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

COSMIC-Linked Ras Mutations at the Interface Between H-Ras and PI3KγRBD Frequently Generate Affinity Increases.

Biochemistry - 2 Jun 2026

Mead Elizabeth H, Batz Kaeden C, Shih Kuo-Hsien, Fleming Ian R, Tesdahl Corey D, Lizardos Lucas, Armendariz Joy R, Hannan Jonathan P, Hickey Ava M, Leyk Alan, Erbse Annette H, Falke Joseph J

Abstract excerpt

The three conventional isoforms of the Ras G-protein (H-, K-, N-Ras) function as molecular on-off switches that regulate a wide array of signaling pathways, including the Ras-PI3K-PIP3-PDK-AKT pathway that is central to innate immunity and normal cell growth and is dysregulated in many disease states. Activation of the pathway by Ras requires adequate Ras-PI3K binding affinity. Here we focus on the interface of...

Read the complete abstract on PubMed

Topics

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

Share to Binding Sites
Share to Models, Molecular

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Protein Binding

Share to Proto-Oncogene Proteins p21(ras)

Share to ras Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 42148525
DOI: 10.1021/acs.biochem.5c00815
PMCID: PMC13235541

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 8 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

COSMIC-Linked Ras Mutations at the Interface Between H-Ras and PI3KγRBD Frequently Generate Affinity Increases.PMID 42148525Read ↗

COSMIC-Linked Ras Mutations at the Interface Between H-Ras and PI3Kγ <sub>RBD</sub> Frequently Generate Affinity IncreasesSemantic proximity Read ↗

A cancer-associated K-RAS mutant that preferentially binds GDP displays gain-of-function and atypical signalingSemantic proximity Read ↗

Oncogenic K-Ras4B Dimerization Enhances Downstream Mitogen-activated Protein Kinase Signaling.Semantic proximity Read ↗

The Ins and Outs of RAS Effector Complexes.Semantic proximity Read ↗

Oncogenic G12D mutation alters local conformations and dynamics of K-RasSemantic proximity Read ↗

The K-Ras, N-Ras, and H-Ras Isoforms: Unique Conformational Preferences and Implications for Targeting Oncogenic Mutants.Semantic proximity Read ↗

PI3K Driver Mutations: A Biophysical Membrane-Centric Perspective.Semantic proximity Read ↗

K-Ras G-domain binding with signaling lipid phosphoinositides: PIP2 association, orientation, functionSemantic proximity Read ↗

Oncogenic mutations mimic and enhance dynamic events in the natural activation of phosphoinositide 3-kinase p110α (PIK3CA).Semantic proximity Read ↗

Structural insights into isoform-specific RAS-PI3Kα interactions and the role of RAS in PI3Kα activationSemantic proximity Read ↗

The Structural Basis of Oncogenic Mutations G12, G13 and Q61 in Small GTPase K-Ras4B.Semantic proximity Read ↗

What makes Ras an efficient molecular switch: a computational, biophysical, and structural study of Ras-GDP interactions with mutants of Raf.Semantic proximity Read ↗

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