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  • Kinetics  (26)
  • American Association for the Advancement of Science (AAAS)  (26)
  • American Institute of Physics (AIP)
  • Annual Reviews
  • 1985-1989  (26)
  • 1980-1984
  • 1975-1979
  • 1940-1944
  • 1986  (26)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (26)
  • American Institute of Physics (AIP)
  • Annual Reviews
  • Springer  (4)
Years
  • 1985-1989  (26)
  • 1980-1984
  • 1975-1979
  • 1940-1944
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  • 1
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    Irreversible block of the mycelial-to-yeast phase transition of Histoplasma capsulatum (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-01-31
    Description: p-Chloromercuriphenylsulfonic acid (PCMS), a sulfhydryl inhibitor, prevented the mycelial-to-yeast transition of the dimorphic fungal pathogen, Histoplasma capsulatum. The effect of PCMS was specific for the mycelial-to-yeast transformation; it had no effect on growth of either the yeast or mycelial forms or on the yeast-to-mycelial transition. The failure of PCMS-treated mycelia to transform to yeast was permanent and irreversible. PCMS-treated mycelia could not infect mice but could stimulate resistance to infection by a pathogenic strain of Histoplasma capsulatum. These results suggest a new general strategy for vaccine development in diseases caused by dimorphic pathogens.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Medoff, G -- Sacco, M -- Maresca, B -- Schlessinger, D -- Painter, A -- Kobayashi, G S -- Carratu, L -- AI 07015/AI/NIAID NIH HHS/ -- AI 07172/AI/NIAID NIH HHS/ -- AI 16228/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1986 Jan 31;231(4737):476-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3001938" target="_blank"〉PubMed〈/a〉
    Keywords: 4-Chloromercuribenzenesulfonate/pharmacology ; Animals ; Cytochromes/metabolism ; Energy Metabolism/drug effects ; Fungal Proteins/biosynthesis ; Histoplasma/drug effects/pathogenicity/*physiology ; Histoplasmosis/etiology ; Kinetics ; Mice ; Oxidative Phosphorylation/drug effects ; Oxygen Consumption/drug effects
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  • 2
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    Receptor-coupled activation of phosphoinositide-specific phospholipase C by an N protein (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-04-04
    Description: Cleavage of phosphatidylinositol 4,5-bisphosphate by phospholipase C results in the production of two important second messengers: inositol-1,4,5-trisphosphate and 1,2-diacylglycerol. Although several receptors promote this cleavage, the molecular details of phospholipase C activation have remained unresolved. In this study, occupancy of a Ca2+-mobilizing receptor, the oligopeptide chemoattractant receptor on human polymorphonuclear leukocyte plasma membranes, was found to lead to the activation of a guanine nucleotide regulatory (N) protein by guanosine 5'-triphosphate. The activated N protein then stimulated a polyphosphoinositide-specific phospholipase C by reducing the Ca2+ requirement for expression of this activity from superphysiological to normal intracellular concentrations. Therefore, the N protein-mediated activation of phospholipase C may be a key step in the pathway of cellular activation by chemoattractants and certain other hormones.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, C D -- Cox, C C -- Snyderman, R -- 5PO1-CA-29589-04/CA/NCI NIH HHS/ -- 5RO1 DEO 3738-12/DE/NIDCR NIH HHS/ -- New York, N.Y. -- Science. 1986 Apr 4;232(4746):97-100.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3006254" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/blood ; Cell Membrane/metabolism ; Enzyme Activation ; GTP-Binding Proteins/*metabolism ; Humans ; Kinetics ; N-Formylmethionine Leucyl-Phenylalanine/pharmacology ; Neutrophils/metabolism ; Phosphatidylinositols/*blood ; Phosphorus Radioisotopes ; Ribonucleotides/blood ; Type C Phospholipases/*blood
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  • 3
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    Metabolite transfer via enzyme-enzyme complexes (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-11-28
    Description: The concentrations of enzyme sites in cells are usually higher than the concentrations of cognate intermediary metabolites. Therefore metabolic pathways or substantial segments of pathways may proceed by the direct transfer of metabolites from one enzyme site to the next by means of enzyme-enzyme complex formation. This mechanism of metabolite transfer differs from that usually assumed where dissociation and random diffusion of metabolite through the aqueous environment is responsible for the transfer to the next enzyme site. Since the direct transfer mechanism does not involve the aqueous environment, the energetics of metabolite interconversion can differ from expectations based on aqueous solution data. Evidence is summarized suggesting that metabolite is transformed and transferred with equal facility everywhere in the direct transfer pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Srivastava, D K -- Bernhard, S A -- GM10451/GM/NIGMS NIH HHS/ -- GM37056/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Nov 28;234(4780):1081-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3775377" target="_blank"〉PubMed〈/a〉
