Cleavage from the N-terminal region of βBp crystallin during aging of the human lens
Author:
Publisher
Elsevier BV
Subject
Cellular and Molecular Neuroscience,Sensory Systems,Ophthalmology
Reference17 articles.
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2. A rapid and sensitive method of quantitation of microgram quantities of protein utilizing the principle of protein-dye binding;Bradford;Anal. Biochem.,1976
3. The β-crystallin Bp chain is internally duplicated and homologous with γ-crystallin;Driessen;Exp. Eye Res.,1980
4. India ink staining of proteins on nitrocellulose paper;Hancock;Anal. Biochem.,1983
5. Monoclonal antiserum to gamma crystallin: characterization and use as a probe of changes in the aging human lens;Hansen;Lens Res.,1984
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1. N-Terminal Extension of βB1-Crystallin: Identification of a Critical Region That Modulates Protein Interaction with βA3-Crystallin;Biochemistry;2009-09-21
2. Solution conformation of bovine lens α-and βB2-crystallin terminal extensions;International Journal of Peptide and Protein Research;2009-01-12
3. Truncation of Motifs III and IV in Human Lens βA3-Crystallin Destabilizes the Structure;Biochemistry;2006-07-29
4. Energetics of Domain−Domain Interactions and Entropy Driven Association of β-Crystallins;Biochemistry;2003-12-18
5. βB2-crystallin undergoes extensive truncation during aging in human lenses;Biochemical and Biophysical Research Communications;2003-01
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