Document Detail

Development of inhibitors for protein tyrosine kinases.
MedLine Citation:
PMID:  11114749     Owner:  NLM     Status:  MEDLINE    
In the last 5 years, through combinatorial chemistry, high-throughput screening, computational chemistry, and traditional medicinal chemistry, numerous inhibitors for various protein tyrosine kinases (PTKs) have been developed. The majority of these compounds are small molecules that compete at the ATP binding site of the catalytic domain of the enzymes. Some compounds such as pseudosubstrate-based peptide inhibitor binds to the peptide/protein substrate site of the catalytic domain. Some inhibitors, primarily monoclonal antibodies, bind to the extracellular domain of receptor tyrosine kinases. Some of these inhibitors are highly potent and selective. Several are currently undergoing clinical trials for a number of diseases such as cancer.
F A Al-Obeidi; K S Lam
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Publication Detail:
Type:  Journal Article; Research Support, U.S. Gov't, Non-P.H.S.; Review    
Journal Detail:
Title:  Oncogene     Volume:  19     ISSN:  0950-9232     ISO Abbreviation:  Oncogene     Publication Date:  2000 Nov 
Date Detail:
Created Date:  2000-12-18     Completed Date:  2001-01-11     Revised Date:  2009-11-19    
Medline Journal Info:
Nlm Unique ID:  8711562     Medline TA:  Oncogene     Country:  ENGLAND    
Other Details:
Languages:  eng     Pagination:  5690-701     Citation Subset:  IM    
Selectide Corporation, A Subsidiary of Avantis., 1580 E. Hanely Blvd., Tucson, Arizona, AZ 85737, USA.
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MeSH Terms
Catalytic Domain
Combinatorial Chemistry Techniques
Enzyme Inhibitors / chemical synthesis,  pharmacology*
Protein-Tyrosine Kinases / antagonists & inhibitors*,  metabolism
Reg. No./Substance:
0/Enzyme Inhibitors; EC Kinases

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