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  • Binding Sites
  • American Association for the Advancement of Science (AAAS)  (34)
  • Springer
  • American Institute of Physics (AIP)
  • 1980-1984  (34)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (34)
  • Springer
  • American Institute of Physics (AIP)
Years
Year
  • 1
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    Cyclic AMP receptor protein: role in transcription activation (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-05-25
    Description: The structure of this pleiotropic activator of gene transcription in bacteria and its interaction sites at promoter DNA's as well as the role of this protein in the RNA polymerase-promoter interactions are reviewed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉de Crombrugghe, B -- Busby, S -- Buc, H -- New York, N.Y. -- Science. 1984 May 25;224(4651):831-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6372090" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Crystallography ; DNA, Bacterial/metabolism ; DNA-Directed RNA Polymerases/metabolism ; Galactose/genetics ; *Gene Expression Regulation ; Lac Operon ; Operon ; Protein Conformation ; Receptors, Cyclic AMP/*physiology ; *Transcription, Genetic
    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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  • 2
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    Amphiphilic secondary structure: design of peptide hormones (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-01-20
    Description: Peptide synthesis can be used for elucidating the roles of secondary structures in the specificity of hormones, antigens, and toxins. Intermediate sized peptides with these activities assume amphiphilic secondary structures in the presence of membranes. When models are designed to optimize the amphiphilicity of the secondary structure, stronger interactions can be observed with the synthetic peptides than with the naturally occurring analogs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kaiser, E T -- Kezdy, F J -- HL-18577/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1984 Jan 20;223(4633):249-55.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6322295" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Apolipoprotein A-I ; Apolipoproteins ; Binding Sites ; Calcitonin ; Chemical Phenomena ; Chemistry ; Corticotropin-Releasing Hormone ; Endorphins ; Glucagon ; Growth Hormone-Releasing Hormone ; *Hormones/pharmacology ; Lipoproteins, HDL ; Melitten ; Models, Structural ; *Peptides/chemical synthesis/metabolism/pharmacology ; Protein Conformation ; Structure-Activity Relationship ; beta-Endorphin
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Analyzing nonlinear scatchard plots (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-01-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Light, K E -- New York, N.Y. -- Science. 1984 Jan 6;223(4631):76-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6546323" target="_blank"〉PubMed〈/a〉
    Keywords: Amphetamines/*metabolism ; Animals ; Binding Sites ; Brain Chemistry ; *Carrier Proteins ; Mathematics ; *Radioligand Assay ; Rats ; Receptors, Adrenergic/*metabolism ; Software
    Print ISSN: 0036-8075
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  • 4
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    Studying enzyme mechanism by 13C nuclear magnetic resonance (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-08-31
    Description: High-resolution carbon-13 nuclear magnetic resonance (NMR) spectra of enzyme-inhibitor and enzyme-substrate complexes provide detailed structural and stereochemical information on the mechanism of enzyme action. The proteases trypsin and papain are shown to form tetrahedrally coordinated complexes and acyl derivatives with a variety of compounds artificially enriched at the site or sites of interest. These results are compared with the structural information derived from x-ray diffraction. Detailed NMR studies have provided a clearer picture of the ionization state of the residues participating in enzyme-catalyzed processes than other more classical techniques. The dynamics of enzymic catalysis can be observed at sub-zero temperatures by a combination of cryoenzymology and carbon-13 NMR spectroscopy. With these powerful techniques, transient, covalently bound intermediates in enzyme-catalyzed reactions can be detected and their structures rigorously assigned.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mackenzie, N E -- Malthouse, J P -- Scott, A I -- New York, N.Y. -- Science. 1984 Aug 31;225(4665):883-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6433481" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Carbon Isotopes ; Carboxypeptidases/metabolism ; Carboxypeptidases A ; Catalysis ; Chemical Phenomena ; Chemistry ; Coenzymes/*metabolism ; Endopeptidases/metabolism ; Enzymes/*metabolism ; Freezing ; Fructose-Bisphosphate Aldolase/metabolism ; Magnetic Resonance Spectroscopy ; Papain/metabolism ; Pepsin A/metabolism ; Peptide Hydrolases/*metabolism ; Protease Inhibitors ; Pterins/metabolism ; Pyridoxal Phosphate/metabolism ; Serine Endopeptidases
    Print ISSN: 0036-8075
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  • 5
