Evidence map›Paper›PMID 25277655›Full record

ReviewJournal of molecular biology2015

Mechanisms of integral membrane protein insertion and folding.

Florian Cymer, Gunnar von Heijne, Stephen H White

Open access · greenAbstract readReview
In one paragraph

Review in Journal of molecular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 205 papers.

0numbers the graph read from it
0cells of the map it votes in
205citing papers in PubMed
15.2field-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

205 citing papers in PubMed, 355 citations in OpenAlex.

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  15. Spatially regulated mRNA translation enables functional membrane protein integration in synthetic cells.Proceedings of the National Academy of Sciences of the United States of America · 2026
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145 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

3 authors at 1 institution in 1 country.

Florian Cymer *Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm.
Gunnar von Heijne *Center for Biomembrane Research, Department of Biochemistry and Biophysics, Stockholm University, SE-106 91 Stockholm.
Stephen H White *Department of Physiology and Biophysics and the Center for Biomembrane Systems University of California, Irvine Irvine, CA 92697.
Science for Life Laboratory · SE

Funding

Project 3: Structural Studies of Voltage-Gated Potassium Channels as FunctionP01GM086685 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI WORCESTER, DAVID · 2009 to 2013
$6.7M
Membrane Protein Folding and AssemblyR01GM074637 · NIGMS · UNIVERSITY OF CALIFORNIA-IRVINE · PI WHITE, STEPHEN H. · 2006 to 2020
$4.5M
European Research Council 232648NIGMS NIH HHS P01 GM086685NIGMS NIH HHS P01 GM86685NIGMS NIH HHS R01 GM074637
6 · The paper itself

Abstract

The biogenesis, folding, and structure of α-helical membrane proteins (MPs) are important to understand because they underlie virtually all physiological processes in cells including key metabolic pathways, such as the respiratory chain and the photosystems, as well as the transport of solutes and signals across membranes. Nearly all MPs require translocons--often referred to as protein-conducting channels--for proper insertion into their target membrane. Remarkable progress toward understanding the structure and functioning of translocons has been made during the past decade. Here, we review and assess this progress critically. All available evidence indicates that MPs are equilibrium structures that achieve their final structural states by folding along thermodynamically controlled pathways. The main challenge for cells is the targeting and membrane insertion of highly hydrophobic amino acid sequences. Targeting and insertion are managed in cells principally by interactions between ribosomes and membrane-embedded translocons. Our review examines the biophysical and biological boundaries of MP insertion and the folding of polytopic MPs in vivo. A theme of the review is the under-appreciated role of basic thermodynamic principles in MP folding and assembly. Thermodynamics not only dictates the final folded structure but also is the driving force for the evolution of the ribosome-translocon system of assembly. We conclude the review with a perspective suggesting a new view of translocon-guided MP insertion.

Indexed as

Cell MembraneMembrane ProteinsProtein FoldingProtein Structure, TertiaryRibosomesThermodynamicsMembrane Proteinslipid–protein interactionsmembrane protein biogenesismembrane protein foldingtransmembrane helix

Identifiers

PMID25277655
PMCPMC4339636
OpenAlexW1969549030

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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.