• Publications
  • Influence
Cisplatin-induced nephrotoxicity in porcine proximal tubular cells: mitochondrial dysfunction by inhibition of complexes I to IV of the respiratory chain.
TLDR
ROS formation does occur during cisplatin-induced toxicity, but it is not the direct cause of cell death, and additional inhibition of complexes I to IV reduced ROS formation.
The UDP glucuronosyltransferase gene superfamily: suggested nomenclature based on evolutionary divergence.
TLDR
A nomenclature system for the UDP glucuronosyltransferase superfamily is proposed, based on divergent evolution of the genes, which leads to the definition of two families and a total of three subfamilies and the suggestion that the human nomenClature system be used for species other than the mouse.
Glucuronidation and its role in regulation of biological activity of drugs.
  • G. Mulder
  • Biology
    Annual review of pharmacology and toxicology
  • 1992
Conjugation reactions in drug metabolism : an integrated approach : substrates, co-substrates, enzymes and their interactions in vivo and in vitro
TLDR
Pang competition between conjugations for the same substate, G.J.Mulder kinetics of conjugation reactions in eliminating organs, K.R.Stevens and J.S.Guenthner.
Role of mitochondrial Ca2+ in the oxidative stress-induced dissipation of the mitochondrial membrane potential. Studies in isolated proximal tubular cells using the nephrotoxin
TLDR
The relationship between mitochondrial Ca2+, oxidative stress, and a dissipation of the mitochondrial membrane potential (delta psi) was investigated in proximal tubular kidney cells, suggesting that oxidative stress is the consequence rather than the cause of the cellular calcium perturbations in DCVC-induced cell killing.
GLUTATHIONE CONJUGATES AND THEIR SYNTHETIC DERIVATIVES AS INHIBITORS OF GLUTATHIONE-DEPENDENT ENZYMES INVOLVED IN CANCER AND DRUG RESISTANCE
TLDR
This review focuses on the function of glutathione-dependent enzymes and carriers in cancer and anti-cancer drug resistance, in relation to their inhibition by GSH-conjugate analogs.
Phenol sulphotransferase and uridine diphosphate glucuronyltransferase from rat liver in vivo and vitro. 2,6-Dichloro-4-nitrophenol as selective inhibitor of sulphation.
TLDR
It is concluded that 2,6-dichloro-4-nitrophenol is a selective inhibitor of sulphation and, further, that its long duration of action makes it suitable for studies on the regulatory role of sulphations in some biological processes.
The glutathione-binding site in glutathione S-transferases. Investigation of the cysteinyl, glycyl and gamma-glutamyl domains.
TLDR
The GSH-binding site of glutathione S-transferase (GST) isoenzymes was studied by investigating their substrate-specificity for three series of GSH analogues; further, a model of the interactions of G SH with the G-site is proposed and appears to be very critical with respect to a correct orientation of the thiol group of the GSH analogue.
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