Zobrazeno 1 - 10
of 21
pro vyhledávání: '"M D, Faiman"'
Publikováno v:
Advances in experimental medicine and biology. 442
Cysteine sulfinic acid decarboxylase (CSAD), the rate-limiting enzyme in taurine biosynthesis, was found to be activated under conditions that favor protein phosphorylation and inactivated under conditions favoring protein dephosphorylation. Direct i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::1a4c564aaba602aa6d7bfed90dd25384
https://pubmed.ncbi.nlm.nih.gov/9635049
https://pubmed.ncbi.nlm.nih.gov/9635049
Publikováno v:
Biochemical pharmacology. 55(6)
S-Methyl N,N-diethylthiolcarbamate sulfoxide (DETC-MeSO) and sulfone (DETC-MeSO2) both inhibit rat liver low Km aldehyde dehydrogenase (ALDH2) in vitro and in vivo (Nagendra et al., Biochem Pharmacol 47: 1465-1467, 1994). DETC-MeSO has been shown to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::c8edcea767fd76b9b54c77f2d16e72ee
https://pubmed.ncbi.nlm.nih.gov/9586946
https://pubmed.ncbi.nlm.nih.gov/9586946
Publikováno v:
Drug metabolism and disposition: the biological fate of chemicals. 23(10)
The present study investigated the role of rat and human cytochrome P450 enzymes in the sulfoxidation of S-methyl N,N-diethylthiolcarbamate (DETC-Me) to S-methyl N,N-diathylthiolcarbamate sulfoxide (DETC-Me sulfoxide), the putative active metabolite
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::c5275fe60bbb02f7225dac3f5ba37d5a
https://pubmed.ncbi.nlm.nih.gov/8654205
https://pubmed.ncbi.nlm.nih.gov/8654205
Autor:
A, Madan, M D, Faiman
Publikováno v:
The Journal of pharmacology and experimental therapeutics. 272(2)
Disulfiram is bioactivated through a series of intermediates, ultimately forming S-methyl-N,N-diethylthiolcarbamate sulfoxide (DETC-Me sulfoxide), the metabolite proposed to be responsible for the in vivo inhibition of rat liver mitochondrial low Km
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::6aabad09f128e241250b3655be2cb228
https://pubmed.ncbi.nlm.nih.gov/7853193
https://pubmed.ncbi.nlm.nih.gov/7853193
Autor:
B W, Hart, M D, Faiman
Publikováno v:
Biochemical pharmacology. 49(2)
S-Methyl N,N-diethylthiolcarbamate (DETC-Me) is a metabolite formed during the bioactivation of disulfiram. The formation of its corresponding sulfoxide, S-methyl N,N-diethylthiolcarbamate sulfoxide (DETC-MeSO), from DETC-Me is required for low Km mi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::4abadea0d40272b69630279d87124dd2
https://pubmed.ncbi.nlm.nih.gov/7840792
https://pubmed.ncbi.nlm.nih.gov/7840792
Publikováno v:
Molecular pharmacology. 46(6)
Oxidative desulfuration of diethyldithiocarbamate methyl ester (DDTC-Me), a thione xenobiotic and a metabolite of disulfiram, was studied. Using a rat liver microsomal incubation system, DDTC-Me was oxidized at the thionosulfur group, forming DDTC-Me
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::244e7d9f0486328e992ffc37ba3ae05d
https://pubmed.ncbi.nlm.nih.gov/7808445
https://pubmed.ncbi.nlm.nih.gov/7808445
Autor:
A, Madan, M D, Faiman
Publikováno v:
Drug metabolism and disposition: the biological fate of chemicals. 22(2)
The present study describes the NADPH-dependent, regioselective oxidation of diethyldithiocarbamate methyl ester (DDTC-Me), a dithiocarbamate ester containing both a thionosulfur (C = S) and a thioether (S-CH3) group, to two novel S-oxidized metaboli
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::c262fdd0aff99631ae6a1be72f9347d0
https://pubmed.ncbi.nlm.nih.gov/8013289
https://pubmed.ncbi.nlm.nih.gov/8013289
Autor:
B W, Hart, M D, Faiman
Publikováno v:
Biochemical pharmacology. 46(12)
Diethyldithiocarbamate (DDTC), diethyldithiocarbamate methyl ester (DDTC-Me), S-methyl N,N-diethylthiolcarbamate (DETC-Me) and S-methyl N,N-diethylthiolcarbamate sulfoxide (DETC-MeSO) are all metabolites of disulfiram. All inhibit rat liver low Km al
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::4c52ec641d9f26f41f00523a46247eb5
https://pubmed.ncbi.nlm.nih.gov/8274162
https://pubmed.ncbi.nlm.nih.gov/8274162
Publikováno v:
Novel Pharmacological Interventions for Alcoholism ISBN: 9781461277057
The inhibition of liver aldehyde dehydrogenase (ALDH) and subsequent increase in acetaldehyde after ethanol ingestion, form the basis for the clinical use of disulfiram (DS) in the treatment of alcoholism. This is referred to as the disulfiram-ethano
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::db04dd37a8645e53c246a0b92b48c25b
https://doi.org/10.1007/978-1-4612-2878-3_26
https://doi.org/10.1007/978-1-4612-2878-3_26
Autor:
M D Faiman, D E Dodd
Publikováno v:
Biochemical Journal. 174:769-775
NADP+, NADPH and glucose 6-phosphate dehydrogenase were determined in the cerebral cortex of mice exposed to high O2 pressure for 0, 8 and 16 min. These time intervals corresponded to 0, 50 and 100% of the CT50 (the time taken for 50% of the mice to
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a18eceea76b8e0e76de8283021004611
https://doi.org/10.1042/bj1740769
https://doi.org/10.1042/bj1740769