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    Acetylcholine receptor: an allosteric protein (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-09-21
    Description: The nicotine receptor for the neurotransmitter acetylcholine is an allosteric protein composed of four different subunits assembled in a transmembrane pentamer alpha 2 beta gamma delta. The protein carries two acetylcholine sites at the level of the alpha subunits and contains the ion channel. The complete sequence of the four subunits is known. The membrane-bound protein undergoes conformational transitions that regulate the opening of the ion channel and are affected by various categories of pharmacologically active ligands.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Changeux, J P -- Devillers-Thiery, A -- Chemouilli, P -- New York, N.Y. -- Science. 1984 Sep 21;225(4668):1335-45.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6382611" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; Amino Acid Sequence ; Animals ; Binding Sites ; Cell Membrane/ultrastructure ; Cloning, Molecular ; DNA/analysis ; Electric Organ/metabolism ; Electrophorus ; Macromolecular Substances ; Protein Conformation ; *Receptors, Nicotinic/genetics/metabolism ; Torpedo
    Print ISSN: 0036-8075
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  • 6
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    Reaction of the antitumor antibiotic CC-1065 with DNA: structure of a DNA adduct with DNA sequence specificity (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-11-16
    Description: Sequence-dependent variations in DNA revealed by x-ray crystallographic studies have suggested that certain DNA-reactive drugs may react preferentially with defined sequences in DNA. Drugs that wind around the helix and reside within one of the grooves of DNA have perhaps the greatest chance of recognizing sequence-dependent features of DNA. The antitumor antibiotic CC-1065 covalently binds through N-3 of adenine and resides within the minor groove of DNA. This drug overlaps with five base pairs for which a high sequence specificity exists.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hurley, L H -- Reynolds, V L -- Swenson, D H -- Petzold, G L -- Scahill, T A -- New York, N.Y. -- Science. 1984 Nov 16;226(4676):843-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6494915" target="_blank"〉PubMed〈/a〉
    Keywords: Antibiotics, Antineoplastic/*metabolism ; *Base Sequence ; Binding Sites ; Chemical Phenomena ; Chemistry ; DNA/*metabolism ; *Indoles ; Leucomycins/*metabolism ; Molecular Conformation ; X-Ray Diffraction
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  • 7
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    Inhibition of human estrogen synthetase (aromatase) by flavones (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-09-07
    Description: Several naturally occurring and synthetic flavones were found to inhibit the aromatization of androstenedione and testosterone to estrogens catalyzed by human placental and ovarian microsomes. These flavones include (in order of decreasing potency) 7,8-benzoflavone, chrysin, apigenin, flavone, flavanone, and quercetin; 5,6-benzoflavone was not inhibitory. 7,8-Benzoflavone and chrysin were potent competitive inhibitors and induced spectral changes in the aromatase cytochrome P-450 indicative of substrate displacement. Flavones may thus compete with steroids in their interaction with certain monooxygenases and thereby alter steroid hormone metabolism.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kellis, J T Jr -- Vickery, L E -- AM1005/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1984 Sep 7;225(4666):1032-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6474163" target="_blank"〉PubMed〈/a〉
    Keywords: Androstenedione/*metabolism ; *Aromatase Inhibitors ; Benzoflavones/metabolism/pharmacology ; Binding Sites ; Binding, Competitive ; Female ; Flavonoids/metabolism/*pharmacology ; Humans ; Kinetics ; Microsomes/enzymology ; Ovary/*enzymology ; Oxidoreductases/*antagonists & inhibitors ; Placenta/*enzymology ; Pregnancy ; Testosterone/*metabolism ; beta-Naphthoflavone
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  • 8
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    Brain enzyme is the target of drug toxin (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-09-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lewin, R -- New York, N.Y. -- Science. 1984 Sep 28;225(4669):1460-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6433484" target="_blank"〉PubMed〈/a〉
    Keywords: 1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine ; Animals ; Binding Sites ; Brain/drug effects/*enzymology/metabolism ; Haplorhini ; Humans ; Mice ; Monoamine Oxidase/*metabolism ; Oxidation-Reduction ; Parkinson Disease, Secondary/*chemically induced ; Pyridines/*metabolism/pharmacology/toxicity ; Rats
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  • 9
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    Primary structure of v-raf: relatedness to the src family of oncogenes (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-04-20
