Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
2005-6-22
pubmed:abstractText
The annotation and visualization of medicinally relevant kinase space revealed that kinase inhibitors in the clinic are, on average, of higher molecular weight and more lipophilic than all other clinically investigated drugs. Tyrosine kinases from the vascular endothelial growth factor and epidermal growth factor receptor families are the most pursued targets. Furthermore, oncological indications account for 75% of all kinase-related clinical interest. In addition, analysis of the similarity between kinase targets with respect to sequence, selectivity and structure has revealed that kinases with > or =60% sequence identity are most likely to be inhibited by the same classes of compounds and have similar ATP-binding sites. The identification of this threshold, together with the widely accepted representation of the sequence-based kinase space, is expanding our understanding of the clinical and structural space of the kinome.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
1359-6446
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
10
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
839-46
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Kinomics: characterizing the therapeutically validated kinase space.
pubmed:affiliation
Discovery Chemistry Research, Lilly Research Laboratories, Lilly Corporate Center, DC 1513, Indianapolis, IN 46285, USA. m.vieth@lilly.com
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't