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

Identification of functionally relevant lysine residues that modulate human farnesoid X receptor activation.

Molecular pharmacology - 1 May 2013

Sun An-Qiang, Luo Yuhuan, Backos Donald S, Xu Shuhua, Balasubramaniyan Natarajan, Reigan Philip, Suchy Frederick J

Abstract excerpt

Base amino acid lysine residues play an important role in regulation of nuclear receptors [e.g., farnesyl X receptor (FXR)], leading to enhanced or suppressed biologic activity. To understand the molecular mechanisms and the subsequent effects in modulating FXR functions in diverse biologic processes, we individually replaced eight highly conserved lysine residues of human FXR (hFXR) with arginine. The effects of...

Read the complete abstract on PubMed

Topics

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

Share to ATP Binding Cassette Transporter, Subfamily B, Member 11
Share to Caco-2 Cells

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Histone Deacetylase Inhibitors

Share to Lysine

Share to Methyltransferases

Share to Protein Interaction Domains and Motifs

Share to Receptors, Cytoplasmic and Nuclear

Share to Retinoid X Receptors

Source

Open in PubMed Open full text

Identifiers

PMID: 23462506
DOI: 10.1124/mol.113.084772
PMCID: PMC3920091

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

Identification of functionally relevant lysine residues that modulate human farnesoid X receptor activation.PMID 23462506Read ↗

Mechanistic insights into isoform-dependent and species-specific regulation of bile salt export pump by farnesoid X receptor.Semantic proximity Read ↗

A common polymorphism in the bile acid receptor farnesoid X receptor is associated with decreased hepatic target gene expression.Semantic proximity Read ↗

Genome‐wide tissue‐specific farnesoid X receptor binding in mouse liver and intestine†Semantic proximity Read ↗

Impaired transitioning of the FXR ligand binding domain to an active state underlies an FXR-associated PFIC phenotypeSemantic proximity Read ↗

A CK2-RNF4 interplay coordinates non-canonical SUMOylation and degradation of nuclear receptor FXR.Semantic proximity Read ↗

Phosphorylation of a conserved serine in the deoxyribonucleic acid binding domain of nuclear receptors alters intracellular localization.Semantic proximity Read ↗

Tryptophan 299 is a conserved residue of human pregnane X receptor critical for the functional consequence of ligand binding.Semantic proximity Read ↗

Serine 350 of human pregnane X receptor is crucial for its heterodimerization with retinoid X receptor alpha and transactivation of target genes in vitro and in vivo.Semantic proximity Read ↗

Lysine methylation of nuclear co-repressor receptor interacting protein 140.Semantic proximity Read ↗

Postprandial FGF19-induced phosphorylation by Src is critical for FXR function in bile acid homeostasis.Semantic proximity Read ↗

Human FXR regulates SHP expression through direct binding to an LRH-1 binding site, independent of an IR-1 and LRH-1.Semantic proximity Read ↗

A comprehensive analysis and functional characterization of naturally occurring non-synonymous variants of nuclear receptor PXR.Semantic proximity Read ↗

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