Evidence map›Paper›PMID 26487717›Full record

ArticleThe Journal of biological chemistry2015

N-helix and Cysteines Inter-regulate Human Mitochondrial VDAC-2 Function and Biochemistry.

Svetlana Rajkumar Maurya, Radhakrishnan Mahalakshmi

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.4field-weighted citation impact, top 11% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

22 citing papers in PubMed, 31 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. VDAC2: an emerging pivotal and multifaceted regulator in tumor biology.Apoptosis : an international journal on programmed cell death · 2026
    Review
  5. Article
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  16. Article
  17. Transmembrane β-barrels: Evolution, folding and energetics.Biochimica et biophysica acta. Biomembranes · 2017
    Review
  18. Article
  19. Review
  20. Role of cysteines in mammalian VDAC isoforms' function.Biochimica et biophysica acta · 2016
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Svetlana Rajkumar MauryaFrom the Department of Biological Sciences, Molecular Biophysics Laboratory, Indian Institute of Science Education and Research, Bhopal 462023, India.
Radhakrishnan MahalakshmiFrom the Department of Biological Sciences, Molecular Biophysics Laboratory, Indian Institute of Science Education and Research, Bhopal 462023, India maha@iiserb.ac.in.ORCID http://orcid.org/0000-0003-1549-7550
Indian Institute of Science Education and Research, Bhopal · IN

Funding

DBT-Wellcome Trust India Alliance IA/I/14/1/501305Wellcome Trust IA/I/14/1/501305
6 · The paper itself

Abstract

Human voltage-dependent anion channel-2 (hVDAC-2) functions primarily as the crucial anti-apoptotic protein in the outer mitochondrial membrane, and additionally as a gated bidirectional metabolite transporter. The N-terminal helix (NTH), involved in voltage sensing, bears an additional 11-residue extension (NTE) only in hVDAC-2. In this study, we assign a unique role for the NTE as influencing the chaperone-independent refolding kinetics and overall thermodynamic stability of hVDAC-2. Our electrophysiology data shows that the N-helix is crucial for channel activity, whereas NTE sensitizes this isoform to voltage gating. Additionally, hVDAC-2 possesses the highest cysteine content, possibly for regulating reactive oxygen species content. We identify interdependent contributions of the N-helix and cysteines to channel function, and the measured stability in micellar environments with differing physicochemical properties. The evolutionary demand for the NTE in the presence of cysteines clearly emerges from our biochemical and functional studies, providing insight into factors that functionally demarcate hVDAC-2 from the other VDACs.

Indexed as

Ion Channel GatingCysteineHumansMitochondrial ProteinsProtein Structure, SecondaryStructure-Activity RelationshipThermodynamicsVoltage-Dependent Anion Channel 2CysteineMitochondrial ProteinsVDAC2 protein, humanVoltage-Dependent Anion Channel 2gatingion channelmembrane proteinN-terminal domainprotein foldingthermodynamicsvoltage-dependent anion channel (VDAC)

Identifiers

PMID26487717
PMCPMC4683249
OpenAlexW1749320268

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.