The following articles (labelled with PubMed ID or TBD) are for your review
PMID | Data | Article Title | Organization |
28249207 |
78 |
Discovery of benzofuran-3(2H)-one derivatives as novel DRAK2 inhibitors that protect islet?-cells from apoptosis. |
East China Normal University |
27391133 |
76 |
Discovery of a Selective Aurora A Kinase Inhibitor by Virtual Screening. |
University Of Berne |
26985319 |
36 |
Potent and Selective CK2 Kinase Inhibitors with Effects on Wnt Pathway Signaling in Vivo. |
Astrazeneca |
27106709 |
92 |
Discovery of indirubin derivatives as new class of DRAK2 inhibitors from high throughput screening. |
Korea Research Institute Of Chemical Technology |
26762835 |
342 |
Discovery of 2-(1H-indol-5-ylamino)-6-(2,4-difluorophenylsulfonyl)-8-methylpyrido[2,3-d]pyrimidin-7(8H)-one (7ao) as a potent selective inhibitor of Polo like kinase 2 (PLK2). |
Icahn School Of Medicine At Mount Sinai |
23352510 |
37 |
Development of amino-pyrimidine inhibitors of c-Jun N-terminal kinase (JNK): kinase profiling guided optimization of a 1,2,3-benzotriazole lead. |
Roche Palo Alto |
23394126 |
170 |
Discovery of a novel class of highly potent, selective, ATP-competitive, and orally bioavailable inhibitors of the mammalian target of rapamycin (mTOR). |
Exelixis |
23142618 |
66 |
Discovery of a novel series of 4-quinolone JNK inhibitors. |
Roche Palo Alto |
18183025 |
12060 |
A quantitative analysis of kinase inhibitor selectivity. |
Ambit Biosciences |
18077425 |
197 |
Identification of genotype-correlated sensitivity to selective kinase inhibitors by using high-throughput tumor cell line profiling. |
Harvard Medical School |
22037378 |
31824 |
Comprehensive analysis of kinase inhibitor selectivity. |
Ambit Biosciences |
19654408 |
2521 |
AC220 is a uniquely potent and selective inhibitor of FLT3 for the treatment of acute myeloid leukemia (AML). |
Ambit Biosciences |
15711537 |
653 |
A small molecule-kinase interaction map for clinical kinase inhibitors. |
Ambit Biosciences |
20979384 |
35 |
Characterization of nicotinamidases: steady state kinetic parameters, classwide inhibition by nicotinaldehydes, and catalytic mechanism. |
Cornell University |