A multiscale modeling approach to investigate molecular mechanisms of pseudokinase activation and drug resistance in the HER3/ErbB3 receptor tyrosine kinase signaling network

A multiscale modeling approach to investigate molecular mechanisms of pseudokinase activation and drug resistance in the HER3/ErbB3 receptor tyrosine kinase signaling network

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http://www.wikidata.org/entity/Q35111697
Orchestration of ErbB3 signaling through heterointeractions and homointeractions.Dual Inhibition of Topoisomerase II and Tyrosine Kinases by the Novel Bis-Fluoroquinolone Chalcone-Like Derivative HMNE3 in Human Pancreatic Cancer CellsStructure-based network analysis of activation mechanisms in the ErbB family of receptor tyrosine kinases: the regulatory spine residues are global mediators of structural stability and allosteric interactions.Exploring Molecular Mechanisms of Paradoxical Activation in the BRAF Kinase Dimers: Atomistic Simulations of Conformational Dynamics and Modeling of Allosteric Communication Networks and Signaling Pathways.Computational delineation of tyrosyl-substrate recognition and catalytic landscapes by the epidermal growth factor receptor tyrosine kinase domain.Computational modeling of allosteric communication reveals organizing principles of mutation-induced signaling in ABL and EGFR kinases.Analysis of Somatic Mutations in Cancer: Molecular Mechanisms of Activation in the ErbB Family of Receptor Tyrosine Kinases.Integrated analysis reveals that STAT3 is central to the crosstalk between HER/ErbB receptor signaling pathways in human mammary epithelial cells.Structural systems biology and multiscale signaling models.Molecular modeling of ErbB4/HER4 kinase in the context of the HER4 signaling network helps rationalize the effects of clinically identified HER4 somatic mutations on the cell phenotype.erbB3 is an active tyrosine kinase capable of homo- and heterointeractions.The ErbB3 receptor tyrosine kinase negatively regulates Paneth cells by PI3K-dependent suppression of Atoh1.Specificity rendering 'hot-spots' for aurora kinase inhibitor design: the role of non-covalent interactions and conformational transitions.Conformational flexibility of the ErbB2 ectodomain and trastuzumab antibody complex as revealed by molecular dynamics and principal component analysis.EGFR-TKIs resistance via EGFR-independent signaling pathways.Exploring the dynamics and interaction of a full ErbB2 receptor and Trastuzumab-Fab antibody in a lipid bilayer model using Martini coarse-grained force field.
P2860

A multiscale modeling approach to investigate molecular mechanisms of pseudokinase activation and drug resistance in the HER3/ErbB3 receptor tyrosine kinase signaling network

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http://www.wikidata.org/entity/Q35111697
description
2011 nî lūn-bûn
@nan
2011 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
A multiscale modeling approach ...... osine kinase signaling network
@ast
A multiscale modeling approach ...... osine kinase signaling network
@en
type
label
A multiscale modeling approach ...... osine kinase signaling network
@ast
A multiscale modeling approach ...... osine kinase signaling network
@en
prefLabel
A multiscale modeling approach ...... osine kinase signaling network
@ast
A multiscale modeling approach ...... osine kinase signaling network
@en
P1433
P1476
P2093
P2860
P304
P31
P356
P433
P478
P577
P5875
P698
P932
P356
P1433
P1476
A multiscale modeling approach ...... osine kinase signaling network
@en
P2093
P2860
P304
P31
P356
P433
P478
P577
P5875
P698
P932