Glycation of proteins by ADP-ribose
- 1 December 1994
- journal article
- review article
- Published by Springer Nature in Molecular and Cellular Biochemistry
- Vol. 138 (1-2) , 207-212
- https://doi.org/10.1007/bf00928463
Abstract
Numerous metabolic pathways generate free ADP-ribose at many locations within cells. The metabolic fates of this nucleotide are poorly understood and measurement of itin situ is technically difficult at present. Yet considerable evidence has accumulated implicating that protein glycation by ADP-ribose can occur. This evidence is reviewed here along with recent developments in characterizing the chemistry of this reaction and the application of this information to the identification of this posttranslational modification in proteinin situ.Keywords
This publication has 44 references indexed in Scilit:
- Adenosine Diphosphate Ribulose in Human Erythrocytes: A New Metabolite with Membrane Binding PropertiesBiochemical and Biophysical Research Communications, 1993
- Presence and turnover of adenosine diphosphate ribose in human erythrocytesBiochemical and Biophysical Research Communications, 1992
- Enzymic and nonenzymic mono ADP-ribosylation of proteins in skeletal muscleBiochemical and Biophysical Research Communications, 1989
- A specific, low K m ADP-ribose pyrophosphatase from rat liverFEBS Letters, 1989
- Recent advances in ocular cataract researchTrends in Pharmacological Sciences, 1986
- Modification of proteins by mono(ADP-ribosylation) in vivoBiochemistry, 1985
- Nonenzymic ADP-ribosylation of poly(adenosine diphosphate ribose)Biochemistry, 1985
- Hemoglobin AIc and Diabetes MellitusAnnual Review of Medicine, 1980
- Further identification of the nature and linkage of the carbohydrate in hemoglobin A1cBiochemical and Biophysical Research Communications, 1975
- The Amadori Rearrangement under New Conditions and its Significance for Non-enzymatic Browning Reactions2Journal of the American Chemical Society, 1953