    Keywords: Enzymes/metabolism ; Kinetics ; Metabolism ; Multienzyme Complexes/biosynthesis/*metabolism ; NAD/metabolism
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  • 4
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    Elimination of anesthetics from rabbit brain (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-12-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Strum, D P -- Johnson, B H -- Eger, E I 2nd -- New York, N.Y. -- Science. 1986 Dec 19;234(4783):1586-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3787265" target="_blank"〉PubMed〈/a〉
    Keywords: Adipose Tissue/metabolism ; Animals ; Brain/*metabolism ; Halothane/*metabolism ; Isoflurane/*metabolism ; Kinetics ; Muscles/metabolism ; Rabbits
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  • 5
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    Three-dimensional structure of an antigen-antibody complex at 2.8 A resolution (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-08-15
    Description: The 2.8 A resolution three-dimensional structure of a complex between an antigen (lysozyme) and the Fab fragment from a monoclonal antibody against lysozyme has been determined and refined by x-ray crystallographic techniques. No conformational changes can be observed in the tertiary structure of lysozyme compared with that determined in native crystalline forms. The quaternary structure of Fab is that of an extended conformation. The antibody combining site is a rather flat surface with protuberances and depressions formed by its amino acid side chains. The antigen-antibody interface is tightly packed, with 16 lysozyme and 17 antibody residues making close contacts. The antigen contacting residues belong to two stretches of the lysozyme polypeptide chain: residues 18 to 27 and 116 to 129. All the complementarity-determining regions and two residues outside hypervariable positions of the antibody make contact with the antigen. Most of these contacts (10 residues out of 17) are made by the heavy chain, and in particular by its third complementarity-determining region. Antigen variability and antibody specificity and affinity are discussed on the basis of the determined structure.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Amit, A G -- Mariuzza, R A -- Phillips, S E -- Poljak, R J -- New York, N.Y. -- Science. 1986 Aug 15;233(4765):747-53.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2426778" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antibodies, Monoclonal ; *Antigen-Antibody Complex ; Chickens ; Egg White ; Epitopes ; *Immunoglobulin Fab Fragments ; Immunoglobulin Heavy Chains ; Immunoglobulin Light Chains ; In Vitro Techniques ; Kinetics ; Models, Molecular ; Muramidase/*immunology ; Protein Conformation ; X-Ray Diffraction
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  • 6
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    Calcium modulation activates Epstein-Barr virus genome in latently infected cells (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-06-20
    Description: In many viral infections the host cell carries the viral genome without producing viral particles, a phenomenon known as viral latency. The cellular mechanisms by which viral latency is maintained or viral replication is induced are not known. The modulation of intracellular calcium concentrations by calcium ionophores induced Epstein-Barr viral antigens in lymphoblastoid cell lines that carry the virus. When calcium ionophores were used in conjunction with direct activators of protein kinase C (12-O-tetradecanoyl phorbol-13-acetate and a synthetic diacylglycerol), a greater induction of viral antigens was observed than with either agent alone. Activation of protein kinase C may be required for the expression of the viral genome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Faggioni, A -- Zompetta, C -- Grimaldi, S -- Barile, G -- Frati, L -- Lazdins, J -- New York, N.Y. -- Science. 1986 Jun 20;232(4757):1554-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3012779" target="_blank"〉PubMed〈/a〉
    Keywords: Aminoquinolines ; Burkitt Lymphoma ; Calcimycin/pharmacology ; Calcium/*pharmacology ; Cell Line ; Cell Transformation, Viral/*drug effects ; Culture Media ; Ethers/pharmacology ; Fluorescent Dyes ; Genes, Viral/*drug effects ; Herpesvirus 4, Human/drug effects/*genetics ; Humans ; Ionomycin ; Kinetics ; Tetradecanoylphorbol Acetate/pharmacology
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  • 7
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    Indirect observation by 13C NMR spectroscopy of a novel CO2 fixation pathway in methanogens (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-01-31
