Evidence map›Paper›PMID 36768981›Full record

ArticleInternational journal of molecular sciences2023

Factors That Control the Force Needed to Unfold a Membrane Protein in Silico Depend on the Mode of Denaturation.

Nabil F Faruk, Xiangda Peng, Tobin R Sosnick

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in International journal of molecular sciences, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing 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

5 citing papers in PubMed.

  1. Review
  2. Article
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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.

Nabil F FarukDepartment of Biochemistry & Molecular Biology, Institute for Biophysical Dynamics, The University of Chicago, Chicago, IL 60637, USA.
Xiangda PengDepartment of Biochemistry & Molecular Biology, Institute for Biophysical Dynamics, The University of Chicago, Chicago, IL 60637, USA.ORCID 0000-0001-9013-3090
Tobin R SosnickDepartment of Biochemistry & Molecular Biology, Institute for Biophysical Dynamics, The University of Chicago, Chicago, IL 60637, USA.ORCID 0000-0002-2871-7244

Funding

Kinetic studies of protein foldingR01GM055694 · NIGMS · UNIVERSITY OF CHICAGO · PI SOSNICK, TOBIN R · 2001 to 2022
$7.6M
FOLDING OF AN ALPHA-HELICAL COILED COILR29GM055694 · NIGMS · UNIVERSITY OF CHICAGO · PI SOSNICK, TOBIN R · 1996 to 2000
$107k
National Science Foundation MCB 2023077NIH HHS GM55694
6 · The paper itself

Abstract

Single-molecule force spectroscopy methods, such as AFM and magnetic tweezers, have proved extremely beneficial in elucidating folding pathways for soluble and membrane proteins. To identify factors that determine the force rupture levels in force-induced membrane protein unfolding, we applied our near-atomic-level

Indexed as

BacteriorhodopsinsMicroscopy, Atomic ForceMolecular Dynamics SimulationProtein DenaturationProtein FoldingProtein UnfoldingBacteriorhodopsinsAFMdenaturedmagnetic tweezerssimulationSMFSunfolded

Identifiers

PMID36768981
PMCPMC9917119

What OpenQuestion holds

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Registered trials

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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.