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Volumn 20, Issue 11, 2010, Pages 1457-1470

Bruton's tyrosine kinase as a molecular target in treatment of leukemias and lymphomas as well as inflammatory disorders and autoimmunity

Author keywords

Bruton's tyrosine kinase; graft versus host disease; inflammatory disorders; leukemia; lymphoma; rational drug design; thromboembolism

Indexed keywords

2 CYANO N (2,5 DIBROMOPHENYL) 3 HYDROXYCROTONAMIDE; AVL 101; AVL 291; BRUTON TYROSINE KINASE; DASATINIB; PCI 32765; PROTEIN TYROSINE KINASE INHIBITOR; UNCLASSIFIED DRUG;

EID: 77958497298     PISSN: 13543776     EISSN: None     Source Type: Journal    
DOI: 10.1517/13543776.2010.517750     Document Type: Review
Times cited : (25)

References (146)
  • 1
    • 0037032835 scopus 로고    scopus 로고
    • The protein kinase complement of the human genome
    • Manning G, Whyte DB, Martinez R, et al. The protein kinase complement of the human genome. Science 2002;298:1912-34
    • (2002) Science , vol.298 , pp. 1912-34
    • Manning, G.1    Whyte, D.B.2    Martinez, R.3
  • 3
    • 0037399412 scopus 로고    scopus 로고
    • Tyrosine kinases as targets in cancer therapy-successes and failures
    • Traxler P. Tyrosine kinases as targets in cancer therapy-successes and failures. Expert Opin Ther Targets 2003;7:215-25
    • (2003) Expert Opin Ther Targets , vol.7 , pp. 215-25
    • Traxler, P.1
  • 4
    • 13844316734 scopus 로고    scopus 로고
    • Kurzrock R Tyrosine kinase inhibitors and the dawn of molecular cancer therapeutics
    • Tibes R, Trent J, Kurzrock R Tyrosine kinase inhibitors and the dawn of molecular cancer therapeutics. Annu Rev Pharmacol Toxicol 2005;45:357-63
    • (2005) Annu Rev Pharmacol Toxicol , vol.45 , pp. 357-63
    • Tibes, R.1    Trent, J.2
  • 5
    • 22044442973 scopus 로고    scopus 로고
    • Tyrosine kinases as targets for cancer therapy
    • Krause DS, Van Etten RA. Tyrosine kinases as targets for cancer therapy. N Engl J Med 2005;353:172-7
    • (2005) N Engl J Med , vol.353 , pp. 172-7
    • Krause, D.S.1    Van Etten, R.A.2
  • 6
    • 27544479318 scopus 로고    scopus 로고
    • Role of tyrosine kinase inhibitors in cancer therapy
    • Arora A, and Scholar EM. Role of tyrosine kinase inhibitors in cancer therapy. J Pharmacol Exp Ther 2005;315:971-9
    • (2005) J Pharmacol Exp Ther , vol.315 , pp. 971-9
    • Arora, A.1    Scholar, E.M.2
  • 7
    • 0033053383 scopus 로고    scopus 로고
    • Structure-based design of specific inhibitors of Janus kinase 3 as apoptosis-inducing antileukemic agents
    • Sudbeck EA, Liu XP, Narla RK, et al. Structure-based design of specific inhibitors of Janus kinase 3 as apoptosis-inducing antileukemic agents. Clin Cancer Res 1999;5:1569-82
    • (1999) Clin Cancer Res , vol.5 , pp. 1569-82
    • Sudbeck, E.A.1    Liu, X.P.2    Narla, R.K.3
  • 8
    • 0033515450 scopus 로고    scopus 로고
    • Rational design and synthesis of a novel anti-leukemic agent targeting Bruton's tyrosine kinase (BTK), LFM-A13 [alpha-cyano-beta-hydroxy-beta-methyl-N- (2, 5-dibromophenyl) propenamide]
    • Mahajan S, Ghosh S, Sudbeck EA, Uckun FM. Rational design and synthesis of a novel anti-leukemic agent targeting Bruton's tyrosine kinase (BTK), LFM-A13 [alpha-cyano-beta-hydroxy-beta-methyl-N-(2, 5-dibromophenyl) propenamide]. J Biol Chem 1999;274:9587-93
    • (1999) J Biol Chem , vol.274 , pp. 9587-93
    • Mahajan, S.1    Ghosh, S.2    Sudbeck, E.A.3    Uckun, F.M.4
  • 9
    • 0034693754 scopus 로고    scopus 로고
    • Signaling network of the Btk family kinases
    • Qiu Y, Kung HJ. Signaling network of the Btk family kinases. Oncogene 2000;19:5651-5
    • (2000) Oncogene , vol.19 , pp. 5651-5
    • Qiu, Y.1    Kung, H.J.2
  • 10
    • 61849141064 scopus 로고    scopus 로고