    Description: High-field carbon-13 nuclear magnetic resonance (NMR) spectroscopy has been used to monitor the isotopic dilution of doubly carbon-13-labeled precursors for 2,3-cyclopyrophosphoglycerate, a novel primary metabolite that occurs in certain methanogens. A unique carbon dioxide fixation pathway that gives rise to asymmetric labeling of acetyl coenzyme A has been demonstrated in Methanobacterium thermoautotrophicum. The effect of selected metabolic inhibitors on the labeled species in the pathway has been examined by NMR. These techniques establish a general, sensitive method for the delineation of convergent biosynthetic pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Evans, J N -- Tolman, C J -- Roberts, M F -- RR 00995/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1986 Jan 31;231(4737):488-91.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3079919" target="_blank"〉PubMed〈/a〉
    Keywords: Acetates/metabolism ; Carbon Dioxide/*metabolism ; Carbon Isotopes ; Euryarchaeota/growth & development/*metabolism ; Kinetics ; Magnetic Resonance Spectroscopy/methods ; Pyruvates/metabolism
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  • 8
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    Active human-yeast chimeric phosphoglycerate kinases engineered by domain interchange (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-08-15
    Description: Phosphoglycerate kinase (PGK) is a monomeric protein composed of two domains of approximately equal size, connected by a hinge. Substrate-induced conformational change results in the closure of the active site cleft, which is situated between these two domains. In a study of the relations between structure and function of this enzyme, two interspecies hybrids were constructed, each composed of one domain from the human enzyme and one domain from the yeast enzyme. Despite a 35% difference in the amino acid composition between human and yeast PGK, catalytic properties of the hybrid enzymes are very similar to those of the parental proteins. This result demonstrates that the evolutionary substitutions within these two distantly related molecules do not significantly affect formation of the active site cleft, mechanism of domain closure, or enzyme activity itself.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mas, M T -- Chen, C Y -- Hitzeman, R A -- Riggs, A D -- R01 GM31263/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Aug 15;233(4765):788-90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3526552" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; *Chimera ; *Genes ; *Genes, Fungal ; Genetic Engineering ; Humans ; Kinetics ; Models, Molecular ; Phosphoglycerate Kinase/*genetics/metabolism ; Plasmids ; Protein Conformation ; Protein Multimerization ; Saccharomyces cerevisiae/enzymology/*genetics
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  • 9
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    Stimulation of gonadotropin release by a non-GnRH peptide sequence of the GnRH precursor (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-04-04
    Description: The human gonadotropin-releasing hormone (GnRH) precursor comprises the GnRH sequence followed by an extension of 59 amino acids. Basic amino acid residues in the carboxyl terminal extension may represent sites of processing to biologically active peptides. A synthetic peptide comprising the first 13 amino acids (H X Asp-Ala-Glu-Asn-Leu-Ile-Asp-Ser-Phe-Gln-Glu-Ile-Val X OH) of the 59-amino acid peptide was found to stimulate the release of gonadotropic hormones from human and baboon anterior pituitary cells in culture. The peptide did not affect thyrotropin or prolactin secretion. A GnRH antagonist did not inhibit gonadotropin stimulation by the peptide, and the peptide did not compete with GnRH for GnRH pituitary receptors, indicating that the action of the peptide is independent of the GnRH receptor. The GnRH precursor contains two distinct peptide sequences capable of stimulating gonadotropin release from human and baboon pituitary cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Millar, R P -- Wormald, P J -- Milton, R C -- New York, N.Y. -- Science. 1986 Apr 4;232(4746):68-70.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3082009" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cells, Cultured ; Follicle Stimulating Hormone/*secretion ; Gonadotropin-Releasing Hormone/*analogs & derivatives/*pharmacology ; Humans ; Kinetics ; Luteinizing Hormone/*secretion ; Papio ; Peptide Fragments/*pharmacology ; Peptides/*pharmacology ; Pituitary Gland, Anterior/drug effects/*secretion ; Protein Precursors/*pharmacology ; Structure-Activity Relationship
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  • 10
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    Protein-tyrosine kinase activity in Saccharomyces cerevisiae (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-01-24
