Evidence map›Paper›PMID 39471802›Full record

ArticleStructure (London, England : 1993)2024

Native mass spectrometry prescreening of G protein-coupled receptor complexes for cryo-EM structure determination.

Donggyun Kim, Weijing Liu, Rosa Viner, Vadim Cherezov

Abstract read
In one paragraph

Article in Structure (London, England : 1993), 2024. 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. 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

4 authors.

Donggyun KimBridge Institute, Michelson Center for Convergent Bioscience, University of Southern California, Los Angeles, CA 90089, USA; Department of Chemistry, University of Southern California, Los Angeles, CA 90089, USA.
Weijing LiuThermo Fisher Scientific, 355 River Oaks Pkwy, San Jose, CA 95134, USA.
Rosa VinerThermo Fisher Scientific, 355 River Oaks Pkwy, San Jose, CA 95134, USA. Electronic address: rosa.viner@thermofisher.com.
Vadim CherezovBridge Institute, Michelson Center for Convergent Bioscience, University of Southern California, Los Angeles, CA 90089, USA; Department of Chemistry, University of Southern California, Los Angeles, CA 90089, USA. Electronic address: cherezov@usc.edu.

Funding

Structural Biology Of G Protein-Coupled ReceptorsR35GM127086 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI Vadim Cherezov · 2018 to 2026
$3.6M
NIGMS NIH HHS R35 GM127086
6 · The paper itself

Abstract

G protein-coupled receptors (GPCRs) are essential transmembrane proteins playing key roles in human health and disease. Understanding their atomic-level molecular structure and conformational states is imperative for advancing drug development. Recent breakthroughs in single-particle cryogenic electron microscopy (cryo-EM) have propelled the structural biology of GPCRs into a new era. Nevertheless, the preparation of suitable GPCR samples and their complexes for cryo-EM analysis remains challenging due to their poor stability and highly dynamic nature. Here, we present our online buffer exchange-native MS method combined with Direct Mass Technology (OBE-nMS+DMT) which facilitates high-throughput analysis and guides sample preparation. We applied this method to optimize the GPR119-G

Indexed as

Cryoelectron MicroscopyReceptors, G-Protein-CoupledHumansMass SpectrometryModels, MolecularProtein BindingProtein ConformationReceptors, G-Protein-Coupledcryo-EMDirect Mass TechnologyGPR119G protein-coupled receptormembrane proteinnative mass spectrometryonline buffer exchange

Identifiers

PMID39471802
PMCPMC11625002

What Socratic 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 Socratic graph.