    • Tyrosine kinases and their substrates in B lymphocytes
    • Kurosaki T, Hikida M. Tyrosine kinases and their substrates in B lymphocytes. Immunol Rev 2009;228:132-48
    • (2009) Immunol Rev , vol.228 , pp. 132-48
    • Kurosaki, T.1    Hikida, M.2
  • 11
    • 0031708849 scopus 로고    scopus 로고
    • Bruton's tyrosine kinase (BTK) as a dual-function regulator of apoptosis
    • Uckun FM. Bruton's tyrosine kinase (BTK) as a dual-function regulator of apoptosis. Biochem Pharmacol 1998;56:683-99
    • (1998) Biochem Pharmacol , vol.56 , pp. 683-99
    • Uckun, F.M.1
  • 12
    • 0036676540 scopus 로고    scopus 로고
    • Beyond calcium: New signaling pathways for TEC family kinases
    • Takesono A, Finkelstein, LD, Schwartzberg PL. Beyond calcium: new signaling pathways for TEC family kinases. J Cell Sci 2002;115:3039-48
    • (2002) J Cell Sci , vol.115 , pp. 3039-48
    • Takesono, A.1    Finkelstein, L.D.2    Schwartzberg, P.L.3
  • 14
    • 4143074805 scopus 로고    scopus 로고
    • TEC kinases: Shaping T-cell activation through actin
    • Finkelstein LD, Schwartzberg PL. TEC kinases: shaping T-cell activation through actin. Trends Cell Biol 2004;14:443-51
    • (2004) Trends Cell Biol , vol.14 , pp. 443-51
    • Finkelstein, L.D.1    Schwartzberg, P.L.2
  • 15
    • 1842299315 scopus 로고    scopus 로고
    • Direct stimulation of Bruton's tyrosine kinase by G(q)-protein alpha-subunit
    • Bence K, Ma W, Kozasa T, Huang XY. Direct stimulation of Bruton's tyrosine kinase by G(q)-protein alpha-subunit. Nature 1997;389:296-9
    • (1997) Nature , vol.389 , pp. 296-9
    • Bence, K.1    Ma, W.2    Kozasa, T.3    Huang, X.Y.4
  • 16
    • 0029824848 scopus 로고    scopus 로고
    • Mutation of the pleckstrin homology domain of Bruton's tyrosine kinase in immunodeficiency impaired inositol 1, 3, 4,5-tetrakisphosphate binding capacity
    • Fukuda M, Kojima T, Kabayama H, Mikoshiba K. Mutation of the pleckstrin homology domain of Bruton's tyrosine kinase in immunodeficiency impaired inositol 1,3,4,5-tetrakisphosphate binding capacity. J Biol Chem 1996;271(48):30303-6
    • (1996) J Biol Chem , vol.271 , Issue.48 , pp. 30303-6
    • Fukuda, M.1    Kojima, T.2    Kabayama, H.3    Mikoshiba, K.4
  • 17
    • 0031577297 scopus 로고    scopus 로고
    • Characterization of the pleckstrin homology domain of Btk as an inositol polyphosphate and phosphoinositide binding domain
    • Kojima T, Fukuda M, Watanabe Y, et al. Characterization of the pleckstrin homology domain of Btk as an inositol polyphosphate and phosphoinositide binding domain. Biochem Biophys Res Commun 1997;236:333-9
    • (1997) Biochem Biophys Res Commun , vol.236 , pp. 333-9
    • Kojima, T.1    Fukuda, M.2    Watanabe, Y.3
  • 18
    • 10544219605 scopus 로고    scopus 로고
    • Distinct specificity in the recognition of phosphoinositides by the pleckstrin homology domains of dynamin and Bruton's tyrosine kinase
    • Salim K, Bottomley MJ, Querfurth E, et al. Distinct specificity in the recognition of phosphoinositides by the pleckstrin homology domains of dynamin and Bruton's tyrosine kinase. Embo J 1996;15:6241-50
    • (1996) Embo J , vol.15 , pp. 6241-50
    • Salim, K.1    Bottomley, M.J.2    Querfurth, E.3
  • 19
    • 0028896344 scopus 로고
    • Activation of Tsk and Btk tyrosine kinases by G protein beta gamma subunits
    • Langhans-Rajasekaran SA, Wan Y, Huang XY. Activation of Tsk and Btk tyrosine kinases by G protein beta gamma subunits. Proc Natl Acad Sci USA 1995;92:8601-5
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8601-5
    • Langhans-Rajasekaran, S.A.1    Wan, Y.2    Huang, X.Y.3
  • 20
    • 0028173394 scopus 로고
    • Binding of beta gamma subunits of heterotrimeric G proteins to the PH domain of Bruton tyrosine kinase
