Abstract
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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 5690-5701 |
| Number of pages | 12 |
| Journal | Oncogene |
| Volume | 19 |
| Issue number | 49 |
| State | Published - Nov 20 2000 |
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Keywords
- Cancer therapy
- Clinical studies
- Drug development
- Inhibitors
- Preclinical studies
- Protein tyrosine kinase
ASJC Scopus subject areas
- Molecular Biology
- Cancer Research
- Genetics
Cite this
Development of inhibitors for protein tyrosine kinases. / Al-Obeidi, Fahad A.; Lam, Kit.
In: Oncogene, Vol. 19, No. 49, 20.11.2000, p. 5690-5701.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Development of inhibitors for protein tyrosine kinases
AU - Al-Obeidi, Fahad A.
AU - Lam, Kit
PY - 2000/11/20
Y1 - 2000/11/20
N2 - 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.
AB - 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.
KW - Cancer therapy
KW - Clinical studies
KW - Drug development
KW - Inhibitors
KW - Preclinical studies
KW - Protein tyrosine kinase
UR - http://www.scopus.com/inward/record.url?scp=0034693811&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0034693811&partnerID=8YFLogxK
M3 - Article
C2 - 11114749
AN - SCOPUS:0034693811
VL - 19
SP - 5690
EP - 5701
JO - Oncogene
JF - Oncogene
SN - 0950-9232
IS - 49
ER -