R. Roskoski and . Jr, Signaling by Kit protein-tyrosine kinase???The stem cell factor receptor, Biochemical and Biophysical Research Communications, vol.337, issue.1, pp.1-13, 2005.
DOI : 10.1016/j.bbrc.2005.08.055

V. Broudy, Stem cell factor and hematopoiesis, Blood, vol.90, pp.1345-64, 1997.

L. Reber, D. Silva, C. Frossard, and N. , Stem cell factor and its receptor c-Kit as targets for inflammatory diseases, European Journal of Pharmacology, vol.533, issue.1-3, pp.327-367, 2006.
DOI : 10.1016/j.ejphar.2005.12.067

J. Lennarttson, T. Jelacic, D. Linnekin, and R. Shivakrupa, Normal and Oncogenic Forms of the Receptor Tyrosine Kinase Kit, Stem Cells, vol.14, issue.1, pp.16-43, 2005.
DOI : 10.1634/stemcells.2004-0117

A. Orfao, A. Garcia-montero, L. Sanchez, and L. Escribano, Recent advances in the understanding of mastocytosis: the role of KIT mutations, British Journal of Haematology, vol.30, issue.1, pp.12-30, 2007.
DOI : 10.1073/pnas.97.14.7732

A. Arora and E. Scholar, Role of Tyrosine Kinase Inhibitors in Cancer Therapy, Journal of Pharmacology and Experimental Therapeutics, vol.315, issue.3, pp.971-980, 2005.
DOI : 10.1124/jpet.105.084145

E. Buchdunger, J. Zimmermann, H. Mett, T. Meyer, and M. Muller, Selective inhibition of the platelet-derived growth factor signal transduction pathway by a protein-tyrosine kinase inhibitor of the 2-phenylaminopyrimidine class., Proceedings of the National Academy of Sciences, vol.92, issue.7, pp.2558-62, 1995.
DOI : 10.1073/pnas.92.7.2558

E. Buchdunger, J. Zimmermann, H. Mett, T. Meyer, and M. Muller, Inhibition of the Abl protein-tyrosine kinase in vitro and in vivo by a 2- phenylaminopyrimidine derivative, Cancer Res, vol.56, pp.100-104, 1996.

A. Dewar, A. Cambareri, A. Zannettino, B. Miller, and K. Doherty, Macrophage colony-stimulating factor receptor c-fms is a novel target of imatinib, Blood, vol.105, issue.8, pp.3127-3159, 2005.
DOI : 10.1182/blood-2004-10-3967

S. Atwell, J. Adams, J. Badger, M. Buchanan, and I. Feil, A Novel Mode of Gleevec Binding Is Revealed by the Structure of Spleen Tyrosine Kinase, Journal of Biological Chemistry, vol.279, issue.53, pp.55827-55859, 2004.
DOI : 10.1074/jbc.M409792200

B. Rubin and A. Duensing, Mechanisms of resistance to small molecule kinase inhibition in the treatment of solid tumors, Laboratory Investigation, vol.23, issue.10, pp.981-987, 2006.
DOI : 10.1182/blood.V101.2.690

Y. Ma, S. Zeng, D. Metcalfe, C. Akin, and S. Dimitrijevic, The c-KIT mutation causing human mastocytosis is resistant to STI571 and other KIT kinase inhibitors; kinases with enzymatic site mutations show different inhibitor sensitivity profiles than wild-type kinases and those with regulatory-type mutations, Blood, vol.99, issue.5, pp.1741-1745, 2002.
DOI : 10.1182/blood.V99.5.1741

S. Ueda, H. Ikeda, M. Mizuki, J. Ishiko, and I. Matsumura, Constitutive Activation of C-kit by the Juxtamembrane but Not the Catalytic Domain Mutations Is Inhibited Selectively by Tyrosine Kinase Inhibitors STI571 and AG1296, International Journal of Hematology, vol.36, issue.5, pp.427-462, 2002.
DOI : 10.1007/BF02982808

R. Kerkela, L. Grazette, R. Yacobi, C. Iliescu, and R. Patten, Cardiotoxicity of the cancer therapeutic agent imatinib mesylate, Nature Medicine, vol.9, issue.8, pp.908-924, 2006.
DOI : 10.1038/nm1446

A. Fernandez, A. Sanguino, Z. Peng, E. Ozturk, and J. Chen, An anticancer C-Kit kinase inhibitor is reengineered to make it more active and less cardiotoxic, Journal of Clinical Investigation, vol.117, issue.12, pp.4044-54, 2007.
DOI : 10.1172/JCI32373DS1

H. Kitayama, Y. Kanakura, T. Furitsu, T. Tsujimura, and K. Oritani, Constitutively activating mutations of c-kit receptor tyrosine kinase confer factorindependent growth and tumourigenicity of factor-dependent hematopoietic cell lines, Blood, vol.85, pp.790-798, 1995.

C. Meininger, H. Yano, R. Rottapel, A. Bernstein, and K. Zsebo, The ckit receptor ligand functions as a mast cell chemoattractant, Blood, vol.79, pp.958-63, 1992.

