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

Conserved allosteric perturbation of the GTPase domains by region 1 of Ras hypervariable regions.

Biophysical journal - 2 Apr 2024

Gu Xue, Zhang Yalong, Long Dong

Abstract excerpt

Ras proteins are important intracellular signaling hubs that can interact with numerous downstream effectors and upstream regulators through their GTPase domains (G-domains) anchored to plasma membranes by the C-terminal hypervariable regions (HVRs). The biological functions of Ras were proposed to be regulated at multiple levels including the intramolecular G-domain-HVR interactions, of which the exact mechanism...

Read the complete abstract on PubMed

Topics

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

Share to Cell Membrane
Share to Mutation
Share to Protein Isoforms

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Proto-Oncogene Proteins p21(ras)

Share to ras Proteins

Share to Signal Transduction

Source

Open in PubMed Open full text

Identifiers

PMID: 38419331
DOI: 10.1016/j.bpj.2024.02.022
PMCID: PMC10995424

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Conserved allosteric perturbation of the GTPase domains by region 1 of Ras hypervariable regions.PMID 38419331Read ↗

GTP Binding and Oncogenic Mutations May Attenuate Hypervariable Region (HVR)-Catalytic Domain Interactions in Small GTPase K-Ras4B, Exposing the Effector Binding Site.Semantic proximity Read ↗

The disordered hypervariable region and the folded catalytic domain of oncogenic K-Ras4B partner in phospholipid binding.Semantic proximity Read ↗

NMR in integrated biophysical drug discovery for RAS: past, present, and future.Semantic proximity Read ↗

Allosteric site variants affect GTP hydrolysis on RASSemantic proximity Read ↗

Mechanisms of isoform-specific residue influence on GTP-bound HRas, KRas, and NRas.Semantic proximity Read ↗

Dynamically encoded reactivity of Ras enzymes: opening new frontiers for drug discovery.Semantic proximity Read ↗

Molecular Dynamics Simulations and Dynamic Network Analysis Reveal the Allosteric Unbinding of Monobody to H-Ras Triggered by R135K Mutation.Semantic proximity Read ↗

Mutations in the α4-α5 allosteric lobe of RAS do not significantly impair RAS signaling or self-association.Semantic proximity Read ↗

The Hypervariable Region of K-Ras4B Governs Molecular Recognition and Function.Semantic proximity Read ↗

Defining An Expanded RAS Conformational Landscape Based on Over 700 Experimentally Determined Structures of KRAS, NRAS, and HRASSemantic proximity Read ↗

Structures of RGL1 RAS-Association Domain in Complex with KRAS and the Oncogenic G12V Mutant.Semantic proximity Read ↗

Unveiling the Domain-Specific and RAS Isoform-Specific Details of BRAF RegulationSemantic proximity Read ↗

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