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  • Articles  (12)
  • Binding Sites
  • American Association for the Advancement of Science (AAAS)  (12)
  • American Institute of Physics
  • 2020-2022
  • 1980-1984  (9)
  • 1975-1979  (3)
  • 1940-1944
  • 1
    Publication Date: 1978-06-16
    Description: Throbin-activated human platelets cause agglutination of trypsinized, formalinized bovine erythrocytes. This lectin activity of stimulated platelets was blocked by galactosamine, glucosamine, mannosamine, lysine, and arginine, but not by N-acetylated sugars, other neutral sugars, or other amino acids. Inhibitors of the thrombin-induced lectin activity also blocked thrombin-induced platelet aggregation. It appears that a membrane surface component that has lectin activity mediates platelet aggregation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gartner, T K -- Williams, D C -- Minion, F C -- Phillips, D R -- New York, N.Y. -- Science. 1978 Jun 16;200(4347):1281-3.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/663608" target="_blank"〉PubMed〈/a〉
    Keywords: *Agglutinins ; Amino Acids/pharmacology ; Amino Sugars/pharmacology ; Animals ; Binding Sites ; Cytochalasin B/pharmacology ; *Hemagglutinins ; Humans ; Membrane Proteins/blood ; Platelet Aggregation/*drug effects ; Prostaglandins E/pharmacology ; Species Specificity ; Thrombin/*pharmacology
    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
    Publication Date: 1979-12-07
    Description: A laser-induced luminescence technique is introduced for probing the structure and equilibria of lanthanide complexes and lanthanide ion binding to macromolecules. The method involves the excitation of the 7F0 leads to 5D0 transition between nondegenerate levels in the europium(III) ion by means of an intense pulsed dye laser source. Excitation profits obtained by scanning the laser through the transition region reveal distinct peaks characteristic of individual europium(III) ion environments. The technique may be used to characterize the species present in complex equilibria in solution or to study europium(III) binding to macromolecules. Distinct europium(III) binding sites in thermolysin with long and short excited state lifetimes are observed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Horrocks, W D Jr -- Sudnick, D R -- New York, N.Y. -- Science. 1979 Dec 7;206(4423):1194-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/505007" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; *Europium ; Luminescence ; Protein Binding ; Spectrum Analysis/methods ; Thermolysin
    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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  • 3
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    American Association for the Advancement of Science (AAAS)
    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
    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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  • 4
    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
    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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  • 5
    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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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
    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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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 7
    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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    American Association for the Advancement of Science (AAAS)
    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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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
    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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  • 10
    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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    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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