Evidence map›Paper›PMID 31474832›Full record

ArticleFrontiers in cellular neuroscience2019

A VDAC1-Derived N-Terminal Peptide Inhibits Mutant SOD1-VDAC1 Interactions and Toxicity in the SOD1 Model of ALS.

Anna Shteinfer-Kuzmine, Shirel Argueti, Rajeev Gupta, Neta Shvil, Salah Abu-Hamad, Yael Gropper, Jan Hoeber, Andrea Magrì, Angela Messina, Elena N Kozlova and 2 more

Open access · goldAbstract read
In one paragraph

Article in Frontiers in cellular neuroscience, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing 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

29 citing papers in PubMed, 39 citations in OpenAlex.

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  11. Apoptotic proteins with non-apoptotic activity: expression and function in cancer.Apoptosis : an international journal on programmed cell death · 2023
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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

12 authors at 3 institutions in 3 countries.

Anna Shteinfer-KuzmineDepartment of Life Sciences, The National Institute for Biotechnology in the Negev, Ben-Gurion University of the Negev, Beersheba, Israel.
Shirel ArguetiDepartment of Physiology and Cell Biology, Faculty of Health Sciences, The Zlotowski Center for Neuroscience, Ben-Gurion University of the Negev, Beersheba, Israel.
Rajeev GuptaDepartment of Life Sciences, The National Institute for Biotechnology in the Negev, Ben-Gurion University of the Negev, Beersheba, Israel.
Neta ShvilDepartment of Physiology and Cell Biology, Faculty of Health Sciences, The Zlotowski Center for Neuroscience, Ben-Gurion University of the Negev, Beersheba, Israel.
Salah Abu-HamadDepartment of Physiology and Cell Biology, Faculty of Health Sciences, The Zlotowski Center for Neuroscience, Ben-Gurion University of the Negev, Beersheba, Israel.
Yael GropperDepartment of Physiology and Cell Biology, Faculty of Health Sciences, The Zlotowski Center for Neuroscience, Ben-Gurion University of the Negev, Beersheba, Israel.
Jan HoeberDepartment of Neuroscience, Uppsala University, Uppsala, Sweden.
Andrea MagrìDepartment of Biological, Geological and Environmental Sciences, University of Catania, Catania, Italy.
Angela MessinaDepartment of Biological, Geological and Environmental Sciences, University of Catania, Catania, Italy.
Elena N KozlovaDepartment of Neuroscience, Uppsala University, Uppsala, Sweden.
Varda Shoshan-BarmatzDepartment of Life Sciences, The National Institute for Biotechnology in the Negev, Ben-Gurion University of the Negev, Beersheba, Israel.
Adrian IsraelsonDepartment of Physiology and Cell Biology, Faculty of Health Sciences, The Zlotowski Center for Neuroscience, Ben-Gurion University of the Negev, Beersheba, Israel.
Ben-Gurion University of the Negev · ILUniversity of Catania · ITUppsala University · SE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mutations in superoxide dismutase (SOD1) are the second most common cause of familial amyotrophic lateral sclerosis (ALS), a fatal neurodegenerative disease caused by the death of motor neurons in the brain and spinal cord. SOD1 neurotoxicity has been attributed to aberrant accumulation of misfolded SOD1, which in its soluble form binds to intracellular organelles, such as mitochondria and ER, disrupting their functions. Here, we demonstrate that mutant SOD1 binds specifically to the N-terminal domain of the voltage-dependent anion channel (VDAC1), an outer mitochondrial membrane protein controlling cell energy, metabolic and survival pathways. Mutant SOD1

Indexed as

ALSmisfolded SOD1mutant SOD1N-terminal peptideVDAC1

Identifiers

PMID31474832
PMCPMC6702328
OpenAlexW2957531246

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.