Structural instability in an autophosphorylating kinase switch

DOI10.1016/J.MBS.2009.02.005MaRDI QIDQ2270531zbMATH OpenOpenAlexWikidataFDO

Authors M. Grinfeld, Steven D. Webb

Publication date 28 July 2009

Published in Mathematical Biosciences (Search for Journal in Brave)

Full work available at URL https://strathprints.strath.ac.uk/13399/

zbMATH Keywords

bistabilityordinary differential equations modelprotein turnoverstructural instability

Mathematics Subject Classification ID

Dynamical systems in biology (37N25) Biochemistry, molecular biology (92C40) Kinetics in biochemical problems (pharmacokinetics, enzyme kinetics, etc.) (92C45)

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Cites work

• scientific article; zbMATH DE number 758785 (Why is no real title available?)
• Multi-stability in monotone input/output systems
• Understanding bistability in complex enzyme-driven reaction networks

Cited in

(5)

• Switching characteristics of a model for biochemical-reation networks describing autophosphorylation versus dephosphorylation of Ca\(^{2+}\)/calmodulin-dependent protein kinase. II
• Phosphorylation-induced changes in the energetic frustration in human tank binding kinase 1
• Antagonism and bistability in protein interaction networks
• Switching dynamics and the transient memory storage in a model enzyme network involving \(\text{Ca}^{2+}\)/calmodulin-dependent protein kinase II in synapses
• Autophosphorylation and the dynamics of the activation of Lck

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