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

Molecular basis for the functional roles of the multimorphic T95R mutation of IRF4 causing human autosomal dominant combined immunodeficiency.

Structure (London, England : 1993) - 2 Nov 2023

Wang Guanchao, Feng Xueqian, Ding Jianping

Abstract excerpt

Interferon regulatory factor 4 (IRF4) is a transcription factor that regulates the development and function of immune cells. Recently, a new multimorphic mutation T95R was identified in the IRF4 DNA-binding domain (DBD) in patients with autosomal dominant combined immune deficiency. Here, we characterized the interactions of the wild-type IRF4-DBD (IRF4-DBDWT) and T95R mutant (IRF4-DBDT95R) with a canonical DNA...

Read the complete abstract on PubMed

Topics

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

Share to DNA
Share to DNA-Binding Proteins
Share to Gene Expression Regulation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Interferon Regulatory Factors

Share to Mutation

Source

Identifiers

PMID: 37683642
DOI: 10.1016/j.str.2023.08.013

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

Molecular basis for the functional roles of the multimorphic T95R mutation of IRF4 causing human autosomal dominant combined immunodeficiency.PMID 37683642Read ↗

A multimorphic mutation in IRF4 causes human autosomal dominant combined immunodeficiency.Semantic proximity Read ↗

Transcriptional reprogramming by mutated IRF4 in lymphomaSemantic proximity Read ↗

A new type of transcriptional reprogramming by an IRF4 mutation in lymphomaSemantic proximity Read ↗

DNA-binding landscape of IRF3, IRF5 and IRF7 dimers: implications for dimer-specific gene regulationSemantic proximity Read ↗

Biochemical and structural studies of NFIA and NFIC reveal a conserved mechanism for specific DNA recognition and provide insight into potential pathogenicity of disease-associated mutations.Semantic proximity Read ↗

Evolution of the repertoire of nuclear receptor binding sites in genomes.Semantic proximity Read ↗

Effect of novel leukemia mutations (K75E & E222K) on interferon regulatory factor 1 and its interaction with DNA: insights from molecular dynamics simulations and docking studies.Semantic proximity Read ↗

Assessing Interferon Regulatory Factor 4 Complex Formation: Differential Behavior of Homocomplexes Versus Heterocomplexes Induced by Mutations.Semantic proximity Read ↗

DNA Conformation Induces Adaptable Binding by Tandem Zinc Finger Proteins.Semantic proximity Read ↗

The crystal structure of the second Z-DNA binding domain of human DAI (ZBP1) in complex with Z-DNA reveals an unusual binding mode to Z-DNA.Semantic proximity Read ↗

A neomorphic mutation in the interferon activation domain of IRF4 causes a dominant primary immunodeficiency.Semantic proximity Read ↗

Structural basis of binding of homodimers of the nuclear receptor NR4A2 to selective Nur-responsive DNA elements.Semantic proximity Read ↗

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