Evidence map›Paper›PMID 36077343›Full record

ArticleInternational journal of molecular sciences2022

Targeting the Mitochondrial Protein VDAC1 as a Potential Therapeutic Strategy in ALS.

Anna Shteinfer-Kuzmine, Shirel Argueti-Ostrovsky, Marcel F Leyton-Jaimes, Uttpal Anand, Salah Abu-Hamad, Ran Zalk, Varda Shoshan-Barmatz, Adrian Israelson

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.3field-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

20 citing papers in PubMed, 29 citations in OpenAlex.

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  12. Targeting mitochondrial CaThe Journal of physiology · 2024
    Review
  13. Article
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  16. Article
  17. VDAC as a Cellular Hub: Docking Molecules and Interactions.International journal of molecular sciences · 2023
    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

8 authors at 1 institution in 2 countries.

Anna Shteinfer-KuzmineDepartment of Life Sciences and the National Institute for Biotechnology in the Negev, Ben-Gurion University of the Negev, Beer-Sheva 84105, Israel.
Shirel Argueti-OstrovskyDepartment of Physiology and Cell Biology, Faculty of Health Sciences and The Zlotowski Center for Neuroscience, Ben-Gurion University of the Negev, Beer-Sheva 84105, Israel.
Marcel F Leyton-JaimesDepartment of Physiology and Cell Biology, Faculty of Health Sciences and The Zlotowski Center for Neuroscience, Ben-Gurion University of the Negev, Beer-Sheva 84105, Israel.
Uttpal AnandDepartment of Life Sciences and the National Institute for Biotechnology in the Negev, Ben-Gurion University of the Negev, Beer-Sheva 84105, Israel.ORCID 0000-0001-5924-7866
Salah Abu-HamadDepartment of Physiology and Cell Biology, Faculty of Health Sciences and The Zlotowski Center for Neuroscience, Ben-Gurion University of the Negev, Beer-Sheva 84105, Israel.
Ran ZalkIlse Katz Institute for Nanoscale Science & Technology, Ben-Gurion University of the Negev, Beer-Sheva 84105, Israel.ORCID 0000-0003-4251-6497
Varda Shoshan-BarmatzDepartment of Life Sciences and the National Institute for Biotechnology in the Negev, Ben-Gurion University of the Negev, Beer-Sheva 84105, Israel.ORCID 0000-0002-6756-4340
Adrian IsraelsonDepartment of Physiology and Cell Biology, Faculty of Health Sciences and The Zlotowski Center for Neuroscience, Ben-Gurion University of the Negev, Beer-Sheva 84105, Israel.ORCID 0000-0002-8289-7653
Ben-Gurion University of the Negev · IL

Funding

Israel Science Foundation 284/19Israel Science Foundation 974/19
6 · The paper itself

Abstract

Impaired mitochondrial function has been proposed as a causative factor in neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS), caused by motor neuron degeneration. Mutations in superoxide dismutase (SOD1) cause ALS and SOD1 mutants were shown to interact with the voltage-dependent anion channel 1 (VDAC1), affecting its normal function. VDAC1 is a multi-functional channel located at the outer mitochondrial membrane that serves as a mitochondrial gatekeeper controlling metabolic and energetic crosstalk between mitochondria and the rest of the cell and it is a key player in mitochondria-mediated apoptosis. Previously, we showed that VDAC1 interacts with SOD1 and that the VDAC1-N-terminal-derived peptide prevented mutant SOD1 cytotoxic effects. In this study, using a peptide array, we identified the SOD1 sequence that interacts with VDAC1. Synthetic peptides generated from the identified VDAC1-binding sequences in SOD1 directly interacted with purified VDAC1. We also show that VDAC1 oligomerization increased in spinal cord mitochondria isolated from mutant SOD1

Indexed as

Amyotrophic Lateral SclerosisAnimalsDisease Models, AnimalMiceMice, TransgenicMitochondrial ProteinsRatsSuperoxide DismutaseSuperoxide Dismutase-1Voltage-Dependent Anion Channel 1Mitochondrial ProteinsSuperoxide DismutaseSuperoxide Dismutase-1Vdac1 protein, ratVoltage-Dependent Anion Channel 1ALSapoptosismisfolded proteinsmitochondriamutant SOD1VDAC1

Identifiers

PMID36077343
PMCPMC9456491
OpenAlexW4294151721

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.