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Articles 91 - 95 of 95
Full-Text Articles in Pharmacy and Pharmaceutical Sciences
Cooperative Interactions Among Subunits Of A Voltage-Dependent Potassium Channel. Evidence From Expression Of Concatenated Cdnas, Raymond S. Hurst, Michael Kavanaugh, Jerrel Yakel, John P. Adelman, R. Alan North
Cooperative Interactions Among Subunits Of A Voltage-Dependent Potassium Channel. Evidence From Expression Of Concatenated Cdnas, Raymond S. Hurst, Michael Kavanaugh, Jerrel Yakel, John P. Adelman, R. Alan North
Biomedical and Pharmaceutical Sciences Faculty Publications
Four copies of the coding sequence for a voltage-dependent potassium channel (RBK1, rat Kv1.1) were ligated contiguously and transcribed in vitro. The resulting RNA encodes four covalently linked subunit domains ([4]RBK1). Injection of this RNA into Xenopus oocytes resulted in the expression of voltage-dependent potassium currents. A single amino acid substitution, Tyr-->Val, located within the outer mouth of the pore, introduced into the equivalent position of any of the four domains, reduced affinity for external tetraethylammonium by approximately the same amount. In constructs containing 0, 1, 2, 3, or 4 Tyr residues the free energy of binding tetraethylammonium was …
Effects Of Ecotropic Murine Retroviruses On The Dual-Function Cell Surface Receptor/Basic Amino Acid Transporter, Hao Wang, Esther Dechant, Michael Kavanaugh, R. Alan North, David Kabat
Effects Of Ecotropic Murine Retroviruses On The Dual-Function Cell Surface Receptor/Basic Amino Acid Transporter, Hao Wang, Esther Dechant, Michael Kavanaugh, R. Alan North, David Kabat
Biomedical and Pharmaceutical Sciences Faculty Publications
The widely expressed Na(+)-independent transporter for basic amino acids (system y+) is the cell surface receptor (ecoR) for ecotropic host-range mouse retroviruses (murine leukemia viruses (MuLVs)), a class of retroviruses that naturally infects only mice or rats. Accordingly, expression of mouse ecoR cDNA in mink CCL64 fibroblasts yields cells (CEN cells) that have y+ transporter activity above the endogenous background and that bind and are infected by ecotropic MuLVs. The effect of ecotropic MuLV infection on expression of y+ transporter was analyzed in mouse and in mink CEN fibroblasts. Chronic infection with ecotropic MuLVs caused 50-70% loss (down-modulation) of mouse …
Interaction Between Tetraethylammonium And Amino Acid Residues In The Pore Of Cloned Voltage-Dependent Potassium Channels, Michael Kavanaugh, Michael D. Varnum, Peregrine B. Osborne, Macdonald J. Christie, Andreas E. Busch, John P. Adelman, R. Alan North
Interaction Between Tetraethylammonium And Amino Acid Residues In The Pore Of Cloned Voltage-Dependent Potassium Channels, Michael Kavanaugh, Michael D. Varnum, Peregrine B. Osborne, Macdonald J. Christie, Andreas E. Busch, John P. Adelman, R. Alan North
Biomedical and Pharmaceutical Sciences Faculty Publications
Extracellular tetraethylammonium (TEA) inhibits currents in Xenopus oocytes that have been injected with mRNAs encoding voltage-dependent potassium channels. Concentration-response curves were used to measure the affinity of TEA; this differed up to 700-fold among channels RBK1 (KD 0.3 mM), RGK5 (KD 11 mM), and RBK2 (KD greater than 200 mM). Studies in which chimeric channels were expressed localized TEA binding to the putative extracellular loop between trans-membrane domains S5 and S6. Site-directed mutagenesis of residues in this region identified the residue Tyr379 of RBK1 as a crucial determinant of TEA sensitivity; substitution of Tyr in the equivalent positions of RBK2 …
Structure And Function Of Human Hemoglobin Covalently Labeled With Periodate-Oxidized Adenosine Triphosphate, Michael Kavanaugh, Max F. Perutz, Giulio Fermi, Daniel T. Shih, Richard T. Jones
Structure And Function Of Human Hemoglobin Covalently Labeled With Periodate-Oxidized Adenosine Triphosphate, Michael Kavanaugh, Max F. Perutz, Giulio Fermi, Daniel T. Shih, Richard T. Jones
Biomedical and Pharmaceutical Sciences Faculty Publications
Periodate-oxidized adenosine triphosphate (o-ATP), a ribose ring-opened dialdehyde derivative of ATP, reacts specifically with human deoxyhemoglobin to give a single major covalently modified product after reduction with sodium borohydride. This product, designated di-ATP Hb, was isolated using ion-exchange chromatography and shown to have incorporated two molecules of o-ATP/tetramer. Peptide mapping and x-ray crystallography at 2.8-A resolution indicate that a covalent adduct is formed between the ligand and residues Lys-82 EF6 of each beta chain in the organic phosphate-binding site of the molecule. di-ATP Hb exhibits a significantly decreased oxygen affinity (P50 = 20.8 mm Hg versus 5.8 mm Hg control; …
Identification Of The Binding Subunit Of The Sigma-Type Opiate Receptor By Photoaffinity Labeling With 1-(4-Azido-2-Methyl[6-3h]Phenyl)-3-(2-Methyl[4,6-3h]Phenyl)Guanidine, Michael Kavanaugh, Barbara C. Tester, Michael W. Scherz, John F. W. Keana, Eckard Weber
Identification Of The Binding Subunit Of The Sigma-Type Opiate Receptor By Photoaffinity Labeling With 1-(4-Azido-2-Methyl[6-3h]Phenyl)-3-(2-Methyl[4,6-3h]Phenyl)Guanidine, Michael Kavanaugh, Barbara C. Tester, Michael W. Scherz, John F. W. Keana, Eckard Weber
Biomedical and Pharmaceutical Sciences Faculty Publications
The sigma-type opiate receptor is a distinct binding site in the brain that may mediate some of the psychotomimetic effects caused by benzomorphan opiates and phencyclidine in humans. We have developed a synthetic, highly selective ligand for this receptor, 1,3-di-o-tolylguanidine (DTG). To identify the binding protein(s) of the sigma receptor, we have now synthesized a radiolabeled azide derivative of DTG, 1-(4-azido-2-methyl[6-3H]phenyl)-3-(2-methyl[4,6-3H]phenyl)-guanidine ([3H]N3DTG). In guinea pig brain membrane binding assays conducted in the dark, [3H]N3DTG bound reversibly, selectively, and with high affinity (Kd = 10 nM) to sigma receptors. The drug specificity profile of reversible [3H]-N3DTG binding was identical to that …