Molecular Chaperones Protect Against Glycation-Induced Inactivation of Glucose-6-Phosphate Dehydrogenase
- 1 July 1995
- journal article
- Published by Wiley in European Journal of Biochemistry
- Vol. 231 (1) , 181-185
- https://doi.org/10.1111/j.1432-1033.1995.0181f.x
Abstract
No abstract availableThis publication has 19 references indexed in Scilit:
- Inactivation of glucose-6-phosphate dehydrogenase by glycationBiochemical Society Transactions, 1994
- A Possible Chaperone-like Quaternary Structure for α-CrystallinExperimental Eye Research, 1994
- Identification of the site of glycation of γ-II-crystallin by (14C)-fructoseBiochimica et Biophysica Acta (BBA) - Molecular Basis of Disease, 1994
- Localization of the Chaperone Binding-SiteBiochemical and Biophysical Research Communications, 1993
- Molecular Chaperone Functions of Heat-Shock ProteinsAnnual Review of Biochemistry, 1993
- Glycation (non-enzymic glycosylation) inactivates glutathione reductaseBiochemical Journal, 1992
- Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediateNature, 1991
- Rapid separation of bovine β-crystallin subunits βB1, βB2, βB3, βA3 and βA4Experimental Eye Research, 1990
- Rat lens superoxide dismutase and glucose-6-phosphate dehydrogenase: Studies on the catalytic activity and the fate of enzyme antigen as a function of ageExperimental Eye Research, 1981
- Glucose 6-phosphate dehydrogenase in the mammalian lensExperimental Eye Research, 1971