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Markevich2004_MAPK_phosphoRandomMM


ABSTRACT: The model corresponds to the schema 3 of Markevich et al 2004, as described in the figure 2 and the supplementary table S3, and modelled using Michaelis-Menten like kinetics. Phosphorylations follow distributive random kinetics, while dephosphorylations follow an ordered mechanism. This model originates from BioModels Database: A Database of Annotated Published Models. It is copyright (c) 2005-2007 The BioModels Team. For more information see the terms of use .

REANALYSED by: BIOMD0000000223

SUBMITTER: Nicolas Le Novère  

PROVIDER: BIOMD0000000029 | BioModels | 2005-05-24

REPOSITORIES: BioModels

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Publications

Signaling switches and bistability arising from multisite phosphorylation in protein kinase cascades.

Markevich Nick I NI   Hoek Jan B JB   Kholodenko Boris N BN  

The Journal of cell biology 20040126 3


Mitogen-activated protein kinase (MAPK) cascades can operate as bistable switches residing in either of two different stable states. MAPK cascades are often embedded in positive feedback loops, which are considered to be a prerequisite for bistable behavior. Here we demonstrate that in the absence of any imposed feedback regulation, bistability and hysteresis can arise solely from a distributive kinetic mechanism of the two-site MAPK phosphorylation and dephosphorylation. Importantly, the report  ...[more]

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