Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Selectivity for inhibition of nilotinib on the catalytic activity of human UDP-glucuronosyltransferases.

Xenobiotica; the fate of foreign compounds in biological systems - 1 Apr 2014

Ai Limei, Zhu Liangliang, Yang Lu, Ge Guangbo, Cao Yunfeng, Liu Yong, Fang Zhongze, Zhang Yanyan

Abstract excerpt

1. Nilotinib, a tyrosine kinase inhibitor, could potently inhibit SN-38 glucuronidation mainly catalyzed by UDP-glucuronosyltransferase (UGT) 1A1. This study was designed to investigate whether nilotinib can be used as a selective inhibitor of UGT1A1 in human liver. 2. Assays with recombinant UGTs indicated that nilotinib could strongly inhibit the activity of UGT1A1 and decreased the activity of extra-hepatic...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Catalysis
Share to Enzyme Inhibitors

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glucuronides

Share to Glucuronosyltransferase

Share to Microsomes, Liver

Share to Pyrimidines

Share to Recombinant Proteins

Source

Identifiers

PMID: 24066723
DOI: 10.3109/00498254.2013.840750

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Selectivity for inhibition of nilotinib on the catalytic activity of human UDP-glucuronosyltransferases.PMID 24066723Read ↗

Role of human UDP-glucuronosyltransferases in the biotransformation of the triazoloacridinone and imidazoacridinone antitumor agents C-1305 and C-1311: highly selective substrates for UGT1A10.Semantic proximity Read ↗

Characterization of niflumic acid as a selective inhibitor of human liver microsomal UDP-glucuronosyltransferase 1A9: application to the reaction phenotyping of acetaminophen glucuronidation.Semantic proximity Read ↗

Emerging roles for UDP-glucuronosyltransferases in drug resistance and cancer progressionSemantic proximity Read ↗

Influence of N-terminal domain histidine and proline residues on the substrate selectivities of human UDP-glucuronosyltransferase 1A1, 1A6, 1A9, 2B7, and 2B10.Semantic proximity Read ↗

Glucuronidation of OTS167 in Humans Is Catalyzed by UDP-Glucuronosyltransferases UGT1A1, UGT1A3, UGT1A8, and UGT1A10.Semantic proximity Read ↗

The UGT1A1*28 polymorphism correlates with erlotinib's effect on SN-38 glucuronidation.Semantic proximity Read ↗

Glucuronidation by UGT1A1 is the dominant pathway of the metabolic disposition of belinostat in liver cancer patients.Semantic proximity Read ↗

Influence of UGT1A1 6, 27, and 28 polymorphisms on nilotinib-induced hyperbilirubinemia in Japanese patients with chronic myeloid leukemia.Semantic proximity Read ↗

Absolute 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.Semantic proximity Read ↗

UGT1A1 promoter polymorphism increases risk of nilotinib-induced hyperbilirubinemia.Semantic proximity Read ↗

Identification of selective inhibitors of uridine 5'-diphospho-glucuronosyltransferase (UGT) 1A3 and UGT1A8 and their application in UGT reaction phenotyping studies in human liver and intestinal microsomes.Semantic proximity Read ↗

Effects of nilotinib on single-dose warfarin pharmacokinetics and pharmacodynamics: a randomized, single-blind, two-period crossover study in healthy subjects.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.