Evidence map›Paper›PMID 28283573›Full record

ArticleThe Journal of biological chemistry2017

Genetically encoded photocross-linkers determine the biological binding site of exendin-4 peptide in the N-terminal domain of the intact human glucagon-like peptide-1 receptor (GLP-1R).

Cassandra Koole, Christopher A Reynolds, Juan C Mobarec, Caroline Hick, Patrick M Sexton, Thomas P Sakmar

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

27 citing papers in PubMed, 55 citations in OpenAlex.

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  12. Capturing Peptide-GPCR Interactions and Their Dynamics.Molecules (Basel, Switzerland) · 2020
    Review
  13. A Paradigm for Peptide Hormone-GPCR Analyses.Molecules (Basel, Switzerland) · 2020
    Review
  14. Article
  15. Article
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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

6 authors at 3 institutions in 3 countries.

Cassandra KooleFrom the Laboratory of Chemical Biology and Signal Transduction, The Rockefeller University, New York, New York 10065.
Christopher A Reynoldsthe School of Biological Sciences, University of Essex, Wivenhoe Park, Colchester CO4 3SQ, United Kingdom.
Juan C Mobarecthe School of Biological Sciences, University of Essex, Wivenhoe Park, Colchester CO4 3SQ, United Kingdom.
Caroline HickDrug Discovery Biology, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville, Victoria 3052, Australia, and.
Patrick M SextonDrug Discovery Biology, Monash Institute of Pharmaceutical Sciences, Monash University, Parkville, Victoria 3052, Australia, and.
Thomas P SakmarFrom the Laboratory of Chemical Biology and Signal Transduction, The Rockefeller University, New York, New York 10065, sakmar@mail.rockefeller.edu.
Monash University · AURockefeller University · USUniversity of Essex · GB

Funding

Biotechnology and Biological Sciences Research Council BB/M006883/1
6 · The paper itself

Abstract

The glucagon-like peptide-1 receptor (GLP-1R) is a key therapeutic target in the management of type II diabetes mellitus, with actions including regulation of insulin biosynthesis and secretion, promotion of satiety, and preservation of β-cell mass. Like most class B G protein-coupled receptors (GPCRs), there is limited knowledge linking biological activity of the GLP-1R with the molecular structure of an intact, full-length, and functional receptor·ligand complex. In this study, we have utilized genetic code expansion to site-specifically incorporate the photoactive amino acid

Indexed as

AzidesBinding SitesCyclic AMPDiabetes Mellitus, Type 2ExenatideGlucagon-Like Peptide-1 ReceptorHEK293 CellsHumansLigandsMolecular Dynamics SimulationMolecular StructureMutagenesisMutationPeptidesPhenylalanineProtein Domains4-azidophenylalanineAzidesCyclic AMPExenatideGLP1R protein, humanGlucagon-Like Peptide-1 ReceptorLigandsPeptidesPhenylalanineVenomsgenetic code expansionglucagon-like peptide-1 receptor (GLP-1R)G protein-coupled receptor (GPCR)molecular modelingmutagenesispeptide hormonephotocross-linkingstructural biologystructure-functionunnatural amino acid

Identifiers

PMID28283573
PMCPMC5409479
OpenAlexW2593841038

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.