    • Tsukada S, Simon MI, Witte ON, Katz A. Binding of beta gamma subunits of heterotrimeric G proteins to the PH domain of Bruton tyrosine kinase. Proc Natl Acad Sci USA 1994;91:11256-60
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 11256-60
    • Tsukada, S.1    Simon, M.I.2    Witte, O.N.3    Katz, A.4
  • 21
    • 0029739626 scopus 로고    scopus 로고
    • Immunodeficiency in protein kinase cbeta-deficient mice
    • Leitges M, Schmedt C, Guinamard R, et al. Immunodeficiency in protein kinase cbeta-deficient mice. Science 1996;273:788-91
    • (1996) Science , vol.273 , pp. 788-91
    • Leitges, M.1    Schmedt, C.2    Guinamard, R.3
  • 22
    • 0030697510 scopus 로고    scopus 로고
    • The Bmx tyrosine kinase induces activation of the Stat signaling pathway, which is specifically inhibited by protein kinase Cdelta
    • Saharinen P, Ekman N, Sarvas K, et al. The Bmx tyrosine kinase induces activation of the Stat signaling pathway, which is specifically inhibited by protein kinase Cdelta. Blood 1997;90:4341-53
    • (1997) Blood , vol.90 , pp. 4341-53
    • Saharinen, P.1    Ekman, N.2    Sarvas, K.3
  • 23
    • 0037155856 scopus 로고    scopus 로고
    • Interaction of Bruton's tyrosine kinase and protein kinase Ctheta in platelets. Cross-talk between tyrosine and serine/threonine kinases
    • Crosby D, Poole AW. Interaction of Bruton's tyrosine kinase and protein kinase Ctheta in platelets. Cross-talk between tyrosine and serine/threonine kinases. J Biol Chem 2002;277:9958-65
    • (2002) J Biol Chem , vol.277 , pp. 9958-65
    • Crosby, D.1    Poole, A.W.2
  • 24
    • 0043092028 scopus 로고    scopus 로고
    • Physical and functional interaction between PKCdelta and Fyn tyrosine kinase in human platelets
    • Crosby D, Poole AW. Physical and functional interaction between PKCdelta and Fyn tyrosine kinase in human platelets. J Biol Chem 2003;278:24533-41
    • (2003) J Biol Chem , vol.278 , pp. 24533-41
    • Crosby, D.1    Poole, A.W.2
  • 25
    • 0033538524 scopus 로고    scopus 로고
    • Pleckstrin homology domains interact with filamentous actin
    • Yao L, Janmey P, Frigeri LG, et al. Pleckstrin homology domains interact with filamentous actin. J Biol Chem 1999;274:19752-61
    • (1999) J Biol Chem , vol.274 , pp. 19752-61
    • Yao, L.1    Janmey, P.2    Frigeri, L.G.3
  • 26
    • 0028183398 scopus 로고
    • Bruton's tyrosine kinase is a key regulator in B-cell development
    • Rawlings DJ, Witte ON. Bruton's tyrosine kinase is a key regulator in B-cell development. Immunol Rev 1994;138:105-19
    • (1994) Immunol Rev , vol.138 , pp. 105-19
    • Rawlings, D.J.1    Witte, O.N.2
  • 27
    • 0029838226 scopus 로고    scopus 로고
    • BTK as a mediator of radiation-induced apoptosis in DT-40 lymphoma B cells
    • Uckun FM, Waddick KG, Mahajan S, et al. BTK as a mediator of radiation-induced apoptosis in DT-40 lymphoma B cells. Science 1996;273:1096-100
    • (1996) Science , vol.273 , pp. 1096-100
    • Uckun, F.M.1    Waddick, K.G.2    Mahajan, S.3
  • 28
    • 33645795941 scopus 로고    scopus 로고
    • Bruton's tyrosine kinase and SLP-65 regulate pre-B cell differentiation and the induction of Ig light chain gene rearrangement
    • Kersseboom R, Ta VB, Zijlstra AJ, et al. Bruton's tyrosine kinase and SLP-65 regulate pre-B cell differentiation and the induction of Ig light chain gene rearrangement. J Immunol 2006;176:4543-52
    • (2006) J Immunol , vol.176 , pp. 4543-52
    • Kersseboom, R.1    Ta, V.B.2    Zijlstra, A.J.3
  • 29
    • 33751195937 scopus 로고    scopus 로고
    • Levy R Altered B cell receptor signaling kinetics distinguish human follicular lymphoma B cells from tumor infiltrating non-malignant B cells
