; Kinetics ; Models, Structural ; Molecular Sequence Data ; Naloxone/pharmacology ; Narcotics/pharmacology ; Protein Structure, Secondary ; Receptors, Opioid, delta/chemistry/*genetics/*metabolism ; Sequence Homology, Amino Acid ; Transfection ; Tumor Cells, Cultured
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  • 169
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    Interaction of p107 with cyclin A independent of complex formation with viral oncoproteins (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-01-03
    Description: The p107 protein and the retinoblastoma protein (RB) both bind specifically to two viral oncoproteins, the SV40 T antigen (T) and adenoviral protein E1A (E1A). Like RB, p107 contains a segment (the pocket) that, alone, can bind specifically to T, E1A, and multiple cellular proteins. Cyclin A bound to the p107 pocket, but not the RB pocket. Although both pockets contain two, related collinear subsegments (A and B), the unique sequence in the p107 pocket that occupies the space between A and B is required for the interaction with cyclin A.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ewen, M E -- Faha, B -- Harlow, E -- Livingston, D M -- New York, N.Y. -- Science. 1992 Jan 3;255(5040):85-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Dana-Farber Cancer Institute, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1532457" target="_blank"〉PubMed〈/a〉
    Keywords: Adenovirus Early Proteins ; Amino Acid Sequence ; Antigens, Polyomavirus Transforming/*metabolism ; Base Sequence ; Binding Sites ; Cell Line ; Cloning, Molecular ; Cyclins/*metabolism ; Escherichia coli/genetics ; Eye Neoplasms ; Glutathione Transferase/genetics/metabolism ; Humans ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; *Nuclear Proteins ; Oligodeoxyribonucleotides ; Oncogene Proteins, Viral/genetics/*metabolism ; Protein Conformation ; Proteins/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Retinoblastoma ; Retinoblastoma Protein/genetics/*metabolism ; Retinoblastoma-Like Protein p107 ; Structure-Activity Relationship
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  • 170
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    Cloning and characterization of inducible nitric oxide synthase from mouse macrophages (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-04-10
    Description: Nitric oxide (NO) conveys a variety of messages between cells, including signals for vasorelaxation, neurotransmission, and cytotoxicity. In some endothelial cells and neurons, a constitutive NO synthase is activated transiently by agonists that elevate intracellular calcium concentrations and promote the binding of calmodulin. In contrast, in macrophages, NO synthase activity appears slowly after exposure of the cells to cytokines and bacterial products, is sustained, and functions independently of calcium and calmodulin. A monospecific antibody was used to clone complementary DNA that encoded two isoforms of NO synthase from immunologically activated mouse macrophages. Liquid chromatography-mass spectrometry was used to confirm most of the amino acid sequence. Macrophage NO synthase differs extensively from cerebellar NO synthase. The macrophage enzyme is immunologically induced at the transcriptional level and closely resembles the enzyme in cytokine-treated tumor cells and inflammatory neutrophils.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Xie, Q W -- Cho, H J -- Calaycay, J -- Mumford, R A -- Swiderek, K M -- Lee, T D -- Ding, A -- Troso, T -- Nathan, C -- AI30165/AI/NIAID NIH HHS/ -- CA43610/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 Apr 10;256(5054):225-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Beatrice and Samuel A. Seaver Laboratory, Department of Medicine, Cornell University Medical College, New York, NY 10021.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1373522" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Oxidoreductases/biosynthesis/*genetics ; Amino Acid Sequence ; Animals ; Base Sequence ; Cell Line ; Cells, Cultured ; Cloning, Molecular ; Codon ; Enzyme Induction ; Interferon-gamma/pharmacology ; Isoenzymes/biosynthesis/*genetics ; Kinetics ; Lipopolysaccharides ; Macrophages/drug effects/*enzymology ; Mammary Neoplasms, Experimental ; Mice ; Molecular Sequence Data ; Molecular Weight ; Neutrophils/drug effects/enzymology ; Nitric Oxide Synthase ; Oligodeoxyribonucleotides ; Poly A/genetics ; RNA/genetics ; RNA, Messenger ; Rats ; Sequence Homology, Nucleic Acid ; Transcription, Genetic
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  • 171
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    Tyrosine phosphorylation of the vav proto-oncogene product in activated B cells (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-05-22
    Description: Activation of B lymphocytes by engagement of their immunoglobulin M antigen receptors results in phosphorylation of a number of proteins on tyrosine residues. One such protein is p95vav, the product of the vav proto-oncogene. Tyrosine phosphorylation of p95vav occurred within seconds of immunoglobulin M cross-linking and was independent of other events induced during stimulation of B cells, such as protein kinase C activation, guanosine triphosphate-binding protein signaling, and calcium mobilization. Moreover, engagement of antigen receptors induced the rapid (approximately 5 seconds) and transient (approximately 60 seconds) association of p95vav with a 70-kilodalton tyrosine-phosphorylated protein, Vap-1, an interaction mediated by the Src homology 2 domain of p95vav. These results suggest that the vav proto-oncogene participates in the signaling processes that mediate the antigen-induced activation of B lymphocytes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bustelo, X R -- Barbacid, M -- New York, N.Y. -- Science. 1992 May 22;256(5060):1196-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Bristol-Myers Squibb Pharmaceutical Research Institute, Princeton, NJ 08543-4000.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1375396" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acids/analysis ; Animals ; B-Lymphocytes/immunology/*physiology ; *Cell Cycle Proteins ; Cell Line ; Kinetics ; *Lymphocyte Activation ; Mice ; Phosphorylation ; Phosphotyrosine ; Polymerase Chain Reaction ; Protein-Tyrosine Kinases/*metabolism ; Proto-Oncogene Proteins/genetics/*metabolism ; Proto-Oncogene Proteins c-vav ; *Proto-Oncogenes ; Tyrosine/analogs & derivatives/analysis
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  • 172
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    Lithium-sensitive production of inositol phosphates during amphibian embryonic mesoderm induction (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-04-10
    Description: Mesoderm induction and body axis determination in frog (Xenopus) embryos are thought to involve growth factor-mediated cell-cell signaling, but the signal transduction pathways are unknown. Li+, which inhibits the polyphosphoinositide (PI) cycle signal transduction pathway in many cells, also disrupts axis determination and mesoderm induction. Amounts of the PI cycle-derived second messenger, inositol 1,4,5-trisphosphate, increased during mesoderm induction in normal embryos; addition of Li+ inhibited the embryonic inositol monophosphatase and reversed this increase. Embryonic PI cycle activity thus shows characteristics that indicate it may function in mesoderm induction and axis determination.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maslanski, J A -- Leshko, L -- Busa, W B -- HD22879/HD/NICHD NIH HHS/ -- HD27546/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1992 Apr 10;256(5054):243-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, Johns Hopkins University, Baltimore, MD 21218.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1314424" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chlorides/*pharmacology ; Choline/pharmacology ; Embryo, Nonmammalian/physiology ; Female ; Inositol 1,4,5-Trisphosphate/metabolism ; Inositol Phosphates/*metabolism ; Kinetics ; Lithium/*pharmacology ; Lithium Chloride ; Mesoderm/drug effects/*physiology ; Signal Transduction/drug effects ; Teratogens/*pharmacology ; Xenopus/*embryology
