Evidence map›Paper›PMID 21455262›Full record

ReviewBiochemistry and cell biology = Biochimie et biologie cellulaire2011

Biophysical characterization of G-protein coupled receptor-peptide ligand binding.

David N Langelaan, Pascaline Ngweniform, Jan K Rainey

Open access · greenAbstract readReview
In one paragraph

Review in Biochemistry and cell biology = Biochimie et biologie cellulaire, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
2.1field-weighted citation impact, top 14% 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

8 citing papers in PubMed, 16 citations in OpenAlex.

  1. Article
  2. Article
  3. Apelinergic System Structure and Function.Comprehensive Physiology · 2017
    Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. 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

3 authors at 1 institution in 1 country.

David N LangelaanDepartment of Biochemistry & Molecular Biology, Dalhousie University, 5850 College Street, Halifax, Nova Scotia, Canada.
Pascaline Ngweniform
Jan K Rainey
Dalhousie University · CA

Funding

CIHR 91807CIHR ROP-91807
6 · The paper itself

Abstract

G-protein coupled receptors (GPCRs) are ubiquitous membrane proteins allowing intracellular responses to extracellular factors that range from photons of light to small molecules to proteins. Despite extensive exploitation of GPCRs as therapeutic targets, biophysical characterization of GPCR-ligand interactions remains challenging. In this minireview, we focus on techniques that have been successfully used for structural and biophysical characterization of peptide ligands binding to their cognate GPCRs. The techniques reviewed include solution-state nuclear magnetic resonance (NMR) spectroscopy, solid-state NMR, X-ray diffraction, fluorescence spectroscopy and single-molecule fluorescence methods, flow cytometry, surface plasmon resonance, isothermal titration calorimetry, and atomic force microscopy. The goal herein is to provide a cohesive starting point to allow selection of techniques appropriate to the elucidation of a given GPCR-peptide interaction.

Indexed as

LigandsProtein BindingCalorimetryMicroscopy, Atomic ForceNuclear Magnetic Resonance, BiomolecularPeptidesReceptors, G-Protein-CoupledSpectrometry, FluorescenceSurface Plasmon ResonanceX-Ray DiffractionLigandsPeptidesReceptors, G-Protein-Coupled

Identifiers

PMID21455262
PMCPMC3096653
OpenAlexW2117192206

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.