Evidence map›Paper›PMID 32499369›Full record

ReviewThe Journal of biological chemistry2020

Role of the lipid bilayer in outer membrane protein folding in Gram-negative bacteria.

Jim E Horne, David J Brockwell, Sheena E Radford

Open access · hybridAbstract readReview
In one paragraph

Review in The Journal of biological chemistry, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.

0numbers the graph read from it
0cells of the map it votes in
97citing papers in PubMed
7.8field-weighted citation impact, top 2% 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

97 citing papers in PubMed, 179 citations in OpenAlex.

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  9. A secreted citrus protease cleaves an outer membrane protein of the Huanglongbing pathogen.Proceedings of the National Academy of Sciences of the United States of America · 2026
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37 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.

Jim E HorneAstbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, United Kingdom.
David J BrockwellAstbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, United Kingdom.
Sheena E RadfordAstbury Centre for Structural Molecular Biology, School of Molecular and Cellular Biology, Faculty of Biological Sciences, University of Leeds, Leeds, United Kingdom s.e.radford@leeds.ac.uk.ORCID 0000-0002-3079-8039
University of Leeds · GB

Funding

Biotechnology and Biological Sciences Research Council BB/K000659/1Biotechnology and Biological Sciences Research Council BB/M01151/1Biotechnology and Biological Sciences Research Council BB/N007603/1Biotechnology and Biological Sciences Research Council BB/T000635/1Medical Research Council MR/P018491/1
6 · The paper itself

Abstract

β-Barrel outer membrane proteins (OMPs) represent the major proteinaceous component of the outer membrane (OM) of Gram-negative bacteria. These proteins perform key roles in cell structure and morphology, nutrient acquisition, colonization and invasion, and protection against external toxic threats such as antibiotics. To become functional, OMPs must fold and insert into a crowded and asymmetric OM that lacks much freely accessible lipid. This feat is accomplished in the absence of an external energy source and is thought to be driven by the high thermodynamic stability of folded OMPs in the OM. With such a stable fold, the challenge that bacteria face in assembling OMPs into the OM is how to overcome the initial energy barrier of membrane insertion. In this review, we highlight the roles of the lipid environment and the OM in modulating the OMP-folding landscape and discuss the factors that guide folding

Indexed as

Protein FoldingBacterial Outer Membrane ProteinsCell MembraneGram-Negative BacteriaLipid BilayersProtein MultimerizationBacterial Outer Membrane ProteinsLipid Bilayersantibiotic resistanceBAM complexdisorderasefolding kineticsGram-negative bacterialipidlipid membranemembrane bilayermembrane proteinmembrane protein foldingOMPomeouter membraneprotein foldingprotein-lipid interactionsβ-barrel assembly machinery (BAM) complex

Identifiers

PMID32499369
PMCPMC7383365
OpenAlexW3033772165

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.