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  • 173
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    Fast perceptual learning in visual hyperacuity (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-05-15
    Description: In many different spatial discrimination tasks, such as in determining the sign of the offset in a vernier stimulus, the human visual system exhibits hyperacuity by evaluating spatial relations with the precision of a fraction of a photoreceptor's diameter. It is proposed that this impressive performance depends in part on a fast learning process that uses relatively few examples and that occurs at an early processing stage in the visual pathway. This hypothesis is given support by the demonstration that it is possible to synthesize, from a small number of examples of a given task, a simple network that attains the required performance level. Psychophysical experiments agree with some of the key predictions of the model. In particular, fast stimulus-specific learning is found to take place in the human visual system, and this learning does not transfer between two slightly different hyperacuity tasks.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Poggio, T -- Fahle, M -- Edelman, S -- New York, N.Y. -- Science. 1992 May 15;256(5059):1018-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Artificial Intelligence Laboratory, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1589770" target="_blank"〉PubMed〈/a〉
    Keywords: Algorithms ; Computer Simulation ; Humans ; Kinetics ; Learning/*physiology ; Models, Biological ; Photoreceptor Cells/physiology ; Visual Acuity/*physiology ; Visual Pathways/physiology ; Visual Perception/*physiology
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  • 174
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    Range of messenger action of calcium ion and inositol 1,4,5-trisphosphate (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-12-11
    Description: The range of messenger action of a point source of Ca2+ or inositol 1,4,5-trisphosphate (IP3) was determined from measurements of their diffusion coefficients in a cytosolic extract from Xenopus laevis oocytes. The diffusion coefficient (D) of [3H]IP3 injected into an extract was 283 microns 2/s. D for Ca2+ increased from 13 to 65 microns 2/s when the free calcium concentration was raised from about 90 nM to 1 microM. The slow diffusion of Ca2+ in the physiologic concentration range results from its binding to slowly mobile or immobile buffers. The calculated effective ranges of free Ca2+ before it is buffered, buffered Ca2+, and IP3 determined from their diffusion coefficients and lifetimes were 0.1 micron, 5 microns, and 24 microns, respectively. Thus, for a transient point source of messenger in cells smaller than 20 microns, IP3 is a global messenger, whereas Ca2+ acts in restricted domains.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Allbritton, N L -- Meyer, T -- Stryer, L -- 5F32AI0814203/AI/NIAID NIH HHS/ -- MH45324/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1992 Dec 11;258(5089):1812-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Stanford University, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1465619" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/*metabolism ; Calcium-Transporting ATPases/antagonists & inhibitors ; Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone/pharmacology ; Chromatography, High Pressure Liquid ; Cytosol/metabolism ; Diffusion ; Inositol 1,4,5-Trisphosphate/*metabolism ; Kinetics ; Oocytes/drug effects/*metabolism ; *Second Messenger Systems ; *Signal Transduction ; Terpenes/pharmacology ; Thapsigargin ; Time Factors ; Xenopus laevis
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  • 175
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    Cloning of a second type of activin receptor and functional characterization in Xenopus embryos (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-03-27
    Description: A complementary DNA coding for a second type of activin receptor (ActRIIB) has been cloned from Xenopus laevis that fulfills the structural criteria of a transmembrane protein serine kinase. Ectodermal explants from embryos injected with activin receptor RNA show increased sensitivity to activin, as measured by the induction of muscle actin RNA. In addition, injected embryos display developmental defects characterized by inappropriate formation of dorsal mesodermal tissue. These results demonstrate that this receptor is involved in signal transduction and are consistent with the proposed role of activin in the induction and patterning of mesoderm in Xenopus embryos.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mathews, L S -- Vale, W W -- Kintner, C R -- DK-26741/DK/NIDDK NIH HHS/ -- HD-07343/HD/NICHD NIH HHS/ -- HD-13275/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1992 Mar 27;255(5052):1702-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Clayton Foundation Laboratories for Peptide Biology, Salk Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1313188" target="_blank"〉PubMed〈/a〉
    Keywords: Activin Receptors ; Activins ; Amino Acid Sequence ; Animals ; Cloning, Molecular ; DNA/genetics ; Inhibins/*physiology ; Membrane Proteins/genetics ; Molecular Sequence Data ; Protein Kinases/genetics ; Protein-Serine-Threonine Kinases ; Receptors, Cell Surface/*genetics ; Signal Transduction ; Xenopus laevis/embryology/*genetics
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  • 176
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    Roles of SWI1, SWI2, and SWI3 proteins for transcriptional enhancement by steroid receptors (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-12-04
    Description: The SWI1, SWI2, and SWI3 proteins, which are required for regulated transcription of numerous yeast genes, were found also to be essential for rat glucocorticoid receptor function in yeast; the receptor failed to activate transcription in strains with mutations in the SWI1, SWI2, or SWI3 genes. Certain mutations in genes encoding components of chromatin, identified as suppressors of swi mutations, partially relieved the SWI- requirement for receptor function. Immunoprecipitation of glucocorticoid receptor derivatives from wild-type (SWI+) yeast extracts coprecipitated the SWI3 protein; such receptor-SWI3 complexes were not detected in swi1- or swi2- mutant strains, implying that a complex of multiple SWI proteins may associate with the receptor. Prior incubation of a Drosophila embryo transcription extract with the yeast SWI3-specific antibody inhibited receptor function in vitro whereas the antibody had no effect if added after initiation complex formation. Thus, positive regulation by the glucocorticoid receptor in vivo and in vitro appears to require its interaction, at an early step, with one or more SWI proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yoshinaga, S K -- Peterson, C L -- Herskowitz, I -- Yamamoto, K R -- New York, N.Y. -- Science. 1992 Dec 4;258(5088):1598-604.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of California, San Francisco 94143-0448.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1360703" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphatases ; Animals ; Chromosomal Proteins, Non-Histone ; Cloning, Molecular ; DNA-Binding Proteins/genetics/*metabolism ; Fungal Proteins/genetics/*metabolism ; Gene Deletion ; *Gene Expression Regulation, Fungal ; Glucosephosphate Dehydrogenase/genetics/metabolism ; Nuclear Proteins/genetics/*metabolism ; Promoter Regions, Genetic ; RNA Polymerase II/metabolism ; Rats ; Receptors, Glucocorticoid/*genetics/metabolism ; Receptors, Steroid/*genetics/metabolism ; Saccharomyces cerevisiae/*genetics ; *Saccharomyces cerevisiae Proteins ; TATA Box ; *Trans-Activators ; Transcription Factors/genetics/*metabolism ; *Transcription, Genetic ; Tyrosine Transaminase/genetics/metabolism ; beta-Galactosidase/genetics/metabolism
