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Receptor Activity-modifying Protein-directed G Protein Signaling Specificity for the Calcitonin Gene-related Peptide Family of Receptors

The Journal of biological chemistry, 2016-10, Vol.291 (42), p.21925-21944

2016

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The structure of secretin family GPCR peptide ligands: implications for receptor pharmacology and drug development

Drug discovery today, 2012-09, Vol.17 (17-18), p.1006-1014

2012

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Structural and Functional Characterization of an RNase HI Domain from the Bifunctional Protein Rv2228c from Mycobacterium tuberculosis

Journal of Bacteriology, 2010-06, Vol.192 (11), p.2878-2886

2010

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Molecular Mechanisms of Class B GPCR Activation: Insights from Adrenomedullin Receptors

ACS pharmacology & translational science, 2020-04, Vol.3 (2), p.246-262

2020

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Structural and Functional Analysis of Rv3214 from Mycobacterium tuberculosis, a Protein with Conflicting Functional Annotations, Leads to Its Characterization as a Phosphatase

Journal of Bacteriology, 2006-05, Vol.188 (10), p.3589-3599

2006

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Structure–activity relationships for α‐calcitonin gene‐related peptide

British journal of pharmacology, 2013-12, Vol.170 (7), p.1308-1322

2013

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Structural insights into RAMP modification of secretin family G protein-coupled receptors: implications for drug development

Trends in pharmacological sciences (Regular ed.), 2011-10, Vol.32 (10), p.591-600

2011

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Calcitonin and calcitonin receptor‐like receptors: common themes with family B GPCRs?

British journal of pharmacology, 2012-05, Vol.166 (1), p.51-65

2012

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Pharmacological Characterization and Investigation of N‑Terminal Loop Amino Acids of Adrenomedullin 2 That Are Important for Receptor Activation

Biochemistry (Easton), 2019-08, Vol.58 (32), p.3468-3474

2019

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Receptor Activity-modifying Proteins 2 and 3 Generate Adrenomedullin Receptor Subtypes with Distinct Molecular Properties

The Journal of biological chemistry, 2016-05, Vol.291 (22), p.11657-11675

2016

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Receptor Activity Modifying Proteins Have Limited Effects on the Class B G Protein-Coupled Receptor Calcitonin Receptor-Like Receptor Stalk

Biochemistry (Easton), 2018-02, Vol.57 (8), p.1410-1422

2018

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An allosteric role for receptor activity-modifying proteins in defining GPCR pharmacology

Cell discovery, 2016-05, Vol.2 (1), p.16012-16012, Article 16012

2016

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Receptor activity-modifying protein-directed G protein signaling specificity for the calcitonin gene-related peptide family of receptors

The Journal of biological chemistry, 2016-12, Vol.291 (49), p.25763-25763

2016

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The role of ECL2 in CGRP receptor activation: a combined modelling and experimental approach

Journal of the Royal Society interface, 2013-11, Vol.10 (88), p.20130589

2013

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An allosteric role for receptor activity-modifying proteins in defining GPCR pharmacology

Cell discovery, 2016-06, Vol.2, p.16020

2016

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Recent progress in unraveling the complexities of receptor biology: towards new therapeutics

Expert review of clinical pharmacology, 2012-03, Vol.5 (2), p.145-147

2012

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Erratum: An allosteric role for receptor activity-modifying proteins in defining GPCR pharmacology

Cell discovery, 2016-06, Vol.2 (1), p.16020-16020, Article 16020

2016

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Cloning, expression, purification and preliminary crystallographic analysis of the RNase HI domain of the Mycobacterium tuberculosis protein Rv2228c as a maltose-binding protein fusion

Acta crystallographica. Section F, Structural biology and crystallization communications, 2008-08, Vol.64 (8), p.746-749

2008

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Corrigendum to “The structure of secretin family GPCR peptide ligands: implications for receptor pharmacology and drug development” [Drug Discov. Today 17 (17–18) (2012) 1006–1014]

Drug discovery today, 2013-03, Vol.18 (5-6), p.312-313

2013

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Structure-activity relationships for [alpha]-calcitonin gene-related peptide

