Evidence map›Paper›PMID 26947058›Full record

ReviewBiochimica et biophysica acta2016

Role of cysteines in mammalian VDAC isoforms' function.

Vito De Pinto, Simona Reina, Ankit Gupta, Angela Messina, Radhakrishnan Mahalakshmi

Open access · greenAbstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

52 citing papers in PubMed, 79 citations in OpenAlex.

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  10. Developing a Novel and Optimized Yeast Model for Human VDAC Research.International journal of molecular sciences · 2024
    Article
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  12. Redox regulation of UPR signalling and mitochondrial ER contact sites.Cellular and molecular life sciences : CMLS · 2024
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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

5 authors at 2 institutions in 2 countries.

Vito De PintoDepartment of Biomedicine and Biotechnology BIOMETEC, Section of Biology and Genetics, University of Catania, Italy; National Institute for Biomembranes and Biosystems, Section of Catania, Italy. Electronic address: vdpbiofa@unict.it.
Simona ReinaDepartment of Biomedicine and Biotechnology BIOMETEC, Section of Biology and Genetics, University of Catania, Italy; National Institute for Biomembranes and Biosystems, Section of Catania, Italy; Department of Biological, Geological and Environmental Sciences, Section of Molecular Biology, University of Catania, Italy.
Ankit GuptaMolecular Biophysics Laboratory, Department of Biological Sciences, Indian Institute of Science Education and Research, Bhopal, India.
Angela MessinaNational Institute for Biomembranes and Biosystems, Section of Catania, Italy; Department of Biological, Geological and Environmental Sciences, Section of Molecular Biology, University of Catania, Italy.
Radhakrishnan MahalakshmiMolecular Biophysics Laboratory, Department of Biological Sciences, Indian Institute of Science Education and Research, Bhopal, India.
University of Catania · ITIndian Institute of Science Education and Research, Bhopal · IN

Funding

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

Abstract

In this mini-review, we analyze the influence of cysteines in the structure and activity of mitochondrial outer membrane mammalian VDAC isoforms. The three VDAC isoforms show conserved sequences, similar structures and the same gene organization. The meaning of three proteins encoded in different chromosomes must thus be searched for subtle differences at the amino acid level. Among others, cysteine content is noticeable. In humans, VDAC1 has 2, VDAC2 has 9 and VDAC3 has 6 cysteines. Recent works have shown that, at variance from VDAC1, VDAC2 and VDAC3 exhibit cysteines predicted to protrude towards the intermembrane space, making them a preferred target for oxidation by ROS. Mass spectrometry in VDAC3 revealed that a disulfide bridge can be formed and other cysteine oxidations are also detectable. Both VDAC2 and VDAC3 cysteines were mutagenized to highlight their role in vitro and in complementation assays in Δporin1 yeast. Chemico-physical techniques revealed an important function of cysteines in the structural stabilization of the pore. In conclusion, the works available on VDAC cysteines support the notion that the three proteins are paralogs with a similar pore-function and slightly different, but important, ancillary biological functions. This article is part of a Special Issue entitled 'EBEC 2016: 19th European Bioenergetics Conference, Riva del Garda, Italy, July 2-6, 2016', edited by Prof. Paolo Bernardi.

Indexed as

AnimalsConserved SequenceCysteineEvolution, MolecularGene ExpressionHumansIon TransportMitochondriaMitochondrial MembranesMitochondrial Membrane Transport ProteinsModels, MolecularMutationProtein MultimerizationSaccharomyces cerevisiaeVoltage-Dependent Anion Channel 1Voltage-Dependent Anion Channel 2CysteineMitochondrial Membrane Transport ProteinsVDAC1 protein, humanVDAC2 protein, humanVDAC3 protein, humanVoltage-Dependent Anion Channel 1Voltage-Dependent Anion Channel 2Voltage-Dependent Anion Channels

Identifiers

PMID26947058
PMCPMC7115947
OpenAlexW2288973740

What OpenQuestion holds

Textmetadata
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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.