Phosphorylation of a UDP-glucuronosyltransferase regulates substrate specificity
about
The major chemical-detoxifying system of UDP-glucuronosyltransferases requires regulated phosphorylation supported by protein kinase CAnti-cancer drugs elicit re-expression of UDP-glucuronosyltransferases in melanoma cellsTwo Medicago truncatula half-ABC transporters are essential for arbuscule development in arbuscular mycorrhizal symbiosisAbsolute quantification of UGT1A1 in various tissues and cell lines using isotope label-free UPLC-MS/MS method determines its turnover number and correlates with its glucuronidation activities.Brain-derived neurotrophic factor involved epigenetic repression of UGT2B7 in colorectal carcinoma: A mechanism to alter morphine glucuronidation in tumor.Redox regulation in cancer: a double-edged sword with therapeutic potential.Regulated phosphorylation of a major UDP-glucuronosyltransferase isozyme by tyrosine kinases dictates endogenous substrate selection for detoxification.Analysis of R- and S-hydroxywarfarin glucuronidation catalyzed by human liver microsomes and recombinant UDP-glucuronosyltransferasesDifferences in the glucuronidation of resveratrol and pterostilbene: altered enzyme specificity and potential gender differencesTargeted inhibition of glucuronidation markedly improves drug efficacy in mice - a model.Protein kinase Cα and Src kinase support human prostate-distributed dihydrotestosterone-metabolizing UDP-glucuronosyltransferase 2B15 activity.First-pass metabolism via UDP-glucuronosyltransferase: a barrier to oral bioavailability of phenolics.Effect of a herbal extract containing curcumin and piperine on midazolam, flurbiprofen and paracetamol (acetaminophen) pharmacokinetics in healthy volunteersIntestinal UGTs as potential modifiers of pharmacokinetics and biological responses to drugs and xenobiotics.Src supports UDP-glucuronosyltransferase-2B7 detoxification of catechol estrogens associated with breast cancerGenetic polymorphism in metabolism and host defense enzymes: implications for human health risk assessment.Transcriptional regulation of human UDP-glucuronosyltransferase genes.Posttranscriptional regulation of uridine diphosphate glucuronosyltransferases.Regulation of uridine diphosphate-glucuronosyltransferase 1A3 activity by protein phosphorylation.Role for protein kinase C delta in the functional activity of human UGT1A6: implications for drug-drug interactions between PKC inhibitors and UGT1A6.
P2860
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P2860
Phosphorylation of a UDP-glucuronosyltransferase regulates substrate specificity
description
2005 nî lūn-bûn
@nan
2005 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
Phosphorylation of a UDP-glucuronosyltransferase regulates substrate specificity
@ast
Phosphorylation of a UDP-glucuronosyltransferase regulates substrate specificity
@en
type
label
Phosphorylation of a UDP-glucuronosyltransferase regulates substrate specificity
@ast
Phosphorylation of a UDP-glucuronosyltransferase regulates substrate specificity
@en
prefLabel
Phosphorylation of a UDP-glucuronosyltransferase regulates substrate specificity
@ast
Phosphorylation of a UDP-glucuronosyltransferase regulates substrate specificity
@en
P2093
P2860
P356
P1476
Phosphorylation of a UDP-glucuronosyltransferase regulates substrate specificity
@en
P2093
Amanda Garza
Ida S Owens
Juan Rivera
Martina Kovarova
Nikhil K Basu
Partha S Mitra
Rajat Banerjee
Shigeki Kubota
Tapas Saha
P2860
P304
P356
10.1073/PNAS.0407872102
P407
P577
2005-04-21T00:00:00Z