The Experts below are selected from a list of 27 Experts worldwide ranked by ideXlab platform
Heidi E Hamm - One of the best experts on this subject based on the ideXlab platform.
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antagonists of the receptor g protein Interface Block gi coupled signal transduction
Journal of Biological Chemistry, 1998Co-Authors: Annette Gilchrist, Maria R Mazzoni, Brigid Dineen, Andrew Dice, Joel Linden, William R Proctor, Carl R Lupica, Thomas V Dunwiddie, Heidi E HammAbstract:The carboxyl terminus of heterotrimeric G protein α subunits plays an important role in receptor interaction. We demonstrate that peptides corresponding to the last 11 residues of Gαi1/2 or Gαo1 impair agonist binding to A1 adenosine receptors, whereas Gαs or Gαt peptides have no effect. Previously, by using a combinatorial library we identified a series of Gαtpeptide analogs that bind rhodopsin with high affinity (Martin, E. L., Rens-Domiano, S., Schatz, P. J., and Hamm, H. E. (1996)J. Biol. Chem. 271, 361–366). Native Gαi1/2 peptide as well as several analogs were tested for their ability to modulate agonist binding or antagonist-agonist competition using cells overexpressing human A1 adenosine receptors. Three peptide analogs decreased the K i, suggesting that they disrupt the high affinity receptor-G protein interaction and stabilize an intermediate affinity state. To study the ability of the peptides to compete with endogenous Gαiproteins and Block signal transduction in a native setting, we measured activation of G protein-coupled K+ channels through A1 adenosine or γ-aminobutyric acid, type B, receptors in hippocampal CA1 pyramidal neurons. Native Gαi1/2, peptide, and certain analog peptides inhibited receptor-mediated K+ channel gating, dependent on which receptor was activated. This differential perturbation of receptor-G protein interaction suggests that receptors that act on the same G protein can be selectively disrupted.
Maria R Mazzoni - One of the best experts on this subject based on the ideXlab platform.
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antagonists of the receptor g protein Interface Block gi coupled signal transduction
Journal of Biological Chemistry, 1998Co-Authors: Annette Gilchrist, Maria R Mazzoni, Brigid Dineen, Andrew Dice, Joel Linden, William R Proctor, Carl R Lupica, Thomas V Dunwiddie, Heidi E HammAbstract:The carboxyl terminus of heterotrimeric G protein α subunits plays an important role in receptor interaction. We demonstrate that peptides corresponding to the last 11 residues of Gαi1/2 or Gαo1 impair agonist binding to A1 adenosine receptors, whereas Gαs or Gαt peptides have no effect. Previously, by using a combinatorial library we identified a series of Gαtpeptide analogs that bind rhodopsin with high affinity (Martin, E. L., Rens-Domiano, S., Schatz, P. J., and Hamm, H. E. (1996)J. Biol. Chem. 271, 361–366). Native Gαi1/2 peptide as well as several analogs were tested for their ability to modulate agonist binding or antagonist-agonist competition using cells overexpressing human A1 adenosine receptors. Three peptide analogs decreased the K i, suggesting that they disrupt the high affinity receptor-G protein interaction and stabilize an intermediate affinity state. To study the ability of the peptides to compete with endogenous Gαiproteins and Block signal transduction in a native setting, we measured activation of G protein-coupled K+ channels through A1 adenosine or γ-aminobutyric acid, type B, receptors in hippocampal CA1 pyramidal neurons. Native Gαi1/2, peptide, and certain analog peptides inhibited receptor-mediated K+ channel gating, dependent on which receptor was activated. This differential perturbation of receptor-G protein interaction suggests that receptors that act on the same G protein can be selectively disrupted.
Annette Gilchrist - One of the best experts on this subject based on the ideXlab platform.
