Evidence map›Paper›PMID 25084457›Full record

ArticlePloS one2014

Charged residues distribution modulates selectivity of the open state of human isoforms of the voltage dependent anion-selective channel.

Giuseppe Federico Amodeo, Mariano Andrea Scorciapino, Angela Messina, Vito De Pinto, Matteo Ceccarelli

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

25 citing papers in PubMed, 51 citations in OpenAlex.

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  19. Role of cysteines in mammalian VDAC isoforms' function.Biochimica et biophysica acta · 2016
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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 3 institutions in 1 country.

Giuseppe Federico AmodeoDepartment of Chemical and Geological Science, University of Cagliari, Cagliari, Italy.
Mariano Andrea ScorciapinoDepartment of Physics, University of Cagliari, Cagliari, Italy; Istituto Officina dei Materiali, Consiglio Nazionale delle Ricerche, Cagliari, Italy.
Angela MessinaDepartment of Biological, Geological and Environmental Sciences, Section of Molecular Biology, University of Catania, Catania, Italy; National Institute for Biomembranes and Biosystems, Catania, Italy.
Vito De PintoDepartment of Biological, Geological and Environmental Sciences, Section of Molecular Biology, University of Catania, Catania, Italy; National Institute for Biomembranes and Biosystems, Catania, Italy.
Matteo CeccarelliDepartment of Physics, University of Cagliari, Cagliari, Italy; Istituto Officina dei Materiali, Consiglio Nazionale delle Ricerche, Cagliari, Italy.
University of Cagliari · ITUniversity of Catania · ITIstituto Officina dei Materiali · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Voltage Dependent Anion-selective Channels (VDACs) are pore-forming proteins located in the outer mitochondrial membrane. They are responsible for the access of ions and energetic metabolites into the inner membrane transport systems. Three VDAC isoforms exist in mammalian, but their specific role is unknown. In this work we have performed extensive (overall ∼5 µs) Molecular Dynamics (MD) simulations of the human VDAC isoforms to detect structural and conformational variations among them, possibly related to specific functional roles of these proteins. Secondary structure analysis of the N-terminal domain shows a high similarity among the three human isoforms of VDAC but with a different plasticity. In particular, the N-terminal domain of the hVDAC1 is characterized by a higher plasticity, with a ∼20% occurrence for the 'unstructured' conformation throughout the folded segment, while hVDAC2, containing a peculiar extension of 11 amino acids at the N-terminal end, presents an additional 310-helical folded portion comprising residues 10' to 3, adhering to the barrel wall. The N-terminal sequences of hVDAC isoforms are predicted to have a low flexibility, with possible consequences in the dynamics of the human VDACs. Clear differences were found between hVDAC1 and hVDAC3 against hVDAC2: a significantly modified dynamics with possible important consequence on the voltage-gating mechanism. Charge distribution inside and at the mouth of the pore is responsible for a different preferential localization of ions with opposite charge and provide a valuable rationale for hVDAC1 and hVDAC3 having a Cl-/K+ selectivity ratio of 1.8, whereas hVDAC2 of 1.4. Our conclusion is that hVDAC isoforms, despite sharing a similar scaffold, have modified working features and a biological work is now requested to give evidence to the described dissimilarities.

Indexed as

Amino Acid SequenceHumansMitochondrial Membrane Transport ProteinsMolecular Dynamics SimulationMolecular Sequence DataProtein IsoformsSequence Homology, Amino AcidVoltage-Dependent Anion Channel 1Voltage-Dependent Anion ChannelsMitochondrial Membrane Transport ProteinsProtein IsoformsVDAC1 protein, humanVDAC3 protein, humanVoltage-Dependent Anion Channel 1Voltage-Dependent Anion Channels

Identifiers

PMID25084457
PMCPMC4146382
OpenAlexW1980090229

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.