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  • 177
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    IP3 receptor: localization to plasma membrane of T cells and cocapping with the T cell receptor (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-07
    Description: Immune responses in lymphocytes require cellular accumulation of large amounts of calcium (Ca2+) from extracellular sources. In the T cell tumor line Jurkat, receptors for the Ca(2+)-releasing messenger inositol 1,4,5-trisphosphate (IP3) were localized to the plasma membrane (PM). Capping of the T cell receptor-CD3 complex, which is associated with signal transduction, was accompanied by capping of IP3 receptors. The IP3 receptor on T cells appears to be responsible for the entry of Ca2+ that initiates proliferative responses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Khan, A A -- Steiner, J P -- Klein, M G -- Schneider, M F -- Snyder, S H -- DA-00074/DA/NIDA NIH HHS/ -- MH-18501/MH/NIMH NIH HHS/ -- P01-HL27867/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1992 Aug 7;257(5071):815-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Johns Hopkins University School of Medicine, Department of Neuroscience, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1323146" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, CD/metabolism ; Antigens, CD3 ; Antigens, Differentiation, T-Lymphocyte/analysis/*metabolism ; Burkitt Lymphoma ; Calcium/*metabolism ; *Calcium Channels ; Cell Line ; Cell Membrane/*metabolism ; Cells, Cultured ; Concanavalin A/pharmacology ; Fluorescent Antibody Technique ; Humans ; Inositol 1,4,5-Trisphosphate/*metabolism ; Inositol 1,4,5-Trisphosphate Receptors ; Kinetics ; Receptors, Antigen, T-Cell/analysis/*metabolism ; Receptors, Cell Surface/analysis/*metabolism ; *Receptors, Cytoplasmic and Nuclear ; Second Messenger Systems ; T-Lymphocytes/*immunology
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    Myoglobin in a cyanobacterium (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-06-19
    Description: Myoglobin was found in the nitrogen-fixing cyanobacterium Nostoc commune. This cyanobacterial myoglobin, referred to as cyanoglobin, was shown to be a soluble hemoprotein of 12.5 kilodaltons with an amino acid sequence that is related to that of myoglobins from two lower eukaryotes, the ciliated protozoa Paramecium caudatum and Tetrahymena pyriformis. Cyanoglobin is encoded by the glbN gene, which is positioned between nifU and nifH-two genes essential for nitrogen fixation-in the genome of Nostoc. Cyanoglobin was detected in Nostoc cells only when they were starved for nitrogen and incubated microaerobically.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Potts, M -- Angeloni, S V -- Ebel, R E -- Bassam, D -- New York, N.Y. -- Science. 1992 Jun 19;256(5064):1690-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg Va 24061.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1609281" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Chromosome Mapping ; Cloning, Molecular ; Cyanobacteria/*genetics ; Electrophoresis, Polyacrylamide Gel ; Molecular Sequence Data ; Myoglobin/*genetics ; Polymerase Chain Reaction ; Sequence Homology, Nucleic Acid
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    Solution structure of the SH3 domain of Src and identification of its ligand-binding site (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-12-04
    Description: The Src homology 3 (SH3) region is a protein domain of 55 to 75 amino acids found in many cytoplasmic proteins, including those that participate in signal transduction pathways. The solution structure of the SH3 domain of the tyrosine kinase Src was determined by multidimensional nuclear magnetic resonance methods. The molecule is composed of two short three-stranded anti-parallel beta sheets packed together at approximately right angles. Studies of the SH3 domain bound to proline-rich peptide ligands revealed a hydrophobic binding site on the surface of the protein that is lined with the side chains of conserved aromatic amino acids.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yu, H -- Rosen, M K -- Shin, T B -- Seidel-Dugan, C -- Brugge, J S -- Schreiber, S L -- 1-S10-RR04870/RR/NCRR NIH HHS/ -- CA27951/CA/NCI NIH HHS/ -- GM44993/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Dec 4;258(5088):1665-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, Harvard University, Cambridge, MA 02138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1280858" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Cloning, Molecular ; Escherichia coli/genetics ; Glutathione Transferase/chemistry/genetics/isolation & purification ; Ligands ; Magnetic Resonance Spectroscopy ; Molecular Sequence Data ; Neurons/physiology ; Protein Conformation ; *Protein Structure, Secondary ; Protein-Tyrosine Kinases/*genetics ; Proto-Oncogene Proteins pp60(c-src)/*chemistry ; Recombinant Fusion Proteins/chemistry/isolation & purification ; Solutions ; X-Ray Diffraction
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Modulation of an NCAM-related adhesion molecule with long-term synaptic plasticity in Aplysia (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-05-01
    Description: A form of learning in the marine mollusk Aplysia, long-term sensitization of the gill- and siphon-withdrawal reflex, results in the formation of new synaptic connections between the presynaptic siphon sensory neurons and their target cells. These structural changes can be mimicked, when the cells are maintained in culture, by application of serotonin, an endogenous facilitating neurotransmitter in Aplysia. A group of cell surface proteins, designated Aplysia cell adhesion molecules (apCAM's) was down-regulated in the sensory neurons in response to serotonin. The deduced amino acid sequence obtained from complementary DNA clones indicated that the apCAM's are a family of proteins that seem to arise from a single gene. The apCAM's are members of the immunoglobulin class of cell adhesion molecules and resemble two neural cell adhesion molecules, NCAM and fasciclin II. In addition to regulating newly synthesized apCAM, serotonin also altered the amount of preexisting apCAM on the cell surface of the presynaptic sensory neurons. By contrast, the apCAM on the surface of the postsynaptic motor neuron was not modulated by serotonin. This rapid, transmitter-mediated down-regulation of a cell adhesion molecule in the sensory neurons may be one of the early molecular changes in long-term synaptic facilitation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mayford, M -- Barzilai, A -- Keller, F -- Schacher, S -- Kandel, E R -- New York, N.Y. -- Science. 1992 May 1;256(5057):638-44.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, College of Physicians and Surgeons of Columbia University, New York, NY 10032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1585176" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Aplysia/*metabolism ; Blotting, Northern ; Cell Adhesion Molecules, Neuronal/chemistry/genetics/*metabolism ; Cells, Cultured ; Cloning, Molecular ; DNA/chemistry/genetics ; Fluorescent Antibody Technique ; Molecular Sequence Data ; Motor Neurons/drug effects/metabolism ; Neuronal Plasticity/*physiology ; Neurons, Afferent/drug effects/metabolism ; Protein Sorting Signals/chemistry ; Serotonin/pharmacology ; Synapses/*physiology