    • Irish JM, Czerwinski DK, Nolan GP, Levy R Altered B cell receptor signaling kinetics distinguish human follicular lymphoma B cells from tumor infiltrating non-malignant B cells. Blood 2006;108(9):3135-42
    • (2006) Blood , vol.108 , Issue.9 , pp. 3135-42
    • Irish, J.M.1    Czerwinski, D.K.2    Nolan, G.P.3
  • 30
    • 33745023808 scopus 로고    scopus 로고
    • Induction of immunoglobulin heavy-chain transcription through the transcription factor Bright requires TFII-I
    • Rajaiya J, Nixon JC, Ayers N, et al. Induction of immunoglobulin heavy-chain transcription through the transcription factor Bright requires TFII-I. Mol Cell Biol 2006;26:4758-68
    • (2006) Mol Cell Biol , vol.26 , pp. 4758-68
    • Rajaiya, J.1    Nixon, J.C.2    Ayers, N.3
  • 31
    • 26944450881 scopus 로고    scopus 로고
    • Differential expression and molecular characterisation of Lmo7, Myo1e, Sash1, and Mcoln2 genes in Btk-defective B-cells
    • Lindvall JM, Blomberg KE, Wennborg A, Smith CI. Differential expression and molecular characterisation of Lmo7, Myo1e, Sash1, and Mcoln2 genes in Btk-defective B-cells. Cell Immunol 2005;235:46-55
    • (2005) Cell Immunol , vol.235 , pp. 46-55
    • Lindvall, J.M.1    Blomberg, K.E.2    Wennborg, A.3    Smith, C.I.4
  • 32
    • 0034657235 scopus 로고    scopus 로고
    • Bruton's tyrosine kinase links the B cell receptor to nuclear factor kappaB activation
    • Bajpai UD, Zhang K, Teutsch M, et al. Bruton's tyrosine kinase links the B cell receptor to nuclear factor kappaB activation. J Exp Med 2000;191:1735-44
    • (2000) J Exp Med , vol.191 , pp. 1735-44
    • Bajpai, U.D.1    Zhang, K.2    Teutsch, M.3
  • 33
    • 0035958958 scopus 로고    scopus 로고
    • Identification of phosphorylation sites for Bruton's tyrosine kinase within the transcriptional regulator BAP/TFII-I
    • EgloffAM, Desiderio S. Identification of phosphorylation sites for Bruton's tyrosine kinase within the transcriptional regulator BAP/TFII-I. J Biol Chem 2001;276:27806-15
    • (2001) J Biol Chem , vol.276 , pp. 27806-15
    • Egloff, A.M.1    Desiderio, S.2
  • 34
    • 0031886974 scopus 로고    scopus 로고
    • A duplicated gene in the breakpoint regions of the 7q11.23 Williams-Beuren syndrome deletion encodes the initiator binding protein TFII-I and BAP-135, a phosphorylation target of BTK
    • Perez Jurado LA, Wang, YK, Peoples R, et al. A duplicated gene in the breakpoint regions of the 7q11.23 Williams-Beuren syndrome deletion encodes the initiator binding protein TFII-I and BAP-135, a phosphorylation target of BTK. Hum Mol Genet 1998;7:325-34
    • (1998) Hum Mol Genet , vol.7 , pp. 325-34
    • Perez Jurado, L.A.1    Wang, Y.K.2    Peoples, R.3
  • 35
    • 0031038046 scopus 로고    scopus 로고
    • BAP-135, a target for Bruton's tyrosine kinase in response to B cell receptor engagement
    • Yang W, Desiderio S. BAP-135, a target for Bruton's tyrosine kinase in response to B cell receptor engagement. Proc Natl Acad Sci USA 1997;94:604-9
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 604-9
    • Yang, W.1    Desiderio, S.2
  • 36
    • 0032927536 scopus 로고    scopus 로고
    • Tyrosine phosphorylation enhances the SH2 domain-binding activity of Bcr and inhibits Bcr interaction with 14-3-3 proteins
    • Peters KL, Smithgall TE. Tyrosine phosphorylation enhances the SH2 domain-binding activity of Bcr and inhibits Bcr interaction with 14-3-3 proteins. Cell Signal 1999;11:507-14
    • (1999) Cell Signal , vol.11 , pp. 507-14
    • Peters, K.L.1    Smithgall, T.E.2
  • 37
    • 0035903207 scopus 로고    scopus 로고
    • Transcription factor STAT5A is a substrate of Bruton's tyrosine kinase in B cells
    • Mahajan S, Vassilev A, Sun, N, et al. Transcription factor STAT5A is a substrate of Bruton's tyrosine kinase in B cells. J Biol Chem 2001;276:31216-28
    • (2001) J Biol Chem , vol.276 , pp. 31216-28
