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

Network approach of the conformational change of c-Src, a tyrosine kinase, by molecular dynamics simulation.

Scientific reports - 4 Apr 2018

Yoon Hyun Jung, Lee Sungmin, Park Sun Joo, Wu Sangwook

Abstract excerpt

Non-receptor tyrosine kinase c-Src plays a critical role in numerous cellular signalling pathways. Activation of c-Src from its inactive to the active state involves large-scale conformational changes, and is controlled by the phosphorylation state of two major phosphorylation sites, Tyr416 and Tyr527. A detailed mechanism for the entire conformational transition of c-Src via phosphorylation control of Tyr416 and...

Read the complete abstract on PubMed

Topics

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

Share to Amino Acids
Share to CSK Tyrosine-Protein Kinase
Share to Molecular Dynamics Simulation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Phosphorylation

Share to Protein Conformation

Share to src-Family Kinases

Share to Tyrosine

Source

Open in PubMed Open full text

Identifiers

PMID: 29618744
DOI: 10.1038/s41598-018-23964-5
PMCID: PMC5884825

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 3 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Network approach of the conformational change of c-Src, a tyrosine kinase, by molecular dynamics simulation.PMID 29618744Read ↗

Tyrosine Kinase Activation and Conformational Flexibility: Lessons from Src-Family Tyrosine Kinases.Semantic proximity Read ↗

Structural basis of constitutive c-Src kinase activity due to R175L and W118A mutations.Semantic proximity Read ↗

A Catalytically Disabled Double Mutant of Src Tyrosine Kinase Can Be Stabilized into an Active-Like Conformation.Semantic proximity Read ↗

Computational study of the W260A activating mutant of Src tyrosine kinase.Semantic proximity Read ↗

Structure and Molecular Dynamics Simulations of Protein Tyrosine Phosphatase Non-Receptor 12 Provide Insights into the Catalytic Mechanism of the Enzyme.Semantic proximity Read ↗

Structural characterization of the active and inactive states of Src kinase in solution by small-angle X-ray scattering.Semantic proximity Read ↗

The impact of Thr91 mutation on c-Src resistance to UM-164: molecular dynamics study revealed a new opportunity for drug design.Semantic proximity Read ↗

Understanding the conformation transition in the activation pathway of β2 adrenergic receptor via a targeted molecular dynamics simulation.Semantic proximity Read ↗

Regulation of Src tumor activity by its N-terminal intrinsically disordered regionSemantic proximity Read ↗

Crosstalk between the catalytic and regulatory domains allows bidirectional regulation of Src.Semantic proximity Read ↗

F1174V mutation alters the ALK active conformation in response to Crizotinib in NSCLC: Insight from molecular simulations.Semantic proximity Read ↗

Allosteric networks governing regulation and catalysis of Src-family protein tyrosine kinases: implications for disease-associated kinases.Semantic proximity Read ↗

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