Evidence map›Paper›PMID 23873934›Full record

ArticleThe Journal of biological chemistry2013

Modulation of human mitochondrial voltage-dependent anion channel 2 (hVDAC-2) structural stability by cysteine-assisted barrel-lipid interactions.

Svetlana Rajkumar Maurya, Radhakrishnan Mahalakshmi

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

26 citing papers in PubMed, 43 citations in OpenAlex.

  1. Review
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  11. Transmembrane β-barrels: Evolution, folding and energetics.Biochimica et biophysica acta. Biomembranes · 2017
    Review
  12. Article
  13. Article
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  15. Review
  16. Role of cysteines in mammalian VDAC isoforms' function.Biochimica et biophysica acta · 2016
    Review
  17. Review
  18. Article
  19. Article
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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 Molecular Biophysics Laboratory, Department of Biological Sciences, Indian Institute of Science Education and Research, Bhopal 462023, India.
Radhakrishnan MahalakshmiFrom the Molecular Biophysics Laboratory, Department of Biological Sciences, Indian Institute of Science Education and Research, Bhopal 462023, India. Electronic address: maha@iiserb.ac.in.
Indian Institute of Science Education and Research, Bhopal · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human mitochondrial voltage-dependent anion channel 2 (hVDAC-2), the most predominant isoform seen in brain mitochondria, is not only crucial for cell survival but is also implicated in Alzheimer disease. The abundance of cysteines in this isoform is particularly fascinating, as hVDAC-1 cysteines have no associated functional role. We report a detailed biophysical examination of a Cys-less mutant of hVDAC-2, and its behavioral comparison with the wild type protein. Our findings suggest that cysteine mutation results in the formation of a better barrel at the expense of weakened protein-lipid interactions. The wild type protein displays stronger lipid association, despite being less structured. A reversal in behavior of both proteins is observed in the case of chemical denaturation, with the Cys-less mutant exhibiting lowered unfolding free energies. In bicellar systems comprising 14-C phosphocholines, we observe that protein-lipid interactions are weakened in both constructs, resulting in barrel structure destabilization. Our biochemical and biophysical studies together reveal key structural roles for the cysteine residues. We find that minor conformational variations in local residues are sufficient to define the membrane protein dynamics in hVDAC-2. Such subtle sequence variations contribute to differential stability of VDACs and may have implications in their in vivo regulation and recycling.

Indexed as

Protein FoldingAlzheimer DiseaseCysteineHumansMutationPhosphorylcholineProtein StabilityProtein Structure, TertiaryVoltage-Dependent Anion Channel 2CysteinePhosphorylcholineVDAC2 protein, humanVoltage-Dependent Anion Channel 2Anion ChannelCysteine MutationKineticsMembrane BiophysicsMembrane ProteinsProtein DenaturationProtein FoldingProtein-Lipid InteractionSpectroscopyThermodynamics

Identifiers

PMID23873934
PMCPMC3757219
OpenAlexW2103945004

What OpenQuestion holds

Textmetadata
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.