ArticleJournal of protein chemistry2000
Dissociation of human alphaB-crystallin aggregates by thiocyanate is structurally and functionally reversible.
Article in Journal of protein chemistry, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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.
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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
3 citing papers in PubMed, 5 citations in OpenAlex.
- Effectiveness of TRIzol in Inactivating Animal Pathogens.Applied biosafety : journal of the American Biological Safety Association · 2023Review
- Nitration and Glycation Turn Mature NGF into a Toxic Factor for Motor Neurons: A Role for p75Antioxidants & redox signaling · 2018Article
- Characterization of non-covalent oligomers of proteins treated with hypochlorous acid.The Biochemical journal · 2003Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Conformational modifications and changes in the aggregation state of human alphaB-crystallin were investigated at different concentrations of SDS, KBr, urea, and NH4SCN and at different temperatures. Intrinsic fluorescence measurements indicated complete and reversible unfolding of the protein at 2 M NH4SCN, whereas the concentration of urea required for complete and irreversible unfolding was 6 M. Gel permeation chromatography indicated almost complete dissociation of the micelle-like aggregate of alphaB-crystallin in 2 M NH4SCN, but only partial dissociation into large-sized aggregates in 6 M urea. Thiocyanate-treated alphaB-crystallin recovered its chaperone-like activity upon dilution of the dissociating agent, whereas the urea-treated protein did not.
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Registered trials
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