Evidence map›Paper›PMID 20682279›Full record

ArticleArchives of biochemistry and biophysics2010

Aggregation modulating elements in mutant human superoxide dismutase 1.

Celeste M Karch, David R Borchelt

Open access · greenAbstract readComparative Study
In one paragraph

Article in Archives of biochemistry and biophysics, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.0field-weighted citation impact, top 14% 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

14 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
  2. AAV2/9-mediated overexpression of MIF inhibits SOD1 misfolding, delays disease onset, and extends survival in mouse models of ALS.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  3. Review
  4. Article
  5. Article
  6. Solid-state NMR studies of metal-free SOD1 fibrillar structures.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2014
    Article
  7. Article
  8. Article
  9. Article
  10. Fibrillation precursor of superoxide dismutase 1 revealed by gradual tuning of the protein-folding equilibrium.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
  11. Article
  12. Article
  13. Review
  14. Structures of mouse SOD1 and human/mouse SOD1 chimeras.Archives of biochemistry and biophysics · 2010
    Article
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 2 institutions in 1 country.

Celeste M KarchDepartment of Neuroscience, University of Florida, McKnight Brain Institute, Gainesville, 32610, USA. karchc@psychiatry.wustl.edu
David R Borchelt
Allen Institute for Brain Science · USUniversity of Florida · US

Funding

Testing Hypotheses by Site Directed Mutagenesis of SOD1P01NS049134 · NINDS · UNIVERSITY OF CALIFORNIA LOS ANGELES · PI WHITELEGGE, JULIAN P · 2005 to 2014
$10.9M
NINDS NIH HHS P01 NS049134
6 · The paper itself

Abstract

Mutations in superoxide dismutase 1 (SOD1) cause some forms of familial amyotrophic lateral sclerosis (fALS). Affected tissues of patients and transgenic mouse models of the disease accumulate misfolded and aggregated forms of the mutant protein. In the present study we have identified specific sequences in human SOD1 that modulate the aggregation of fALS mutant proteins. From our study of a panel of mutant proteins, we identify two sequence elements in human SOD1 (residues 42-50 and 109-123) that are critical in modulating the aggregation of the protein. These sequences are components of the 4th and 7th β-strands of the protein, and in the native structure are normally juxtaposed as elements of the core β-barrel. Our data suggest that some type of intermolecular interaction between these elements may occur in promoting mutant SOD1 aggregation.

Indexed as

Amino Acid SequenceAnimalsCell LineConserved SequenceHumansMiceMutationProtein FoldingProtein Structure, SecondarySuperoxide DismutaseSuperoxide Dismutase-1TransfectionSOD1 protein, humanSod1 protein, mouseSuperoxide DismutaseSuperoxide Dismutase-1

Identifiers

PMID20682279
PMCPMC2997613
OpenAlexW2017042451

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.