Chaperone-like Activity of Bovine Lens α-Crystallin in the Presence of Dithiothreitol-Destabilized Proteins: Characterization of the Formed Complexes
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference18 articles.
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2. Structure and modifications of the junior chaperone α-crystallin. From lens transparency to molecular pathology;Groenen;Eur. J. Biochem.,1994
3. A possible structure for α-crystallin;Augusteyn;FEBS Lett.,1987
4. Micellar subunit assembly in a three-layer model of oligomeric α-crystallin;Walsh;J. Biol. Chem.,1991
5. A possible chaperone-like quaternary structure for α-crystallin;Carver;Exp. Eye Res.,1994
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1. The mechanism for thermal-enhanced chaperone-like activity of α-crystallin against UV irradiation-induced aggregation of γD-crystallin;Biophysical Journal;2022-06
2. Structure and function of α-crystallins: Traversing from in vitro to in vivo;Biochimica et Biophysica Acta (BBA) - General Subjects;2016-01
3. Quantification of anti-aggregation activity of UV-irradiated α-crystallin;International Journal of Biological Macromolecules;2015-02
4. Quantification of Anti-Aggregation Activity of Chaperones: A Test-System Based on Dithiothreitol-Induced Aggregation of Bovine Serum Albumin;PLoS ONE;2013-09-10
5. Chaperone-independent mitochondrial translocation and protection by alpha B-crystallin in RPE cells;EXP EYE RES;2013
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