    Description: Saccharomyces cerevisiae was examined for tyrosine kinase activity in vitro because this organism offers molecular and genetic approaches for analyzing the role of tyrosine phosphorylation in cellular growth control that are unavailable in higher eukaryotes. Yeast extracts phosphorylated a random copolymer (glutamic acid:tyrosine, 80:20) at tyrosine in a reaction that was linear with respect to time and protein concentration. In the absence of added copolymer, phosphotyrosine was 0.1 percent of the total phosphoamino acids labeled with [gamma-32P]adenosine triphosphate in endogenous yeast proteins. However, specific activities of these reactions were low (approximately 1 percent of those in extracts of chick embryo fibroblasts). Lack of significant incorporation of label from [alpha-32P]adenosine triphosphate into the copolymer or endogenous yeast proteins demonstrated that nucleotide interconversion, adenylylation, and subsequent hydrolysis could not account for the generation of phosphotyrosine observed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schieven, G -- Thorner, J -- Martin, G S -- CA17546/CA/NCI NIH HHS/ -- ES07075/ES/NIEHS NIH HHS/ -- GM21841/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Jan 24;231(4736):390-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2417318" target="_blank"〉PubMed〈/a〉
    Keywords: Kinetics ; Peptides/metabolism ; Phosphorylation ; Phosphotyrosine ; Protein-Tyrosine Kinases/*metabolism ; Saccharomyces cerevisiae/*enzymology/metabolism ; Tyrosine/analogs & derivatives/metabolism
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  • 11
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    In vivo competition between a metallothionein regulatory element and the SV40 enhancer (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-04-04
    Description: The human metallothionein-IIA (hMT-IIA) gene contains an enhancer element within its 5' regulatory region. This enhancer element can compete with the SV40 enhancer for one or more cellular factors in vivo. The competition between the two elements is modulated by cadmium, an inducer of hMT-IIA transcription. The data presented are consistent with a model in which heavy metal ions control the ability of the hMT-IIA enhancer to bind a positive factor, leading to increased transcription. The same factor is required for maximal activity of the SV40 enhancer, which suggests that viruses utilize factors that have a normal role in cellular gene expression to control their own genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scholer, H -- Haslinger, A -- Heguy, A -- Holtgreve, H -- Karin, M -- ES03222/ES/NIEHS NIH HHS/ -- New York, N.Y. -- Science. 1986 Apr 4;232(4746):76-80.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3006253" target="_blank"〉PubMed〈/a〉
    Keywords: Acetyltransferases/genetics ; Animals ; Base Sequence ; Cadmium/pharmacology ; Cell Line ; Cercopithecus aethiops ; Chloramphenicol O-Acetyltransferase ; *Enhancer Elements, Genetic ; *Genes ; *Genes, Regulator ; *Genes, Viral ; Humans ; Kidney ; Kinetics ; Metallothionein/*genetics ; Plasmids ; Simian virus 40/*genetics ; Transcription, Genetic/drug effects ; Transfection
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  • 12
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    Catalytic antibodies (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-12-19
    Description: Monoclonal antibodies elicited to haptens that are analogs of the transition state for hydrolysis of carboxylic esters behaved as enzymic catalysts with the appropriate substrates. These substrates are distinguished by the structural congruence of both hydrolysis products with haptenic fragments. The haptens were potent inhibitors of this esterolytic activity, in agreement with their classification as transition state analogs. Mechanisms are proposed to account for the different chemical behavior of these antibodies with two types of ester substrates. The generation of an artificial enzyme through transition state stabilization by antibodies was thus demonstrated. These studies indicate a potentially general approach to catalyst design.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tramontano, A -- Janda, K D -- Lerner, R A -- GM35318/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Dec 19;234(4783):1566-70.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3787261" target="_blank"〉PubMed〈/a〉
    Keywords: *Antibodies, Monoclonal/immunology ; Binding Sites ; Carboxylic Ester Hydrolases ; *Catalysis ; Chemical Phenomena ; Chemistry ; Esters/immunology/metabolism ; Haptens/immunology ; Hydrolysis ; Kinetics
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  • 13
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    Selectivity of intracellular proteolysis: protein substrates activate the ATP-dependent protease (La) (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-04-25
    Description: A critical enzyme in protein breakdown in Escherichia coli is protease La (the lon gene product), which hydrolyzes proteins and adenosine triphosphate (ATP) in a coupled process. The mechanism of this process was studied with fluorogenic tripeptides. Although proteins and peptides are degraded at the same active site, protein substrates enhance the ability of the enzyme to degrade these peptides two- to tenfold. Proteins that are not substrates had little or no effect. Thus, protein substrates must bind to protease La at two sites, the active site and an allosteric site whose occupancy enhances proteolytic activity. This effect did not require that the proteins themselves be degraded. Proteins could induce peptide breakdown even in the absence of ATP, and proteins and ATP had additive effects in stimulating peptidase activity. A multistep cyclical mechanism is proposed in which the binding of the substrate and ATP activates the protease. The enzyme can then cleave a peptide bond, but is inactivated through ATP hydrolysis. Such a mechanism may help account for the selectivity of protein breakdown and prevent inappropriate or excessive proteolysis in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Waxman, L -- Goldberg, A L -- New York, N.Y. -- Science. 1986 Apr 25;232(4749):500-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2938257" target="_blank"〉PubMed〈/a〉
