Evidence map›Paper›PMID 9448275›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1998

ATP-enhanced molecular chaperone functions of the small heat shock protein human alphaB crystallin.

P J Muchowski, J I Clark

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
4.4field-weighted citation impact, top 5% 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

34 citing papers in PubMed, 142 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Novel roles for α-crystallins in retinal function and disease.Progress in retinal and eye research · 2012
    Review
  11. Myofibrillar myopathies.Neuromuscular disorders : NMD · 2011
    Review
  12. Article
  13. Article
  14. Lens aging: effects of crystallins.Biochimica et biophysica acta · 2009
    Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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 1 institution in 1 country.

P J MuchowskiDepartment of Biological Structure, Box 357420, University of Washington, Seattle, WA, 98195-7420, USA.
J I Clark
University of Washington · US

Funding

DEVELOPMENT AND MAINTENANCE OF TRANSPARENCY IN LENSESR01EY004542 · NEI · UNIVERSITY OF WASHINGTON · PI CLARK, JOHN IRWIN · 1985 to 2013
$7.1M
Intramural NIH HHS Z01 EY000452NEI NIH HHS EY07031NEI NIH HHS R01 EY004542
6 · The paper itself

Abstract

We report direct experimental evidence that human alphaB-crystallin, a member of the small heat shock protein family, actively participates in the refolding of citrate synthase (CS) in vitro. In the presence of 3.5 mM ATP, CS reactivation by alphaB-crystallin was enhanced approximately twofold. Similarly, 3.5 mM ATP enhanced the chaperone activity of alphaB-crystallin on the unfolding and aggregation of CS at 45 degrees C. Consistent with these findings, cell viability at 50 degrees C was improved nearly five orders of magnitude in Escherichia coli expressing alphaB-crystallin. SDS/PAGE analysis of cell lysates suggested that alphaB-crystallin protects cells against physiological stress in vivo by maintaining cytosolic proteins in their native and functional conformations. This report confirms the action of alphaB-crystallin as a molecular chaperone both in vitro and in vivo and describes the enhancement of alphaB-crystallin chaperone functions by ATP.

Indexed as

Escherichia coli ProteinsProtein FoldingAdenosine TriphosphateCell SurvivalChaperonin 60Citrate (si)-SynthaseCrystallinsEnzyme ActivationHeat-Shock ProteinsHSP70 Heat-Shock ProteinsHumansMolecular ChaperonesProtein ConformationSpectrometry, FluorescenceAdenosine TriphosphateChaperonin 60Citrate (si)-SynthaseCrystallinsdnaK protein, E coliEscherichia coli ProteinsHeat-Shock ProteinsHSP70 Heat-Shock ProteinsMolecular Chaperones

Identifiers

PMID9448275
PMCPMC18652
OpenAlexW1978545193

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.