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Study of posttranslational modifications in lenticular αA-Crystallin of mice using proteomic analysis techniques

  • Published:2006-12 Issue:12 Volume:1764 Page:1948-1962
  • ISSN:1570-9639
  • Container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics
  • language:en
  • Short-container-title:Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics

Author:

Schaefer Heike,Chamrad Daniel C.,Herrmann Marion,Stuwe Janine,Becker Gabriele,Klose Joachim,Blueggel Martin,Meyer Helmut E.,Marcus Katrin

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics,Analytical Chemistry

Reference58 articles.

1. Eye-lens proteins: structure, superstructure, stability, genetics;Jaenicke;Naturwissenschaften,1994

2. Alpha-crystallin as a molecular chaperone;Derham;Prog. Retinal Eye Res.,1999

3. Alpha-crystallin can function as a molecular chaperone;Horwitz;Proc. Natl. Acad. Sci. U. S. A.,1992

4. Alpha A- and alpha B-crystallin in the retina. Association with the post-Golgi compartment of frog retinal photoreceptors;Deretic;J. Biol. Chem.,1994

5. Release of alpha-A sequence 158–173 correlates with a decrease in the molecular chaperone properties of native alpha-crystallin;Takemoto;Exp. Eye Res.,1994

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