    Keywords: ATP-Dependent Proteases ; Adenosine Triphosphatases/metabolism ; Adenosine Triphosphate/*metabolism ; Caseins/pharmacology ; Endopeptidases/*metabolism ; Enzyme Activation/drug effects ; Escherichia coli/enzymology ; *Escherichia coli Proteins ; Glucagon/pharmacology ; *Heat-Shock Proteins ; Intracellular Fluid/enzymology/metabolism ; Kinetics ; *Protease La ; Proteins/metabolism ; *Serine Endopeptidases ; Substrate Specificity
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  • 14
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    The intervening sequence RNA of Tetrahymena is an enzyme (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-01-31
    Description: A shortened form of the self-splicing ribosomal RNA (rRNA) intervening sequence of Tetrahymena thermophila acts as an enzyme in vitro. The enzyme catalyzes the cleavage and rejoining of oligonucleotide substrates in a sequence-dependent manner with Km = 42 microM and kcat = 2 min-1. The reaction mechanism resembles that of rRNA precursor self-splicing. With pentacytidylic acid as the substrate, successive cleavage and rejoining reactions lead to the synthesis of polycytidylic acid. Thus, the RNA molecule can act as an RNA polymerase, differing from the protein enzyme in that it uses an internal rather than an external template. At pH 9, the same RNA enzyme has activity as a sequence-specific ribonuclease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zaug, A J -- Cech, T R -- GM28039/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Jan 31;231(4737):470-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3941911" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding, Competitive ; *DNA-Directed RNA Polymerases ; Kinetics ; *RNA Splicing ; RNA, Ribosomal/*genetics/metabolism ; Tetrahymena/*genetics
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  • 15
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    Self-assembling cytotoxins (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-08-01
    Description: Decanal and N-amino-N'-1-octylguanidine (AOG), combined at 28 microM each, mediated erythrocyte lysis within 80 minutes under physiological conditions. By contrast, no lysis was observed after 20 hours with either decanal (56 microM) or AOG (100 microM) alone. The pronounced synergism observed for these chemicals and similar reactive pairs of chemicals is due to the self-assembly of more cytotoxic hydrazones in situ. Decanal and AOG also exhibit synergistic activity against cultured human cells (HeLa) and bacteria (Escherichia coli J96). This synergism may be useful in the design of cytotoxins that would self-assemble selectively from nontoxic precursors within tumors, while sparing normal tissue.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rideout, D -- 1-F32-CA07723/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1986 Aug 1;233(4763):561-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3523757" target="_blank"〉PubMed〈/a〉
    Keywords: Aldehydes/*metabolism/pharmacology ; Cytotoxins/*metabolism/pharmacology ; Dose-Response Relationship, Drug ; Drug Synergism ; Erythrocytes/drug effects ; Escherichia coli/drug effects ; Guanidines/*metabolism/*pharmacology ; HeLa Cells/drug effects ; Humans ; Kinetics ; Neoplasms/drug therapy
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  • 16
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    Selective chemical catalysis by an antibody (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-12-19
    Description: The immunoglobulin MOPC167, which binds the transition state analog p-nitrophenylphosphorylcholine with high affinity, catalyzed the hydrolysis of the corresponding carbonate 1. MOPC167 catalysis displayed saturation kinetics with catalytic constant (kcat) = 0.4 min-1 and Michaelis constant (Km) = 208 microM, showed substrate specificity, and was inhibited by p-nitrophenylphosphorylcholine. The rate of the reaction was first order in hydroxide ion concentration between pH 6.0 and 8.0. The lower limit for the rate of acceleration of hydrolysis by the antibody above the uncatalyzed reaction was 770. This study begins to define the rules for the generation of catalytic antibodies.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pollack, S J -- Jacobs, J W -- Schultz, P G -- New York, N.Y. -- Science. 1986 Dec 19;234(4783):1570-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3787262" target="_blank"〉PubMed〈/a〉
    Keywords: *Antibodies ; Binding Sites ; Carbonates/metabolism ; *Catalysis ; Choline/*analogs & derivatives ; Hydrolysis ; Immunoglobulin A/*metabolism ; Kinetics ; Nitrophenols/metabolism ; Phosphorylcholine/*analogs & derivatives/immunology/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 17
