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

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

The Journal of biological chemistry - 30 Mar 2012

Teijido Oscar, Ujwal Rachna, Hillerdal Carl-Olof, Kullman Lisen, Rostovtseva Tatiana K, Abramson Jeff

Abstract excerpt

The voltage-dependent anion channel (VDAC) governs the free exchange of ions and metabolites between the mitochondria and the rest of the cell. The three-dimensional structure of VDAC1 reveals a channel formed by 19 β-strands and an N-terminal α-helix located near the midpoint of the pore. The position of this α-helix causes a narrowing of the cavity, but ample space for metabolite passage remains. The...

Read the complete abstract on PubMed

Topics

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

Share to Cloning, Molecular
Share to Ion Channel Gating

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

Share to Lipid Bilayers

Share to Models, Molecular

Share to Porosity

Share to Protein Engineering

Share to Protein Structure, Secondary

Source

Open in PubMed Open full text

Identifiers

PMID: 22275367
DOI: 10.1074/jbc.M111.314229
PMCID: PMC3322836

Genes

VDAC1

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

Affixing N-terminal α-helix to the wall of the voltage-dependent anion channel does not prevent its voltage gating.PMID 22275367Read ↗

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

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

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

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

Structural and molecular insight into the pH-induced low-permeability of the voltage-gated potassium channel Kv1.2 through dewetting of the water cavity.Semantic proximity Read ↗

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

Insights into the structure and function of HV1 from a meta-analysis of mutation studies.Semantic proximity Read ↗

Evolutionary selection of a 19-stranded mitochondrial β-barrel scaffold bears structural and functional significance.Semantic proximity Read ↗

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

Structure of the human volume regulated anion channelSemantic proximity Read ↗

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

Conformational changes required for H(+)/Cl(-) exchange mediated by a CLC transporter.Semantic proximity Read ↗

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