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

Evading inhibitory constraints--destabilizing p110α/p85α interactions.

The FEBS journal - 1 Sept 2015

Sheridan Clare

Abstract excerpt

No abstract is available from the source.

Read the complete abstract on PubMed

Topics

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

Share to Mutation
Share to Oncogenes
Share to Phosphatidylinositol 3-Kinases

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 26237180
DOI: 10.1111/febs.13392

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

Evading inhibitory constraints--destabilizing p110α/p85α interactions.PMID 26237180Read ↗

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

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

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

Structure, function and inhibition of the phosphoinositide 3-kinase p110α enzyme.Semantic proximity Read ↗

Activity and Dynamics of p110α are not Differentially Modulated by Regulatory Subunit IsoformsSemantic proximity Read ↗

Targeting the protein-protein interaction between IRS1 and mutant p110α for cancer therapy.Semantic proximity Read ↗

Structure of lipid kinase p110β/p85β elucidates an unusual SH2-domain-mediated inhibitory mechanism.Semantic proximity Read ↗

Structure of the phosphoinositide 3-kinase p110γ-p101 complex reveals molecular mechanism of GPCR activationSemantic proximity Read ↗

Cancer-associated mutations in the p85α N-terminal SH2 domain activate a spectrum of receptor tyrosine kinases.Semantic proximity Read ↗

Molecular chaperone complexes with antagonizing activities regulate stability and activity of the tumor suppressor LKB1Semantic proximity Read ↗

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

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 ↗

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