ISSN:
1573-4919
Keywords:
free ADP-ribose
;
protein glycation
;
model conjugates of ADP-ribosyl lysine
;
histone glycation
;
non-enzymatic ADP-ribosylation
;
stability of ADP-ribosyl amino acids
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Chemistry and Pharmacology
,
Medicine
Notes:
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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00928463
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