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    Calmodulin trapping by calcium-calmodulin-dependent protein kinase (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-05-22
    Description: Multifunctional calcium-calmodulin-dependent protein kinase (CaM kinase) transduces transient elevations in intracellular calcium into changes in the phosphorylation state and activity of target proteins. By fluorescence emission anisotropy, the affinity of CaM kinase for dansylated calmodulin was measured and found to increase 1000 times after autophosphorylation of the threonine at position 286 of the protein. Autophosphorylation markedly slowed the release of bound calcium-calmodulin; the release time increased from less than a second to several hundred seconds. In essence, calmodulin is trapped by autophosphorylation. The shift in affinity does not occur in a site-directed mutant in which threonine at position 286 has been replaced by a non-phosphorylatable amino acid. These experiments demonstrate the existence of a new state in which calmodulin is bound to CaM kinase even though the concentration of calcium is basal. Calmodulin trapping provides for molecular potentiation of calcium transients and may enable detection of their frequency.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meyer, T -- Hanson, P I -- Stryer, L -- Schulman, H -- GM 40600/GM/NIGMS NIH HHS/ -- GM24032/GM/NIGMS NIH HHS/ -- MH45324/MH/NIMH NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1992 May 22;256(5060):1199-202.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Stanford University School of Medicine, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1317063" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding, Competitive ; Calcium/pharmacology ; Calcium-Calmodulin-Dependent Protein Kinases ; Calmodulin/*metabolism ; Cell Line ; Egtazic Acid/pharmacology ; Kinetics ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Phosphorylation ; Protein Binding ; Protein Kinases/genetics/*metabolism ; Recombinant Proteins/metabolism ; Spectrometry, Fluorescence ; Threonine ; Time Factors ; Transfection
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    Selective role of N-type calcium channels in neuronal migration (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-07
    Description: Analysis of neuronal migration in mouse cerebellar slice preparations by a laser scanning confocal microscope revealed that postmitotic granule cells initiate their migration only after the expression of N-type calcium channels on their plasmalemmal surface. Furthermore, selective blockade of these channels by addition of omega-conotoxin to the incubation medium curtailed cell movement. In contrast, inhibitors of L- and T-type calcium channels, as well as those of sodium and potassium channels, had no effect on the rate of granule cell migration. These results suggest that N-type calcium channels, which have been predominantly associated with neurotransmitter release in adult brain, also play a transient but specific developmental role in directed migration of immature neurons before the establishment of their synaptic circuits.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Komuro, H -- Rakic, P -- New York, N.Y. -- Science. 1992 Aug 7;257(5071):806-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Section of Neurobiology, Yale University School of Medicine, New Haven, CT 06510.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1323145" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/pharmacology ; Calcium Channels/drug effects/*physiology ; Cell Movement/drug effects ; Cells, Cultured ; Cerebellum/cytology/*physiology ; In Vitro Techniques ; Kinetics ; Mice ; Mollusk Venoms/pharmacology ; Neurons/cytology/drug effects/*physiology ; Peptides, Cyclic/pharmacology ; Time Factors ; *omega-Conotoxins
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  • 183
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    Malignant transformation by a mutant of the IFN-inducible dsRNA-dependent protein kinase (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-09-18
    Description: The double-stranded RNA-dependent protein kinase (dsRNA-PK) is thought to be a key mediator of the antiviral and antiproliferative effects of interferons (IFNs). Studies examining the physiological function of the kinase suggest that it participates in cell growth and differentiation by regulating protein synthesis. Autophosphorylation and consequent activation of dsRNA-PK in vitro and in vivo result in phosphorylation of the alpha subunit of eukaryotic initiation factor-2 (eIF-2) and inhibition of protein synthesis. Expression of a functionally defective mutant of human dsRNA-PK in NIH 3T3 cells resulted in malignant transformation, suggesting that dsRNA-PK may function as a suppressor of cell proliferation and tumorigenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koromilas, A E -- Roy, S -- Barber, G N -- Katze, M G -- Sonenberg, N -- AI22646/AI/NIAID NIH HHS/ -- RR00166/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1992 Sep 18;257(5077):1685-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Faculty of Medicine, McGill University, Montreal, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1382315" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; Cell Division ; Cell Line ; *Cell Transformation, Neoplastic ; Cloning, Molecular ; DNA/genetics ; Enzyme Induction ; Gene Expression ; Humans ; Immunoblotting ; Interferons/*pharmacology ; Mice ; Molecular Sequence Data ; *Mutation ; Phosphorylation ; Protein Kinases/chemistry/*genetics/physiology ; Transfection ; eIF-2 Kinase
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    Primary structure and functional expression of the beta 1 subunit of the rat brain sodium channel (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-05-08
    Description: Voltage-sensitive sodium channels are responsible for the initiation and propagation of the action potential and therefore are important for neuronal excitability. Complementary DNA clones encoding the beta 1 subunit of the rat brain sodium channel were isolated by a combination of polymerase chain reaction and library screening techniques. The deduced primary structure indicates that the beta 1 subunit is a 22,851-dalton protein that contains a single putative transmembrane domain and four potential extracellular N-linked glycosylation sites, consistent with biochemical data. Northern blot analysis reveals a 1,400-nucleotide messenger RNA in rat brain, heart, skeletal muscle, and spinal cord. Coexpression of beta 1 subunits with alpha subunits increases the size of the peak sodium current, accelerates its inactivation, and shifts the voltage dependence of inactivation to more negative membrane potentials. These results indicate that the beta 1 subunit is crucial in the assembly, expression, and functional modulation of the heterotrimeric complex of the rat brain sodium channel.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Isom, L L -- De Jongh, K S -- Patton, D E -- Reber, B F -- Offord, J -- Charbonneau, H -- Walsh, K -- Goldin, A L -- Catterall, W A -- NS15751/NS/NINDS NIH HHS/ -- NS25704/NS/NINDS NIH HHS/ -- NS26729/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1992 May 8;256(5058):839-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Washington, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1375395" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Blotting, Northern ; Brain/*physiology ; Cloning, Molecular ; DNA/genetics/isolation & purification ; Female ; Kinetics ; Macromolecular Substances ; Membrane Potentials ; Molecular Sequence Data ; Oocytes/physiology ; Polymerase Chain Reaction/methods ; Protein Conformation ; RNA/genetics/isolation & purification ; RNA, Messenger/genetics ; Rats ; Sodium Channels/*genetics/*physiology ; Voltage-Gated Sodium Channel beta-1 Subunit ; Xenopus