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antagonists of the receptor g protein Interface Block gi coupled signal transduction
Journal of Biological Chemistry, 1998Co-Authors: Annette Gilchrist, Maria R Mazzoni, Brigid Dineen, Andrew Dice, Joel Linden, William R Proctor, Carl R Lupica, Thomas V Dunwiddie, Heidi E HammAbstract:The carboxyl terminus of heterotrimeric G protein α subunits plays an important role in receptor interaction. We demonstrate that peptides corresponding to the last 11 residues of Gαi1/2 or Gαo1 impair agonist binding to A1 adenosine receptors, whereas Gαs or Gαt peptides have no effect. Previously, by using a combinatorial library we identified a series of Gαtpeptide analogs that bind rhodopsin with high affinity (Martin, E. L., Rens-Domiano, S., Schatz, P. J., and Hamm, H. E. (1996)J. Biol. Chem. 271, 361–366). Native Gαi1/2 peptide as well as several analogs were tested for their ability to modulate agonist binding or antagonist-agonist competition using cells overexpressing human A1 adenosine receptors. Three peptide analogs decreased the K i, suggesting that they disrupt the high affinity receptor-G protein interaction and stabilize an intermediate affinity state. To study the ability of the peptides to compete with endogenous Gαiproteins and Block signal transduction in a native setting, we measured activation of G protein-coupled K+ channels through A1 adenosine or γ-aminobutyric acid, type B, receptors in hippocampal CA1 pyramidal neurons. Native Gαi1/2, peptide, and certain analog peptides inhibited receptor-mediated K+ channel gating, dependent on which receptor was activated. This differential perturbation of receptor-G protein interaction suggests that receptors that act on the same G protein can be selectively disrupted.
Brigid Dineen - One of the best experts on this subject based on the ideXlab platform.
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antagonists of the receptor g protein Interface Block gi coupled signal transduction
Journal of Biological Chemistry, 1998Co-Authors: Annette Gilchrist, Maria R Mazzoni, Brigid Dineen, Andrew Dice, Joel Linden, William R Proctor, Carl R Lupica, Thomas V Dunwiddie, Heidi E HammAbstract:The carboxyl terminus of heterotrimeric G protein α subunits plays an important role in receptor interaction. We demonstrate that peptides corresponding to the last 11 residues of Gαi1/2 or Gαo1 impair agonist binding to A1 adenosine receptors, whereas Gαs or Gαt peptides have no effect. Previously, by using a combinatorial library we identified a series of Gαtpeptide analogs that bind rhodopsin with high affinity (Martin, E. L., Rens-Domiano, S., Schatz, P. J., and Hamm, H. E. (1996)J. Biol. Chem. 271, 361–366). Native Gαi1/2 peptide as well as several analogs were tested for their ability to modulate agonist binding or antagonist-agonist competition using cells overexpressing human A1 adenosine receptors. Three peptide analogs decreased the K i, suggesting that they disrupt the high affinity receptor-G protein interaction and stabilize an intermediate affinity state. To study the ability of the peptides to compete with endogenous Gαiproteins and Block signal transduction in a native setting, we measured activation of G protein-coupled K+ channels through A1 adenosine or γ-aminobutyric acid, type B, receptors in hippocampal CA1 pyramidal neurons. Native Gαi1/2, peptide, and certain analog peptides inhibited receptor-mediated K+ channel gating, dependent on which receptor was activated. This differential perturbation of receptor-G protein interaction suggests that receptors that act on the same G protein can be selectively disrupted.
Andrew Dice - One of the best experts on this subject based on the ideXlab platform.
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antagonists of the receptor g protein Interface Block gi coupled signal transduction
Journal of Biological Chemistry, 1998Co-Authors: Annette Gilchrist, Maria R Mazzoni, Brigid Dineen, Andrew Dice, Joel Linden, William R Proctor, Carl R Lupica, Thomas V Dunwiddie, Heidi E HammAbstract:The carboxyl terminus of heterotrimeric G protein α subunits plays an important role in receptor interaction. We demonstrate that peptides corresponding to the last 11 residues of Gαi1/2 or Gαo1 impair agonist binding to A1 adenosine receptors, whereas Gαs or Gαt peptides have no effect. Previously, by using a combinatorial library we identified a series of Gαtpeptide analogs that bind rhodopsin with high affinity (Martin, E. L., Rens-Domiano, S., Schatz, P. J., and Hamm, H. E. (1996)J. Biol. Chem. 271, 361–366). Native Gαi1/2 peptide as well as several analogs were tested for their ability to modulate agonist binding or antagonist-agonist competition using cells overexpressing human A1 adenosine receptors. Three peptide analogs decreased the K i, suggesting that they disrupt the high affinity receptor-G protein interaction and stabilize an intermediate affinity state. To study the ability of the peptides to compete with endogenous Gαiproteins and Block signal transduction in a native setting, we measured activation of G protein-coupled K+ channels through A1 adenosine or γ-aminobutyric acid, type B, receptors in hippocampal CA1 pyramidal neurons. Native Gαi1/2, peptide, and certain analog peptides inhibited receptor-mediated K+ channel gating, dependent on which receptor was activated. This differential perturbation of receptor-G protein interaction suggests that receptors that act on the same G protein can be selectively disrupted.