Difference between revisions of "Extracellular signal-regulated kinase (ERK)"
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<h2>Equilibrium constants</h2> | <h2>Equilibrium constants</h2> | ||
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<h2>References</h2> | <h2>References</h2> | ||
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Revision as of 11:44, 13 March 2014
Description of the model
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According to the topology which is found as most likely by Xu et al (2010)[1] a kinetic model is created. Literature data is used to estimate the parameter values and their error. In one (non-modified model) only one reaction kinetic differs from Xu et al. (2010)[1], the Sos-Activation (purple reaction) and is assumed be a binding process rather than enzyme catalysed. Furthermore we modelled the ERK-Activation as two step reaction, with the monophosphorylated ERK as intermediate. In the other one (modified model) further kinetics were changed in addition to these modifications (marked in red). So are the activation of EPAC and PKA by an agonist modelled as binding, C3G-Activation is modelled in two steps, first a binding to the receptor than a phosphorylation, and the Ras-Activation process is splitted in its elementary reactions, and their kinetics are therefore mass action.
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Reactions
Model File
Equilibrium constants
Parameter Overview
References
- ↑ 1.0 1.1 1.2 Tian-Rui Xu et al. (2010) "Inferring signaling pathway topologies from multiple perturbation measurements of specific biochemical species." Sci Signal. 3(134):ra20. (pmid:20234003) Cite error: Invalid
<ref>tag; name "Xu2010" defined multiple times with different content
