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Molecular Endocrinology (Baltimore, Md.)
|
March 5, 2002
A single residue (arg46) located within the N-terminus of the V1a vasopressin receptor is critical for binding vasopressin but not peptide or nonpeptide antagonists
Stuart R Hawtin, Victoria J Wesley, Rosemary A Parslow, et al.
The Journal of Biological Chemistry
|
September 23, 2006
Charged extracellular residues, conserved throughout a G-protein-coupled receptor family, are required for ligand binding, receptor activation, and cell-surface expression
Stuart R Hawtin, John Simms, Matthew Conner, et al.
Biochemistry
|
December 19, 2009
Structure-function analysis of RAMP1-RAMP3 chimeras
Tao Qi, John Simms, Richard J Bailey, et al.
Journal of Molecular Biology
|
February 10, 2020
Calcitonin Receptor N-Glycosylation Enhances Peptide Hormone Affinity by Controlling Receptor Dynamics
Sang-Min Lee, Yejin Jeong, John Simms, et al.
Biochimica Et Biophysica Acta. Biomembranes
|
March 4, 2019
Interactions between RAMP2 and CRF receptors: The effect of receptor subtypes, splice variants and cell context
Sian Bailey, Matthew Harris, Kerry Barkan, et al.
Methods in Molecular Biology (Clifton, N.J.)
|
June 11, 2009
Homology modeling of GPCRs
John Simms, Nathan E Hall, Polo H C Lam, et al.
European Journal of Biochemistry
|
November 19, 2003
An arginyl in the N-terminus of the V1a vasopressin receptor is part of the conformational switch controlling activation by agonist
Stuart R Hawtin, Victoria J Wesley, John Simms, et al.
The Journal of Biological Chemistry
|
April 4, 2007
Systematic analysis of the entire second extracellular loop of the V(1a) vasopressin receptor: key residues, conserved throughout a G-protein-coupled receptor family, identified
Matthew Conner, Stuart R Hawtin, John Simms, et al.
Molecular Pharmacology
|
December 24, 2004
A key role for transmembrane prolines in calcitonin receptor-like receptor agonist binding and signalling: implications for family B G-protein-coupled receptors
Alex C Conner, Debbie L Hay, John Simms, et al.
Cell Discovery
|
July 28, 2016
Erratum: An allosteric role for receptor activity-modifying proteins in defining GPCR pharmacology
Joseph J Gingell, John Simms, James Barwell, et al.
Page
of 6
Search research articles
Search
Showing results (31-40 of 53) with videos related to
Sort By:
Page
of 6
Molecular Endocrinology (Baltimore, Md.)
|
March 5, 2002
A single residue (arg46) located within the N-terminus of the V1a vasopressin receptor is critical for binding vasopressin but not peptide or nonpeptide antagonists
Stuart R Hawtin, Victoria J Wesley, Rosemary A Parslow, et al.
The Journal of Biological Chemistry
|
September 23, 2006
Charged extracellular residues, conserved throughout a G-protein-coupled receptor family, are required for ligand binding, receptor activation, and cell-surface expression
Stuart R Hawtin, John Simms, Matthew Conner, et al.
Biochemistry
|
December 19, 2009
Structure-function analysis of RAMP1-RAMP3 chimeras
Tao Qi, John Simms, Richard J Bailey, et al.
Journal of Molecular Biology
|
February 10, 2020
Calcitonin Receptor N-Glycosylation Enhances Peptide Hormone Affinity by Controlling Receptor Dynamics
Sang-Min Lee, Yejin Jeong, John Simms, et al.
Biochimica Et Biophysica Acta. Biomembranes
|
March 4, 2019
Interactions between RAMP2 and CRF receptors: The effect of receptor subtypes, splice variants and cell context
Sian Bailey, Matthew Harris, Kerry Barkan, et al.
Methods in Molecular Biology (Clifton, N.J.)
|
June 11, 2009
Homology modeling of GPCRs
John Simms, Nathan E Hall, Polo H C Lam, et al.
European Journal of Biochemistry
|
November 19, 2003
An arginyl in the N-terminus of the V1a vasopressin receptor is part of the conformational switch controlling activation by agonist
Stuart R Hawtin, Victoria J Wesley, John Simms, et al.
The Journal of Biological Chemistry
|
April 4, 2007
Systematic analysis of the entire second extracellular loop of the V(1a) vasopressin receptor: key residues, conserved throughout a G-protein-coupled receptor family, identified
Matthew Conner, Stuart R Hawtin, John Simms, et al.
Molecular Pharmacology
|
December 24, 2004
A key role for transmembrane prolines in calcitonin receptor-like receptor agonist binding and signalling: implications for family B G-protein-coupled receptors
Alex C Conner, Debbie L Hay, John Simms, et al.
Cell Discovery
|
July 28, 2016
Erratum: An allosteric role for receptor activity-modifying proteins in defining GPCR pharmacology
Joseph J Gingell, John Simms, James Barwell, et al.
Page
of 6