Evidence map›Paper›PMID 21208602›Full record

ReviewEuropean journal of pharmacology2011

Structure, function and regulation of the melanocortin receptors.

Yingkui Yang

Abstract readReview
In one paragraph

Review in European journal of pharmacology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

65 citing papers in PubMed, 137 citations in OpenAlex.

  1. Trial
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  4. Review
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  6. Review
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  8. Carbocyclic setmelanotide analogs maintain biochemical potency at melanocortin 4 receptors.Journal of peptide science : an official publication of the European Peptide Society · 2025
    Article
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  10. Review
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  16. Review
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  18. Review
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5 more citing papers are in PubMed but not listed here.

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

1 author at 1 institution in 1 country.

Yingkui YangDepartment of Surgery, University of Alabama at Birmingham, Birmingham, AL, 35294, United States. ying-kui.yang@ccc.uab.edu
University of Alabama at Birmingham · US

Funding

Molecular determinants of melanocortin 4 receptor for selective agonist bindingR03HD058789 · NICHD · UNIVERSITY OF ALABAMA AT BIRMINGHAM · PI YANG, YINGKUI · 2008 to 2009
$145k
NICHD NIH HHS R03 HD058789
6 · The paper itself

Abstract

Melanocortin receptors belong to the seven-transmembrane (TM) domain proteins that are coupled to G-proteins and signaled through intracellular cyclic adenosine monophosphate. Many structural features conserved in other G-protein coupled receptors (GPCRs) are found in the melanocortin receptors. There are five melanocortin receptor subtypes and each of the melanocortin receptor subtypes has a different pattern of tissue expression and has its own profile regarding the relative potency of different melanocortin peptides. α-, β-, and γ-MSH and ACTH are known endogenous agonist ligands for the melanocortin receptors. Agouti and AgRP are the only known naturally occurring antagonists of the melanocortin receptors. We have examined the molecular basis of all five human melanocortin receptors for different ligand binding affinities and potencies using chimeric and mutated receptors. Our studies indicate that human melanocortin MC(1) receptor, human melanocortin MC(3) receptor, human melanocortin MC(4) receptor and human melanocortin MC(5) receptor utilize orthosteric sites for non selective agonists, α-MSH and NDP-α-MSH, high affinity binding and utilize allosteric sites for selective agonist or antagonist binding. Furthermore, our results indicate that molecular determinants of human melanocortin MC(2) receptor for ACTH binding and signaling are different from that of other melanocortin receptors. Many studies also indicate that agonists can induce different conformation changes of melanocortin receptors, which then lead to the activation of different signaling pathways, even when the expression level of receptor and the strength of stimulus-response coupling are the same. This finding may provide new information for the design of drugs for targeting melanocortin receptors.

Indexed as

Allosteric SiteAmino Acid SequenceAnimalsHumansModels, MolecularMolecular Sequence DataReceptors, MelanocortinSignal TransductionSubstrate SpecificityReceptors, Melanocortin

Identifiers

PMID21208602
PMCPMC3095696
OpenAlexW2150327763

What OpenQuestion holds

Textmetadata
LicenceTDM
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.