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    Positron emission tomography reveals elevated D2 dopamine receptors in drug-naive schizophrenics (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-12-19
    Description: In postmortem studies of patients with schizophrenia, D2 dopamine receptors in the basal ganglia have been observed to be more numerous than in patients with no history of neurological or psychiatric disease. Because most patients with schizophrenia are treated with neuroleptic drugs that block D2 dopamine receptors in the caudate nucleus, it has been suggested that this increase in the number of receptors is a result of adaptation to these drugs rather than a biochemical abnormality intrinsic to schizophrenia. With positron emission tomography (PET), the D2 dopamine receptor density in the caudate nucleus of living human beings was measured in normal volunteers and in two groups of patients with schizophrenia--one group that had never been treated with neuroleptics and another group that had been treated with these drugs. D2 dopamine receptor densities in the caudate nucleus were higher in both groups of patients than in the normal volunteers. Thus, schizophrenia itself is associated with an increase in brain D2 dopamine receptor density.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wong, D F -- Wagner, H N Jr -- Tune, L E -- Dannals, R F -- Pearlson, G D -- Links, J M -- Tamminga, C A -- Broussolle, E P -- Ravert, H T -- Wilson, A A -- Toung, J K -- Malat, J -- Williams, J A -- O'Tuama, L A -- Snyder, S H -- Kuhar, M J -- Gjedde, A -- 1RO1 53146/PHS HHS/ -- NS15080/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1986 Dec 19;234(4783):1558-63.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2878495" target="_blank"〉PubMed〈/a〉
    Keywords: Adult ; Antipsychotic Agents/*therapeutic use ; Caudate Nucleus/*metabolism ; Haloperidol/therapeutic use ; Humans ; Kinetics ; Receptors, Dopamine/*metabolism ; Receptors, Dopamine D2 ; Schizophrenia/drug therapy/*metabolism ; Spiperone/analogs & derivatives/metabolism ; Tomography, Emission-Computed
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  • 18
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    Role of platelet-activating factor-acether in mediating guinea pig anaphylaxis (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-04-04
    Description: The pathophysiology of anaphylaxis is very complex, and the sequelae of events are not fully explained in terms of the effects of histamine and peptide leukotrienes alone. Platelet-activating factor (1-O-alkyl-2-acetyl-sn-glyceryl-3-phosphorylcholine, PAF-acether) has been detected in animals undergoing anaphylaxis. Injection of synthetic PAF-acether induces similar effects, including bronchoconstriction, respiratory arrest, systemic hypotension, neutropenia, and thrombocytopenia. The results reported here demonstrate that the histamine- and leukotriene-independent component of guinea pig anaphylaxis in vivo and in isolated lung parenchymal strips in vitro is mediated by PAF-acether. However, PAF-acether is not responsible for the anaphylaxis-induced thrombocytopenia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Darius, H -- Lefer, D J -- Smith, J B -- Lefer, A M -- HL-25575/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1986 Apr 4;232(4746):58-60.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3082008" target="_blank"〉PubMed〈/a〉
    Keywords: 4,5-Dihydro-1-(3-(trifluoromethyl)phenyl)-1H-pyrazol-3-amine ; Alprazolam ; *Anaphylaxis ; Animals ; Anti-Inflammatory Agents/pharmacology ; Benzodiazepines/pharmacology ; Blood Pressure ; Diphenhydramine/pharmacology ; Guinea Pigs ; In Vitro Techniques ; Kinetics ; Lung/drug effects/*immunology ; Male ; Ovalbumin ; Platelet Activating Factor/*immunology ; Platelet Count/drug effects ; Pyrazoles/pharmacology
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  • 19
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    Genetic control of melatonin synthesis in the pineal gland of the mouse (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-01-31
    Description: Pineal melatonin may play an important role in regulation of vertebrate circadian rhythms and in human affective disorders. In some mammals, such as hamsters and sheep, melatonin is involved in photoperiodic time measurement and in control of reproduction. Although wild mice (Mus domesticus) and some wild-derived inbred strains of mice have melatonin in their pineal glands, several inbred strains of laboratory mice (for example, C57BL/6J) were found not to have detectable melatonin in their pineal glands. Genetic analysis suggests that melatonin deficiency in C57BL/6J mice results from mutations in two independently segregating, autosomal recessive genes. Synthesis of melatonin from serotonin in the pineal gland requires the enzymes N-acetyltransferase (NAT) and hydroxyindole-O-methyltransferase (HIOMT). Pineal glands from C57BL/6J mice have neither NAT nor HIOMT activity. These results suggest that the two genes involved in melatonin deficiency are responsible for the absence of normal NAT and HIOMT enzyme activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ebihara, S -- Marks, T -- Hudson, D J -- Menaker, M -- 13162/PHS HHS/ -- FO5TW03377/TW/FIC NIH HHS/ -- New York, N.Y. -- Science. 1986 Jan 31;231(4737):491-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3941912" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Chromatography, High Pressure Liquid ; Female ; Kinetics ; Male ; Melatonin/biosynthesis/deficiency/*genetics ; Mice ; Mice, Inbred C57BL ; Mice, Inbred Strains ; Pineal Gland/*metabolism ; Reference Values ; Species Specificity
