Skip to search formSkip to main content
You are currently offline. Some features of the site may not work correctly.

PD 173955

Known as: PD-173955, PD173955 
 
National Institutes of Health

Related topics

Related topics

2 relations

Broader (2)

PyridonesPyrimidines

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
2018
2018
Abstract 1661: Discovery of potent Abelson kinase inhibitors from the scaffold of pyrano[2,3-d]pyrimidin-7-one
Tyrosine kinases regulate cell proliferation, survival, invasion and angiogenesis during tumor initiation and progression. The… Expand
2017
2017
Chemoproteomics‐Aided Medicinal Chemistry for the Discovery of EPHA2 Inhibitors
The receptor tyrosine kinase EPHA2 has gained attention as a therapeutic drug target for cancer and infectious diseases. However… Expand
2010
2010
New effective inhibitors of the Abelson kinase.
The effects of substituents on the aryl ring were studied by the preparation and testing of several PD173955 analogs. Inserting a… Expand
2008
2008
Induced disorder in protein-ligand complexes as a drug-design strategy.
Protein associations are poorly understood from a chemical perspective. If the contrary were true, drug inhibitors would be… Expand
Highly Cited
2006
Highly Cited
2006
MASPIT: three-hybrid trap for quantitative proteome fingerprinting of small molecule-protein interactions in mammalian cells.
Organic small molecules generally act by perturbing the function of one or more cellular target proteins, the identification of… Expand
2006
2006
Phosphorylation of IkappaB-beta is necessary for neuronal survival.
Cerebellar granule neurons undergo apoptosis when switched from culture medium containing depolarizing levels of potassium (high… Expand
2006
2006
Imprint of evolutionary conservation and protein structure variation on the binding function of protein tyrosine kinases
MOTIVATION According to the models of divergent molecular evolution, the evolvability of new protein function may depend on the… Expand
  • figure 1
  • figure 2
  • figure 3
  • figure 4
2005
2005
Conformational plasticity in drug design: Towards the development of inhibitors of oncogenic fusion proteins with protein tyrosine kinase activity
BMS354825 is a SRC-Abl dual inhibitor active against several imatinib-resistant Bcr-Abl mutants except T315I. BMS354825 has been… Expand
  • figure 1.4
  • figure 1.5
  • figure 1.6
  • table 1.2
  • table 1.2
Highly Cited
2002
Highly Cited
2002
Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI-571).
The inadvertent fusion of the bcr gene with the abl gene results in a constitutively active tyrosine kinase (Bcr-Abl) that… Expand
  • figure 1
  • table 1
  • figure 2
  • figure 3
  • figure 4
Highly Cited
2002
Highly Cited
2002
Characterization of potent inhibitors of the Bcr-Abl and the c-kit receptor tyrosine kinases.
The early stage of chronic myelogenous leukemia (CML) is caused by the tyrosine kinase Bcr-Abl. Imatinib mesylate (also known as… Expand
  • figure 1
  • figure 2
  • table 1
  • figure 3
  • figure 5
By clicking accept or continuing to use the site, you agree to the terms outlined in our Privacy Policy, Terms of Service, and Dataset License
ACCEPT & CONTINUE