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

PI 3-kinase: structural and functional analysis of intersubunit interactions.

The EMBO journal - 1 Feb 1994

Dhand R, Hara K, Hiles I, Bax B, Gout I, Panayotou G, Fry M J, Yonezawa K, Kasuga M, Waterfield M D

Abstract excerpt

Phosphatidylinositol (PI) 3-kinase has an 85 kDa subunit (p85 alpha) which mediates its association with activated protein tyrosine kinase receptors through SH2 domains, and an 110 kDa subunit (p110) which has intrinsic catalytic activity. Here p85 alpha and a related protein p85 beta are shown to form stable complexes with recombinant p110 in vivo and in vitro. Using a panel of glutathione S-transferase (GST)...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acid Sequence
Share to Binding Sites
Share to Cell Line

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Molecular Sequence Data

Share to Mutation

Share to Restriction Mapping

Share to Transfection

Source

Open in PubMed Open full text

Identifiers

PMID: 8313896
DOI: 10.1002/j.1460-2075.1994.tb06289.x
PMCID: PMC394840

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. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

PI 3-kinase: structural and functional analysis of intersubunit interactions.PMID 8313896Read ↗

Mutations in the inter-SH2 domain of the regulatory subunit of phosphoinositide 3-kinase: effects on catalytic subunit binding and holoenzyme function.Semantic proximity Read ↗

Class IA PI3K regulatory subunits: p110-independent roles and structures.Semantic proximity Read ↗

The structure of a human p110alpha/p85alpha complex elucidates the effects of oncogenic PI3Kalpha mutations.Semantic proximity Read ↗

Direct positive regulation of PTEN by the p85 subunit of phosphatidylinositol 3-kinase.Semantic proximity Read ↗

Phosphatidylinositol 3-kinase p85{alpha} subunit-dependent interaction with BCR/ABL-related fusion tyrosine kinases: molecular mechanisms and biological consequences.Semantic proximity Read ↗

The regulation of class IA PI 3-kinases by inter-subunit interactions.Semantic proximity Read ↗

Insights into the oncogenic effects of PIK3CA mutations from the structure of p110alpha/p85alpha.Semantic proximity Read ↗

A frequent kinase domain mutation that changes the interaction between PI3Kalpha and the membrane.Semantic proximity Read ↗

The negative regulation of phosphoinositide 3-kinase signaling by p85 and it's implication in cancer.Semantic proximity Read ↗

The structural basis of PI3K cancer mutations: from mechanism to therapy.Semantic proximity Read ↗

Regulation of class IA PI3Ks.Semantic proximity Read ↗

Domain analysis reveals striking functional differences between the regulatory subunits of phosphatidylinositol 3-kinase (PI3K), p85α and p85βSemantic proximity Read ↗

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