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

Large scale rearrangement of protein domains is associated with voltage gating of the VDAC channel.

Biophysical journal - 1 Apr 1992

Peng S, Blachly-Dyson E, Forte M, Colombini M

Abstract excerpt

The VDAC channel of the mitochondrial outer membrane is voltage-gated like the larger, more complex voltage-gated channels of the plasma membrane. However, VDAC is a low molecular weight (30 kDa), abundant protein, which is readily purified and reconstituted, making it an ideal system for analyzing the molecular basis for ion selectivity and voltage-gating. We have probed the VDAC channel by subjecting the cloned...

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 Ion Channels
Share to Membrane Proteins

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

Share to Mitochondria

Share to Molecular Sequence Data

Share to Mutation

Share to Protein Conformation

Share to Saccharomyces cerevisiae

Source

Open in PubMed Open full text

Identifiers

PMID: 1376163
DOI: 10.1016/S0006-3495(92)81799-X
PMCID: PMC1260505

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

Large scale rearrangement of protein domains is associated with voltage gating of the VDAC channel.PMID 1376163Read ↗

Structure and Gating Behavior of the Human Integral Membrane Protein VDAC1 in a Lipid Bilayer.Semantic proximity Read ↗

Selectivity changes in site-directed mutants of the VDAC ion channel: structural implications.Semantic proximity Read ↗

Affixing N-terminal α-helix to the wall of the voltage-dependent anion channel does not prevent its voltage gating.Semantic proximity Read ↗

The intrinsically disordered N-terminus of the voltage-dependent anion channelSemantic proximity Read ↗

Role of cysteines in mammalian VDAC isoforms' function.Semantic proximity Read ↗

Structural basis of complex formation between mitochondrial anion channel VDAC1 and Hexokinase-II.Semantic proximity Read ↗

NMR Structural and Biophysical Analysis of the Disease-Linked Inner Mitochondrial Membrane Protein MPV17.Semantic proximity Read ↗

The 3.5-Å CryoEM Structure of Nanodisc-Reconstituted Yeast Vacuolar ATPase Vo Proton Channel.Semantic proximity Read ↗

The intrinsically disordered N-terminus of the voltage-dependent anion channel.Semantic proximity Read ↗

A tag at the carboxy terminus prevents membrane integration of VDAC1 in mammalian mitochondria.Semantic proximity Read ↗

Multicopy suppressors of phenotypes resulting from the absence of yeast VDAC encode a VDAC-like protein.Semantic proximity Read ↗

An N-terminal nucleotide-binding site in VDAC1: involvement in regulating mitochondrial function.Semantic proximity Read ↗

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