    • Mahajan, S.1    Vassilev, A.2    Sun, N.3
  • 38
    • 16844377506 scopus 로고    scopus 로고
    • Recent advances in understanding the cell death pathways activated by anticancer therapy
    • Kim R. Recent advances in understanding the cell death pathways activated by anticancer therapy. Cancer 2005;103:1551-60
    • (2005) Cancer , vol.103 , pp. 1551-60
    • Kim, R.1
  • 39
    • 8844263797 scopus 로고    scopus 로고
    • Targeting apoptosis pathways in cancer therapy
    • Fulda S, Debatin KM. Targeting apoptosis pathways in cancer therapy. Curr Cancer Drug Targets 2004;4:569-76
    • (2004) Curr Cancer Drug Targets , vol.4 , pp. 569-76
    • Fulda, S.1    Debatin, K.M.2
  • 40
    • 0344393783 scopus 로고    scopus 로고
    • Alterations in the apoptotic machinery and their potential role in anticancer drug resistance
    • Kaufmann SH, Vaux DL. Alterations in the apoptotic machinery and their potential role in anticancer drug resistance. Oncogene 2003;22:7414-30
    • (2003) Oncogene , vol.22 , pp. 7414-30
    • Kaufmann, S.H.1    Vaux, D.L.2
  • 41
    • 0033555546 scopus 로고    scopus 로고
    • Bruton's tyrosine kinase as an inhibitor of the Fas/CD95 death-inducing signaling complex
    • Vassilev A, Ozer Z, Navara C, et al. Bruton's tyrosine kinase as an inhibitor of the Fas/CD95 death-inducing signaling complex. J Biol Chem 1999;274:1646-56
    • (1999) J Biol Chem , vol.274 , pp. 1646-56
    • Vassilev, A.1    Ozer, Z.2    Navara, C.3
  • 42
    • 22344440682 scopus 로고    scopus 로고
    • Mimicry of a constitutively active pre-B cell receptor in acute lymphoblastic leukemia cells
    • Feldhahn N, Klein F, Mooster JL, et al. Mimicry of a constitutively active pre-B cell receptor in acute lymphoblastic leukemia cells. J Exp Med 2005;201:1837-52
    • (2005) J Exp Med , vol.201 , pp. 1837-52
    • Feldhahn, N.1    Klein, F.2    Mooster, J.L.3
  • 43
    • 0038671744 scopus 로고    scopus 로고
    • BCR targets cyclin D2 via Btk and the p85alpha subunit of PI3-K to induce cell cycle progression in primary mouse B cells
    • Glassford J, Soeiro I, Skarell SM, et al. BCR targets cyclin D2 via Btk and the p85alpha subunit of PI3-K to induce cell cycle progression in primary mouse B cells. Oncogene 2003;22:2248-59
    • (2003) Oncogene , vol.22 , pp. 2248-59
    • Glassford, J.1    Soeiro, I.2    Skarell, S.M.3
  • 44
    • 0034657235 scopus 로고    scopus 로고
    • Bruton's tyrosine kinase links the B cell receptor to nuclear factor kappaB activation
    • Bajpai UD, Zhang K, Teutsch M, et al. Bruton's tyrosine kinase links the B cell receptor to nuclear factor kappaB activation. J Exp Med 2000;191:1735-44
    • (2000) J Exp Med , vol.191 , pp. 1735-44
    • Bajpai, U.D.1    Zhang, K.2    Teutsch, M.3
  • 45
    • 0035910580 scopus 로고    scopus 로고
    • Phospholipase C-gamma 2 couples Bruton's tyrosine kinase to the NF-kappaB signaling pathway in B lymphocytes
    • Petro JB, Khan WN. Phospholipase C-gamma 2 couples Bruton's tyrosine kinase to the NF-kappaB signaling pathway in B lymphocytes. J Biol Chem 2001;276:1715-9
    • (2001) J Biol Chem , vol.276 , pp. 1715-9
    • Petro, J.B.1    Khan, W.N.2
  • 46
    • 0036190076 scopus 로고    scopus 로고
    • Constitutive activation of STAT3 and STAT5 is induced by leukemic furion proteins with protein tyrosine kinase activity and is sufficient for transformation of hematopoietic precursor cells
    • Spiekermann K, Pau M, Schwab R, et al. Constitutive activation of STAT3 and STAT5 is induced by leukemic furion proteins with protein tyrosine kinase activity and is sufficient for transformation of hematopoietic precursor cells. Exp Hematol 2002;30:262-71
    • (2002) Exp Hematol , vol.30 , pp. 262-71
    • Spiekermann, K.1    Pau, M.2    Schwab, R.3
