Evidence map›Paper›PMID 8978668›Full record

ArticleThe EMBO journal1996

TolA central domain interacts with Escherichia coli porins.

R Derouiche, M Gavioli, H Bénédetti, A Prilipov, C Lazdunski, R Lloubès

Open access · bronzeAbstract read
In one paragraph

Article in The EMBO journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
4.6field-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

28 citing papers in PubMed, 72 citations in OpenAlex.

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  4. Suppressor Mutations inJournal of bacteriology · 2019
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  9. Colicin biology.Microbiology and molecular biology reviews : MMBR · 2007
    Review
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  12. Article
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  15. 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 1 institution in 1 country.

R DerouicheLaboratoire d'Ingénierie et de Dynamique des Systèmes Membranaires, CNRS, Marseille, France.
M Gavioli
H Bénédetti
A Prilipov
C Lazdunski
R Lloubès
Centre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

TolA is an inner membrane protein with three domains: a transmembrane N-terminus and periplasmic central and C-terminal domains. The interaction of TolA with outer membrane porins of Escherichia coli was investigated. Western blot analyses of cell extracts with anti-TolA antibodies indicated that TolA forms high molecular weight complexes specifically with trimeric OmpF, OmpC, PhoE and LamB, but not with OmpA. The interaction of purified TolA domains with purified porins was also studied. TolA interacted with OmpF, PhoE and LamB porins via its central domain, but not with either their denatured monomeric forms or OmpA. Moreover, the presence or absence of lipopolysaccharides associated with trimeric porins did not modify the interactions. These results suggest that the specific interaction of TolA with outer membrane porins might be relevant to the function of Tol proteins.

Indexed as

Escherichia coli ProteinsAmino Acid SequenceAntibodiesBacterial ProteinsBinding SitesEscherichia coliGenotypeImmunoblottingMembrane ProteinsMolecular Sequence DataPorinsRecombinant ProteinsAntibodiesBacterial ProteinsEscherichia coli ProteinsMembrane ProteinsPorinsRecombinant ProteinstolA protein, E coli

Identifiers

PMID8978668
PMCPMC452466
OpenAlexW1533354453

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.