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

The distinct conformational dynamics of K-Ras and H-Ras A59G.

PLoS computational biology - 9 Sept 2010

Lukman Suryani, Grant Barry J, Gorfe Alemayehu A, Grant Guy H, McCammon J Andrew

Abstract excerpt

Ras proteins regulate signaling cascades crucial for cell proliferation and differentiation by switching between GTP- and GDP-bound conformations. Distinct Ras isoforms have unique physiological functions with individual isoforms associated with different cancers and developmental diseases. Given the small structural differences among isoforms and mutants, it is currently unclear how these functional differences...

Read the complete abstract on PubMed

Topics

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

Share to Catalytic Domain
Share to Crystallography
Share to Guanosine Diphosphate

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Guanosine Triphosphate

Share to Molecular Dynamics Simulation

Share to Principal Component Analysis

Share to Protein Isoforms

Share to ras Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 20838576
DOI: 10.1371/journal.pcbi.1000922
PMCID: PMC2936511

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

The distinct conformational dynamics of K-Ras and H-Ras A59G.PMID 20838576Read ↗

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

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

The Importance of Mg2+ -Free State in Nucleotide Exchange of Oncogenic K-Ras Mutants.Semantic proximity Read ↗

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

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

K-Ras Populates Conformational States Differently from Its Isoform H-Ras and Oncogenic Mutant K-RasG12D.Semantic proximity Read ↗

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

Comparative effects of oncogenic mutations G12C, G12V, G13D, and Q61H on local conformations and dynamics of K-RasSemantic proximity Read ↗

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

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

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