Evidence map›Paper›PMID 25420508›Full record

ArticleQuarterly reviews of biophysics2015

The safety dance: biophysics of membrane protein folding and misfolding in a cellular context.

Jonathan P Schlebach, Charles R Sanders

Open access · greenAbstract read
In one paragraph

Article in Quarterly reviews of biophysics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

24 citing papers in PubMed, 49 citations in OpenAlex.

  1. Review
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  6. Review
  7. Fast slow folding of an outer membrane porin.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  8. Spiers Memorial Lecture: Analysis andFaraday discussions · 2021
    Article
  9. Article
  10. Article
  11. Quarterly reviews of biophysics · 2020
    Review
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  17. Review
  18. Miscoding-induced stalling of substrate translocation on the bacterial ribosome.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  19. Article
  20. 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

2 authors at 1 institution in 1 country.

Jonathan P SchlebachDepartment of Biochemistry and Center for Structural Biology,Vanderbilt University School of Medicine,Nashville,Tennessee 37232,USA.
Charles R SandersDepartment of Biochemistry and Center for Structural Biology,Vanderbilt University School of Medicine,Nashville,Tennessee 37232,USA.
Vanderbilt University · US

Funding

Decrypting Variants of Uncertain Significance in Long-QT SyndromeR01HL122010 · NHLBI · VANDERBILT UNIVERSITY · PI GEORGE, ALFRED L., SANDERS, CHARLES R · 2014 to 2025
$15.5M
Project 4 (Goethe University of Frankfurt)U54GM094608 · NIGMS · HARVARD MEDICAL SCHOOL · PI CHOU, JAMES JEIWEN · 2010 to 2014
$11.5M
Structural Basis for KCNE Modulation of the KCNQ1 ChannelR01DC007416 · NIDCD · VANDERBILT UNIVERSITY · PI SANDERS, CHARLES R, VANOYE, CARLOS G. · 2006 to 2014
$3.0M
Structure Function Analysis of Integrins alpha1beta1 and alpha2beta2R01DK083187 · NIDDK · VANDERBILT UNIVERSITY MEDICAL CENTER · PI SANDERS, CHARLES R, ZENT, ROY · 2010 to 2013
$1.3M
Cholesterol and the Amyloid Precursor ProteinR01GM106672 · NIGMS · VANDERBILT UNIVERSITY · PI SANDERS, CHARLES R · 2013 to 2016
$1.2M
Structural Basis for the Partitioning of C99 into Liquid-Ordered Membrane DomainsF32GM110929 · NIGMS · VANDERBILT UNIVERSITY · PI SCHLEBACH, JONATHAN PATRICK · 2014 to 2015
$109k
NHLBI NIH HHS R01 HL122010NIDCD NIH HHS R01 DC007416NIDDK NIH HHS R01 DK083187NIGMS NIH HHS F32 GM110929NIGMS NIH HHS R01 GM106672NIGMS NIH HHS U54 GM094608
6 · The paper itself

Abstract

Most biological processes require the production and degradation of proteins, a task that weighs heavily on the cell. Mutations that compromise the conformational stability of proteins place both specific and general burdens on cellular protein homeostasis (proteostasis) in ways that contribute to numerous diseases. Efforts to elucidate the chain of molecular events responsible for diseases of protein folding address one of the foremost challenges in biomedical science. However, relatively little is known about the processes by which mutations prompt the misfolding of α-helical membrane proteins, which rely on an intricate network of cellular machinery to acquire and maintain their functional structures within cellular membranes. In this review, we summarize the current understanding of the physical principles that guide membrane protein biogenesis and folding in the context of mammalian cells. Additionally, we explore how pathogenic mutations that influence biogenesis may differ from those that disrupt folding and assembly, as well as how this may relate to disease mechanisms and therapeutic intervention. These perspectives indicate an imperative for the use of information from structural, cellular, and biochemical studies of membrane proteins in the design of novel therapeutics and in personalized medicine.

Indexed as

Protein FoldingAmino Acid SequenceAnimalsCellsHomeostasisHumansMembrane ProteinsMolecular Sequence DataProtein Structure, SecondaryProtein TransportMembrane Proteins

Identifiers

PMID25420508
PMCPMC4339315
OpenAlexW2314581359

What OpenQuestion 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 OpenQuestion graph.