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

KRAS K104 modification affects the KRASG12D-GEF interaction and mediates cell growth and motility.

Scientific reports - 15 Oct 2020

Chen Chih-Chieh, Hsu Chia-Yi, Lin Hsiao-Yun, Zeng Hong-Qi, Cheng Kuang-Hung, Wu Chia-Wei, Tsai Eing-Mei, Hsieh Tsung-Hua

Abstract excerpt

Mutant RAS genes play an important role in regulating tumors through lysine residue 104 to impair GEF-induced nucleotide exchange, but the regulatory role of KRAS K104 modification on the KRASG12D mutant remains unclear. Therefore, we simulated the acetylation site on the KRASG12D three-dimensional protein structure, including KRASG12D, KRASG12D/K104A and KRASG12D/K104Q, and determined their trajectories and...

Read the complete abstract on PubMed

Topics

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

Share to Wound Healing
Share to Cell Movement

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Molecular Dynamics Simulation

Share to Oligonucleotides

Share to Ovarian Neoplasms

Share to Protein Domains

Share to Proto-Oncogene Proteins p21(ras)

Share to Thermodynamics

Source

Open in PubMed Open full text

Identifiers

PMID: 33060649
DOI: 10.1038/s41598-020-74463-5
PMCID: PMC7567070

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

KRAS K104 modification affects the KRASG12D-GEF interaction and mediates cell growth and motility.PMID 33060649Read ↗

Mutations influence the conformational dynamics of the GDP/KRAS complex.Semantic proximity Read ↗

Conformations of KRAS4B Affected by Its Partner Binding and G12C Mutation: Insights from GaMD Trajectory-Image Transformation-Based Deep Learning.Semantic proximity Read ↗

Allosteric Regulation of Switch-II Domain Controls KRAS Oncogenicity.Semantic proximity Read ↗

Elucidating conformational dynamics of GDP/GTP-KRAS complexes caused by mutations from the switch domain I through Gaussian accelerated molecular dynamics simulations.Semantic proximity Read ↗

Impacts of Mutations in the P-Loop on Conformational Alterations of KRAS Investigated with Gaussian Accelerated Molecular Dynamics Simulations.Semantic proximity Read ↗

Beyond Structural Bioinformatics for Genomics with Dynamics Characterization of an Expanded KRAS Mutational LandscapeSemantic proximity Read ↗

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

Pathogenic KRAS variants disrupt structure and dynamics: Insights from integrated computational analyses.Semantic proximity Read ↗

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

G12V Kras mutations in cervical cancer under virtual microscope of molecular dynamics simulations.Semantic proximity Read ↗

Biochemical and Structural Analysis of Common Cancer-Associated KRAS Mutations.Semantic proximity Read ↗

Structural and Energetic Determinants of Monobody Recognition of Oncogenic KRAS VariantsSemantic proximity Read ↗

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