bosutinib has been researched along with Neoplasms* in 2 studies
1 review(s) available for bosutinib and Neoplasms
| Article | Year |
|---|---|
AXL Inhibitors in Cancer: A Medicinal Chemistry Perspective.
Dysregulation of the AXL receptor tyrosine kinase has been associated with many types of cancer. It has not been until recently, however, that targeting AXL has come under the spotlight because of ever accumulating evidence of its strong correlation with poor prognosis and drug resistance. The entry of the first AXL-branded inhibitor in clinical trials in 2013 marked an important milestone for the clinical validation of AXL as an anticancer target. Nevertheless, to weigh the current contribution and potential future impact of AXL inhibition in the clinic, it is fundamental to recognize that several kinase inhibitors approved or in clinical development have AXL as either a prominent secondary or even the primary target. Through this review, the chemical and biological properties of the main inhibitors targeting AXL (either intentionally or unintentionally) will be discussed, along with the prospects and challenges to translate AXL inhibitors into a bona fide therapeutic option. Topics: Axl Receptor Tyrosine Kinase; Chemistry, Pharmaceutical; Humans; Neoplasms; Protein Kinase Inhibitors; Proto-Oncogene Proteins; Receptor Protein-Tyrosine Kinases | 2016 |
1 other study(ies) available for bosutinib and Neoplasms
| Article | Year |
|---|---|
Development of novel ACK1/TNK2 inhibitors using a fragment-based approach.
The tyrosine kinase ACK1, a critical signal transducer regulating survival of hormone-refractory cancers, is an important therapeutic target, for which there are no selective inhibitors in clinical trials to date. This work reports the discovery of novel and potent inhibitors for ACK1 tyrosine kinase (also known as TNK2) using an innovative fragment-based approach. Focused libraries were designed and synthesized by selecting fragments from reported ACK inhibitors to create hybrid structures in a mix and match process. The hybrid library was screened by enzyme-linked immunosorbent assay-based kinase inhibition and (33)P HotSpot assays. Systematic structure-activity relationship studies led to the identification of compound (R)-9b, which shows potent in vitro (IC50 = 56 nM, n = 3, (33)P HotSpot assay) and in vivo (IC50 < 2 μM, human cancer cell lines) ACK1 inhibition. Both (R)-9b and (S)-9b were stable in human plasma and displayed a long half-life (t(1/2) > 6 h). Topics: Antineoplastic Agents; Cell Line, Tumor; Drug Design; Humans; Molecular Docking Simulation; Neoplasms; Protein Kinase Inhibitors; Protein-Tyrosine Kinases; Small Molecule Libraries; Structure-Activity Relationship | 2015 |