N. Casteran, D. Sepulveda, P. Beslu, N. Aoubala, M. Letard et al., Signal transduction by several KIT juxtamembrane domain mutations, Oncogene, vol.22, issue.30, pp.4710-4732, 2003.
DOI : 10.1038/sj.onc.1206587

T. Tsujimura, M. Morimoto, K. Hashimoto, Y. Moriyama, and H. Kitayama, Constitutive activation of c-kit in FMA3 murine mastocytoma cells caused by deletion of seven amino acids at the juxtamembrane domain, Blood, vol.87, pp.273-83, 1996.

B. Nagar, W. Bornmann, P. Pellicena, T. Schindler, and D. Veach, Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI-571), Cancer Res, vol.62, pp.4236-4279, 2002.

C. Mol, D. Dougan, T. Schneider, R. Skene, and M. Kraus, Structural Basis for the Autoinhibition and STI-571 Inhibition of c-Kit Tyrosine Kinase, Journal of Biological Chemistry, vol.279, issue.30, pp.31655-63, 2004.
DOI : 10.1074/jbc.M403319200

S. Wilhelm, C. Carter, L. Tang, D. Wilkie, and A. Mcnabola, BAY 43-9006 Exhibits Broad Spectrum Oral Antitumor Activity and Targets the RAF/MEK/ERK Pathway and Receptor Tyrosine Kinases Involved in Tumor Progression and Angiogenesis, Cancer Research, vol.64, issue.19, pp.7099-109, 2004.
DOI : 10.1158/0008-5472.CAN-04-1443

D. Mendel, A. Laird, X. Xin, S. Louie, and J. Christensen, In vivo antitumour activity of SU11248, a novel tyrosine kinase inhibitor targeting vascular endothelial growth factor and platelet-derived growth factor receptors: determination of a pharmacokinetic/pharmacodynamic relationship, Clin Cancer Res, vol.9, pp.327-364, 2003.

I. Shchemelinin, L. Sefc, and E. Necas, Protein kinase inhibitors, Folia Biol (Praha), vol.52, pp.137-185, 2006.

Y. Zermati, D. Sepulveda, P. Feger, F. Letard, S. Kersual et al., Effect of tyrosine kinase inhibitor STI571 on the kinase activity of wild-type and various mutated c-kit receptors found in mast cell neoplasms, Oncogene, vol.22, issue.5, pp.660-664, 2003.
DOI : 10.1038/sj.onc.1206120

URL : https://hal.archives-ouvertes.fr/hal-00282566

M. Frost, P. Ferrao, T. Hughes, and L. Ashman, Juxtamembrane mutant V560GKit is more sensitive to Imatinib (STI571) compared with wild-type c-kit whereas the kinase domain mutant D816VKit is resistant, Mol Cancer Ther, vol.1, pp.1115-1139, 2002.

J. Cools, D. Deangelo, J. Gotlib, E. Stover, and R. Legare, Genes as a Therapeutic Target of Imatinib in Idiopathic Hypereosinophilic Syndrome, New England Journal of Medicine, vol.348, issue.13, pp.1201-1215, 2003.
DOI : 10.1056/NEJMoa025217

K. Hahn, G. Oglivie, T. Rusk, P. Devauchelle, and A. Leblanc, Masitinib is Safe and Effective for the Treatment of Canine Mast Cell Tumors, Journal of Veterinary Internal Medicine, vol.22, issue.6, pp.1301-1309, 2008.
DOI : 10.1111/j.1939-1676.2008.0190.x

M. Gabillot-carre, Y. Lepelletier, M. Humbert, P. De-sepuvelda, and N. Hamouda, Rapamycin inhibits growth and survival of D816V-mutated c-kit mast cells, Blood, vol.108, issue.3, pp.1065-72, 2006.
DOI : 10.1182/blood-2005-06-2433

URL : https://hal.archives-ouvertes.fr/hal-00282505

B. Royer, S. Varadaradjalou, P. Saas, A. Gabiot, and B. Kantelip, Autocrine regulation of cord blood???derived human mast cell activation by IL-10???, Journal of Allergy and Clinical Immunology, vol.108, issue.1, pp.80-86, 2001.
DOI : 10.1067/mai.2001.115753

E. Razin, J. Mencia-huerta, R. Stevens, R. Lewis, and F. Liu, IgE-mediated release of leukotriene C4, chondroitin sulfate E proteoglycan, beta-hexosaminidase, and histamine from cultured bone marrow-derived mouse mast cells, Journal of Experimental Medicine, vol.157, issue.1, pp.189-201, 1983.
DOI : 10.1084/jem.157.1.189

Y. Zou, A. Kottmann, M. Kuroda, I. Taniuchi, and D. Littman, Function of the chemokine receptor CXCR4 in haematopoiesis and in cerebellar development, Nature, vol.140, issue.6685, pp.595-604, 1998.
DOI : 10.1038/31269

R. Wang, Y. Lu, and S. Wang, Comparative Evaluation of 11 Scoring Functions for Molecular Docking, Journal of Medicinal Chemistry, vol.46, issue.12, pp.2287-303, 2003.
DOI : 10.1021/jm0203783