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    An efficient antibody-catalyzed aminoacylation reaction (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-04-17
    Description: An antibody generated against a neutral phosphonate diester transition-state analog was found to catalyze the aminoacylation of the 3'-hydroxyl group of thymidine with an alanyl ester. A comparison of the apparent second-order rate constant of the antibody-catalyzed reaction [5.4 x 10(4) molar-1 minute-1 (M-1 min-1)] with that of the uncatalyzed reaction (2.6 x 10(-4) M-1 min-1) revealed this to be a remarkably efficient catalyst. Moreover, although the concentration of water (55 M) greatly exceeds that of the secondary alcohol, the antibody selectively catalyzes acyl transfer to thymidine. The antibody exhibits sequential binding, with Michaelis constants of 770 microM and 260 microM for acyl acceptor and donor, respectively, and a dissociation constant of 240 pM for hapten. This antibody-catalyzed reaction provides increased insight into the requirements for efficient aminoacylation catalysts and may represent a first step toward the generation of "aminoacyl transfer RNA synthetases" with novel specificities.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jacobsen, J R -- Prudent, J R -- Kochersperger, L -- Yonkovich, S -- Schultz, P G -- AI24695/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1992 Apr 17;256(5055):365-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1566082" target="_blank"〉PubMed〈/a〉
    Keywords: Acylation ; Alanine/*metabolism ; Amino Acyl-tRNA Synthetases/metabolism ; Antibodies, Monoclonal/*metabolism ; *Catalysis ; Chromatography, High Pressure Liquid ; Esterification ; Haptens/immunology ; Hemocyanin/immunology ; Kinetics ; Organophosphonates/*immunology ; Serum Albumin, Bovine/immunology ; Thymidine/*metabolism
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    Dynamics of ribozyme binding of substrate revealed by fluorescence-detected stopped-flow methods (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-11-20
    Description: Fluorescence-detected stopped-flow and equilibrium methods have been used to study the mechanism for binding of pyrene (pyr)-labeled RNA oligomer substrates to the ribozyme (catalytic RNA) from Tetrahymena thermophila. The fluorescence of these substrates increases up to 25-fold on binding to the ribozyme. Stopped-flow experiments provide evidence that pyr experiences at least three different microenvironments during the binding process. A minimal mechanism is presented in which substrate initially base pairs to ribozyme and subsequently forms tertiary contacts in an RNA folding step. All four microscopic rate constants are measured for ribozyme binding of pyrCCUCU.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bevilacqua, P C -- Kierzek, R -- Johnson, K A -- Turner, D H -- GM 22939/GM/NIGMS NIH HHS/ -- GM44613/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Nov 20;258(5086):1355-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry, University of Rochester, NY 14627.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1455230" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Hydrogen Bonding ; Kinetics ; *RNA Splicing ; RNA, Catalytic/*metabolism ; RNA, Guide/*metabolism ; RNA, Protozoan/*metabolism ; RNA, Ribosomal/*metabolism ; Substrate Specificity ; Tetrahymena thermophila ; Thermodynamics
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  • 187
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    Activation of transcription factors by interferon-alpha in a cell-free system (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-07
    Description: The signal transduction mechanisms of interferons (IFNs) remain unclear partly because no effect of IFN has been reproducible in a cell-free system. IFN-alpha rapidly induces the transcription of a set of early response genes, and a multicomponent transcriptional activator, interferon stimulated gene factor 3 (ISGF3), is activated within minutes after binding of IFN-alpha to its receptor. A system was developed in which IFN-alpha activated ISGF3 in homogenates of HeLa cells. Subcellular fractionation revealed that incubation of a plasma membrane-enriched fraction with IFN-alpha was sufficient to activate the regulatory subcomponent of ISGF3.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉David, M -- Larner, A C -- New York, N.Y. -- Science. 1992 Aug 7;257(5071):813-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Cytokine Biology, Center for Biologics Evaluation and Research, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1496402" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cell-Free System ; DNA-Binding Proteins/biosynthesis/isolation & purification/*metabolism ; HeLa Cells ; Humans ; Interferon-Stimulated Gene Factor 3 ; Interferon-Stimulated Gene Factor 3, gamma Subunit ; Interferon-alpha/*pharmacology ; Interferon-gamma/pharmacology ; Kinetics ; Molecular Sequence Data ; Molecular Weight ; Oligonucleotide Probes ; Transcription Factors/biosynthesis/isolation & purification/*metabolism ; Transcription, Genetic/*drug effects
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  • 188
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    Molecular code for cooperativity in hemoglobin (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-01-03
    Description: Although tetrameric hemoglobin has been studied extensively as a prototype for understanding mechanisms of allosteric regulation, the functional and structural properties of its eight intermediate ligation forms have remained elusive. Recent experiments on the energetics of cooperativity of these intermediates, along with assignments of their quaternary structures, have revealed that the allosteric mechanism is controlled by a previously unrecognized symmetry feature: quaternary switching from form T to form R occurs whenever heme-site binding creates a tetramer with at least one ligated subunit on each dimeric half-molecule. This "symmetry rule" translates the configurational isomers of heme-site ligation into six observed switchpoints of quaternary transition. Cooperativity arises from both "concerted" quaternary switching and "sequential" modulation of binding within each quaternary form, T and R. Binding affinity is regulated through a hierarchical code of tertiary-quaternary coupling that includes the classical allosteric models as limiting cases.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ackers, G K -- Doyle, M L -- Myers, D -- Daugherty, M A -- P01-HL40453/HL/NHLBI NIH HHS/ -- R37-GM24486/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Jan 3;255(5040):54-63.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1553532" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Calorimetry ; Circular Dichroism ; Hemoglobins/*chemistry/genetics/metabolism ; Kinetics ; Ligands ; Macromolecular Substances ; Models, Molecular ; Mutation ; Oxyhemoglobins/chemistry/metabolism ; Protein Conformation ; Thermodynamics