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  • 20
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    Modification of the active site of alkaline phosphatase by site-directed mutagenesis (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-01-10
    Description: The catalytically essential amino acid in the active site of bacterial alkaline phosphatase (Ser-102) has been replaced with a cysteine by site-directed mutagenesis. The resulting thiol enzyme catalyzes the hydrolysis of a variety of phosphate monoesters. The rate-determining step of hydrolysis, however, is no longer the same for catalysis when the active protein nucleophile is changed from the hydroxyl of serine to the thiol of cysteine. Unlike the steady-state kinetics of native alkaline phosphatase, those of the mutant show sensitivity to the leaving group of the phosphate ester.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ghosh, S S -- Bock, S C -- Rokita, S E -- Kaiser, E T -- AM 07122-02/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1986 Jan 10;231(4734):145-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3510454" target="_blank"〉PubMed〈/a〉
    Keywords: *2,4-Dinitrophenol/*analogs & derivatives ; Alkaline Phosphatase/*genetics/metabolism ; Amino Acid Sequence ; Binding Sites ; DNA/genetics ; Dinitrophenols/metabolism ; Escherichia coli/enzymology/genetics ; Kinetics ; Mutation ; Nitrophenols/metabolism ; Organophosphates/metabolism ; Organophosphorus Compounds/metabolism ; Plasmids
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  • 21
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    Vasoconstriction: a new activity for platelet-derived growth factor (1986)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1986-04-04
    Description: Platelet-derived growth factor (PDGF) is a potent mitogen for vascular smooth muscle cells that has been implicated in the pathogenesis of atherosclerosis. The potential role of PDGF in the altered vasoreactivity of atherosclerotic vessels has been studied through an examination of its effects on contractility in the rat aorta. PDGF caused a concentration-dependent contraction of aortic strips and was significantly more potent on a molar basis than the classic vasoconstrictor peptide angiotensin II. Furthermore, PDGF increased the cytosolic free calcium concentration in cultured rat aortic smooth muscle cells. These observations suggest a new biological activity for PDGF that may contribute to the enhanced vasoreactivity of certain atherosclerotic vessels.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berk, B C -- Alexander, R W -- Brock, T A -- Gimbrone, M A Jr -- Webb, R C -- HL20054/HL/NHLBI NIH HHS/ -- HL22602/HL/NHLBI NIH HHS/ -- HL35013/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1986 Apr 4;232(4746):87-90.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3485309" target="_blank"〉PubMed〈/a〉
    Keywords: Aminoquinolines ; Angiotensin II/pharmacology ; Animals ; Aorta/*drug effects/metabolism/physiology ; Calcium/metabolism ; Cytosol/metabolism ; Dose-Response Relationship, Drug ; Epidermal Growth Factor/pharmacology ; Fluorescent Dyes ; Homeostasis/drug effects ; Humans ; In Vitro Techniques ; Kinetics ; Platelet-Derived Growth Factor/*pharmacology ; Rats ; Vasoconstriction/*drug effects
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  • 22
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    A receptor-mediated pathway for cholesterol homeostasis (1986)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1986-04-04
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brown, M S -- Goldstein, J L -- New York, N.Y. -- Science. 1986 Apr 4;232(4746):34-47.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3513311" target="_blank"〉PubMed〈/a〉
    Keywords: Biological Transport ; Cholesterol/*metabolism ; Endocytosis ; *Homeostasis ; Humans ; Hyperlipoproteinemia Type II/*metabolism ; Kinetics ; Lipid Metabolism, Inborn Errors/metabolism ; Lipoproteins, HDL/blood ; Lipoproteins, LDL/blood/*metabolism ; Models, Biological ; Mutation ; Receptors, LDL/genetics/*metabolism
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  • 23
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    Curvilinear, three-dimensional motion of chromatin domains and nucleoli in neuronal interphase nuclei (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-11-14