    Description: A replication-defective, acute transforming retrovirus (murine sarcoma virus 3611) was isolated from mouse and molecularly cloned. The nucleotide sequence of 1.5 kilobases encompassing the transforming gene (v-raf) was determined. This sequence, which predicts the amino acid sequence of a gag-raf fusion protein, terminates 180 nucleotides from the 3' end of the acquired cellular sequence. Comparison of the predicted amino acid sequence of v-raf with the predicted amino acid sequences of other oncogenes reveals significant homologies to the src family of oncogenes. There is a lack of homology within the sequence of the tyrosine acceptor domain described for the phosphotyrosine kinase members of the src family of transforming proteins. Phylogenetic arrangement of this family of oncogenes suggests that tyrosine-specific phosphorylation may be a recently acquired activity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mark, G E -- Rapp, U R -- New York, N.Y. -- Science. 1984 Apr 20;224(4646):285-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6324342" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; Biological Evolution ; Cell Transformation, Neoplastic ; Cell Transformation, Viral ; DNA Restriction Enzymes ; Gene Products, gag ; *Genes, Viral ; Mice ; *Oncogenes ; Protein Biosynthesis ; Protein Kinases/metabolism ; Protein-Tyrosine Kinases ; Sarcoma Viruses, Murine/*genetics ; Transcription, Genetic ; Tyrosine/metabolism ; Viral Proteins/analysis/*genetics
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  • 10
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    Need a catalyst? Design an enzyme (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-01-20
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Maugh, T H 2nd -- New York, N.Y. -- Science. 1984 Jan 20;223(4633):269-71.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6608147" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Biochemistry/*methods ; Catalysis ; *Cloning, Molecular ; Enzymes/genetics/*metabolism ; Mutation ; Structure-Activity Relationship ; Substrate Specificity ; Tetrahydrofolate Dehydrogenase/metabolism ; Tyrosine-tRNA Ligase/metabolism ; beta-Lactamases/metabolism
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  • 11
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    Functional properties of antigen-specific T cells infected by human T-cell leukemia-lymphoma virus (HTLV-I) (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-09-28
    Description: Tetanus-toxoid specific helper-inducer T-cell clones, which had been infected and transformed by human T-cell leukemia-lymphoma virus (HTLV-I), were obtained from an antigen-specific human T cell line by using a limiting dilution technique in the presence of the virus. These HTLV-I-infected T-cell clones proliferated specifically in response to soluble tetanus toxoid but, unlike normal T cells, they could do so in the absence of accessory cells. The HTLV-I-infected T-cell clones did not present the antigen to autologous antigen-specific T cells that were not infected with HTLV-I. The capacity of helper-inducer T cells to retain antigen-specific reactivity after infection by HTLV-I, while losing the normal T-cell requirement for accessory cells, has clinical and theoretical implications.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mitsuya, H -- Guo, H G -- Cossman, J -- Megson, M -- Reitz, M S Jr -- Broder, S -- New York, N.Y. -- Science. 1984 Sep 28;225(4669):1484-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6206569" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, Surface/analysis ; Binding Sites ; Cell Line ; Cell Transformation, Viral ; Deltaretrovirus/genetics/*physiology ; Epitopes/metabolism ; Genes, Viral ; Humans ; *Lymphocyte Activation ; Phenotype ; T-Lymphocytes/*immunology/microbiology ; Tetanus Toxoid/immunology ; Viral Proteins/biosynthesis
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  • 12
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    Evolution of proteolytic enzymes (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-04-27
    Description: Proteolytic enzymes have many physiological functions, ranging from generalized protein digestion to more specific regulated processes such as the activation of zymogens, blood coagulation and the lysis of fibrin clots, the release of hormones and pharmacologically active peptides from precursor proteins, and the transport of secretory proteins across membranes. They are present in all forms of living organisms. Comparisons of amino acid sequences, three-dimensional structures, and enzymatic reaction mechanisms of proteases indicate that there are distinct families of these proteins. Changes in molecular structure and function have accompanied the evolution of proteolytic enzymes and their inhibitors, each having relatively simple roles in primitive organisms and more diverse and more complex functions in higher organisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Neurath, H -- GM-15731/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1984 Apr 27;224(4647):350-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6369538" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; *Biological Evolution ; Blood Coagulation ; Chemistry, Physical ; Enzyme Activation ; Enzyme Precursors/metabolism ; Genes ; Humans ; Mutation ; *Peptide Hydrolases/analysis/genetics/metabolism ; Peptides/metabolism ; Physicochemical Phenomena ; Protease Inhibitors/analysis/metabolism ; Protein Conformation ; Protein Sorting Signals ; Substrate Specificity