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  • 189
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    The skeletal muscle chloride channel in dominant and recessive human myotonia (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-08-07
    Description: Autosomal recessive generalized myotonia (Becker's disease) (GM) and autosomal dominant myotonia congenita (Thomsen's disease) (MC) are characterized by skeletal muscle stiffness that is a result of muscle membrane hyperexcitability. For both diseases, alterations in muscle chloride or sodium currents or both have been observed. A complementary DNA for a human skeletal muscle chloride channel (CLC-1) was cloned, physically localized on chromosome 7, and linked to the T cell receptor beta (TCRB) locus. Tight linkage of these two loci to GM and MC was found in German families. An unusual restriction site in the CLC-1 locus in two GM families identified a mutation associated with that disease, a phenylalanine-to-cysteine substitution in putative transmembrane domain D8. This suggests that different mutations in CLC-1 may cause dominant or recessive myotonia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koch, M C -- Steinmeyer, K -- Lorenz, C -- Ricker, K -- Wolf, F -- Otto, M -- Zoll, B -- Lehmann-Horn, F -- Grzeschik, K H -- Jentsch, T J -- New York, N.Y. -- Science. 1992 Aug 7;257(5071):797-800.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Center for Human Genetics, Marburg University, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1379744" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Blotting, Southern ; Chloride Channels ; *Chromosomes, Human, Pair 7 ; Cloning, Molecular ; DNA/genetics ; Female ; *Genes, Dominant ; *Genes, Recessive ; Genetic Linkage ; Humans ; Ion Channels/*genetics ; Lod Score ; Male ; Membrane Proteins/*genetics ; Molecular Sequence Data ; Muscular Dystrophies/*genetics ; Myotonia Congenita/*genetics ; Pedigree ; Polymorphism, Restriction Fragment Length ; Receptors, Antigen, T-Cell/genetics ; Recombination, Genetic ; Sequence Homology, Nucleic Acid
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    Activation of a plant gene by T-DNA tagging: auxin-independent growth in vitro (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-11-20
    Description: A transferred DNA (T-DNA) tagging vector with the potential to produce dominant mutations was used with cocultured Agrobacterium tumefaciens and protoplasts to tag genes involved in the action of the plant growth substance auxin. Transgenic calli were selected for their ability to grow in the absence of auxin in the culture media. From one experiment, 12 calli that displayed this phenotype were recovered, of which 11 were able to regenerate into plants. In one plant studied in detail, protoplast division in the absence of auxin genetically cosegregated with a single T-DNA insert. A messenger RNA encoded by a 6.4-kilobase sequence of plant genomic DNA rescued from the mutant is overexpressed relative to untransformed plants. The genomic DNA, as well as a cognate complementary DNA, once transfected into protoplasts promote growth and cell division in vitro in the absence of exogenously added auxin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hayashi, H -- Czaja, I -- Lubenow, H -- Schell, J -- Walden, R -- New York, N.Y. -- Science. 1992 Nov 20;258(5086):1350-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Faculty of Agriculture, University of Tokyo, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1455228" target="_blank"〉PubMed〈/a〉
    Keywords: Agrobacterium tumefaciens/genetics ; Amino Acid Sequence ; Cloning, Molecular ; *Gene Expression Regulation ; Genes, Plant ; *Genetic Vectors ; In Vitro Techniques ; Indoleacetic Acids/*genetics ; Molecular Sequence Data ; Plants, Genetically Modified/*genetics/growth & development ; Restriction Mapping
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  • 191
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    Total chemical synthesis of a D-enzyme: the enantiomers of HIV-1 protease show reciprocal chiral substrate specificity [corrected] (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-06-05
    Description: The D and L forms of the enzyme HIV-1 protease have been prepared by total chemical synthesis. The two proteins had identical covalent structures. However, the folded protein-enzyme enantiomers showed reciprocal chiral specificity on peptide substrates. That is, each enzyme enantiomer cut only the corresponding substrate enantiomer. Reciprocal chiral specificity was also evident in the effect of enantiomeric inhibitors. These data imply that the folded forms of the chemically synthesized D- and L-enzyme molecules are mirror images of one another in all elements of the three-dimensional structure. Enantiomeric proteins are expected to display reciprocal chiral specificity in all aspects of their biochemical interactions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Milton, R C -- Milton, S C -- Kent, S B -- New York, N.Y. -- Science. 1992 Jun 5;256(5062):1445-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Scripps Research Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1604320" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Amino Acids ; HIV Protease/chemical synthesis/*chemistry/*metabolism ; Kinetics ; Macromolecular Substances ; Models, Molecular ; Molecular Sequence Data ; Oligopeptides/pharmacology ; Protein Conformation ; Stereoisomerism ; Substrate Specificity ; X-Ray Diffraction
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  • 192
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    Inhibition of neutrophil chemokinesis on vitronectin by inhibitors of calcineurin (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-10-09
    Description: Migration of human polymorphonuclear neutrophils on vitronectin is dependent on repeated transient increases in the concentration of intracellular free calcium ([Ca2+]i). A specific peptide inhibitor of the Ca(2+)-calmodulin-dependent phosphatase calcineurin was introduced into the cytoplasm of neutrophils. The peptide inhibited neutrophil migration on vitronectin by interfering with the release of the cells from sites of attachment. A similar reduction in motility on vitronectin occurred when cells were treated with the immunosuppressant FK506, which also inhibits calcineurin when bound to its binding protein, FKBP. These results indicate that a rise in [Ca2+]i reduces integrin-mediated adhesion to vitronectin by a mechanism that requires calcineurin activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hendey, B -- Klee, C B -- Maxfield, F R -- GM14150/GM/NIGMS NIH HHS/ -- GM34770/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Oct 9;258(5080):296-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, College of Physicians and Surgeons, Columbia University, New York, NY 10032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1384129" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Aminoquinolines/pharmacology ; Calcineurin ; Calmodulin-Binding Proteins/*antagonists & inhibitors/physiology ; Carrier Proteins/metabolism ; Chemotaxis, Leukocyte/*drug effects ; Ethers, Cyclic/pharmacology ; *Glycoproteins ; Humans ; Kinetics ; Molecular Sequence Data ; N-Formylmethionine Leucyl-Phenylalanine/pharmacology ; Neutrophils/cytology/drug effects/*physiology ; Okadaic Acid ; Peptide Fragments/pharmacology ; Peptides/pharmacology ; Phosphoprotein Phosphatases/*antagonists & inhibitors/physiology ; Phosphorylation ; Tacrolimus/pharmacology ; Tacrolimus Binding Proteins ; Vitronectin
