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

Biophysical aspect of phosphatidylinositol 3-kinase and role of oncogenic mutants (E542K & E545K).

Journal of biomolecular structure & dynamics - 1 Dec 2016

Kalsi Namrata, Gopalakrishnan Chandrasekhar, Rajendran Vidya, Purohit Rituraj

Abstract excerpt

Genetic variations in oncogenes can often promote uncontrolled cell proliferation by altering the structure of the encoded protein, thereby altering its function. The PI3KCA oncogene that encodes for p110α, the catalytic subunit of phosphatidylinositol 3-kinase (PI3K), is one the most frequently mutated oncogenes in humans. PI3K plays a pivotal role in cell division. PI3K consists of two subunits: the catalytic...

Read the complete abstract on PubMed

Topics

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

Share to Carrier Proteins
Share to Hydrogen Bonding

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Models, Molecular

Share to Mutation

Share to Phosphatidylinositol 3-Kinases

Share to Protein Binding

Share to Protein Conformation

Share to Structure-Activity Relationship

Source

Identifiers

PMID: 26646651
DOI: 10.1080/07391102.2015.1127774

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

Biophysical aspect of phosphatidylinositol 3-kinase and role of oncogenic mutants (E542K & E545K).PMID 26646651Read ↗

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

Oncogenic mutations weaken the interactions that stabilize the p110α-p85α heterodimer in phosphatidylinositol 3-kinase α.Semantic proximity Read ↗

Phosphorylation and Driver Mutations in PI3Kα and PTEN Autoinhibition.Semantic proximity Read ↗

PI3K in cancer: its structure, activation modes and role in shaping tumor microenvironment.Semantic proximity Read ↗

Advances in subunits of PI3K class I in cancer.Semantic proximity Read ↗

Somatic mutations in PI3Kα: Structural basis for enzyme activation and drug designSemantic proximity Read ↗

Mechanism of two classes of cancer mutations in the phosphoinositide 3-kinase catalytic subunit.Semantic proximity Read ↗

Class I PI3K in oncogenic cellular transformation.Semantic proximity Read ↗

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

Effects of oncogenic p110alpha subunit mutations on the lipid kinase activity of phosphoinositide 3-kinase.Semantic proximity Read ↗

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