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

A dimer interface mutation in glyceraldehyde-3-phosphate dehydrogenase regulates its binding to AU-rich RNA.

The Journal of biological chemistry - 16 Jan 2015

White Michael R, Khan Mohd M, Deredge Daniel, Ross Christina R, Quintyn Royston, Zucconi Beth E, Wysocki Vicki H, Wintrode Patrick L, Wilson Gerald M, Garcin Elsa D

Abstract excerpt

Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is an enzyme best known for its role in glycolysis. However, extra-glycolytic functions of GAPDH have been described, including regulation of protein expression via RNA binding. GAPDH binds to numerous adenine-uridine rich elements (AREs) from various mRNA 3'-untranslated regions in vitro and in vivo despite its lack of a canonical RNA binding motif. How GAPDH...

Read the complete abstract on PubMed

Topics

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

Share to 3' Untranslated Regions
Share to Anisotropy

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Glyceraldehyde-3-Phosphate Dehydrogenases

Share to Glycolysis

Share to Protein Multimerization

Share to Scattering, Radiation

Share to Spectrometry, Mass, Electrospray Ionization

Share to X-Rays

Source

Open in PubMed Open full text

Identifiers

PMID: 25451934
DOI: 10.1074/jbc.M114.618165
PMCID: PMC4340419

Genes

GAPDH

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A dimer interface mutation in glyceraldehyde-3-phosphate dehydrogenase regulates its binding to AU-rich RNA.PMID 25451934Read ↗

Structure, function and stability analysis on potential deleterious mutation ensemble in glyceraldehyde 3-phosphate dehydrogenase (GAPDH) for early detection of LUAD.Semantic proximity Read ↗

Comparison of the structures of wild-type and a N313T mutant of Escherichia coli glyceraldehyde 3-phosphate dehydrogenases: implication for NAD binding and cooperativity.Semantic proximity Read ↗

Brownian dynamics of interactions between glyceraldehyde-3-phosphate dehydrogenase (GAPDH) mutants and F-actin.Semantic proximity Read ↗

Transglutaminase 2 is an RNA-binding protein: Experimental verification and characterisation of a novel transglutaminase featureSemantic proximity Read ↗

Insights into the architecture of the eIF2Bα/β/δ regulatory subcomplex.Semantic proximity Read ↗

A Mathematical Genomics Perspective on the Moonlighting Role of Glyceraldehyde-3-Phosphate Dehydrogenase (GAPDH)Semantic proximity Read ↗

A novel variant in the 3' UTR of human SCN1A gene from a patient with Dravet syndrome decreases mRNA stability mediated by GAPDH's binding.Semantic proximity Read ↗

A novel CRM1-mediated nuclear export signal governs nuclear accumulation of glyceraldehyde-3-phosphate dehydrogenase following genotoxic stress.Semantic proximity Read ↗

Molecular dynamics of the interaction between the ALS/FTD-associated (GGGGCC)n RNA G-quadruplex structure and the three RRM domains of hnRNP HSemantic proximity Read ↗

Functional significance of the interaction of hepatitis A virus RNA with glyceraldehyde 3-phosphate dehydrogenase (GAPDH): opposing effects of GAPDH and polypyrimidine tract binding protein on internal ribosome entry site function.Semantic proximity Read ↗

HuR thermal stability is dependent on domain binding and upon phosphorylation.Semantic proximity Read ↗

The conserved Lys-95 charged residue cluster is critical for the homodimerization and enzyme activity of human ribonucleotide reductase small subunit M2.Semantic proximity Read ↗

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