    Description: The term "nuclear rotation" refers to a motion of nucleoli within interphase nuclei of several cell types. No mechanism or function has been ascribed to this phenomenon, and it was unknown whether nuclear structures in addition to nucleoli participate in this motion. Moreover, it was unclear whether nuclear rotation occurs independent of concurrent motion of juxtanuclear cytoplasm. The work reported here presents quantitative evidence, for three-dimensional intranuclear, tandem motion of fluorescently labeled chromatin domains associated with nucleoli and those remote from nucleoli. The results show that such motion is curvilinear, that it is not restricted to nucleoli, and, moreover, that it occurs independently of motion of juxtanuclear, cytoplasmic structures. These results suggest that this motion represents karyoplasmic streaming and its function is to transpose to nuclear pores those chromatin domains actively transcribed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉De Boni, U -- Mintz, A H -- New York, N.Y. -- Science. 1986 Nov 14;234(4778):863-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3775367" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Nucleolus/*physiology/ultrastructure ; *Chromatin ; Fluorescent Dyes ; Histocytochemistry ; Indoles ; *Interphase ; Kinetics ; Movement ; Neurons/*ultrastructure ; Nuclear Envelope/physiology
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  • 24
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    Calmodulin, cyclophilin, and cyclosporin A (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-08-29
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hait, W N -- Harding, M W -- Handschumacher, R E -- New York, N.Y. -- Science. 1986 Aug 29;233(4767):987-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3016900" target="_blank"〉PubMed〈/a〉
    Keywords: 3',5'-Cyclic-AMP Phosphodiesterases/metabolism ; Animals ; Calmodulin/*metabolism ; Carrier Proteins/*metabolism ; Cattle ; Cyclosporins/*metabolism/pharmacology ; Humans ; Kinetics ; Peptidylprolyl Isomerase ; Rabbits
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  • 25
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    Activation of smooth muscle contraction: relation between myosin phosphorylation and stiffness (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-04-04
    Description: Contraction and myosin light-chain phosphorylation were measured in electrically stimulated tracheal smooth muscle. Latencies for the onset of force, stiffness, and light-chain phosphorylation were 500 milliseconds. Myosin light chain was phosphorylated from 0.04 to 0.80 mole of phosphate per mole of light chain with a pseudo-first-order rate of 1.1 per second with no evidence of an ordered or negatively cooperative process. Following the period of latency, stiffness increased with phosphorylation and both increased more rapidly than isometric force. The linear relation between stiffness and phosphorylation during activation suggests independent attachment of each myosin head upon phosphorylation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kamm, K E -- Stull, J T -- HL 26043/HL/NHLBI NIH HHS/ -- HL 32607/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1986 Apr 4;232(4746):80-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3754063" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carbachol/pharmacology ; Electric Stimulation ; In Vitro Techniques ; Kinetics ; *Muscle Contraction/drug effects ; Muscle, Smooth/*physiology ; Myosin-Light-Chain Kinase ; Myosins/*metabolism ; Phosphorylation ; Protein Kinases/metabolism ; Trachea/physiology
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  • 26
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    Functional role of aspartic acid-27 in dihydrofolate reductase revealed by mutagenesis (1986)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1986-03-07
    Description: The crystal structures and enzymic properties of two mutant dihydrofolate reductases (Escherichia coli) were studied in order to clarify the functional role of an invariant carboxylic acid (aspartic acid at position 27) at the substrate binding site. One mutation, constructed by oligonucleotide-directed mutagenesis, replaces Asp27 with asparagine; the other is a primary-site revertant to Ser27. The only structural perturbations involve two internally bound water molecules. Both mutants have low but readily measurable activity, which increases rapidly with decreasing pH. The mutant enzymes were also characterized with respect to relative folate: dihydrofolate activities and kinetic deuterium isotope effects. It is concluded that Asp27 participates in protonation of the substrate but not in electrostatic stabilization of a positively charged, protonated transition state.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Howell, E E -- Villafranca, J E -- Warren, M S -- Oatley, S J -- Kraut, J -- F32 GM09375/GM/NIGMS NIH HHS/ -- GM10928/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1986 Mar 7;231(4742):1123-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/3511529" target="_blank"〉PubMed〈/a〉
    Keywords: *Aspartic Acid ; Crystallography ; Deuterium ; Escherichia coli ; Kinetics ; Methotrexate/metabolism ; Mutation ; Protein Binding ; Structure-Activity Relationship ; *Tetrahydrofolate Dehydrogenase
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