Linked Life Data

14759520

Source:http://linkedlifedata.com/resource/pubmed/id/14759520

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-3
pubmed:dateCreated
2004-2-4
pubmed:abstractText
A steady-state framework was applied to the ubiquitous tricyclic enzyme cascade structure, as seen in the mitogen-activated protein (MAP) kinase system, to analyze the effect of upstream kinase concentrations on final output response. The results suggest that signal amplification achieved by the cascade structure ensured that the modifying enzymes at various steps of the cascade were nearly saturated. Thus, there was no change in the response sensitivity with increasing upstream kinase concentration. Analysis was also extended to branching of a signaling pathway as an example of cross-talk. It was observed that the cascade structure confers a larger share of the signal transduction properties to its last kinase. This phenomenon in enzyme cascades may explain how the response of the terminal MAP kinase is unaffected by cross-talk of upstream kinases.
pubmed:commentsCorrections
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0014-5793
pubmed:author
pubmed:issnType
Print
pubmed:day
30
pubmed:volume
558
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
79-84
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Robust global sensitivity in multiple enzyme cascade system explains how the downstream cascade structure may remain unaffected by cross-talk.
pubmed:affiliation
Department of Chemical Engineering, Indian Institute of Technology Bombay, Powai, Mumbai-400076, India.
pubmed:publicationType
Journal Article