Imperial College London

Krishnan

Faculty of EngineeringDepartment of Chemical Engineering

Senior Lecturer
 
 
 
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Contact

 

+44 (0)20 7594 6633j.krishnan

 
 
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Location

 

C503Roderic Hill BuildingSouth Kensington Campus

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Summary

 

Publications

Citation

BibTex format

@article{Suwanmajo:2018,
author = {Suwanmajo, T and Krishnan, J},
journal = {Interface},
title = {Exploring the intrinsic kinetics of multisite phosphorylation as part of signalling pathways},
url = {http://hdl.handle.net/10044/1/60297},
year = {2018}
}

RIS format (EndNote, RefMan)

TY  - JOUR
AB - Multisite phosphorylation is a basic way of chemically encoding substrate function and a recurringfeature of cell signalling pathways. A number of studies have explored information processingcharacteristics of multisite phosphorylation, through studies of the intrinsic kinetics. Many of thesestudies focus on the module in isolation. In this paper we build a bridge to connect the behaviour ofmultisite modification in isolation to that as part of pathways. We study the effect of activation of theenzymes (which are basic ways in which the module may be regulated), as well the effects of themodified substrates being involved in further modifications or exiting reaction compartments. Wefind that these effects can induce multiple kinds of transitions, including to behaviour not seenintrinsically in the multisite modification module. We then build on these insights to investigate howthese multisite modification systems can be tuned by enzyme activation to realize a range ofinformation processing outcomes for the design of synthetic phosphorylation circuits. Connecting thecomplexity of multisite modification kinetics, with the pathways in which they are embedded, servesas a basis for teasing out many aspects of their interaction, providing insights of relevance in systemsbiology, synthetic biology/chemistry and chemical information processing.
AU - Suwanmajo,T
AU - Krishnan,J
PY - 2018///
SN - 1742-5662
TI - Exploring the intrinsic kinetics of multisite phosphorylation as part of signalling pathways
T2 - Interface
UR - http://hdl.handle.net/10044/1/60297
ER -