ArticleProceedings of the National Academy of Sciences of the United States of America1996
Modulation of the chaperone-like activity of bovine alpha-crystallin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
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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.
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.
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Who cites it
15 citing papers in PubMed, 57 citations in OpenAlex.
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- Targeting the Hsp90 C-terminal domain to induce allosteric inhibition and selective client downregulation.Biochimica et biophysica acta. General subjects · 2017Article
- Study of conformational changes and protein aggregation of bovine serum albumin in presence of Sb(III) and Sb(V).PloS one · 2017Article
- Functional sequences in human alphaB crystallin.Biochimica et biophysica acta · 2016Review
- Lens Biology and Biochemistry.Progress in molecular biology and translational science · 2015Review
- Self-assembly of protein aggregates in ageing disorders: the lens and cataract model.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013Article
- Cholesterol-derived bile acids enhance the chaperone activity of α-crystallins.Cell stress & chaperones · 2011Article
- Lens aging: effects of crystallins.Biochimica et biophysica acta · 2009Review
- CP12 from Chlamydomonas reinhardtii, a permanent specific "chaperone-like" protein of glyceraldehyde-3-phosphate dehydrogenase.The Journal of biological chemistry · 2009Article
- Structural perturbation and enhancement of the chaperone-like activity of alpha-crystallin by arginine hydrochloride.Protein science : a publication of the Protein Society · 2003Article
- 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 · 1998Article
- Immunological detection of N-formylkynurenine in porphyrin-mediated photooxided lens α-crystallin.Photochemistry and photobiologyArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The effects of pantethine, glutathione, and selected chemical reagents on the anti-aggregation activity of alpha-crystallin was evaluated. Protein aggregation was monitored by light scattering of solutions of denatured beta L-crystallin or alcohol dehydrogenase (ADH). The ratios of beta L-crystallin/alpha-crystallin and ADH/alpha-crystallin were adjusted so that partial inhibition of protein aggregation at 60 degrees C or 37 degrees C, respectively, was observed and modulation of the chaperone action of alpha-crystallin could be evaluated easily with selected endogenous metabolites. Enhancement of the anti-aggregation activity in the beta L-crystallin assay was strongest with pantethine, which appeared to interact with alpha-crystallin. Enhancement of the anti-aggregation activity in the ADH assay was strongest with glutathione which appeared to interact with ADH. The results indicated that the products of common metabolic pathways can modulate the chaperone-like effects of alpha-crystallin on protein aggregation.
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Registered trials
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