Evidence map›Paper›PMID 30012626›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Specific cardiolipin-SecY interactions are required for proton-motive force stimulation of protein secretion.

Robin A Corey, Euan Pyle, William J Allen, Daniel W Watkins, Marina Casiraghi, Bruno Miroux, Ignacio Arechaga, Argyris Politis, Ian Collinson

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

48 citing papers in PubMed, 74 citations in OpenAlex.

  1. Review
  2. Essential Role of LapD in the Absence of Cardiolipins.International journal of molecular sciences · 2026
    Article
  3. A surface-exposed cardiolipin synthase provides an unexpected paradigm for maintaining the Gram-negative outer membrane.Proceedings of the National Academy of Sciences of the United States of America · 2026
    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

9 authors at 4 institutions in 3 countries.

Robin A CoreySchool of Biochemistry, University of Bristol, Bristol BS8 1TD, United Kingdom.
Euan PyleDepartment of Chemistry, King's College London, London SE1 1DB, United Kingdom.ORCID 0000-0002-4633-4917
William J AllenSchool of Biochemistry, University of Bristol, Bristol BS8 1TD, United Kingdom.
Daniel W WatkinsSchool of Biochemistry, University of Bristol, Bristol BS8 1TD, United Kingdom.
Marina CasiraghiLaboratoire de Biologie Physico-Chimique des Protéines Membranaires, Institut de Biologie Physico-Chimique, CNRS, Université Paris Diderot, Sorbonne Paris Cité University, PSL Research University, 75005 Paris, France.
Bruno MirouxLaboratoire de Biologie Physico-Chimique des Protéines Membranaires, Institut de Biologie Physico-Chimique, CNRS, Université Paris Diderot, Sorbonne Paris Cité University, PSL Research University, 75005 Paris, France.ORCID 0000-0002-3066-4700
Ignacio ArechagaDepartamento de Biología Molecular, Universidad de Cantabria-Consejo Superior de Investigaciones Científicas (CSIC)-Sociedad para el Desarrollo Regional de Cantabria (SODDERCAN), 39011 Santander, Spain.
Argyris PolitisDepartment of Chemistry, King's College London, London SE1 1DB, United Kingdom.
Ian CollinsonSchool of Biochemistry, University of Bristol, Bristol BS8 1TD, United Kingdom; ian.collinson@bristol.ac.uk.
University of Bristol · GBCentre National de la Recherche Scientifique · FRKing's College London · GBUniversidad de Cantabria · ES

Funding

Biotechnology and Biological Sciences Research Council BB/I008675/1Biotechnology and Biological Sciences Research Council BB/M003604/1Biotechnology and Biological Sciences Research Council BB/N015126/1Wellcome TrustWellcome Trust 104632Wellcome Trust 109854/Z/15/Z
6 · The paper itself

Abstract

The transport of proteins across or into membranes is a vital biological process, achieved in every cell by the conserved Sec machinery. In bacteria, SecYEG combines with the SecA motor protein for secretion of preproteins across the plasma membrane, powered by ATP hydrolysis and the transmembrane proton-motive force (PMF). The activities of SecYEG and SecA are modulated by membrane lipids, particularly cardiolipin (CL), a specialized phospholipid known to associate with a range of energy-transducing machines. Here, we identify two specific CL binding sites on the

Indexed as

Molecular Dynamics SimulationProton-Motive ForceBacterial Secretion SystemsEscherichia coliEscherichia coli ProteinsSEC Translocation ChannelsThermotoga maritimaBacterial Secretion SystemsEscherichia coli ProteinsSEC Translocation Channelscardiolipinmolecular dynamicsnative mass spectrometryprotein translocationSecYEG

Identifiers

PMID30012626
PMCPMC6077702
OpenAlexW2761757832

What OpenQuestion holds

Textmetadata
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.