Reciprocal enzyme regulation as a source of bistability in covalent modification cycles
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Publication:2635032
DOI10.1016/j.jtbi.2013.04.002zbMath1330.92053OpenAlexW2137260477WikidataQ51069904 ScholiaQ51069904MaRDI QIDQ2635032
Ronny Straube, Carsten Conradi
Publication date: 11 February 2016
Published in: Journal of Theoretical Biology (Search for Journal in Brave)
Full work available at URL: https://doi.org/10.1016/j.jtbi.2013.04.002
symmetrymodularitytotal quasi-steady state approximationpost-translational modificationallosteric regulation
Related Items (2)
A novel transient phase kinetic analysis of the fractional modification of monocyclic enzyme cascades ⋮ Bifunctional enzyme provides absolute concentration robustness in multisite covalent modification networks
Cites Work
- On the validity of the steady state assumption of enzyme kinetics
- Extending the quasi-steady state approximation by changing variables
- The total quasi-steady-state approximation is valid for reversible enzyme kinetics
- Reduced models of networks of coupled enzymatic reactions
- The Quasi-Steady-State Assumption: A Case Study in Perturbation
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