Evidence map›Paper›PMID 24199627›Full record

ArticleBritish journal of pharmacology2014

Receptor activity-modifying protein-dependent effects of mutations in the calcitonin receptor-like receptor: implications for adrenomedullin and calcitonin gene-related peptide pharmacology.

H A Watkins, C S Walker, K N Ly, R J Bailey, J Barwell, D R Poyner, D L Hay

Open access · hybridAbstract readComparative Study
In one paragraph

Article in British journal of pharmacology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.4field-weighted citation impact, top 23% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

20 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Structure and Dynamics of Adrenomedullin Receptors AMACS pharmacology & translational science · 2020
    Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Receptor Activity-Modifying Proteins (RAMPs): New Insights and Roles.Annual review of pharmacology and toxicology · 2016
    Review
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors at 3 institutions in 2 countries.

H A WatkinsSchool of Biological Sciences, University of Auckland, Auckland, New Zealand; Maurice Wilkins Centre for Molecular Biodiscovery, University of Auckland, Auckland, New Zealand.
C S Walker
K N Ly
R J Bailey
J Barwell
D R Poyner
D L Hay
University of Auckland · NZAston University · GBMaurice Wilkins Centre · NZ

Funding

Wellcome Trust 091496
6 · The paper itself

Abstract

background and purposeReceptor activity-modifying proteins (RAMPs) define the pharmacology of the calcitonin receptor-like receptor (CLR). The interactions of the different RAMPs with this class B GPCR yield high-affinity calcitonin gene-related peptide (CGRP) or adrenomedullin (AM) receptors. However, the mechanism for this is unclear. EXPERIMENTAL APPROACH: Guided by receptor models, we mutated residues in the N-terminal helix of CLR, RAMP2 and RAMP3 hypothesized to be involved in peptide interactions. These were assayed for cAMP production with AM, AM2 and CGRP together with their cell surface expression. Binding studies were also conducted for selected mutants. KEY

resultsAn important domain for peptide interactions on CLR from I32 to I52 was defined. Although I41 was universally important for binding and receptor function, the role of other residues depended on both ligand and RAMP. Peptide binding to CLR/RAMP3 involved a more restricted range of residues than that to CLR/RAMP1 or CLR/RAMP2. E101 of RAMP2 had a major role in AM interactions, and F111/W84 of RAMP2/3 was important with each peptide. CONCLUSIONS AND IMPLICATIONS: RAMP-dependent effects of CLR mutations suggest that the different RAMPs control accessibility of peptides to binding residues situated on the CLR N-terminus. RAMP3 appears to alter the role of specific residues at the CLR-RAMP interface compared with RAMP1 and RAMP2.

Indexed as

Models, MolecularSecond Messenger SystemsAdrenomedullinAnimalsCalcitonin Gene-Related PeptideCalcitonin Receptor-Like ProteinChlorocebus aethiopsCOS CellsCyclic AMPHumansMutant ProteinsPeptide FragmentsPeptide HormonesProtein Interaction Domains and MotifsRatsReceptor Activity-Modifying Protein 1ADM2 protein, humanADM protein, humanAdrenomedullinCalcitonin Gene-Related PeptideCalcitonin Receptor-Like ProteinCALCRL protein, humanCyclic AMPMutant ProteinsPeptide FragmentsPeptide HormonesRAMP1 protein, humanRAMP2 protein, humanRAMP3 protein, humanReceptor Activity-Modifying Protein 1Receptor Activity-Modifying Protein 2Receptor Activity-Modifying Protein 3Receptors, AdrenomedullinReceptors, Calcitonin Gene-Related PeptideRecombinant Fusion ProteinsRecombinant ProteinsadrenomedullinCGRPGPCRRAMPreceptor activity-modifying protein

Identifiers

PMID24199627
PMCPMC3969088
OpenAlexW1915599524

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.