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

Elucidating the Role of Wildtype and Variant FGFR2 Structural Dynamics in (Dys)Function and Disorder.

International journal of molecular sciences - 20 Apr 2024

Lian Yiyang, Bodian Dale, Shehu Amarda

Abstract excerpt

The fibroblast growth factor receptor 2 (FGFR2) gene is one of the most extensively studied genes with many known mutations implicated in several human disorders, including oncogenic ones. Most FGFR2 disease-associated gene mutations are missense mutations that result in constitutive activation of the FGFR2 protein and downstream molecular pathways. Many tertiary structures of the FGFR2 kinase domain are publicly...

Read the complete abstract on PubMed

Topics

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

Share to Machine Learning
Share to Models, Molecular
Share to Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation, Missense

Share to Protein Conformation

Share to Protein Domains

Share to Receptor, Fibroblast Growth Factor, Type 2

Share to Structure-Activity Relationship

Source

Open in PubMed Open full text

Identifiers

PMID: 38674107
DOI: 10.3390/ijms25084523
PMCID: PMC11050683

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

Elucidating the Role of Wildtype and Variant FGFR2 Structural Dynamics in (Dys)Function and Disorder.PMID 38674107Read ↗

Predicting the impact of deleterious mutations in the protein kinase domain of FGFR2 in the context of function, structure, and pathogenesis--a bioinformatics approach.Semantic proximity Read ↗

Structural basis for reduced FGFR2 activity in LADD syndrome: Implications for FGFR autoinhibition and activation.Semantic proximity Read ↗

Predicted mechanistic impacts of human protein missense variantsSemantic proximity Read ↗

Cracking the molecular origin of intrinsic tyrosine kinase activity through analysis of pathogenic gain-of-function mutations.Semantic proximity Read ↗

Decoupling the dynamic mechanism revealed by FGFR2 mutation-induced population shift.Semantic proximity Read ↗

Gatekeeper mutations activate FGF receptor tyrosine kinases by destabilizing the autoinhibited state.Semantic proximity Read ↗

A crystallographic snapshot of tyrosine trans-phosphorylation in action.Semantic proximity Read ↗

A molecular brake in the kinase hinge region regulates the activity of receptor tyrosine kinases.Semantic proximity Read ↗

Molecular modeling and molecular dynamic simulation of the effects of variants in the TGFBR2 kinase domain as a paradigm for interpretation of variants obtained by next generation sequencingSemantic proximity Read ↗

Geometry-Constrained Prediction of Catalytically Competent Kinase Domains Across the Human KinomeSemantic proximity Read ↗

Molecular mechanisms of fibroblast growth factor signaling in physiology and pathology.Semantic proximity Read ↗

Disease-causing mutation in extracellular and intracellular domain of FGFR1 protein: computational approach.Semantic proximity Read ↗

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