Evidence map›Paper›PMID 36017890›Full record

ReviewActa biochimica et biophysica Sinica2022

GPCR structural characterization by NMR spectroscopy in solution.

Lingyun Yang, Dongsheng Liu, Kurt Wüthrich

Abstract readReview
In one paragraph

Review in Acta biochimica et biophysica Sinica, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Article
  2. Review
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.

Lingyun YangiHuman Institute, ShanghaiTech University, Shanghai 201210, China.
Dongsheng LiuiHuman Institute, ShanghaiTech University, Shanghai 201210, China.
Kurt WüthrichiHuman Institute, ShanghaiTech University, Shanghai 201210, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In the human proteome, 826 G-protein-coupled receptors (GPCRs) interact with extracellular stimuli to initiate cascades of intracellular signaling. Determining conformational dynamics and intermolecular interactions are key to understand GPCR function as a basis for drug design. X-ray crystallography and cryo-electron microscopy (cryo-EM) contribute molecular architectures of GPCRs and GPCR-signaling complexes. NMR spectroscopy is complementary by providing information on the dynamics of GPCR structures at physiological temperature. In this review, several NMR approaches in use to probe GPCR dynamics and intermolecular interactions are discussed. The topics include uniform stable-isotope labeling, amino acid residue-selective stable-isotope labeling, site-specific labeling by genetic engineering, the introduction of

Indexed as

Receptors, G-Protein-CoupledSignal TransductionCryoelectron MicroscopyCrystallography, X-RayHumansMagnetic Resonance SpectroscopyReceptors, G-Protein-Coupleddrug developmentfluorine-19 NMRGPCR biologyG protein-coupled receptor dynamicsstable-isotope labeling

Identifiers

PMID36017890
PMCPMC9828178

What OpenQuestion holds

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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.