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

Molecular dynamics simulations of Gly-12-->Val mutant of p21(ras): dynamic inhibition mechanism.

Biophysical journal - 1 Dec 2001

Futatsugi N, Tsuda M

Abstract excerpt

The mutant p21(ras) protein is a G protein produced by the point-mutated H-ras gene, and this mutant protein has been shown to cause carcinogenesis due to a reduction in its GTPase activity. However, the mechanism underlying this strange phenomenon has still not been elucidated. In our previous study, we have clarified the mechanism of the GTP-->GDP hydrolysis reaction in the wild-type p21(ras) at the atomic...

Read the complete abstract on PubMed

Topics

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

Share to Hydrogen Peroxide
Share to Glycine
Share to GTPase-Activating Proteins

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

Share to Guanosine Diphosphate

Share to Guanosine Triphosphate

Share to Hydrolysis

Share to Protons

Share to Valine

Source

Open in PubMed Open full text

Identifiers

PMID: 11721009
DOI: 10.1016/S0006-3495(01)75979-6
PMCID: PMC1301803

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

Molecular dynamics simulations of Gly-12-->Val mutant of p21(ras): dynamic inhibition mechanism.PMID 11721009Read ↗

Mutational landscape of K-Ras substitutions at 12th position-a systematic molecular dynamics approach.Semantic proximity Read ↗

Assessing the mechanism of fast-cycling cancer-associated mutations of Rac1 small Rho GTPase.Semantic proximity Read ↗

Probing mutation-induced conformational transformation of the GTP/M-RAS complex through Gaussian accelerated molecular dynamics simulations.Semantic proximity Read ↗

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

Time-Resolved Crystallography Reveals the Mechanisms of GTP hydrolysis for N-RAS and the Oncogenic Mutants G12C, G12V and Q61LSemantic proximity Read ↗

Computational characterization of the chemical step in the GTP hydrolysis by Ras-GAP for the wild-type and G13V mutated Ras.Semantic proximity Read ↗

Conformational Dynamics Allows Sampling of an "Active-like" State by Oncogenic K-Ras-GDP.Semantic proximity Read ↗

Comparative MD simulations and advanced analytics based studies on wild-type and hot-spot mutant A59G HRas.Semantic proximity Read ↗

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

Unveiling conformational dynamics changes of H-Ras induced by mutations based on accelerated molecular dynamics.Semantic proximity Read ↗

Molecular dynamic simulation reveals damaging impact of RAC1 F28L mutation in the switch I region.Semantic proximity Read ↗

Distinct dynamics and interaction patterns in H- and K-Ras oncogenic P-loop mutants.Semantic proximity Read ↗

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