Effect of aging on the chaperone-like function of human α-crystallin assessed by three methods
- 15 December 1997
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 328 (3) , 763-768
- https://doi.org/10.1042/bj3280763
Abstract
No abstract availableKeywords
This publication has 37 references indexed in Scilit:
- Role of the Maillard Reaction in Diabetes Mellitus and Diseases of AgingDrugs & Aging, 1996
- Glycation-induced inactivation of malate dehydrogenase protection by aspirin and a lens molecular chaperone, α-crystallinBiochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, 1996
- The small heat-shock protein αB-crystallin as candidate autoantigen in multiple sclerosisNature, 1995
- Decreased Molecular Chaperone Property of α-Crystallins Due to Posttranslational ModificationsBiochemical and Biophysical Research Communications, 1995
- Comparison of the homologous carboxy-terminal domain and tail of α-crystallin and small heat shock proteinMolecular Biology Reports, 1993
- Rapid separation of bovine β-crystallin subunits βB1, βB2, βB3, βA3 and βA4Experimental Eye Research, 1990
- Non-enzymic post-translational modification of proteins in aging. A reviewMechanisms of Ageing and Development, 1989
- αB-crystallin is expressed in non-lenticular tissues and accumulates in Alexander's disease brainCell, 1989
- αB subunit of lens-specific protein α-crystallin is present in other ocular and non-ocular tissuesBiochemical and Biophysical Research Communications, 1989
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970