CBL mutation-related patterns of phosphorylation and sensitivity to tyrosine kinase inhibitors
نویسندگان
چکیده
منابع مشابه
Myeloproliferative Neoplasms Associated with Mutation in JAK2V617F and Tyrosine Kinase Inhibitors as Therapeutic Strategy
MPNs including a heterogeneous group of clonal or oligoclonal hamtopathies characterized by proliferation and accumulation of mature myeloid cells. JAK2 tyrosine kinase mutation is the most common molecular lesion identified in 90% of cases. JAK2 is involved in EPO signaling pathway, and mutations in it lead to EPO-independent spontaneous phosphorylation. Most tyrosine kinase inhibitors (TKI) a...
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Background: When Staphylococcus aureus is grown in the presence of high concentration of external glucose, this sugar is phosphorylated by glucokinase (glkA) to form glucose-6-phosphate. This product subsequently enters into anabolic phase, which favors biofilm formation. The presence of ROK (repressor protein, open reading frame, sugar kinase) motif, phosphate-1 and -2 sites, and tyrosine kina...
متن کاملmyeloproliferative neoplasms associated with mutation in jak2v617f and tyrosine kinase inhibitors as therapeutic strategy
mpns including a heterogeneous group of clonal or oligoclonal hamtopathies characterized by proliferation and accumulation of mature myeloid cells. jak2 tyrosine kinase mutation is the most common molecular lesion identified in 90% of cases. jak2 is involved in epo signaling pathway, and mutations in it lead to epo-independent spontaneous phosphorylation. most tyrosine kinase inhibitors (tki) a...
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FMS-like tyrosine kinase-3 is a receptor tyrosine kinase expressed by immature hematopoietic cells and is important for the normal development of stem cells and the immune system. Mutations of FMS-like tyrosine kinase-3 have been detected in about 30% of patients with acute myelogenous leukemia and a small number of patients with acute lymphoblastic leukemia. The FMS-like tyrosine kinase-3 muta...
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ژورنال
عنوان ژورنال: Leukemia
سال: 2012
ISSN: 0887-6924,1476-5551
DOI: 10.1038/leu.2012.7