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

Mutations in the N-domain of aryl hydrocarbon receptor interacting protein affect interactions with heat shock protein 90β and phosphodiesterase 4A5.

Biochimie - 1 Jan 2025

Vella Marita, Manfield Iain W, Seychell Brandon C, Trinh Chi H, Rambo Robert, Nasir Khan G, Vassallo Josanne, Hunter Thérèse, Hunter Gary J

Abstract excerpt

The aryl hydrocarbon receptor interacting protein (AIP) is a cytoplasmic molecular co-chaperone and tumour suppressor that assists in protein stability and complex formation involving the aryl hydrocarbon receptor. Germline mutations in the AIP gene predispose to pituitary tumourigenesis with patients exhibiting an aggressive clinical phenotype. Full length AIP proteins harbouring N-domain mutations (R9Q, R16H,...

Read the complete abstract on PubMed

Topics

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

Share to Cyclic Nucleotide Phosphodiesterases, Type 4
Share to HSP90 Heat-Shock Proteins

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Intracellular Signaling Peptides and Proteins

Share to Mutation

Share to Protein Binding

Share to Protein Domains

Source

Identifiers

PMID: 39299536
DOI: 10.1016/j.biochi.2024.09.005

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

Mutations in the N-domain of aryl hydrocarbon receptor interacting protein affect interactions with heat shock protein 90β and phosphodiesterase 4A5.PMID 39299536Read ↗

Structure of the TPR domain of AIP: lack of client protein interaction with the C-terminal α-7 helix of the TPR domain of AIP is sufficient for pituitary adenoma predisposition.Semantic proximity Read ↗

In-frame seven amino-acid duplication in AIP arose over the last 3000 years, disrupts protein interaction and stability and is associated with gigantism.Semantic proximity Read ↗

Molecular genetics of the aip gene in familial pituitary tumorigenesis.Semantic proximity Read ↗

Aryl Hydrocarbon Receptor-Interacting Protein (AIP) N-Terminus Gene Mutations Identified in Pituitary Adenoma Patients Alter Protein Stability and Function.Semantic proximity Read ↗

Characterization of aryl hydrocarbon receptor interacting protein (AIP) mutations in familial isolated pituitary adenoma families.Semantic proximity Read ↗

The integrity and organization of the human AIPL1 functional domains is critical for its role as a HSP90-dependent co-chaperone for rod PDE6.Semantic proximity Read ↗

The Role of the Aryl Hydrocarbon Receptor-Interacting Protein Gene in Familial and Sporadic Pituitary AdenomasSemantic proximity Read ↗

Focus on molecules: the aryl hydrocarbon receptor interacting protein-like 1 (AIPL1).Semantic proximity Read ↗

Rapid Proteasomal Degradation of Mutant Proteins Is the Primary Mechanism Leading to Tumorigenesis in Patients With Missense<i>AIP</i>MutationsSemantic proximity Read ↗

Extended conformation of the proline-rich domain of human aryl hydrocarbon receptor-interacting protein-like 1: implications for retina disease.Semantic proximity Read ↗

Pituitary adenoma predisposition caused by germline mutations in the AIP gene.Semantic proximity Read ↗

An evaluation of single nucleotide polymorphisms in the human aryl hydrocarbon receptor-interacting protein (AIP) gene.Semantic proximity Read ↗

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