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

Multiple Binding Modes between HNF4α and the LXXLL Motifs of PGC-1α Lead to Full Activation

22 Oct 2009

Abstract excerpt

Hepatocyte nuclear factor 4alpha (HNF4alpha) is a novel nuclear receptor that participates in a hierarchical network of transcription factors regulating the development and physiology of such vital organs as the liver, pancreas, and kidney. Among the various transcriptional coregulators with which HNF4alpha interacts, peroxisome proliferation-activated receptor gamma (PPARgamma) coactivator 1alpha (PGC-1alpha)...

Read the complete abstract on PubMed

Topics

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

Share to Endoplasmic Reticulum Stress and Disease
Share to Pancreatic function and diabetes
Share to Peroxisome Proliferator-Activated Receptors

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Source

Identifiers

PMID: 19846556
DOI: 10.1074/jbc.m109.052506

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Multiple Binding Modes between HNF4α and the LXXLL Motifs of PGC-1α Lead to Full ActivationPMID 19846556Read ↗

Multidomain integration in the structure of the HNF-4α nuclear receptor complex.Semantic proximity Read ↗

Distinct amino acid residues may be involved in coactivator and ligand interactions in hepatocyte nuclear factor-4alpha.Semantic proximity Read ↗

Evidence for ligand-independent transcriptional activation of the human estrogen-related receptor alpha (ERRalpha): crystal structure of ERRalpha ligand binding domain in complex with peroxisome proliferator-activated receptor coactivator-1alpha.Semantic proximity Read ↗

Structural insights into the HNF4 biologySemantic proximity Read ↗

Communication between the ERRalpha homodimer interface and the PGC-1alpha binding surface via the helix 8-9 loop.Semantic proximity Read ↗

Pioneer factor Foxa2 enables ligand-dependent activation of LXRαSemantic proximity Read ↗

RNA-bound PGC-1α controls gene expression in liquid-like nuclear condensatesSemantic proximity Read ↗

Structural basis of dimerization, coactivator recognition and MODY3 mutations in HNF-1alpha.Semantic proximity Read ↗

Crystal structure of the HNF4 alpha ligand binding domain in complex with endogenous fatty acid ligand.Semantic proximity Read ↗

Human Hepatocyte Nuclear Factor 4-α Encodes Isoforms with Distinct Transcriptional FunctionsSemantic proximity Read ↗

Structural determinants of the agonist-independent association of human peroxisome proliferator-activated receptors with coactivators.Semantic proximity Read ↗

Human Hepatocyte Nuclear Factor 4-α encodes isoforms with distinct transcriptional functionsSemantic proximity Read ↗

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