Evidence map›Paper›PMID 8159713›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America1994

Alpha-crystallin/small heat shock protein has autokinase activity.

M Kantorow, J Piatigorsky

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
4.7field-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

22 citing papers in PubMed, 136 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Lens Biology and Biochemistry.Progress in molecular biology and translational science · 2015
    Review
  5. Article
  6. Article
  7. Article
  8. Novel roles for α-crystallins in retinal function and disease.Progress in retinal and eye research · 2012
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. The genetics of cataract: our vision becomes clearer.American journal of human genetics · 1998
    Article
  16. ATP-enhanced molecular chaperone functions of the small heat shock protein human alphaB crystallin.Proceedings of the National Academy of Sciences of the United States of America · 1998
    Article
  17. Article
  18. Ceramide formation during heat shock: a potential mediator of alpha B-crystallin transcription.Proceedings of the National Academy of Sciences of the United States of America · 1995
    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.

M KantorowLaboratory of Molecular and Developmental Biology, National Eye Institute, National Institutes of Health, Bethesda, MD 20892.
J Piatigorsky
National Eye Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The alpha-crystallins (alpha A and alpha B) are major water-soluble proteins of the transparent eye lens that are expressed in a variety of tissues and can function as molecular chaperones. alpha B-crystallin is also a small heat shock protein associated with numerous degenerative diseases and abnormal growth patterns. Previous experiments have shown that alpha A-and alpha B-crystallin are phosphorylated on specific serine residues by a cAMP-dependent pathway. Here we provide evidence that either total bovine alpha-crystallin or its isolated polypeptides can autophosphorylate serine by a cAMP-independent mechanism in the presence of Mg2+ and [gamma-32P]ATP; the autophosphorylated products isoelectrically focus with the authentic phosphorylated forms of the alpha-crystallin polypeptides. Thus, the alpha A- and alpha B-crystallin/small heat shock protein polypeptides are enzyme-crystallins which may be involved in metabolic pathways important for the development, maintenance, or pathology of the lens and other tissues.

Indexed as

AnimalsCattleCrystallinsCyclic AMPHeat-Shock ProteinsIsoelectric PointLens, CrystallinePhosphorylationPhosphoserineProtein Serine-Threonine KinasesCrystallinsCyclic AMPHeat-Shock ProteinsPhosphoserineProtein Serine-Threonine Kinases

Identifiers

PMID8159713
PMCPMC43525
OpenAlexW2086352454

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.