Evidence map›Paper›PMID 22955287›Full record

ArticleThe Journal of biological chemistry2012

Chaperone activity of small heat shock proteins underlies therapeutic efficacy in experimental autoimmune encephalomyelitis.

Michael P Kurnellas, Sara E Brownell, Leon Su, Andrey V Malkovskiy, Jayakumar Rajadas, Gregory Dolganov, Sidharth Chopra, Gary K Schoolnik, Raymond A Sobel, Jonathan Webster and 4 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
3.2field-weighted citation impact, top 7% 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

36 citing papers in PubMed, 56 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Small Heat Shock Proteins in Retinal Diseases.Frontiers in molecular biosciences · 2022
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Identification of a common immune regulatory pathway induced by small heat shock proteins, amyloid fibrils, and nicotine.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
  19. Article
  20. Review
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

14 authors at 1 institution in 1 country.

Michael P KurnellasDepartment Neurology and Neurological Sciences, Stanford University School of Medicine, Stanford, California 94305-5316, USA.
Sara E Brownell
Leon Su
Andrey V Malkovskiy
Jayakumar Rajadas
Gregory Dolganov
Sidharth Chopra
Gary K Schoolnik
Raymond A Sobel
Jonathan Webster
Shalina S Ousman
Rachel A Becker
Lawrence Steinman
Jonathan B Rothbard
Stanford University · US

Funding

MOLECULAR &CELLULAR IMMUNOBIOLOGYT32AI007290 · NIAID · STANFORD UNIVERSITY · PI Sean Curtis Bendall, Olivia M Martinez · 1985 to 2026
$27.0M
Immunoregulation of AutoimmunityU01DK078123 · NIDDK · STANFORD UNIVERSITY · PI FATHMAN, CHARLES GARRISON · 2006 to 2011
$1.9M
The Generation and Maintenance of Human Memory B Cells Z01AI000949 · NIAID · NIAID EXTRAMURAL ACTIVITIES · PI PIERCE, SUSAN · 2004 to 2008
$1.8M
Autoantibody Arrays Guide Tolergenic Therapy for Multiple SclerosisR01NS055997 · NINDS · STANFORD UNIVERSITY · PI STEINMAN, LAWRENCE · 2008 to 2012
$1.6M
Intramural NIH HHS Z01 AI000949NIAID NIH HHS 1R43 AI0949NIAID NIH HHS T32 AI007290NIDDK NIH HHS U01 DK078123NIDDK NIH HHS UO1 DK078123NINDS NIH HHS R01 NS055997NINDS NIH HHS R01NS55997
6 · The paper itself

Abstract

To determine whether the therapeutic activity of αB crystallin, small heat shock protein B5 (HspB5), was shared with other human sHsps, a set of seven human family members, a mutant of HspB5 G120 known to exhibit reduced chaperone activity, and a mycobacterial sHsp were expressed and purified from bacteria. Each of the recombinant proteins was shown to be a functional chaperone, capable of inhibiting aggregation of denatured insulin with varying efficiency. When injected into mice at the peak of disease, they were all effective in reducing the paralysis in experimental autoimmune encephalomyelitis. Additional structure activity correlations between chaperone activity and therapeutic function were established when linear regions within HspB5 were examined. A single region, corresponding to residues 73-92 of HspB5, forms amyloid fibrils, exhibited chaperone activity, and was an effective therapeutic for encephalomyelitis. The linkage of the three activities was further established by demonstrating individual substitutions of critical hydrophobic amino acids in the peptide resulted in the loss of all of the functions.

Indexed as

alpha-Crystallin B ChainAmino Acid SubstitutionAnimalsEncephalomyelitis, Autoimmune, ExperimentalFemaleHumansMiceMutation, MissenseParalysisalpha-Crystallin B ChainCRYAB protein, human

Identifiers

PMID22955287
PMCPMC3476308
OpenAlexW2052603766

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.