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  • Structure-Activity Relationship
  • American Association for the Advancement of Science (AAAS)  (68)
  • Annual Reviews
  • 1990-1994  (29)
  • 1980-1984  (26)
  • 1975-1979  (13)
  • 1965-1969
  • 1935-1939
Collection
Keywords
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  • American Association for the Advancement of Science (AAAS)  (68)
  • Annual Reviews
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Year
  • 1
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    Monoclonal antibodies reveal the structural basis of antibody diversity (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-11-18
    Description: Hybridoma technology has made it possible to introduce into continuous culture normal antibody-forming cells and to obtain large amounts of the immunoglobulin produced by each of these cells. Examination of the structure of a number of monoclonal antibodies that react with a single antigen has provided new information on the structural basis of the specificity and affinity of antibodies. Comparisons of families of monoclonal antibodies derived from a single germ line gene revealed the importance of somatic mutation in generating antibody diversity. Monoclonal antibodies that react with variable regions of other monoclonals allow the further dissection and modulation of the immune response. Finally, the continued somatic instability of immunoglobulin genes in cultured antibody-forming cells makes it possible to determine the rate of somatic mutation and to generate mutant monoclonal antibodies that may be more effective serological reagents.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Teillaud, J L -- Desaymard, C -- Giusti, A M -- Haseltine, B -- Pollock, R R -- Yelton, D E -- Zack, D J -- Scharff, M D -- 5T32GM7288/GM/NIGMS NIH HHS/ -- AI05231/AI/NIAID NIH HHS/ -- AI10702/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1983 Nov 18;222(4625):721-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6356353" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antibodies, Monoclonal/genetics/*immunology ; *Antibody Diversity ; Antibody Specificity ; Genes ; Hybridomas/immunology ; Immunoglobulin Idiotypes/immunology ; Immunoglobulin Variable Region/genetics ; Mice ; Mutation ; Protein Conformation ; 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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  • 2
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    Nicarbazin complex yields dinitrocarbanilide as ultrafine crystals with improved anticoccidial activity (1983)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1983-11-11
    Description: Nicarbazin, a drug used to control the protozoal disease coccidiosis in poultry, is a complex of the highly insoluble drug 4,4'-dinitrocarbanilide with 2-hydroxy-4,6-dimethylpyrimidine. The structures of this and other 4,4'-dinitrocarbanilide complexes have not been determined, but an analogous 2:1 complex of 4,4'-dinitrodiphenylamine with 1,4-diacetylpiperazine has been prepared in which the only possible bonds are hydrogen bonds between the amide carbonyls and amino hydrogens. Scanning electron microscopy revealed that micron-size crystals of nicarbazin disintegrate in water to form much smaller dinitrocarbanilide crystals. Similar complex dissolution in the gut of poultry may account for the greater effectiveness of dinitrocarbanilide when administered as complexed rather than uncomplexed drug. Particle size problems associated with other highly insoluble drugs and pesticides may be resolved by the use of nicarbazin-like complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rogers, E F -- Brown, R D -- Brown, J E -- Kazazis, D M -- Leanza, W J -- Nichols, J R -- Ostlind, D A -- Rodino, T M -- New York, N.Y. -- Science. 1983 Nov 11;222(4624):630-2.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6635662" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Carbanilides/*administration & dosage ; Chickens ; Coccidiostats ; Crystallization ; Intestinal Absorption ; Nicarbazin/*administration & dosage ; Poultry Diseases/*prevention & control ; Solubility ; 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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  • 3
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    Hyperglycemia of diabetic rats decreased by a glucagon receptor antagonist (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-02-26
    Description: The glucagon analog [l-N alpha-trinitrophenylhistidine, 12-homoarginine]-glucagon (THG) was examined for its ability to lower blood glucose concentrations in rats made diabetic with streptozotocin. In vitro, THG is a potent antagonist of glucagon activation of the hepatic adenylate cyclase assay system. Intravenous bolus injections of THG caused rapid decreases (20 to 35 percent) of short duration in blood glucose. Continuous infusion of low concentrations of the inhibitor led to larger sustained decreases in blood glucose (30 to 65 percent). These studies demonstrate that a glucagon receptor antagonist can substantially reduce blood glucose levels in diabetic animals without addition of exogenous insulin.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Johnson, D G -- Goebel, C U -- Hruby, V J -- Bregman, M D -- Trivedi, D -- AM21085/AM/NIADDK NIH HHS/ -- AM25318/AM/NIADDK NIH HHS/ -- New York, N.Y. -- Science. 1982 Feb 26;215(4536):1115-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6278587" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Diabetes Mellitus, Experimental/*drug therapy ; Glucagon/*analogs & derivatives/*antagonists & inhibitors/therapeutic use ; Hyperglycemia/*drug therapy ; Male ; Rats ; Receptors, Cell Surface/*drug effects ; Receptors, Glucagon ; Structure-Activity Relationship
