Evidence map›Paper›PMID 29507234›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Allostery revealed within lipid binding events to membrane proteins.

John W Patrick, Christopher D Boone, Wen Liu, Gloria M Conover, Yang Liu, Xiao Cong, Arthur Laganowsky

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
8.8field-weighted citation impact, top 1% 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

62 citing papers in PubMed, 111 citations in OpenAlex.

  1. Article
  2. TREK2 Lipid Binding Preferences Revealed by Native Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2024
    Article
  3. Coordination of bilayer properties by an inward-rectifier KJournal of structural biology: X · 2024
    Article
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  9. Article
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  11. Article
  12. Review
  13. Emergence of mass spectrometry detergents for membrane proteomics.Analytical and bioanalytical chemistry · 2023
    Review
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

2 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

7 authors at 2 institutions in 1 country.

John W PatrickDepartment of Chemistry, Texas A&M University, College Station, TX 77842.
Christopher D BooneDepartment of Chemistry, Texas A&M University, College Station, TX 77842.
Wen LiuInstitute of Biosciences and Technology, Texas A&M Health Science Center, Houston, TX 77030.
Gloria M ConoverDepartment of Chemistry, Texas A&M University, College Station, TX 77842.
Yang LiuInstitute of Biosciences and Technology, Texas A&M Health Science Center, Houston, TX 77030.
Xiao CongInstitute of Biosciences and Technology, Texas A&M Health Science Center, Houston, TX 77030.
Arthur LaganowskyDepartment of Chemistry, Texas A&M University, College Station, TX 77842; alaganowsky@chem.tamu.edu.
Texas A&M University · USTexas A&M Health Science Center · US

Funding

Overall EvaluationP41GM103403 · NIGMS · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2012 to 2017
$14.3M
Native ion mobility mass spectrometry studies of potassium inward rectifier channels: insight into gating and lipid bindingDP2GM123486 · NIGMS · TEXAS A&M UNIVERSITY HEALTH SCIENCE CTR · PI LAGANOWSKY, ARTHUR D · 2016 to 2016
$2.2M
Pixel Array Detector for Macromolecular CrystallographyS10OD021527 · OD · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2016 to 2016
$2.0M
NIGMS NIH HHS DP2 GM123486NIGMS NIH HHS P41 GM103403NIH HHS S10 OD021527
6 · The paper itself

Abstract

Membrane proteins interact with a myriad of lipid species in the biological membrane, leading to a bewildering number of possible protein-lipid assemblies. Despite this inherent complexity, the identification of specific protein-lipid interactions and the crucial role of lipids in the folding, structure, and function of membrane proteins is emerging from an increasing number of reports. Fundamental questions remain, however, regarding the ability of specific lipid binding events to membrane proteins to alter remote binding sites for lipids of a different type, a property referred to as allostery [Monod J, Wyman J, Changeux JP (1965)

Indexed as

Bacterial Outer Membrane ProteinsBinding SitesCation Transport ProteinsEscherichia coliEscherichia coli ProteinsGene Expression Regulation, BacterialLipid MetabolismLipidsMembrane ProteinsModels, MolecularProtein BindingProtein ConformationAmtB protein, E coliBacterial Outer Membrane ProteinsCation Transport ProteinsEscherichia coli ProteinsLipidsMembrane Proteinsallosterylipid−protein interactionslipidsmembrane proteinsnative mass spectrometry

Identifiers

PMID29507234
PMCPMC5866585
OpenAlexW2789582625

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.