Evidence map›Paper›PMID 34969836›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2022

Lipid bilayer induces contraction of the denatured state ensemble of a helical-bundle membrane protein.

Kristen A Gaffney, Ruiqiong Guo, Michael D Bridges, Shaima Muhammednazaar, Daoyang Chen, Miyeon Kim, Zhongyu Yang, Anthony L Schilmiller, Nabil F Faruk, Xiangda Peng and 6 more

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

13 citing papers in PubMed, 17 citations in OpenAlex.

  1. Review
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  11. Folding speeds of helical membrane proteins.Biochemical Society transactions · 2024
    Review
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

16 authors at 4 institutions in 1 country.

Kristen A GaffneyDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824.ORCID 0000-0002-5599-1134
Ruiqiong GuoDepartment of Chemistry, Michigan State University, East Lansing, MI 48824.ORCID 0000-0003-2781-5384
Michael D BridgesJules Stein Eye Institute, University of California, Los Angeles, CA 90095.
Shaima MuhammednazaarDepartment of Chemistry, Michigan State University, East Lansing, MI 48824.
Daoyang ChenDepartment of Chemistry, Michigan State University, East Lansing, MI 48824.
Miyeon KimDepartment of Chemistry, Michigan State University, East Lansing, MI 48824.
Zhongyu YangDepartment of Chemistry and Biochemistry, North Dakota State University, Fargo, ND 58108.ORCID 0000-0002-3018-3608
Anthony L SchilmillerResearch Technology Support Facility Mass Spectrometry and Metabolomics Core, Michigan State University, East Lansing, MI 48824.ORCID 0000-0001-7069-7120
Nabil F FarukGraduate Program in Biophysical Sciences, The University of Chicago, Chicago, IL 60637.
Xiangda PengDepartment of Biochemistry & Molecular Biology, The University of Chicago, Chicago, IL 60637.ORCID 0000-0001-9013-3090
A Daniel JonesDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824.ORCID 0000-0002-7408-6690
Kelly H KimDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824.ORCID 0000-0002-1360-2778
Liangliang SunDepartment of Chemistry, Michigan State University, East Lansing, MI 48824.ORCID 0000-0001-8939-5042
Wayne L HubbellJules Stein Eye Institute, University of California, Los Angeles, CA 90095.ORCID 0000-0003-0577-3312
Tobin R SosnickDepartment of Biochemistry & Molecular Biology, The University of Chicago, Chicago, IL 60637; trsosnic@uchicago.edu honghd@msu.edu.ORCID 0000-0002-2871-7244
Heedeok HongDepartment of Biochemistry and Molecular Biology, Michigan State University, East Lansing, MI 48824; trsosnic@uchicago.edu honghd@msu.edu.ORCID 0000-0003-0118-5193
Michigan State University · USUniversity of Chicago · USUniversity of California, Los Angeles · USNorth Dakota State University · US

Funding

TR&D Project 3P41EB001980 · NIBIB · MEDICAL COLLEGE OF WISCONSIN · PI KLUG, CANDICE S · 2003 to 2017
$16.3M
MOLECULAR BASIS OF MEMBRANE EXCITATIONR01EY005216 · NEI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI HUBBELL, WAYNE L · 1985 to 2019
$9.8M
Kinetic studies of protein foldingR01GM055694 · NIGMS · UNIVERSITY OF CHICAGO · PI SOSNICK, TOBIN R · 2001 to 2022
$7.6M
Vision Science Training ProgramT32EY007026 · NEI · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI Alapakkam P Sampath · 1985 to 2026
$5.7M
Graduate Program in Biophysical Sciences at the University of Chicago - Renewal 0T32EB009412 · NIBIB · UNIVERSITY OF CHICAGO · PI ENGEL, GREGORY S, SOSNICK, TOBIN R · 2009 to 2023
$4.9M
Quantitative proteomics of Zebrafish embryos and blastomeresR01GM125991 · NIGMS · MICHIGAN STATE UNIVERSITY · PI SUN, LIANGLIANG · 2018 to 2022
$1.7M
Folding and degradation of membrane proteinsR35GM144146 · NIGMS · MICHIGAN STATE UNIVERSITY · PI Heedeok Hong · 2022 to 2026
$1.5M
Folding and degradation of membrane proteinsR01GM118685 · NIGMS · MICHIGAN STATE UNIVERSITY · PI HONG, HEEDEOK · 2016 to 2020
$1.5M
Manipulating and predicting the unfolded ensembles of disordered proteinsR01GM130122 · NIGMS · UNIVERSITY OF CHICAGO · PI CLARK, PATRICIA LOUISE, SOSNICK, TOBIN R · 2018 to 2021
$1.4M
NEI NIH HHS R01 EY005216NEI NIH HHS T32 EY007026NIBIB NIH HHS P41 EB001980NIBIB NIH HHS T32 EB009412NIGMS NIH HHS R01 GM055694NIGMS NIH HHS R01 GM118685NIGMS NIH HHS R01 GM125991NIGMS NIH HHS R01 GM130122NIGMS NIH HHS R35 GM144146
6 · The paper itself

Abstract

Defining the denatured state ensemble (DSE) and disordered proteins is essential to understanding folding, chaperone action, degradation, and translocation. As compared with water-soluble proteins, the DSE of membrane proteins is much less characterized. Here, we measure the DSE of the helical membrane protein GlpG of

Indexed as

Protein ConformationBiotinylationCell MembraneCryoelectron MicroscopyDNA-Binding ProteinsEndopeptidasesEscherichia coliEscherichia coli ProteinsLipid BilayersMembrane ProteinsModels, MolecularProtein DenaturationProtein FoldingStreptavidinDNA-Binding ProteinsEndopeptidasesEscherichia coli ProteinsGlpG protein, E coliLipid BilayersMembrane ProteinsStreptavidindenatured stateGlpGmembrane protein foldingsteric trappingUpside simulation

Identifiers

PMID34969836
PMCPMC8740594
OpenAlexW4225886135

What Socratic holds

Textmetadata
LicenceCC BY-NC-ND
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.