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  • 13
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    Echinomycin binding sites on DNA (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-09-14
    Description: The preferred binding sites of echinomycin on DNA can be determined by a method called "footprinting." A 32P end-labeled restriction fragment from pBR322 DNA is protected by binding to echinomycin, and cleaved by a synthetic DNA cleaving reagent, methidiumpropyl--EDTA . Fe(II); the DNA cleavage products are then subjected to high-resolution gel analyses. This method reveals that echinomycin has a binding site size of four base pairs. The strong binding sites for echinomycin contain the central two-base-pair sequence 5'-CG-3'. From an analysis of 15 echinomycin sites on 210 base pairs of DNA, key recognition elements for echinomycin are contained in the sequences (5'-3') ACGT and TCGT (A, adenine; C, cytosine; G, guanine; T, thymine).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Van Dyke, M M -- Dervan, P B -- GM-07616/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1984 Sep 14;225(4667):1122-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6089341" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; DNA/metabolism ; DNA Restriction Enzymes ; *Echinomycin/metabolism ; Electrophoresis ; Escherichia coli/genetics ; Plasmids ; *Quinoxalines/metabolism
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  • 14
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    Receptor binding studies (1984)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1984-01-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Siiteri, P K -- New York, N.Y. -- Science. 1984 Jan 13;223(4632):191-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6318319" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Female ; Hormones/*metabolism ; *Radioligand Assay ; Rats ; Rats, Inbred Strains ; Receptors, Cell Surface/*metabolism
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  • 15
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    Demonstration of a saturable binding site for thyrotropin in Yersinia enterocolitica (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-03-18
    Description: Several lines of evidence suggest that there might be immunologic cross-reactivity between the thyroid plasma membrane in humans and antigenic determinants in the enteric pathogen Yersinia enterocolitica. Studies were therefore performed to determine whether Y. enterocolitica, like the thyroid membrane, contains a thyrotropin binding site. A saturable binding site for bovine thyrotropin was indeed demonstrable, particularly in preparations of the organism that have been treated with ethylenediaminetetraacetate and lysozyme. Hormonal specificity of the binding site, as judged from the inhibition of binding of 125I-labeled bovine thyrotropin, was similar to that of the thyrotropin receptor in human thyroid tissue.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Weiss, M -- Ingbar, S H -- Winblad, S -- Kasper, D L -- AM 18416/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1983 Mar 18;219(4590):1331-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6298936" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Binding, Competitive ; Kinetics ; Receptors, Cell Surface/*metabolism ; Receptors, Thyrotropin ; Thyrotropin/*metabolism ; Yersinia enterocolitica/*metabolism
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  • 16
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    Monocyte chemotaxis: stimulation by specific exosite region in thrombin (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-05-13
    Description: Human alpha-thrombin is a potent chemoattractant for human monocytes, with optimum activity occurring at about 10 nanomoles per liter. A variety of thrombins that were chemically modified to alter procoagulant or esterolytic functions showed a similar optimum activity, but complexes of prothrombin or alpha-thrombin with either antithrombin III or hirudin did not. These findings indicate that the regions in thrombin responsible for monocyte chemotaxis are proximate to those involved in certain protein recognition interactions of alpha-thrombin (for example, hirudin binding) but are distinct from the catalytic site and from certain exosites required for clotting.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bar-Shavit, R -- Kahn, A -- Wilner, G D -- Fenton, J W 2nd -- DE-04629/DE/NIDCR NIH HHS/ -- HL-13160/HL/NHLBI NIH HHS/ -- HL-14147/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1983 May 13;220(4598):728-31.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6836310" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Chemotaxis, Leukocyte/*drug effects ; Hirudins/pharmacology ; Humans ; Monocytes/*drug effects ; Prothrombin/pharmacology ; Thrombin/*pharmacology
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  • 17
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    Correlation of glucocorticoid receptor binding sites on MMTV proviral DNA with hormone inducible transcription (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-12-23