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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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  • 4
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    Intrasubunit signal transduction by the aspartate chemoreceptor (1991)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1991-12-23
    Description: Receptors that transmit signals across cell membranes are typically composed of multiple subunits. To test whether subunit interactions are required for transmembrane signaling by the bacterial aspartate receptor, dimers were constructed with (i) two full-length subunits, (ii) one full-length subunit and one subunit lacking the cytoplasmic domain, or (iii) one full-length subunit and one subunit lacking both the cytoplasmic and the transmembrane domains. Methylation of the cytoplasmic domain of all three receptor constructs was stimulated by the binding of aspartate. These findings demonstrate that transmembrane signaling does not require interactions between cytoplasmic or transmembrane domains of adjacent subunits and suggest that signaling occurs via conformational changes transduced through a single subunit.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Milligan, D L -- Koshland, D E Jr -- DK 09765/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1991 Dec 13;254(5038):1651-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, University of California, Berkeley 94720.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1661030" target="_blank"〉PubMed〈/a〉
    Keywords: Aspartic Acid/*physiology ; DNA Mutational Analysis ; Ligands ; Macromolecular Substances ; Methylation ; Protein Conformation ; *Receptors, Amino Acid ; Receptors, Cell Surface/*chemistry ; Recombinant Proteins ; Salmonella typhimurium ; Signal Transduction ; 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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  • 5
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    Electrophoresis of flexible macromolecules: evidence for a new mode of transport in gels (1990)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1990-06-08
    Description: Movement of macromolecules through low concentration agarose gels was investigated with linear poly(styrenesulfonate), linear DNA, star-shaped poly(styrenesulfonate), and circular DNA. Mobilities of weakly entangled flexible macromolecules were independent of molecular radius; within a homologous chemical sequence, electrophoretic separation at low field strengths depended solely on the degree of polymerization. These observations cannot be explained either by sieving or by reptation mechanisms; transport was apparently controlled by spatial variations of chain configurational entropy. Only when the chain was highly entangled did chain topology affect mobility. Evidence for entropically regulated transport clarifies how gel electrophoresis separates flexible macromolecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smisek, D L -- Hoagland, D A -- New York, N.Y. -- Science. 1990 Jun 8;248(4960):1221-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Polymer Science and Engineering, University of Massachusetts, Amherst 01003.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2349481" target="_blank"〉PubMed〈/a〉
    Keywords: DNA/*isolation & purification ; DNA, Circular/*isolation & purification ; Electrophoresis, Agar Gel/methods ; Molecular Conformation ; Polystyrenes/*isolation & purification ; Resins, Synthetic ; Structure-Activity Relationship
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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
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    Functional consequences of posttranslational isomerization of Ser46 in a calcium channel toxin (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-11-11
    Description: The venom of the funnel-web spider Agelenopsis aperta contains several peptides that paralyze prey by blocking voltage-sensitive calcium channels. Two peptides, omega-Aga-IVB (IVB) and omega-Aga-IVC (IVC), have identical amino acid sequences, yet have opposite absolute configurations at serine 46. These toxins had similar selectivities for blocking voltage-sensitive calcium channel subtypes but different potencies for blocking P-type voltage-sensitive calcium channels in rat cerebellar Purkinje cells as well as calcium-45 influx into rat brain synaptosomes. An enzyme purified from venom converts IVC to IVB by isomerizing serine 46, which is present in the carboxyl-terminal tail, from the L to the D configuration. Unlike the carboxyl terminus of IVC, that of IVB was resistant to the major venom protease. These results show enzymatic activities in A. aperta venom being used in an unprecedented strategy for coproduction of necessary neurotoxins that possess enhanced stability and potency.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heck, S D -- Siok, C J -- Krapcho, K J -- Kelbaugh, P R -- Thadeio, P F -- Welch, M J -- Williams, R D -- Ganong, A H -- Kelly, M E -- Lanzetti, A J -- New York, N.Y. -- Science. 1994 Nov 11;266(5187):1065-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉NPS Pharmaceuticals Incorporated, Salt Lake City, Utah 84108.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973665" target="_blank"〉PubMed〈/a〉
    Keywords: Agatoxins ; Amino Acid Sequence ; Animals ; Base Sequence ; Calcium/metabolism ; Calcium Channel Blockers/chemistry/*metabolism/toxicity ; Calcium Channels/*metabolism ; Isomerases/metabolism ; Molecular Sequence Data ; *Protein Processing, Post-Translational ; Purkinje Cells/metabolism ; Rats ; Serine/*metabolism ; Spider Venoms/chemistry/enzymology/*metabolism/toxicity ; Stereoisomerism ; Structure-Activity Relationship ; Synaptosomes/metabolism
