Linked Life Data

17311425

Source:http://linkedlifedata.com/resource/pubmed/id/17311425

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
2007-3-20
pubmed:abstractText
The allosteric reaction of protein kinase A (PKA) upon binding of cyclic AMP (cAMP) is revealed with an electrochemical technique through the redox current change of an electrochemically active marker. The different effect of cAMP's regulation at a distinct concentration level is obtained in this system. The influence of structural analogues is also examined with respect to the affinity and special selectivity. This study presents an electrochemical approach to the rapid and sensitive investigation of the protein-ligand interaction in the signal transduction networks.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0743-7463
pubmed:author
pubmed:issnType
Print
pubmed:day
27
pubmed:volume
23
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
3506-8
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
2007
pubmed:articleTitle
Electrochemical evaluation of self-disassociation of PKA upon activation by cAMP.
pubmed:affiliation
Department of Biochemistry and National Key Laboratory of Pharmaceutical Biotechnology, Nanjing University, Nanjing 210093, PR China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't