The Role of α- and ε-Amino Groups in the Glycation-mediated Cross-linking of γB-crystallin
Open Access
- 1 May 1997
- journal article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 272 (22) , 14465-14469
- https://doi.org/10.1074/jbc.272.22.14465
Abstract
No abstract availableKeywords
This publication has 32 references indexed in Scilit:
- Role of Glycine 1 and Lysine 2 in the Glycation of Bovine γB-CrystallinPublished by Elsevier ,1995
- N.epsilon.-(Carboxymethyl)lysine Is a Dominant Advanced Glycation End Product (AGE) Antigen in Tissue ProteinsBiochemistry, 1995
- Glycation of lens proteins by the oxidation products of ascorbic acidBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1990
- Site-directed mutagenesis by overlap extension using the polymerase chain reactionGene, 1989
- Advanced Glycosylation End Products in Tissue and the Biochemical Basis of Diabetic ComplicationsNew England Journal of Medicine, 1988
- cDNA Clones encoding bovine γ-crystallinsBiochemical and Biophysical Research Communications, 1987
- Superior resolution of γ-crystallins from microdissected eye lens by cation-exchange high-performance liquid chromatographyBiochemical and Biophysical Research Communications, 1985
- Accumulation of diabetic rat peripheral nerve myelin by macrophages increases with the presence of advanced glycosylation endproducts.The Journal of Experimental Medicine, 1984
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970
- Biochemistry of bovine lens proteins II. The γ-crystallins of adult bovine, calf and embryonic lensesBiochimica et Biophysica Acta (BBA) - General Subjects, 1965