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  • 7
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    Digitalis genin activity: side-group carbonyl oxygen position is a major determinant (1979)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1979-08-31
    Description: The Na+,k+-adenosine triphosphatase-inhibiting activity of digitalis genins and their analogs is a function of side-group carbonyl (C = O) oxygen position. For each 2.2 angstroms that this oxygen is displaced from its position in digitoxigenin, activity drops by one order of magnitude. This quantitative relation resolves previously proposed models which have attempted to describe the molecular basis of genin activity. A multidisciplinary (crystallographic, conformational energy, synthetic, biological) approach to structure-activity relations is described.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fullerton, D S -- Yoshioka, K -- Rohrer, D C -- From, A H -- Ahmed, K -- New York, N.Y. -- Science. 1979 Aug 31;205(4409):917-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/224455" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/enzymology ; Digitalis Glycosides/*pharmacology ; Molecular Conformation ; Rats ; Sodium-Potassium-Exchanging ATPase/*antagonists & inhibitors ; Structure-Activity Relationship
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  • 8
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    Bioactive conformation of luteinizing hormone-releasing hormone: evidence from a conformationally constrained analog (1980)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1980-11-07
    Description: An analog of luteinizing hormone-releasing hormone containing a gamma-lactam as a conformational constraint has been prepared with the use of a novel cyclization of a methionine sulfonium salt. The analog is more active as a luteinizing hormone-releasing hormone agonist that the parent hormone, and provides evidence for a bioactive conformation containing a beta-turn.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Freidinger, R M -- Veber, D F -- Perlow, D S -- Brooks, J R -- Saperstein, R -- New York, N.Y. -- Science. 1980 Nov 7;210(4470):656-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7001627" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Biological Assay ; Cells, Cultured ; Female ; *Gonadotropin-Releasing Hormone/analogs & derivatives ; Hydrogen Bonding ; Lactams ; Protein Conformation ; Rats ; 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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  • 9
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    Tricyclic antidepressants: therapeutic properties and affinity for alpha-noradrenergic receptor binding sites in the brain (1978)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1978-01-13
    Description: Tricyclic antidepressants vary in their capacity to cause psychomotor activation, to relieve agitated depressive states, and to cause sedation and hypotension. We have quantified relative potencies of tricyclic antidepressants in competing for the binding of 3H-labeled WB-4101 to alpha-noradrenergic receptor sites in rat brain membranes. Affinities of tricyclic drugs for alpha-noradrenergic receptor sites in the brain correlate well with the capacity of these agents to relieve psychomotor agitation and to induce sedation and hypotension; these affinities also correlate inversely with tendencies to elicit psychomotor activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉U'Prichard, D C -- Greenberg, D A -- Sheehan, P P -- Snyder, S H -- New York, N.Y. -- Science. 1978 Jan 13;199(4325):197-8.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/202024" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antidepressive Agents, Tricyclic/*metabolism/therapeutic use ; Binding, Competitive ; Brain/*metabolism ; Humans ; Hypotension/chemically induced ; Psychomotor Agitation/*drug therapy ; Rats ; Receptors, Adrenergic/*metabolism ; Receptors, Adrenergic, alpha/*metabolism ; Structure-Activity Relationship
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    Spinal sympathetic neurons: possible sites of opiate-withdrawal suppression by clonidine (1982)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1982-03-26
    Description: Morphine, methadone, meperidine, fentanyl, and clonidine rapidly depressed transmission through sympathetic preganglionic neurons in cats with the spinal cord transected. Naloxone promptly antagonized this effect of the opiates but not that of clonidine which was reversed by alpha 2-adrenergic receptor antagonists. The independent depression of preganglionic neurons by clonidine may contribute to the ability of this drug to depress the symptoms of opiate withdrawal that are characterized by sympathetic hyperactivity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Franz, D N -- Hare, D B -- McCloskey, K L -- GM-07579/GM/NIGMS NIH HHS/ -- HL-24085/HL/NHLBI NIH HHS/ -- RR-05428/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1982 Mar 26;215(4540):1643-5.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/6280276" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cats ; Clonidine/*pharmacology/therapeutic use ; Evoked Potentials/drug effects ; Humans ; Narcotics/pharmacology ; Receptors, Drug/drug effects ; Reflex/drug effects ; Spinal Cord/cytology ; Structure-Activity Relationship ; Substance Withdrawal Syndrome/*drug therapy ; Sympathetic Nervous System/*drug effects ; Synaptic Transmission/*drug effects
    Print ISSN: 0036-8075
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