    Description: Steroid hormones, when complexed to their receptors, recognize and bind specific DNA sequences and subsequently induce increased levels of transcription. The mechanisms of steroid hormone action were analyzed by constructing chimeric DNA molecules from portions of mouse mammary tumor virus envelope and long terminal repeat (LTR) regions ligated to the thymidine kinase (tk) gene of herpes simplex virus. This construction allowed the tk gene to be expressed in a hormone-responsive fashion upon transfection into Ltk- cells. Comparison of transcription data with in vitro binding data showed that hormone-responsive transcription can be directly correlated to the presence of steroid hormone receptor binding sites on the DNA. There are at least two such receptor binding sites in the LTR region, one between -202 and -137 and another between -137 and -50 base pairs from the RNA cap site, as well as a site near the 5' end of the envelope region. These results strengthen the hypothesis that steroid-receptor complexes regulate genes primarily by binding to DNA sites near the promoter region and thereby modulate transcription.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pfahl, M -- McGinnis, D -- Hendricks, M -- Groner, B -- Hynes, N E -- New York, N.Y. -- Science. 1983 Dec 23;222(4630):1341-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6318311" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Cell Line ; Chimera ; DNA, Viral/*metabolism ; Glucocorticoids/metabolism/*pharmacology ; Mammary Tumor Virus, Mouse/*analysis ; Mice ; Receptors, Glucocorticoid/*metabolism ; Receptors, Steroid/*metabolism ; Repetitive Sequences, Nucleic Acid ; Transcription, Genetic/*drug effects ; Transfection ; Triamcinolone Acetonide/metabolism
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  • 18
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    Number of receptor sites from Scatchard and Klotz graphs: a constructive critique (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-05-27
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Munson, P J -- Rodbard, D -- New York, N.Y. -- Science. 1983 May 27;220(4600):979-81.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6302842" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Ligands ; Mathematics ; Models, Biological ; Receptors, Cell Surface/*metabolism
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  • 19
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    Biospecific labeling with undecagold: visualization of the biotin-binding site on avidin (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-10-15
    Description: The biotin-binding site on avidin has been labeled with biotin conjugated to undecagold, an organometallic cluster compound containing 11 gold atoms in a core angestroms in diameter. Examination of unstained specimens by scanning transmission electron microscopy reveals the labeled sites directly, without computational averaging or filtering of the images. This approach should be widely applicable for determining the locations of subunits and functional site in biological macromolecules at a resolution at a resolution in range of 15 angstroms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Safer, D -- Hainfeld, J -- Wall, J S -- Reardon, J E -- AM 28607/AM/NIADDK NIH HHS/ -- GM 12202/GM/NIGMS NIH HHS/ -- GM 28750/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1982 Oct 15;218(4569):290-1.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7123234" target="_blank"〉PubMed〈/a〉
    Keywords: Avidin/*metabolism ; Binding Sites ; Biotin/*metabolism ; Gold/*metabolism ; Organogold Compounds ; Organometallic Compounds/*metabolism ; Ovalbumin/*analogs & derivatives
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  • 20
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    Penicillin target enzyme and the antibiotic binding site (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-10-29
    Description: The three-dimensional structure of a penicillin-sensitive D-alanyl-carboxypeptidase-transpeptidase has been determined by x-ray crystallography to a resolution of 2.8 angstroms. The site of binding of the beta-lactam antibiotics penicillin and cephalosporin has been located. These findings constitute direct observation of the interaction of beta-lactams with a transpeptidase enzyme and establish the feasibility of defining the molecular stereochemistry of this interaction for purposes of drug design.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kelly, J A -- Moews, P C -- Knox, J R -- Frere, J M -- Ghuysen, J M -- AI-13364-05/AI/NIAID NIH HHS/ -- AI-16702/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1982 Oct 29;218(4571):479-81.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7123246" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; *Carboxypeptidases ; *Cephalosporins ; Crystallography ; Models, Molecular ; *Muramoylpentapeptide Carboxypeptidase ; *Penicillins ; Protein Conformation ; X-Ray Diffraction
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  • 21
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    Isolation of biological materials by use of erbium (III)--induced magnetic susceptibilities (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-08-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Evans, C H -- Tew, W P -- New York, N.Y. -- Science. 1981 Aug 7;213(4508):653-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7256262" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Cations ; *Erbium ; Kinetics ; *Magnetics