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  • 193
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    Isolation and structure of a brain constituent that binds to the cannabinoid receptor (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-12-18
    Description: Arachidonylethanolamide, an arachidonic acid derivative in porcine brain, was identified in a screen for endogenous ligands for the cannabinoid receptor. The structure of this compound, which has been named "anandamide," was determined by mass spectrometry and nuclear magnetic resonance spectroscopy and was confirmed by synthesis. Anandamide inhibited the specific binding of a radiolabeled cannabinoid probe to synaptosomal membranes in a manner typical of competitive ligands and produced a concentration-dependent inhibition of the electrically evoked twitch response to the mouse vas deferens, a characteristic effect of psychotropic cannabinoids. These properties suggest that anandamide may function as a natural ligand for the cannabinoid receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Devane, W A -- Hanus, L -- Breuer, A -- Pertwee, R G -- Stevenson, L A -- Griffin, G -- Gibson, D -- Mandelbaum, A -- Etinger, A -- Mechoulam, R -- DA 6481/DA/NIDA NIH HHS/ -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1992 Dec 18;258(5090):1946-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Natural Products, Medical Faculty, Hebrew University, Jerusalem, Israel.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1470919" target="_blank"〉PubMed〈/a〉
    Keywords: Amides/chemistry/*isolation & purification/pharmacology ; Animals ; *Arachidonic Acids ; Binding, Competitive ; Brain/*metabolism ; Brain Chemistry ; Cannabinoids/metabolism ; Chromatography, Thin Layer ; Endocannabinoids ; Fatty Acids, Unsaturated/chemistry/*isolation & purification/pharmacology ; Gas Chromatography-Mass Spectrometry ; Kinetics ; Polyunsaturated Alkamides ; Receptors, Cannabinoid ; Receptors, Drug/*metabolism ; Swine
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  • 194
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    Invariant chain peptides in most HLA-DR molecules of an antigen-processing mutant (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-12-11
    Description: Class II major histocompatibility complexes bind peptides in an endosome-like compartment. When the class II null cell line 721.174 was transfected with class II DR3 genes, DR molecules were produced in normal amounts. However, the DR molecules were abnormally conformed and unstable because deletion of an antigen-processing gene had impaired intracellular formation of most class II-peptide complexes. Yet, 70 percent of the DR molecules still bore peptides, 80 percent of which were 21- to 24-amino acid fragments of the class II-associated invariant chain. These peptides were rare on DR3 from control cells. Thus, a defect in the main antigen-processing pathway revealed a process in which DR molecules bind long peptides derived from proteins present in the same compartment.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sette, A -- Ceman, S -- Kubo, R T -- Sakaguchi, K -- Appella, E -- Hunt, D F -- Davis, T A -- Michel, H -- Shabanowitz, J -- Rudersdorf, R -- AI15486/AI/NIAID NIH HHS/ -- AI18634/AI/NIAID NIH HHS/ -- GM37537/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1992 Dec 11;258(5089):1801-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Genetics, University of Wisconsin, Madison 53706.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1465617" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Cell Line ; Gene Deletion ; *Genes, MHC Class II ; HLA-DR Antigens/*genetics/*metabolism ; HLA-DR3 Antigen/*genetics/metabolism ; Humans ; Kinetics ; Macromolecular Substances ; Molecular Sequence Data ; Peptides/*metabolism ; Transfection
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  • 195
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    Components of sterol biosynthesis assembled on the oxygen-avid hemoglobin of Ascaris (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-12-18
    Description: The parasitic nematode Ascaris infests a billion people worldwide. Much of its proliferative success is due to prodigious egg production, up to 10(6) sterol-replete eggs per day. Sterol synthesis requires molecular oxygen for squalene epoxidation, yet oxygen is scarce in the intestinal folds the worms inhabit. Ascaris has an oxygen-avid hemoglobin in the perienteric fluid that bathes its reproductive organs. Purified hemoglobin contained tightly bound squalene and functioned as an NADPH-dependent, ferrihemoprotein reductase. All components of the squalene epoxidation reaction--squalene, oxygen, NADPH, and NADPH-dependent reductase--are assembled on the hemoglobin. This molecule may thus function in sterol biosynthesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sherman, D R -- Guinn, B -- Perdok, M M -- Goldberg, D E -- AM-20579/AM/NIADDK NIH HHS/ -- RR-00954/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1992 Dec 18;258(5090):1930-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Washington University School of Medicine, St. Louis, MO.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1470914" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Ascaris/*metabolism ; Hemoglobins/*metabolism ; Kinetics ; Mass Spectrometry ; NADPH-Ferrihemoprotein Reductase/metabolism ; Oxyhemoglobins/*metabolism ; Squalene/metabolism ; Sterols/*biosynthesis/isolation & purification
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  • 196
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    Torsional rigidity of positively and negatively supercoiled DNA (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-01-03
    Description: Time-correlated single-photon counting of intercalated ethidium bromide was used to measure the torsion constants of positively supercoiled, relaxed, and negatively supercoiled pBR322 DNA, which range in superhelix density from +0.042 to -0.123. DNA behaves as coupled, nonlinear torsional pendulums under superhelical stress, and the anharmonic term in the Hamiltonian is approximately 15 percent for root-mean-square fluctuations in twist at room temperature. At the level of secondary structure, positively supercoiled DNA is significantly more flexible than negatively supercoiled DNA. These results exclude certain models that account for differential binding affinity of proteins to positively and negatively supercoiled DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Selvin, P R -- Cook, D N -- Pon, N G -- Bauer, W R -- Klein, M P -- Hearst, J E -- FD 8R1 GM 41911A-03-NF-03/92/FD/FDA HHS/ -- New York, N.Y. -- Science. 1992 Jan 3;255(5040):82-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics, University of California, Berkeley.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1553534" target="_blank"〉PubMed〈/a〉
    Keywords: DNA, Superhelical/*chemistry ; Ethidium ; Intercalating Agents ; Kinetics ; Mathematics ; Models, Theoretical ; Nucleic Acid Conformation ; *Plasmids ; Spectrometry, Fluorescence ; Stress, Mechanical ; Thermodynamics
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  • 197
