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

Phosphorylation of a UDP-glucuronosyltransferase regulates substrate specificity.

Proceedings of the National Academy of Sciences of the United States of America - 3 May 2005

Basu Nikhil K, Kovarova Martina, Garza Amanda, Kubota Shigeki, Saha Tapas, Mitra Partha S, Banerjee Rajat, Rivera Juan, Owens Ida S

Abstract excerpt

UDP-glucuronosyltransferase (UGT) isozymes catalyze detoxification of numerous chemical toxins present in our daily diet and environment by conjugation to glucuronic acid. The special properties and enzymatic mechanism(s) that enable endoplasmic reticulum-bound UGT isozymes to convert innumerable structurally diverse lipophiles to excretable glucuronides are unknown. Inhibition of cellular UGT1A7 and UGT1A10...

Read the complete abstract on PubMed

Topics

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

Share to Carbon Radioisotopes
Share to Curcumin

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Estradiol

Share to Glucuronosyltransferase

Share to Naphthalenes

Share to Phosphoserine

Share to Protein Kinase C

Share to Threonine

Source

Open in PubMed Open full text

Identifiers

PMID: 15845768
DOI: 10.1073/pnas.0407872102
PMCID: PMC1088353

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 10 closest

Phosphorylation of a UDP-glucuronosyltransferase regulates substrate specificity.PMID 15845768Read ↗

Gastrointestinally distributed UDP-glucuronosyltransferase 1A10, which metabolizes estrogens and nonsteroidal anti-inflammatory drugs, depends upon phosphorylation.Semantic proximity Read ↗

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

Multisite phosphorylation of human liver cytochrome P450 3A4 enhances Its gp78- and CHIP-mediated ubiquitination: a pivotal role of its Ser-478 residue in the gp78-catalyzed reaction.Semantic proximity Read ↗

An Ambidextrous Polyphenol Glycosyltransferase PaGT2 from Phytolacca americana.Semantic proximity Read ↗

Recent advances in the in silico modelling of UDP glucuronosyltransferase substrates.Semantic proximity Read ↗

Regiospecificity and stereospecificity of human UDP-glucuronosyltransferases in the glucuronidation of estriol, 16-epiestriol, 17-epiestriol, and 13-epiestradiol.Semantic proximity Read ↗

Individual PKC-phosphorylation sites in organic cation transporter 1 determine substrate selectivity and transport regulation.Semantic proximity Read ↗

Ligand orientation governs conjugation capacity of UDP-glucuronosyltransferase 1A1.Semantic proximity Read ↗

Enzyme Kinetics of Uridine Diphosphate Glucuronosyltransferases (UGTs).Semantic proximity Read ↗

Mutation analysis in UGT1A9 suggests a relationship between substrate and catalytic residues in UDP-glucuronosyltransferases.Semantic proximity Read ↗

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