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 22
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    Complete nucleotide sequence and organization of the Moloney murine sarcoma virus genome (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-10-23
    Description: The complete nucleotide sequence of a mammalian transforming retrovirus. Moloney murine sarcoma virus, has been determined. MSV, recombinant virus derived of helper viral and cellular sequences, possesses termini resembling prokaryotic transposable elements. The viral genome has the coding capacity for the Moloney murine leukemia virus gag gene product and contains large deletions in pol and env genes. A large open reading frame encompassing its cell-derived sequences codes for its putative transforming protein. The nature of some of the important domains in the viral genome has been established, and their structure is discussed in relation to their function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reddy, E P -- Smith, M J -- Aaronson, S A -- New York, N.Y. -- Science. 1981 Oct 23;214(4519):445-50.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6170110" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, Viral/genetics ; Base Sequence ; Binding Sites ; Cell Transformation, Viral ; DNA, Viral/*genetics ; Defective Viruses/genetics ; Gene Products, gag ; *Genes, Viral ; Moloney murine leukemia virus/*genetics ; RNA, Transfer/genetics ; RNA-Directed DNA Polymerase/genetics ; Repetitive Sequences, Nucleic Acid ; Sarcoma Viruses, Murine/*genetics ; Transcription, Genetic ; Viral Proteins/genetics
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  • 23
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    Tolerance and cross-tolerance in chronic alcoholics: reduced membrane binding of ethanol and other drugs (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-07-31
    Description: Membrane binding of ethanol, anesthetics, and hydrophobic molecules in brain synaptosomes and liver mitochondria from rats is conspicuously reduced after long-term consumption of ethanol. The membranes are resistant to structural disordering by both ethanol and halothane. Tolerance, cross-tolerance, and dependence in chronic alcoholics may in part result from membrane alterations that inhibit the binding of ethanol and other drugs.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rottenberg, H -- Waring, A -- Rubin, E -- AA3442/AA/NIAAA NIH HHS/ -- GM 28173/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1981 Jul 31;213(4507):583-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6264608" target="_blank"〉PubMed〈/a〉
    Keywords: Alcoholism/*metabolism ; Binding Sites ; Brain/*metabolism ; Cell Membrane/drug effects/metabolism/ultrastructure ; Drug Tolerance ; Electron Spin Resonance Spectroscopy ; Ethanol/*pharmacology ; Halothane/pharmacology ; Humans ; Intracellular Membranes/drug effects/metabolism/ultrastructure ; Mitochondria, Liver/*metabolism ; Spin Labels ; Synaptosomes/*metabolism/ultrastructure
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  • 24
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    Secondary structure of 16S ribosomal RNA (1981)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1981-04-24
    Description: A secondary structure model for 16S ribosomal RNA which is based on available chemical, enzymatic, and comparative sequence data shows good agreement between constraints dictated by the model and a wide variety of experimental observations. The four major structural domains created by the base-pairing scheme correspond closely to RNA fragments isolated after nuclease digestion in the presence of bound ribosomal proteins. Functionally important sites appear to be located in unpaired regions and are phylogenetically highly conserved.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Noller, H F -- Woese, C R -- GM 17129/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1981 Apr 24;212(4493):403-11.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6163215" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; Biological Evolution ; Escherichia coli/ultrastructure ; Hydrogen Bonding ; Nucleic Acid Conformation ; Protein Binding ; *RNA, Bacterial ; *RNA, Ribosomal ; Ribonucleases/metabolism ; Ribosomal Proteins/metabolism ; Ribosomes/*ultrastructure ; Substrate Specificity
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  • 25
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    Side-effect reduction by use of drugs that bind to separate but equivalent binding sites (1981)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1981-12-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ehrenstein, G -- Huang, L Y -- New York, N.Y. -- Science. 1981 Dec 18;214(4527):1365-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7313696" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Dose-Response Relationship, Drug ; Drug Synergism ; *Drug-Related Side Effects and Adverse Reactions ; Models, Biological ; Receptors, Drug/*drug effects
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  • 26
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    Influence of calcium ion on the binding of fibrin amino terminal peptides to fibrinogen (1981)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1981-04-24
