Evidence map›Paper›PMID 32053772›Full record

ArticleStructure (London, England : 1993)2020

Characterizing Membrane Association and Periplasmic Transfer of Bacterial Lipoproteins through Molecular Dynamics Simulations.

Shanlin Rao, George T Bates, Callum R Matthews, Thomas D Newport, Owen N Vickery, Phillip J Stansfeld

Open access · hybridAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.3field-weighted citation impact, top 20% 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

15 citing papers in PubMed, 25 citations in OpenAlex.

  1. 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

6 authors at 2 institutions in 1 country.

Shanlin RaoDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
George T BatesDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Callum R MatthewsDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Thomas D NewportDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK.
Owen N VickeryDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK; School of Life Sciences & Department of Chemistry, University of Warwick, Gibbet Hill Campus, Coventry CV4 7AL, UK.
Phillip J StansfeldDepartment of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, UK; School of Life Sciences & Department of Chemistry, University of Warwick, Gibbet Hill Campus, Coventry CV4 7AL, UK. Electronic address: phillip.stansfeld@warwick.ac.uk.
University of Oxford · GBUniversity of Warwick · GB

Funding

Biotechnology and Biological Sciences Research Council BB/L01386X/1Biotechnology and Biological Sciences Research Council BB/P01948X/1Biotechnology and Biological Sciences Research Council BB/R002517/1Biotechnology and Biological Sciences Research Council BB/S003339/1Medical Research Council MR/S009213/1Wellcome TrustWellcome Trust 208361/Z/17/Z
6 · The paper itself

Abstract

Escherichia coli lipoprotein precursors at the inner membrane undergo three maturation stages before transport by the Lol system to the outer membrane. Here, we develop a pipeline to simulate the membrane association of bacterial lipoproteins in their four maturation states. This has enabled us to model and simulate 81 of the predicted 114 E. coli lipoproteins and reveal their interactions with the host lipid membrane. As part of this set we characterize the membrane contacts of LolB, the lipoprotein involved in periplasmic translocation. We also consider the means and bioenergetics for lipoprotein localization. Our calculations uncover a preference for LolB over LolA and therefore indicate how a lipoprotein may be favorably transferred from the inner to outer membrane. Finally, we reveal that LolC has a role in membrane destabilization, thereby promoting lipoprotein transfer to LolA.

Indexed as

Molecular Dynamics SimulationBacterial Outer MembraneBacterial Outer Membrane ProteinsEscherichia coliEscherichia coli ProteinsMolecular ChaperonesPeriplasmPeriplasmic Binding ProteinsProtein BindingProtein TransportBacterial Outer Membrane ProteinsEscherichia coli ProteinsLolA protein, E coliLolB protein, E coliMolecular ChaperonesPeriplasmic Binding Proteinsantibioticsbiogenesislipoproteinmembrane proteinsmolecular simulation

Identifiers

PMID32053772
PMCPMC7139219
OpenAlexW3005776537

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.