  • 47
    • 61849105375 scopus 로고    scopus 로고
    • BLNK suppresses pre-B cell leukemogenesis through inhibition of JAK3
    • Nakayama J, Yamamoto M, Hayashi K, et al. BLNK suppresses pre-B cell leukemogenesis through inhibition of JAK3. Blood 2009;113:1483-92
    • (2009) Blood , vol.113 , pp. 1483-92
    • Nakayama, J.1    Yamamoto, M.2    Hayashi, K.3
  • 48
    • 33749529310 scopus 로고    scopus 로고
    • A preferential role for STAT5, not constitutively active STAT3, in promoting survival of a human lymphoid tumor
    • Nagy ZS, Rui H, Stepkowski SM, et al. A preferential role for STAT5, not constitutively active STAT3, in promoting survival of a human lymphoid tumor. J Immunol 2006;177:5032-40
    • (2006) J Immunol , vol.177 , pp. 5032-40
    • Nagy, Z.S.1    Rui, H.2    Stepkowski, S.M.3
  • 49
    • 21644458365 scopus 로고    scopus 로고
    • Anti-apoptotic role of STAT5 in hematopoietic cells and in the pathogenesis of malignancies
    • Debierre-Grockiego F. Anti-apoptotic role of STAT5 in hematopoietic cells and in the pathogenesis of malignancies. Apoptosis 2004;9:717-28
    • (2004) Apoptosis , vol.9 , pp. 717-28
    • Debierre-Grockiego, F.1
  • 50
    • 2442677889 scopus 로고    scopus 로고
    • Interleukin 7 induces apoptosis of 697 pre-B cells expressing dominant negative forms of STAT5: Evidence for caspase-dependent and-independent mechanisms
    • Lanvin O, Gouilleux F, Mullie C, et al. Interleukin 7 induces apoptosis of 697 pre-B cells expressing dominant negative forms of STAT5: evidence for caspase-dependent and-independent mechanisms. Oncogene 2004;23:3040-7
    • (2004) Oncogene , vol.23 , pp. 3040-7
    • Lanvin, O.1    Gouilleux, F.2    Mullie, C.3
  • 51
    • 40449121882 scopus 로고    scopus 로고
    • Chemokine CXCL12 enhances proliferation in pre-B ALL via STAT5 activation
    • Mowafi F, Cagigi A, Matskova L, et al. Chemokine CXCL12 enhances proliferation in pre-B ALL via STAT5 activation. Pediatr Blood Cancer 2008;50:812-7
    • (2008) Pediatr Blood Cancer , vol.50 , pp. 812-7
    • Mowafi, F.1    Cagigi, A.2    Matskova, L.3
  • 52
    • 1042274072 scopus 로고    scopus 로고
    • The influence of STAT5 antisense oligonucleotides on the proliferation and apoptosis of selected human leukemic cell lines
    • Baskiewicz-Masiuk M, Machalinski B. The influence of STAT5 antisense oligonucleotides on the proliferation and apoptosis of selected human leukemic cell lines. Cell Prolif 2003;36:265-78
    • (2003) Cell Prolif , vol.36 , pp. 265-78
    • Baskiewicz-Masiuk, M.1    MacHalinski, B.2
  • 53
    • 18544372618 scopus 로고    scopus 로고
    • Functional coorperation among Ras, STAT5, and phosphatidylinositol 3-kinease is required for full oncogenic activities of BCR-ABL in K562 cells
    • Sonoyama J, Matsumura I, Ezoe S, et al. Functional coorperation among Ras, STAT5, and phosphatidylinositol 3-kinease is required for full oncogenic activities of BCR-ABL in K562 cells. J Biol Chem 2002;277:8076-82
    • (2002) J Biol Chem , vol.277 , pp. 8076-82
    • Sonoyama, J.1    Matsumura, I.2    Ezoe, S.3
  • 54
    • 2542619062 scopus 로고    scopus 로고
    • The role of the STAT5 proteins in the proliferation and apoptosis of CML and AML cells
    • Baskiewicz-Masiuk M, Machalinski B. The role of the STAT5 proteins in the proliferation and apoptosis of CML and AML cells. Eur J Hematol 2004;272:420-9
    • (2004) Eur J Hematol , vol.272 , pp. 420-9
    • Baskiewicz-Masiuk, M.1    MacHalinski, B.2
  • 55
    • 34548412863 scopus 로고    scopus 로고
    • The multikinase inhibitor sorafenib induces apoptosis in highly imatinib mesylate-resistant bcr/abl+ human leukemia cells in association with signal transducer and activator of transcription 5 inhibition and myeloid cell leukemia 1-down regulation