    Description: The affinity of the amino terminal tetrapeptide of the beta chain of fibrin, Gly-His-Arg-Pro, for fibrinogen dramatically increases in the presence of 2 millimolar calcium ion. In contrast, there is no significant increase in the affinity of peptides beginning with the amino terminal sequence of the fibrin alpha chain, Gly-Pro-Arg, in the presence of calcium ions, although the number of binding sites increases. In the latter case, the increased number of sites is due to the alpha chain analogs binding to the site ordinarily occupied by the beta chain analogs. These results indicate that structures at the amino terminus of the fibrin beta chain play a more important role in fibrin polymerization when calcium ions are present.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Laudano, A P -- Doolittle, R F -- AM-07233/AM/NIADDK NIH HHS/ -- HE-18, 576/PHS HHS/ -- New York, N.Y. -- Science. 1981 Apr 24;212(4493):457-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7209542" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Calcium/*pharmacology ; Fibrin/*metabolism ; Fibrinogen/*metabolism ; Humans ; Peptide Fragments/metabolism ; Protein Binding/drug effects
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  • 27
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    Cadmium-113 nuclear magnetic resonance studies of bovine insulin: two-zinc insulin hexamer specifically binds calcium (1981)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1981-05-01
    Description: By use of cadmium-113 nuclear magnetic resonance spectroscopy, a specific calcium ion binding site has been identified in the bovine two-zinc insulin hexamer. This site is composed of six glutamyl carboxylate groups clustered in the center of the hexamer, and is distinct from the normal zinc ion binding sites.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sudmeier, J L -- Bell, S J -- Storm, M C -- Dunn, M F -- 5S05RR 07010-09/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1981 May 1;212(4494):560-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7010607" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Cadmium ; Calcium/*metabolism ; Cattle ; *Insulin/metabolism ; Isotopes ; Ligands ; Macromolecular Substances ; Magnetic Resonance Spectroscopy ; Protein Conformation ; Zinc/*metabolism
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  • 28
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    Widespread occurrence in frogs and toads of skin compounds interacting with the ouabain site of Na+, K+-ATPase (1980)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1980-05-02
    Description: Amphibians of the family Bufonidae contain high levels of skin compounds that both inhibit Na+- and K+-dependent adenosinetriphosphatase and antagonize the binding of ouabain to the enzyme. In species of Bufo and Atelopus, these compounds are relatively nonpolar bufodienolides, whereas Dendrophryniscus and Melanophryniscus contain more polar compounds of unknown structure. Skin extracts from 30 of 48 species of frogs representing an additional eight families contained relatively low levels of compounds that inhibit binding of ouabain to Na+,K+-adenosinetriphosphatase. The widespread occurrence of low levels of inhibitory compounds is consonant with the role for these compounds as physiological regulators of Na+,K+-adenosinetriphosphatase in amphibian skin; high levels in the Bufonidae probably also serve as a defense against some predators.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Flier, J -- Edwards, M W -- Daly, J W -- Myers, C W -- New York, N.Y. -- Science. 1980 May 2;208(4443):503-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6245447" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anura/*metabolism ; Binding Sites ; Bufanolides/pharmacology ; Ouabain/antagonists & inhibitors/*metabolism ; Skin/analysis/enzymology/*metabolism ; Sodium-Potassium-Exchanging ATPase/*metabolism ; Species Specificity ; Tissue Extracts/pharmacology
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  • 29
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    Three-dimensional molecular modeling and drug design (1980)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1980-06-27
    Description: A discussion of drug-receptor theory is used to show that the three-dimensional structure, or shape, of molecules is important for biological activity. The computer-assisted molecular modeling system at Merck is described, and it is shown that this system is useful for generating and storing molecular structures, determining preferred conformation, comparing molecular shapes, and computing molecular properties. Applications of the system to the study of anti-inflammatory drugs, somatostatin-like compounds, and dihydrofolate reductase inhibitors are summarized.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gund, P -- Andose, J D -- Rhodes, J B -- Smith, G M -- New York, N.Y. -- Science. 1980 Jun 27;208(4451):1425-31.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6104357" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arachidonic Acids ; Binding Sites ; Computers ; Cyclooxygenase Inhibitors ; Humans ; Indomethacin ; *Models, Molecular ; *Models, Structural ; *Molecular Conformation ; *Pharmaceutical Preparations ; Receptors, Drug/metabolism ; Somatostatin/analogs & derivatives ; Structure-Activity Relationship
