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

Protein translocation across planar bilayers by the colicin Ia channel-forming domain: where will it end?

The Journal of general physiology - 1 Oct 2000

Kienker P K, Jakes K S, Finkelstein A

Abstract excerpt

Colicin Ia, a 626-residue bactericidal protein, consists of three domains, with the carboxy-terminal domain (C domain) responsible for channel formation. Whole colicin Ia or C domain added to a planar lipid bilayer membrane forms voltage-gated channels. We have shown previously that the channel formed by whole colicin Ia has four membrane-spanning segments and an approximately 68-residue segment translocated...

Read the complete abstract on PubMed

Topics

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

Share to Colicins
Share to Escherichia coli
Share to Indicators and Reagents

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

Share to Ion Channel Gating

Share to Ion Channels

Share to Lipid Bilayers

Share to Protein Transport

Share to Streptavidin

Source

Open in PubMed Open full text

Identifiers

PMID: 11004207
DOI: 10.1085/jgp.116.4.587
PMCID: PMC2230624

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

Protein translocation across planar bilayers by the colicin Ia channel-forming domain: where will it end?PMID 11004207Read ↗

Gating movements of colicin A and colicin Ia are different.Semantic proximity Read ↗

The molecular basis for the pH-activation mechanism in the channel-forming bacterial colicin E1.Semantic proximity Read ↗

Identification of a translocated gating charge in a voltage-dependent channel. Colicin E1 channels in planar phospholipid bilayer membranes.Semantic proximity Read ↗

Rearrangements in the KcsA cytoplasmic domain underlie its gating.Semantic proximity Read ↗

Unfolding of colicin A during its translocation through the Escherichia coli envelope as demonstrated by disulfide bond engineering.Semantic proximity Read ↗

Alteration of the pH-dependent ion selectivity of the colicin E1 channel by site-directed mutagenesis.Semantic proximity Read ↗

An intermediate in the assembly of a pore-forming protein trapped with a genetically-engineered switch.Semantic proximity Read ↗

Immunity protein release from a cell-bound nuclease colicin complex requires global conformational rearrangement.Semantic proximity Read ↗

The TolA-recognition site of colicin N. ITC, SPR and stopped-flow fluorescence define a crucial 27-residue segment.Semantic proximity Read ↗

Dynamic gating by ϕ-clamp loop controls peptide translocation through the anthrax toxin nanopore.Semantic proximity Read ↗

Membrane topology of the colicin E1 channel using genetically encoded fluorescence.Semantic proximity Read ↗

A rivet model for channel formation by aerolysin-like pore-forming toxins.Semantic proximity Read ↗

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