作者
Eduard Sergienko, Ekaterina Bobkova, Sharon Colayco, Justin Rascon, Xochella Chan, Stefan Vasile, Ying Su, Russell Dahl, Thomas DY Chung, Shakeela Dad, Tomas Mustelin, Wallace Liu, David A Critton, Rebecca Page, Lutz Tautz
发表日期
2010/10/4
来源
Probe Reports from the NIH Molecular Libraries Program [Internet]
出版商
National Center for Biotechnology Information (US)
简介
Tyrosine phosphorylation is a key mechanism for signal transduction and the regulation of a broad set of physiological processes characteristic of multicellular organisms. Hematopoietic protein tyrosine phosphate (HePTP) is a tyrosine phosphatase expressed in hematopoietic cells with specificity for the dephosphorylation of Erk and p38 MAP kinases (MAPKs). It has been found that HePTP is often dysregulated in the preleukemic disorder myelodysplastic syndrome, as well as in acute myelogeneous leukemia. The identified probe ML120 (CID-4302116) selectively inhibits HePTP activity. Since this probe scaffold was discovered through its activity in the HePTP assays with small molecule substrates, it is proposed that this inhibition occurs through direct targeting of the HePTP active site. No time-dependent inhibition is observed as demonstrated by the linear progress curves of the HePTP phosphatase reaction in …
学术搜索中的文章
E Sergienko, E Bobkova, S Colayco, J Rascon, X Chan… - Probe Reports from the NIH Molecular Libraries …, 2010