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

Modulation of the mitochondrial voltage dependent anion channel (VDAC) by curcumin.

Biochimica et biophysica acta - 1 Jan 2015

Tewari Debanjan, Ahmed Tofayel, Chirasani Venkat R, Singh Pradeep K, Maji Samir K, Senapati Sanjib, Bera Amal Kanti

Abstract excerpt

Voltage dependent anion channel (VDAC) of mitochondria plays a crucial role in apoptosis. Human VDAC-1, reconstituted in planar lipid bilayer showed reduced conductance when treated with curcumin. Curcumin interacts with residues in the α helical N-terminus of VDAC and in the channel wall, as revealed by molecular docking, followed by mutational analysis. N-terminus mimicking peptide showed conformational changes...

Read the complete abstract on PubMed

Topics

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

Share to Circular Dichroism
Share to Curcumin

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Ion Channel Gating

Share to Lipid Bilayers

Share to Mitochondrial Proteins

Share to Molecular Docking Simulation

Share to Molecular Structure

Share to Spectrophotometry

Source

Identifiers

PMID: 25459681
DOI: 10.1016/j.bbamem.2014.10.014

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Modulation of the mitochondrial voltage dependent anion channel (VDAC) by curcumin.PMID 25459681Read ↗

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

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

The anticancer effect of Metformin targets VDAC1 via ER-mitochondria interaction-mediated autophagy in HCCSemantic proximity Read ↗

Phosphorylation by Nek1 regulates opening and closing of voltage dependent anion channel 1.Semantic proximity Read ↗

Mapping ligand binding pockets in chloride ClC-1 channels through an integrated in silico and experimental approach using anthracene-9-carboxylic acid and niflumic acid.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 ↗

Inhibition of chloride intracellular channel protein 1 (CLIC1) ameliorates liver fibrosis phenotype by activating the Ca2+-dependent Nrf2 pathway.Semantic proximity Read ↗

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

External Zn(2+) binding to cysteine-substituted cystic fibrosis transmembrane conductance regulator constructs regulates channel gating and curcumin potentiation.Semantic proximity Read ↗

Molecular Basis for Fe(III)-Independent Curcumin Potentiation of Cystic Fibrosis Transmembrane Conductance Regulator Activity.Semantic proximity Read ↗

Study on the interaction between curcumin and CopC by spectroscopic and docking methods.Semantic proximity Read ↗

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

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