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  • Articles  (3)
  • Structure-Activity Relationship  (3)
  • 1985-1989  (3)
  • Computer Science  (3)
  • 1
    Publication Date: 1989-09-22
    Description: The inhibition by charybdotoxin of A-type potassium channels expressed in Xenopus oocytes was studied for several splicing variants of the Drosophila Shaker gene and for several site-directed mutants of this channel. Charybdotoxin blocking affinity is lowered by a factor of 3.5 upon replacing glutamate-422 with glutamine, and by a factor of about 12 upon substituting lysine in this position. Replacement of glutamate-422 by aspartate had no effect on toxin affinity. Thus, the glutamate residue at position 422 of this potassium channel is near or in the externally facing mouth of the potassium conduction pathway, and the positively charged toxin is electrostatically focused toward its blocking site by the negative potential set up by glutamate-422.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉MacKinnon, R -- Miller, C -- AR 19826/AR/NIAMS NIH HHS/ -- GM 31768/GM/NIGMS NIH HHS/ -- NS 07292/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1989 Sep 22;245(4924):1382-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Brandeis University, Waltham, MA 02254.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2476850" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Charybdotoxin ; DNA Mutational Analysis ; Drosophila melanogaster ; Ions ; Membrane Proteins/genetics/metabolism/ultrastructure ; Potassium Channels/*metabolism/ultrastructure ; Scorpion Venoms/*metabolism ; Structure-Activity Relationship ; Transfection ; Xenopus laevis
    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: 1988-07-22
    Description: The alpha subunits of Gs and Gi link different sets of hormone receptors to stimulation and inhibition, respectively, of adenylyl cyclase. A chimeric alpha i/alpha s cDNA was constructed that encodes a polypeptide composed of the amino terminal 60% of an alpha i chain and the carboxyl terminal 40% of alpha s. The cDNA was introduced via a retroviral vector into S49 cyc- cells, which lack endogenous alpha s. Although less than half of the hybrid alpha chain is derived from alpha s, its ability to mediate beta-adrenoceptor stimulation of adenylyl cyclase matched that of the normal alpha s polypeptide expressed from the same retroviral vector in cyc- cells. This result indicates that carboxyl terminal amino acid sequences of alpha s contain the structural features that are required for specificity of interactions with the effector enzyme, adenylyl cyclase, as well as with the hormone receptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Masters, S B -- Sullivan, K A -- Miller, R T -- Beiderman, B -- Lopez, N G -- Ramachandran, J -- Bourne, H R -- New York, N.Y. -- Science. 1988 Jul 22;241(4864):448-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2899356" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/*physiology ; Animals ; Cell Line ; Cell Membrane/physiology ; Cholera Toxin/pharmacology ; Colforsin/pharmacology ; Enzyme Activation ; GTP-Binding Proteins/*physiology ; Guanosine Triphosphate/pharmacology ; Isoproterenol/pharmacology ; Mice ; Receptors, Adrenergic, beta/*physiology ; Recombinant Proteins ; Somatostatin/pharmacology ; 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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    American Association for the Advancement of Science (AAAS)
    Publication Date: 1987-01-02
    Description: Recent investigations have demonstrated that neurons have a number of different types of calcium channels, each with their own unique properties and pharmacology. These calcium channels may be important in the control of different aspects of nerve activity. Some of the possibilities can now be discussed.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, R J -- DA-02121/DA/NIDA NIH HHS/ -- DA-02575/DA/NIDA NIH HHS/ -- MH-40165/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 1987 Jan 2;235(4784):46-52.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/2432656" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/metabolism ; Calcium/*physiology ; Calcium Channel Blockers ; Calcium Channels ; Ion Channels/*physiology ; Membrane Potentials ; Neurons/*physiology ; Neurotransmitter Agents/*secretion ; Receptors, Nicotinic/metabolism ; Sensory Receptor Cells/physiology ; 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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