Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

TolA central domain interacts with Escherichia coli porins.

The EMBO journal - 2 Dec 1996

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

Abstract excerpt

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....

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Amino Acid Sequence
Share to Bacterial Proteins
Share to Binding Sites

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Escherichia coli

Share to Genotype

Share to Membrane Proteins

Share to Molecular Sequence Data

Share to Recombinant Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 8978668
PMCID: PMC452466

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

TolA central domain interacts with Escherichia coli porins.PMID 8978668Read ↗

Role of TolR N-terminal, central, and C-terminal domains in dimerization and interaction with TolA and tolQ.Semantic proximity Read ↗

Tol-dependent macromolecule import through the Escherichia coli cell envelope requires the presence of an exposed TolA binding motif.Semantic proximity Read ↗

Protein complex within Escherichia coli inner membrane. TolA N-terminal domain interacts with TolQ and TolR proteins.Semantic proximity Read ↗

Allosteric beta-propeller signalling in TolB and its manipulation by translocating colicins.Semantic proximity Read ↗

The role for TolA in enterohemorrhagic Escherichia coli pathogenesis and virulence gene transcriptionSemantic proximity Read ↗

Distinct regions of the colicin A translocation domain are involved in the interaction with TolA and TolB proteins upon import into Escherichia coli.Semantic proximity Read ↗

Functional characterisation of altered outer membrane proteins for tetracycline resistance in Escherichia coli.Semantic proximity Read ↗

Structure of the Escherichia coli TolB protein determined by MAD methods at 1.95 A resolution.Semantic proximity Read ↗

TonB interacts with nonreceptor proteins in the outer membrane of Escherichia coli.Semantic proximity Read ↗

Impairment of cell division in tolA mutants of Escherichia coli at low and high medium osmolarities.Semantic proximity Read ↗

Peptidoglycan-associated lipoprotein-TolB interaction. A possible key to explaining the formation of contact sites between the inner and outer membranes of Escherichia coli.Semantic proximity Read ↗

Transmembrane alpha-helix interactions are required for the functional assembly of the Escherichia coli Tol complex.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.