    • Rahmani M, Nguyen TK, Dent P, Grant S. The multikinase inhibitor sorafenib induces apoptosis in highly imatinib mesylate-resistant bcr/abl+ human leukemia cells in association with signal transducer and activator of transcription 5 inhibition and myeloid cell leukemia 1-down regulation. Mol Pharmacol 2007;72:788-95
    • (2007) Mol Pharmacol , vol.72 , pp. 788-95
    • Rahmani, M.1    Nguyen, T.K.2    Dent, P.3    Grant, S.4
  • 56
    • 34248166041 scopus 로고    scopus 로고
    • Dasatinib (BMS-354825) inhibits STAT5 signaling associated with apoptosis in chronic myelogeneous leukemia cells
    • Nam S, Williams A, Vultur A, et al. Dasatinib (BMS-354825) inhibits STAT5 signaling associated with apoptosis in chronic myelogeneous leukemia cells. Mol Cancer Ther 2007;6:1400-5
    • (2007) Mol Cancer Ther , vol.6 , pp. 1400-5
    • Nam, S.1    Williams, A.2    Vultur, A.3
  • 57
    • 20444419344 scopus 로고    scopus 로고
    • Sensitized RNAi screen of human kinases and phosphatases identifies new regulators of apoptosis and chemoresistance
    • MacKeigan JP, Murphy LO, Blenis J. Sensitized RNAi screen of human kinases and phosphatases identifies new regulators of apoptosis and chemoresistance. Nat Cell Biol 2005;7:591-600
    • (2005) Nat Cell Biol , vol.7 , pp. 591-600
    • MacKeigan, J.P.1    Murphy, L.O.2    Blenis, J.3
  • 58
    • 33750727368 scopus 로고    scopus 로고
    • Genomic signatures to guide the use of chemotherapeutics
    • Potti A, Dressman HK, Bild A, et al. Genomic signatures to guide the use of chemotherapeutics. Nat Med 2006;12:1294-1300
    • (2006) Nat Med , vol.12 , pp. 1294-1300
    • Potti, A.1    Dressman, H.K.2    Bild, A.3
  • 59
    • 2342564353 scopus 로고    scopus 로고
    • A library of siRNA duplexes targeting phosphoinositide 3-kinease pathway: Determinants of gene silencing for use in cell-based screens
    • Hsieh AC, Bo R, Manola J, et al. A library of siRNA duplexes targeting phosphoinositide 3-kinease pathway: determinants of gene silencing for use in cell-based screens. Nucleic Acid Res 2004;32:893-901
    • (2004) Nucleic Acid Res , vol.32 , pp. 893-901
    • Hsieh, A.C.1    Bo, R.2    Manola, J.3
  • 60
    • 23744494993 scopus 로고    scopus 로고
    • Rapamycin stimulates apoptosis of childhood acute lymphoblastic leukemia cells
    • Avellino R, Romano S, Parasole R, et al. Rapamycin stimulates apoptosis of childhood acute lymphoblastic leukemia cells. Blood 2005;106:1400-6
    • (2005) Blood , vol.106 , pp. 1400-6
    • Avellino, R.1    Romano, S.2    Parasole, R.3
  • 61
    • 65349114832 scopus 로고    scopus 로고
    • Potentiating effects of RAD001 (Everolimus) on vincristine therapy in childhood acute lymphoblastic leukemia
    • Cisterne A, Thien M, Hewson J, et al. Potentiating effects of RAD001 (Everolimus) on vincristine therapy in childhood acute lymphoblastic leukemia. Blood 2009;113:3297-306
    • (2009) Blood , vol.113 , pp. 3297-306
    • Cisterne, A.1    Thien, M.2    Hewson, J.3
  • 62
    • 0027358430 scopus 로고
    • The Bruton's tyrosine kinase gene is expressed throughout B cell differentiation, from early precursor B cell stages preceding immunoglobulin gene rearrangement up to mature B cell stages
    • Verschuren MC, Kraakman ME, Mensink RG, et al. The Bruton's tyrosine kinase gene is expressed throughout B cell differentiation, from early precursor B cell stages preceding immunoglobulin gene rearrangement up to mature B cell stages. Eur J Immunol 1993;23:3109-14
    • (1993) Eur J Immunol , vol.23 , pp. 3109-14
    • Verschuren, M.C.1    Kraakman, M.E.2    Mensink, R.G.3
  • 63
    • 6044254953 scopus 로고    scopus 로고
    • Variability in the degree of expression of phosphorylated IkappaBalpha in chronic lymphocytic leukemia cases with nodal involvement
