Rat lens β-crystallins are internally duplicated and homologous to γ-crystallins
Author:
Publisher
Elsevier BV
Subject
Genetics,Biochemistry,Biophysics,Structural Biology
Reference30 articles.
1. Short-range order of crystallin proteins accounts for eye lens transparency
2. Deficiency of Functional Messenger RNA for a Developmentally Regulated β-Crystallin Polypeptide in a Hereditary Cataract
3. Lens Protein
4. Lens Differentiation in Vertebrates
5. Primary Structure of the Bovine beta-Crystallin Bp Chain. Internal Duplication and Homology with gamma-Crystallin
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1. Calcium-binding to lens βB2- and βA3-crystallins suggests that all β-crystallins are calcium-binding proteins;FEBS Journal;2007-07-25
2. Age-Related Degradation of βA3/A1-Crystallin in Human Lenses;Biochemical and Biophysical Research Communications;1999-05
3. Gene Expression of the Proteasome in Rat Lens Development;Experimental Eye Research;1998-03
4. The Sequence of Human βB1-Crystallin cDNA Allows Mass Spectrometric Detection of βB1 Protein Missing Portions of Its N-terminal Extension;Journal of Biological Chemistry;1996-02
5. Assignment of the βB1 Crystallin Gene (CRYBB1) to Human Chromosome 22 and Mouse Chromosome 5;Genomics;1995-10
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