Much attention has been paid recently to bistability and switch-like
behavior that might be resident in important biochemical reaction
networks. There is, in fact, a great deal of subtlety in the relationship
between the structure of a reaction network and its capacity to engender
bistability. In common physicochemical settings, large classes of
extremely complex networks, taken with mass action kinetics, cannot
give rise to bistability no matter what values the rate constants
take. On the other hand, bistable behavior can be induced in those
same settings by certain very simple and classical mass action mechanisms
for enzyme catalysis of a single overall reaction. We present a theorem
that distinguishes between those mass action networks that might
support bistable behavior and those that cannot. Moreover, we indicate
how switch-like behavior results from a well-studied mechanism for
the action of human dihydrofolate reductase, an important anti-cancer
target.
%0 Journal Article
%1 Crac_2006_8697
%A Craciun, Gheorghe
%A Tang, Yangzhong
%A Feinberg, Martin
%D 2006
%J Proc. Natl. Acad. Sci. U. S. A.
%K Dehydrogenase Enzyme Gov't, Humans; Non-P.H.S.; Research Stability; Support, Tetrahydrofolate U.S.
%N 23
%P 8697--8702
%R 10.1073/pnas.0602767103
%T Understanding bistability in complex enzyme-driven reaction networks.
%U http://dx.doi.org/10.1073/pnas.0602767103
%V 103
%X Much attention has been paid recently to bistability and switch-like
behavior that might be resident in important biochemical reaction
networks. There is, in fact, a great deal of subtlety in the relationship
between the structure of a reaction network and its capacity to engender
bistability. In common physicochemical settings, large classes of
extremely complex networks, taken with mass action kinetics, cannot
give rise to bistability no matter what values the rate constants
take. On the other hand, bistable behavior can be induced in those
same settings by certain very simple and classical mass action mechanisms
for enzyme catalysis of a single overall reaction. We present a theorem
that distinguishes between those mass action networks that might
support bistable behavior and those that cannot. Moreover, we indicate
how switch-like behavior results from a well-studied mechanism for
the action of human dihydrofolate reductase, an important anti-cancer
target.
@article{Crac_2006_8697,
abstract = {Much attention has been paid recently to bistability and switch-like
behavior that might be resident in important biochemical reaction
networks. There is, in fact, a great deal of subtlety in the relationship
between the structure of a reaction network and its capacity to engender
bistability. In common physicochemical settings, large classes of
extremely complex networks, taken with mass action kinetics, cannot
give rise to bistability no matter what values the rate constants
take. On the other hand, bistable behavior can be induced in those
same settings by certain very simple and classical mass action mechanisms
for enzyme catalysis of a single overall reaction. We present a theorem
that distinguishes between those mass action networks that might
support bistable behavior and those that cannot. Moreover, we indicate
how switch-like behavior results from a well-studied mechanism for
the action of human dihydrofolate reductase, an important anti-cancer
target.},
added-at = {2009-06-03T11:20:58.000+0200},
author = {Craciun, Gheorghe and Tang, Yangzhong and Feinberg, Martin},
biburl = {https://www.bibsonomy.org/bibtex/22bbbc55645bcb87e10ecbf4ecb7612af/hake},
description = {The whole bibliography file I use.},
doi = {10.1073/pnas.0602767103},
file = {Crac_2006_8697.pdf:Crac_2006_8697.pdf:PDF},
interhash = {fd8a93b7cf645706c91144a192dfc83c},
intrahash = {2bbbc55645bcb87e10ecbf4ecb7612af},
journal = {Proc. Natl. Acad. Sci. U. S. A.},
keywords = {Dehydrogenase Enzyme Gov't, Humans; Non-P.H.S.; Research Stability; Support, Tetrahydrofolate U.S.},
month = Jun,
number = 23,
pages = {8697--8702},
pii = {0602767103},
pmid = {16735474},
timestamp = {2009-06-03T11:21:09.000+0200},
title = {Understanding bistability in complex enzyme-driven reaction networks.},
url = {http://dx.doi.org/10.1073/pnas.0602767103},
volume = 103,
year = 2006
}