Evidence map›Paper›PMID 33465527›Full record

ReviewCurrent opinion in structural biology2021

SOD1 oligomers in amyotrophic lateral sclerosis.

Esther S Choi, Nikolay V Dokholyan

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in structural biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.6field-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

21 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
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  14. Big versus small: The impact of aggregate size in disease.Protein science : a publication of the Protein Society · 2023
    Review
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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.

Esther S ChoiDepartment of Pharmacology, Penn State College of Medicine, Hershey, PA, USA; Medical Scientist Training Program, Penn State College of Medicine, Hershey, PA, USA. Electronic address: euc504@psu.edu.
Nikolay V DokholyanDepartment of Pharmacology, Penn State College of Medicine, Hershey, PA, USA; Department of Biochemistry and Molecular Biology, Penn State College of Medicine, Hershey, PA, USA. Electronic address: nxd338@psu.edu.
Penn State Milton S. Hershey Medical Center · US

Funding

Penn State Clinical and Translational Science InstituteUL1TR002014 · NCATS · PENNSYLVANIA STATE UNIV HERSHEY MED CTR · PI KRASCHNEWSKI, JENNIFER L. · 2016 to 2025
$33.7M
Nanoscale programming of cellular and physiological phenotypes: EquipmentR35GM134864 · NIGMS · UNIVERSITY OF VIRGINIA · PI Nikolay Dokholyan · 2020 to 2026
$5.2M
NCATS NIH HHS UL1 TR002014NIGMS NIH HHS R35 GM134864
6 · The paper itself

Abstract

Identifying nonnative, trimeric forms of SOD1 trimers as the toxic species, rather than large aggregates revolutionizes our understanding of ALS pathophysiology. Large protein aggregates, what was previously thought as the central cause of neurodegeneration, play protective role and are not responsible for neuronal death. SOD1 trimers are implicated at the molecular, cellular, and organismal level. Understanding the formation of the nonnative trimer and its role in the cell, leading to cell death, holds the key to developing a new standard of therapeutics for ALS and for other neurodegenerative diseases. This review highlights recent advances of knowledge for the role of SOD1 oligomers in ALS.

Indexed as

Amyotrophic Lateral SclerosisHumansMutationSuperoxide Dismutase-1SOD1 protein, humanSuperoxide Dismutase-1

Identifiers

PMID33465527
PMCPMC7965251
OpenAlexW3124955744

What OpenQuestion holds

Textmetadata
LicenceTDM
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.