An immunochemical approach of identifying and characterizing protein targets of toxic reactive metabolites

1993 ◽  
Vol 6 (6) ◽  
pp. 786-793 ◽  
Author(s):  
Lance R. Pohl
Keyword(s):  
Reactive Metabolites ◽  
Protein Targets

scholarly journals Protein Targets of Reactive Metabolites of Thiobenzamide in Rat Liver in Vivo

2008 ◽  
Vol 21 (7) ◽  
pp. 1432-1442 ◽  
Author(s):  
Keisuke Ikehata ◽  
Tatyana G. Duzhak ◽  
Nadezhda A. Galeva ◽  
Tao Ji ◽  
Yakov M. Koen ◽  
...  
Keyword(s):  
Rat Liver ◽  
Reactive Metabolites ◽  
Protein Targets

Identification of Three Protein Targets for Reactive Metabolites of Bromobenzene in Rat Liver Cytosol

2000 ◽  
Vol 13 (12) ◽  
pp. 1326-1335 ◽  
Author(s):  
Yakov M. Koen ◽  
Todd D. Williams ◽  
Robert P. Hanzlik
Keyword(s):  
Rat Liver ◽  
Reactive Metabolites ◽  
Protein Targets ◽  
Liver Cytosol ◽  
Rat Liver Cytosol

Protein Targets of Isoniazid-Reactive Metabolites in Mouse Liverin Vivo

2016 ◽  
Vol 29 (6) ◽  
pp. 1064-1072 ◽  
Author(s):  
Yakov M. Koen ◽  
Nadezhda A. Galeva ◽  
Imir G. Metushi ◽  
Jack Uetrecht ◽  
Robert P. Hanzlik
Keyword(s):  
Reactive Metabolites ◽  
Protein Targets

scholarly journals Identification of Protein Targets of Reactive Metabolites of Tienilic Acid in Human Hepatocytes

2012 ◽  
Vol 25 (5) ◽  
pp. 1145-1154 ◽  
Author(s):  
Yakov M. Koen ◽  
Diganta Sarma ◽  
Todd D. Williams ◽  
Nadezhda A. Galeva ◽  
R. Scott Obach ◽  
...  
Keyword(s):  
Human Hepatocytes ◽  
Reactive Metabolites ◽  
Tienilic Acid ◽  
Protein Targets

Dicarbonyl derived post-translational modifications: chemistry bridging biology and aging-related disease

2020 ◽  
Vol 64 (1) ◽  
pp. 97-110
Author(s):  
Christian Sibbersen ◽  
Mogens Johannsen
Keyword(s):  
Mass Spectrometry ◽  
Future Research ◽  
Amino Acid Residues ◽  
Post Translational Modification ◽  
Dicarbonyl Compounds ◽  
Protein Targets ◽  
Post Translational Modifications ◽  
Reactive Protein ◽  
Glycation End Products ◽  
Direct Mass Spectrometry

Abstract In living systems, nucleophilic amino acid residues are prone to non-enzymatic post-translational modification by electrophiles. α-Dicarbonyl compounds are a special type of electrophiles that can react irreversibly with lysine, arginine, and cysteine residues via complex mechanisms to form post-translational modifications known as advanced glycation end-products (AGEs). Glyoxal, methylglyoxal, and 3-deoxyglucosone are the major endogenous dicarbonyls, with methylglyoxal being the most well-studied. There are several routes that lead to the formation of dicarbonyl compounds, most originating from glucose and glucose metabolism, such as the non-enzymatic decomposition of glycolytic intermediates and fructosyl amines. Although dicarbonyls are removed continuously mainly via the glyoxalase system, several conditions lead to an increase in dicarbonyl concentration and thereby AGE formation. AGEs have been implicated in diabetes and aging-related diseases, and for this reason the elucidation of their structure as well as protein targets is of great interest. Though the dicarbonyls and reactive protein side chains are of relatively simple nature, the structures of the adducts as well as their mechanism of formation are not that trivial. Furthermore, detection of sites of modification can be demanding and current best practices rely on either direct mass spectrometry or various methods of enrichment based on antibodies or click chemistry followed by mass spectrometry. Future research into the structure of these adducts and protein targets of dicarbonyl compounds may improve the understanding of how the mechanisms of diabetes and aging-related physiological damage occur.

In Search of Novel Cancer Therapeutics: Assessing the NCI Natural Product Library against Ten Anti-Apoptotic Protein Targets

Planta Medica ◽  
2013 ◽  
Vol 79 (10) ◽  
Author(s):  
DB Divlianska ◽  
AE Wright ◽  
S Francis ◽  
MA Walters ◽  
CE Salomon ◽  
...  
Keyword(s):  
Natural Product ◽  
Cancer Therapeutics ◽  
Protein Targets ◽  
Apoptotic Protein ◽  
Natural Product Library
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