Isolation and characterization of β- and γ-crystallin genes from rat genomic cosmid libraries
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This publication has 17 references indexed in Scilit:
- Homology between the primary structures of the major bovine β‐crystallin chainsEuropean Journal of Biochemistry, 1984
- Strict co-linearity of genetic and protein folding domains in an intragenically duplicated rat lens γ-crystallin geneJournal of Molecular Biology, 1983
- Gene and protein structure of a β-crystallin polypeptide in murine lens: relationship of exons and structural motifsNature, 1983
- Classification of Rat Lens Crystallins and Identification of Proteins Encoded by Rat Lens mRNAEuropean Journal of Biochemistry, 1982
- Primary Structure of the Bovine β‐Crystallin Bp ChainEuropean Journal of Biochemistry, 1981
- Eye‐lens proteins: The three‐dimensional structure of β‐crystallin predicted from monomeric γ‐crystallinFEBS Letters, 1981
- Isolation of β-globin-related genes from a human cosmid libraryGene, 1981
- The β-crystallin bp chain is internally duplicated and homologous with γ-crystallinExperimental Eye Research, 1980
- Primary Structures of the alpha-Crystallin A Chains of Seven Mammalian SpeciesEuropean Journal of Biochemistry, 1975
- The Amino‐Acid Sequence of the αB2 Chain of Bovine α‐CrystallinEuropean Journal of Biochemistry, 1974