An investigation into the stability of α-crystallin by NMR spectroscopy; evidence for a two-domain structure
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics,Structural Biology
Reference27 articles.
1. The effects of isolation buffers on the properties of α-crystallin
2. Definition and comparison of the phosphorylation sites of the A and B chains of bovine α-crystallin
3. The molecular structure and stability of the eye lens: X-ray analysis of γ-crystallin II
4. X-ray analysis of βB2-crystallin and evolution of oligomeric lens proteins
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3. Quantitative NMR study of heat-induced aggregation of eye-lens crystallin proteins under crowding conditions;Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics;2018-10
4. The functional roles of the unstructured N- and C-terminal regions in αB-crystallin and other mammalian small heat-shock proteins;Cell Stress and Chaperones;2017-04-08
5. Multidimensional significance of crystallin protein–protein interactions and their implications in various human diseases;Biochimica et Biophysica Acta (BBA) - General Subjects;2016-01
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