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    CD19: lowering the threshold for antigen receptor stimulation of B lymphocytes (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-04-03
    Description: Lymphocytes must proliferate and differentiate in response to low concentrations of a vast array of antigens. The requirements of broad specificity and sensitivity conflict because the former is met by low-affinity antigen receptors, which precludes achieving the latter with high-affinity receptors. Coligation of the membrane protein CD19 with the antigen receptor of B lymphocytes decreased the threshold for antigen receptor-dependent stimulation by two orders of magnitude. B lymphocytes proliferated when approximately 100 antigen receptors per cell, 0.03 percent of the total, were coligated with CD19. The B cell resolves its dilemma by having an accessory protein that enables activation when few antigen receptors are occupied.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Carter, R H -- Fearon, D T -- AI-22833/AI/NIAID NIH HHS/ -- AI-28191/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1992 Apr 3;256(5053):105-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, 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/1373518" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal/immunology ; Antigens, CD/genetics/*immunology ; Antigens, CD19 ; Antigens, Differentiation, B-Lymphocyte/genetics/*immunology ; B-Lymphocytes/*immunology ; Cell Line ; Cells, Cultured ; DNA Replication ; Humans ; Kinetics ; L Cells (Cell Line) ; *Lymphocyte Activation ; Mice ; Receptors, Antigen, B-Cell/*immunology ; Recombinant Proteins/immunology ; Thymidine/metabolism
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  • 198
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    Rapamycin-induced inhibition of the 70-kilodalton S6 protein kinase (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-14
    Description: The immunosuppressant rapamycin inhibited proliferation of the H4IIEC hepatoma cell line. Rapamycin, but not its structural analog FK506, also inhibited the basal and insulin-stimulated activity of the p70 ribosomal protein S6 kinase. By contrast, insulin stimulation of the p85 Rsk S6 kinase and mitogen-activated protein (MAP) kinase activity were unaffected by drug. Rapamycin treatment of COS cells transfected with recombinant p70 S6 kinase completely inhibited the appearance of the hyperphosphorylated form of p70 S6 kinase concomitant with the inhibition of enzyme activity toward 40S subunits. Thus, rapamycin inhibits a signal transduction element that is necessary for the activation of p70 S6 kinase and mitogenesis but unnecessary for activation of p85 Rsk S6 kinase or MAP kinase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Price, D J -- Grove, J R -- Calvo, V -- Avruch, J -- Bierer, B E -- P01 CA39542/CA/NCI NIH HHS/ -- R01 DK17776/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1992 Aug 14;257(5072):973-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Diabetes Unit, Massachusetts General Hospital, Boston.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1380182" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium-Calmodulin-Dependent Protein Kinases ; Cell Line ; Chromatography, Ion Exchange ; Cyclosporine/pharmacology ; Immunosuppressive Agents/*pharmacology ; Insulin/pharmacology ; Kinetics ; Liver Neoplasms, Experimental ; Polyenes/*pharmacology ; *Protein Kinase Inhibitors ; Protein Kinases/genetics/isolation & purification/*metabolism ; Recombinant Proteins/antagonists & inhibitors/isolation & purification ; Ribosomal Protein S6 Kinases ; Ribosomes/enzymology ; Sirolimus ; Tacrolimus/pharmacology ; Tetradecanoylphorbol Acetate/pharmacology ; Transfection
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  • 199
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    The human Y chromosome: overlapping DNA clones spanning the euchromatic region (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-10-02
    Description: The human Y chromosome was physically mapped by assembling 196 recombinant DNA clones, each containing a segment of the chromosome, into a single overlapping array. This array included more than 98 percent of the euchromatic portion of the Y chromosome. First, a library of yeast artificial chromosome (YAC) clones was prepared from the genomic DNA of a human XYYYY male. The library was screened to identify clones containing 160 sequence-tagged sites and the map was then constructed from this information. In all, 207 Y-chromosomal DNA loci were assigned to 127 ordered intervals on the basis of their presence or absence in the YAC's, yielding ordered landmarks at an average spacing of 220 kilobases across the euchromatic region. The map reveals that Y-chromosomal genes are scattered among a patchwork of X-homologous, Y-specific repetitive, and single-copy DNA sequences. This map of overlapping clones and ordered, densely spaced markers should accelerate studies of the chromosome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Foote, S -- Vollrath, D -- Hilton, A -- Page, D C -- New York, N.Y. -- Science. 1992 Oct 2;258(5079):60-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Research Laboratories, Whitehead Institute, Cambridge, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1359640" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Centromere ; Cloning, Molecular ; DNA Fingerprinting ; Gene Library ; Genes, Fungal ; *Genome, Human ; Humans ; Male ; Molecular Sequence Data ; Multigene Family ; Polymorphism, Restriction Fragment Length ; Sequence Homology ; Sequence Tagged Sites ; X Chromosome ; *Y Chromosome
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  • 200
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    Ablation of transplanted HTLV-I Tax-transformed tumors in mice by antisense inhibition of NF-kappa B (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-12-11
    Description: Mice transgenic for the human T cell leukemia virus (HTLV-I) Tax gene develop fibroblastic tumors that express NF-kappa B-inducible early genes. In vitro inhibition of NF-kappa B expression by antisense oligodeoxynucleotides (ODNs) inhibited growth of these culture-adapted Tax-transformed fibroblasts as well as an HTLV-I-transformed human lymphocyte line. In contrast, antisense inhibition of Tax itself had no apparent effect on cell growth. Mice treated with antisense to NF-kappa B ODNs showed rapid regression of transplanted fibrosarcomas. This suggests that NF-kappa B expression may be necessary for the maintenance of the malignant phenotype and provides a therapeutic approach for HTLV-I-associated disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kitajima, I -- Shinohara, T -- Bilakovics, J -- Brown, D A -- Xu, X -- Nerenberg, M -- CA50234/CA/NCI NIH HHS/ -- MH47680/MH/NIMH NIH HHS/ -- NS01330/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1992 Dec 11;258(5089):1792-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuropharmacology, Scripps Research Institute, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1299224" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; Base Sequence ; Cell Division/drug effects ; Cell Line ; Cell Transformation, Neoplastic ; Fibrosarcoma/*drug therapy/pathology ; *Genes, pX ; Human T-lymphotropic virus 1/*genetics ; Humans ; Kinetics ; Lymphocytes ; Mice ; Mice, Transgenic ; Molecular Sequence Data ; NF-kappa B/*antagonists & inhibitors/genetics ; Oligodeoxyribonucleotides ; Oligonucleotides, Antisense/*pharmacology/*therapeutic use
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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