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John Simms

Showing results (31-40 of 53) with videos related to

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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 antagonistsStuart 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 expressionStuart R Hawtin, John Simms, Matthew Conner, et al.
Biochemistry|December 19, 2009
Structure-function analysis of RAMP1-RAMP3 chimerasTao 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 DynamicsSang-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 contextSian Bailey, Matthew Harris, Kerry Barkan, et al.
Methods in Molecular Biology (Clifton, N.J.)|June 11, 2009
Homology modeling of GPCRsJohn 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 agonistStuart 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, identifiedMatthew 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 receptorsAlex 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 pharmacologyJoseph J Gingell, John Simms, James Barwell, et al.
Pageof 6

Showing results (31-40 of 53) with videos related to

Sort By:
Pageof 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 antagonistsStuart 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 expressionStuart R Hawtin, John Simms, Matthew Conner, et al.
Biochemistry|December 19, 2009
Structure-function analysis of RAMP1-RAMP3 chimerasTao 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 DynamicsSang-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 contextSian Bailey, Matthew Harris, Kerry Barkan, et al.
Methods in Molecular Biology (Clifton, N.J.)|June 11, 2009
Homology modeling of GPCRsJohn 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 agonistStuart 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, identifiedMatthew 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 receptorsAlex 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 pharmacologyJoseph J Gingell, John Simms, James Barwell, et al.
Pageof 6