Hematology

Download Chronic Myeloid Leukemia: Biology and Treatment by Angelo M Carella, George Q Daley, Connie J. Eaves, John M PDF

By Angelo M Carella, George Q Daley, Connie J. Eaves, John M Goldman, Hehlmann Rudiger

During this quantity, a global staff of specialists in power myeloid leukemia proportion their services. particularly, they give a contribution their insights at the most recent advances in knowing this disorder, and the results these advancements have for its administration. They discover many subject matters, together with a evaluate of molecular and mobile biology, dialogue of traditional chemotherapy and interferon remedy, and up to date advancements in allografting and autografting. The reader profits not just an incisive view of the organic constitution of the disorder, yet functions of that biology to therapy modalities. power Myeloid Leukemia is perfect for oncologists and different experts within the box.

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53. oligomerization domain. J Biol Chem 1996; 271: 15353–7. Okuda K, D’Andrea A, Van Etten RA, Griffin JD, A chimeric receptor/oncogene that can be regulated by a ligand in vitro and in vivo. J Clin Invest 1997; 100: 1708–15. Papadopoulos P, Ridge SA, Boucher CA et al, The novel activation of ABL by fusion to an etsrelated gene, TEL. Cancer Res 1995; 55: 34–8. Hannemann JR, McManus DM, Kabarowski JH, Wiedemann LM, Haemopoietic transformation by the TEL/ABL oncogene. Br J Haematol 1998; 102: 475–85.

Lukasova E, Kozubek S, Kozubek M et al, Localization and distance between ABL and BCR genes in interphase nuclei of bone marrow cells of control donors and patients with chronic myeloid leukaemia. Hum Genet 1997; 100: 525–35. Neves H, Ramos C, da Silva MG et al, The nuclear topography of ABL, BCR, PML, and RARalpha genes: evidence for gene proximity in specific phases of the cell cycle and stages of hematopoietic differentiation. Blood 1999; 93: 1197–207. Li WJ, Dreazen O, Kloetzer W et al, 14 28.

Among candidate proteins that function to recruit Grb2 and activate Ras in cells expressing BCR/ABL are the Shc adaptor protein and the SHP-2 protein tyrosine phosphatase. 62,86,89 Regardless, tyrosine-phosphorylated Shc may provide for an alternative route, linking BCR/ABL to Ras. 48 However, demonstration of a direct requirement for Shc in BCR/ABL signaling and transformation will require the use of Shc dominant-negative mutants in cells expressing BCR/ABL. 90 It is not yet known whether SHP-2 is required for BCR/ABL-dependent Ras activation and transformation.

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