British journal of pharmacology, 2013-12, Vol.170 (7), p.1308

2013

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Receptor Activity-modifying Protein-directed G Protein Signaling Specificity for the Calcitonin Gene-related Peptide Family of ReceptorsThis work was supported by the National Heart Foundation of New Zealand (to H. A. W.), the School of Biological Sciences, University of Auckland seed fund (to H. A. W.), Grants BB/M00015X/1 (to G. L.), BB/M000176/1 (to D. R. P.), and BB/M006883/1 (to C. A. R.) from the BBSRC, BBSRC Doctoral Training Partnership Grant BB/JO14540/1 (to M. H.), MRC Doctoral Trainin

The Journal of biological chemistry, 2016-10, Vol.291 (42), p.21925-21944

2016

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Cloning, expression, purification and preliminary crystallographic data for Rv3214 (EntD), a predicted cofactor-dependent phosphoglycerate mutase from Mycobacterium tuberculosis

Acta crystallographica. Section F, Structural biology and crystallization communications, 2005-08, Vol.61 (8), p.753-755

2005

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Calcitonin and calcitonin receptor-like receptors: common themes with family B GPCRs? : Secretin Family (Class B) G Protein-Coupled Receptors - from Molecular to Clinical Perspectives

British journal of pharmacology, 2012, Vol.166 (1), p.51-65

2012

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Characterisation of the soluble n terminal domain of the corticotropin releasing hormone receptor 1

Watkins, Harriet A

2001

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Quantitative MRI reveals differences in striatal myelin in children with DLD

eLife, 2022-09, Vol.11

2022

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Receptor Activity-modifying Protein-directed G Protein Signaling Specificity for the Calcitonin Gene-related Peptide Family of Receptors

The structure of secretin family GPCR peptide ligands: implications for receptor pharmacology and drug development

Structural and Functional Characterization of an RNase HI Domain from the Bifunctional Protein Rv2228c from Mycobacterium tuberculosis

Molecular Mechanisms of Class B GPCR Activation: Insights from Adrenomedullin Receptors

Structural and Functional Analysis of Rv3214 from Mycobacterium tuberculosis, a Protein with Conflicting Functional Annotations, Leads to Its Characterization as a Phosphatase

Structure–activity relationships for α‐calcitonin gene‐related peptide

Structural insights into RAMP modification of secretin family G protein-coupled receptors: implications for drug development

Calcitonin and calcitonin receptor‐like receptors: common themes with family B GPCRs?

Pharmacological Characterization and Investigation of N‑Terminal Loop Amino Acids of Adrenomedullin 2 That Are Important for Receptor Activation

Receptor Activity-modifying Proteins 2 and 3 Generate Adrenomedullin Receptor Subtypes with Distinct Molecular Properties

Receptor Activity Modifying Proteins Have Limited Effects on the Class B G Protein-Coupled Receptor Calcitonin Receptor-Like Receptor Stalk

An allosteric role for receptor activity-modifying proteins in defining GPCR pharmacology

Receptor activity-modifying protein-directed G protein signaling specificity for the calcitonin gene-related peptide family of receptors

The role of ECL2 in CGRP receptor activation: a combined modelling and experimental approach

An allosteric role for receptor activity-modifying proteins in defining GPCR pharmacology

Recent progress in unraveling the complexities of receptor biology: towards new therapeutics

Erratum: An allosteric role for receptor activity-modifying proteins in defining GPCR pharmacology

Cloning, expression, purification and preliminary crystallographic analysis of the RNase HI domain of the Mycobacterium tuberculosis protein Rv2228c as a maltose-binding protein fusion

Corrigendum to “The structure of secretin family GPCR peptide ligands: implications for receptor pharmacology and drug development” [Drug Discov. Today 17 (17–18) (2012) 1006–1014]

Structure-activity relationships for [alpha]-calcitonin gene-related peptide

Cloning, expression, purification and preliminary crystallographic data for Rv3214 (EntD), a predicted cofactor-dependent phosphoglycerate mutase from Mycobacterium tuberculosis

Calcitonin and calcitonin receptor-like receptors: common themes with family B GPCRs? : Secretin Family (Class B) G Protein-Coupled Receptors - from Molecular to Clinical Perspectives

Characterisation of the soluble n terminal domain of the corticotropin releasing hormone receptor 1

Quantitative MRI reveals differences in striatal myelin in children with DLD

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