Evidence map›Paper›PMID 29483249›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2018

Effects of maturation on the conformational free-energy landscape of SOD1.

Robert M Culik, Ashok Sekhar, Jayashree Nagesh, Harmeen Deol, Jessica A O Rumfeldt, Elizabeth M Meiering, Lewis E Kay

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
5.4field-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

31 citing papers in PubMed, 67 citations in OpenAlex.

  1. Nose-to-brain delivery of a SOD1-stabilizing small molecule ameliorates pathology in an ALS mouse model.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2026
    Article
  2. Article
  3. Review
  4. Atomic resolution map of the solvent interactions driving SOD1 unfolding in CAPRIN1 condensates.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  5. Article
  6. Review
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  8. Probing excited stateMethods (San Diego, Calif.) · 2023
    Article
  9. Review
  10. Article
  11. Article
  12. 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

7 authors at 3 institutions in 1 country.

Robert M CulikDepartment of Molecular Genetics, University of Toronto, Toronto, ON M5S 1A8, Canada.
Ashok SekharDepartment of Molecular Genetics, University of Toronto, Toronto, ON M5S 1A8, Canada; ashok.sekhar@utoronto.ca kay@pound.med.utoronto.ca.
Jayashree NageshChemical Physics Theory Group, Department of Chemistry, University of Toronto, Toronto, ON M5S 3H6, Canada.
Harmeen DeolDepartment of Chemistry, University of Waterloo, Waterloo, ON N2L 3G1, Canada.
Jessica A O RumfeldtDepartment of Chemistry, University of Waterloo, Waterloo, ON N2L 3G1, Canada.
Elizabeth M MeieringDepartment of Chemistry, University of Waterloo, Waterloo, ON N2L 3G1, Canada.
Lewis E KayDepartment of Molecular Genetics, University of Toronto, Toronto, ON M5S 1A8, Canada; ashok.sekhar@utoronto.ca kay@pound.med.utoronto.ca.
University of Toronto · CAUniversity of Waterloo · CAHospital for Sick Children · CA

Funding

CIHR IRSC 0148000645
6 · The paper itself

Abstract

Amyotrophic lateral sclerosis (ALS) is a devastating fatal syndrome characterized by very rapid degeneration of motor neurons. A leading hypothesis is that ALS is caused by toxic protein misfolding and aggregation, as also occurs in many other neurodegenerative disorders, such as prion, Alzheimer's, Parkinson's, and Huntington's diseases. A prominent cause of familial ALS is mutations in the protein superoxide dismutase (SOD1), which promote the formation of misfolded SOD1 conformers that are prone to aberrant interactions both with each other and with other cellular components. We have shown previously that immature SOD1, lacking bound Cu and Zn metal ions and the intrasubunit disulfide bond (apoSOD1

Indexed as

Protein FoldingCopperDimerizationEntropyHumansOxidation-ReductionProtein ConformationSuperoxide Dismutase-1ZincCopperSuperoxide Dismutase-1ZincCESTCPMGexcited conformational statesNMRSOD1

Identifiers

PMID29483249
PMCPMC5856554
OpenAlexW2793974314

What OpenQuestion holds

Textmetadata
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.