Structure-based kinetic models of modular signaling protein function: focus on Shp2. - Wikidata - thesis-toulmin - TriplyDB

Structure-based kinetic models of modular signaling protein function: focus on Shp2.

Structure-based kinetic models of modular signaling protein function: focus on Shp2.

http://www.wikidata.org/entity/Q35781235

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RuleMonkey: software for stochastic simulation of rule-based models Cannabinoid 1 receptor and interleukin-6 receptor together induce integration of protein kinase and transcription factor signaling to trigger neurite outgrowth A bipolar clamp mechanism for activation of Jak-family protein tyrosine kinases Hierarchical graphs for rule-based modeling of biochemical systems Kinetic Monte Carlo method for rule-based modeling of biochemical networks.Analytical reduction of combinatorial complexity arising from multiple protein modification sites.Phosphatase specificity and pathway insulation in signaling networks.Guidelines for visualizing and annotating rule-based models Shp2 Associates with and Enhances Nephrin Tyrosine Phosphorylation and Is Necessary for Foot Process Spreading in Mouse Models of Podocyte Injury.Domain-oriented reduction of rule-based network models.Complexity and modularity of intracellular networks: a systematic approach for modelling and simulation Biophysical assay for tethered signaling reactions reveals tether-controlled activity for the phosphatase SHP-1.Modeling formalisms in Systems Biology.Receptor tyrosine kinase (RTK) signalling in the control of neural stem and progenitor cell (NSPC) development.EGFR-activated Src family kinases maintain GAB1-SHP2 complexes distal from EGFR.Model-driven experimental analysis of the function of SHP-2 in IL-6-induced Jak/STAT signaling.Computational models of tandem SRC homology 2 domain interactions and application to phosphoinositide 3-kinase.A multiscale modeling study of particle size effects on the tissue penetration efficacy of drug-delivery nanoparticles.Topological and kinetic determinants of the modal matrices of dynamic models of metabolism.

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Structure-based kinetic models of modular signaling protein function: focus on Shp2.

http://www.wikidata.org/entity/Q35781235

description

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Structure-based kinetic models of modular signaling protein function: focus on Shp2.

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Structure-based kinetic models of modular signaling protein function: focus on Shp2.

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Structure-based kinetic models of modular signaling protein function: focus on Shp2.

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Structure-based kinetic models of modular signaling protein function: focus on Shp2.

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Structure-based kinetic models of modular signaling protein function: focus on Shp2.

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Structure-based kinetic models of modular signaling protein function: focus on Shp2.

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BIOPHYSJ.106.093484

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Biophysical Journal

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Structure-based kinetic models of modular signaling protein function: focus on Shp2

@en

P2093

Dipak Barua

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Jason M Haugh

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P2860

A domain-oriented approach to the reduction of combinatorial complexity in signal transduction networks

Phosphotyrosines 627 and 659 of Gab1 constitute a bisphosphoryl tyrosine-based activation motif (BTAM) conferring binding and activation of SHP2

Site-specific incorporation of a phosphotyrosine mimetic reveals a role for tyrosine phosphorylation of SHP-2 in cell signaling

Mutations in PTPN11, encoding the protein tyrosine phosphatase SHP-2, cause Noonan syndrome

Activation of the SH2-containing protein tyrosine phosphatase, SH-PTP2, by phosphotyrosine-containing peptides derived from insulin receptor substrate-1

Measurement of the binding of tyrosyl phosphopeptides to SH2 domains: a reappraisal

The 64-kDa protein that associates with the platelet-derived growth factor receptor beta subunit via Tyr-1009 is the SH2-containing phosphotyrosine phosphatase Syp

Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by its binding site, phosphotyrosine 1009, on the human platelet-derived growth factor receptor

Spatial constraints on the recognition of phosphoproteins by the tandem SH2 domains of the phosphatase SH-PTP2

Differential functions of the two Src homology 2 domains in protein tyrosine phosphatase SH-PTP1

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2290-2300

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scholarly article

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10.1529/BIOPHYSJ.106.093484

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17208977

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1864834

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