On the structure of alpha m-crystallin. The reversibility of urea dissociation.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference37 articles.
1. The Quaternary Structure of Bovine alpha-Crystallin. Size and Charge Microheterogeneity: More than 1000 Different Hybrids?
2. Intracellular Degradation and Deamidation of alpha-Crystallin Subunits
3. αm-Crystallin: the native form of the protein?
4. Splitting and recombination of α-crystallin
5. Studies on the subunits of α-crystallin and their recombination
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1. Conserved Activity of Reassociated Homotetrameric Protein Subunits Released from Mesoporous Silica Nanoparticles;Langmuir;2017-12-28
2. Unfolding and Refolding of Bovine α-Crystallin in Urea and Its Chaperone Activity;The Protein Journal;2007-05-15
3. The necessity of functional proteomics: protein species and molecular function elucidation exemplified by in vivo alpha A crystallin N-terminal truncation;Amino Acids;2006-09-15
4. Dissociation is not required for α-crystallin's chaperone function;Experimental Eye Research;2004-12
5. α‐crystallin: a review of its structure and function;Clinical and Experimental Optometry;2004-11-01
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