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  • 30
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    Modeling coordination sites in metallobiomolecules (1980)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1980-07-11
    Description: Synthetic metal complexes can closely approach the properties of metal ions in proteins and yield useful information concerning biological structure and function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ibers, J A -- Holm, R H -- New York, N.Y. -- Science. 1980 Jul 11;209(4453):223-35.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7384796" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Electron Transport ; Humans ; Iron-Sulfur Proteins ; *Metalloproteins ; *Metals ; Molecular Conformation ; Myoglobin ; Oxygen/blood ; Oxyhemoglobins ; Protein Binding ; Protein Conformation
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  • 31
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    Nucleosome cores have two specific binding sites for nonhistone chromosomal proteins HMG 14 and HMG 17 (1980)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1980-09-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mardian, J K -- Paton, A E -- Bunick, G J -- Olins, D E -- GM 19334/GM/NIGMS NIH HHS/ -- GM 7438/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1980 Sep 26;209(4464):1534-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7433974" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Chickens ; Chromosomal Proteins, Non-Histone/*metabolism ; Erythrocytes/ultrastructure ; Nucleosomes/*metabolism/ultrastructure ; Poly dA-dT/metabolism ; Protein Binding
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  • 32
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    Folic acid: crystal structure and implications for enzyme binding (1980)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1980-10-17
    Description: The crystal and molecular structure of folic acid dihydrate has been determined by x-ray diffraction. Folic acid is in an extended conformation with the pteridine ring in the keto form. The C(4) oxygen and N(10) atoms are on the same side of the molecule, hydrogen-bonded to the same water. This conformation has the pteridine rotated approximately 180 degrees away from the orientation of the pteridine ring of methotrexate bound to dihydrofolate reductase. The folic acid pteridine and phenyl rings interact in a stacking manner which is suggestive of the type of associations these groups could form in a complex of folate, dihydrofolate reductase, and reduced nicotinamide adenine dinucleotide phosphate.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mastropaolo, D -- Camerman, A -- Camerman, N -- CA-15879/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1980 Oct 17;210(4467):334-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7423195" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Crystallography ; *Folic Acid ; Molecular Conformation ; Protein Conformation ; Tetrahydrofolate Dehydrogenase ; X-Ray Diffraction
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  • 33
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    Newly made proteins zip through the cell (1980)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1980-01-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J L -- New York, N.Y. -- Science. 1980 Jan 11;207(4427):164-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7350651" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Cells/*metabolism ; Cytoplasmic Granules/metabolism ; Endoplasmic Reticulum/metabolism ; Glycoproteins/biosynthesis/metabolism ; Golgi Apparatus/metabolism ; Humans ; Lysosomes/metabolism ; Protein Precursors/metabolism ; Proteins/*metabolism
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  • 34
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    Promoter sequences of eukaryotic protein-coding genes (1980)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1980-09-19
    Description: In vitro genetic techniques were used to study the sequence requirements for the initiation of specific transcription. Deletion mutants were constructed around the putative promoter of the adenovirus-2 major late and chicken conalbumin genes. Specific transcription in vitro by RNA polymerase B together with a HeLa cell cytoplasmic extract was used as the test for promoter function. With this approach sequences which are essential for the initiation of specific transcription in vitro, were shown to be located between 12 and 32 base pairs upstream from the 5' end of these genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Corden, J -- Wasylyk, B -- Buchwalder, A -- Sassone-Corsi, P -- Kedinger, C -- Chambon, P -- New York, N.Y. -- Science. 1980 Sep 19;209(4463):1406-14.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6251548" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites ; *Cell Physiological Phenomena ; DNA/genetics ; DNA Restriction Enzymes ; DNA, Recombinant ; DNA-Directed RNA Polymerases/*metabolism ; Eukaryotic Cells/*physiology ; *Operon ; RNA Polymerase II/*metabolism ; RNA, Messenger/genetics ; *Transcription, Genetic
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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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