Resistance of Human βB2-crystallin to in vivo Modification

Author:

Zhang Zhongli,David Larry L,Smith David L,Smith Jean B

Publisher

Elsevier BV

Subject

Cellular and Molecular Neuroscience,Sensory Systems,Ophthalmology

Reference37 articles.

1. Characterization of low molecular mass γ-crystallin fragments from human lenses;Abbasi;Exp. Eye Res.,1998

2. Size of human lens β-crystallin aggregates are distinguished by N-terminal truncation of βB1;Ajaz;J. Biol. Chem.,1997

3. Structural studies on βH-crystallin from bovine eye lens;Bateman;Exp. Eye Res.,1992

4. Identification of proteins by matrix-assisted laser desorption/ionization mass spectrometry using peptide and fragment ion masses;Courchesna,1999

5. The sequence of human βB1-crystallin cDNA allows mass spectrometric detection of βB1 protein missing portions of its N-terminal extension;David;J. Biol. Chem.,1996

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