    • Martinez N, Camacho FI, Ruiz-Ballesteros E, et al. Variability in the degree of expression of phosphorylated IkappaBalpha in chronic lymphocytic leukemia cases with nodal involvement. Clin Cancer Res 2004;10:6796-806
    • (2004) Clin Cancer Res , vol.10 , pp. 6796-806
    • Martinez, N.1    Camacho, F.I.2    Ruiz-Ballesteros, E.3
  • 64
    • 33646566560 scopus 로고    scopus 로고
    • Roles for phosphoinositide 3-kinases, Bruton's tyrosine kinase, and Jun kinases in B lymphocyte chemotaxis and homing
    • Ortolano S, Hwang IY, Han SB, Kehrl JH. Roles for phosphoinositide 3-kinases, Bruton's tyrosine kinase, and Jun kinases in B lymphocyte chemotaxis and homing. Eur J Immunol 2006;36:1285-95
    • (2006) Eur J Immunol , vol.36 , pp. 1285-95
    • Ortolano, S.1    Hwang, I.Y.2    Han, S.B.3    Kehrl, J.H.4
  • 65
    • 7344262556 scopus 로고    scopus 로고
    • Absence of Bruton's tyrosine kinase (Btk) mutations in patients with acute myeloid leukaemia
    • Ritis K, Speletas M, Tsironidou V, et al. Absence of Bruton's tyrosine kinase (Btk) mutations in patients with acute myeloid leukaemia. Br J Hematol 1998;102:1241-8
    • (1998) Br J Hematol , vol.102 , pp. 1241-8
    • Ritis, K.1    Speletas, M.2    Tsironidou, V.3
  • 66
    • 0029791422 scopus 로고    scopus 로고
    • BMX tyrosine kinase gene is expressed in granulocytes and myeloid leukaemias
    • Kaukonen J, Lahtinen I, Laine S, et al. BMX tyrosine kinase gene is expressed in granulocytes and myeloid leukaemias. Br J Hematol 1996;94:455-60
    • (1996) Br J Hematol , vol.94 , pp. 455-60
    • Kaukonen, J.1    Lahtinen, I.2    Laine, S.3
  • 67
    • 42349086371 scopus 로고    scopus 로고
    • Bone marrow X kinase-mediated signal transduction in irradiated vascular endothelium
    • Tu T, Thotala D, Geng L, et al. Bone marrow X kinase-mediated signal transduction in irradiated vascular endothelium. Cancer Res 2008;68:2861-9
    • (2008) Cancer Res , vol.68 , pp. 2861-9
    • Tu, T.1    Thotala, D.2    Geng, L.3
  • 68
    • 73849145729 scopus 로고    scopus 로고
    • Chronic active B cell receptor signaling in diffuse large B cell lymphoma
    • Davis RE, Ngo VN, Lenz G, et al. Chronic active B cell receptor signaling in diffuse large B cell lymphoma. Nature 2010;463:88-92
    • (2010) Nature , vol.463 , pp. 88-92
    • Davis, R.E.1    Ngo, V.N.2    Lenz, G.3
  • 69
    • 0036098398 scopus 로고    scopus 로고
    • In vivo pharmacokinetic features, toxicity profile, and chemosensitizing activity of alpha-cyano-beta-hydroxy-beta-methyl-N-(2,5-dibromophenyl) propenamide (LFM-A13), a novel antileukemic agent targeting Bruton's tyrosine kinase
    • Uckun FM, Zheng Y, Cetkovic-Cvrlje M, et al. In vivo pharmacokinetic features, toxicity profile, and chemosensitizing activity of alpha-cyano-beta-hydroxy-beta-methyl-N-(2,5-dibromophenyl)propenamide (LFM-A13), a novel antileukemic agent targeting Bruton's tyrosine kinase. Clin Cancer Res 2002;8:1224-33
    • (2002) Clin Cancer Res , vol.8 , pp. 1224-33
    • Uckun, F.M.1    Zheng, Y.2    Cetkovic-Cvrlje, M.3
  • 70
    • 0030623910 scopus 로고    scopus 로고
    • Stem cell transplantation: Past, present and future
    • Thomas ED. Stem cell transplantation: past, present and future. Arch Immunol Ther Exp (Warsz) 1997;45:1-5
    • (1997) Arch Immunol Ther Exp (Warsz) , vol.45 , pp. 1-5
    • Thomas, E.D.1
  • 71
    • 0023687355 scopus 로고
    • Bone marrow transplantation for treatment of leukemia in children
    • Trigg ME. Bone marrow transplantation for treatment of leukemia in children. Pediatr Clin North Am 1988;35:933-48
    • (1988) Pediatr Clin North Am , vol.35 , pp. 933-48
    • Trigg, M.E.1
  • 72
    • 0028535680 scopus 로고
    • Allogeneic bone marrow transplantation for leukemia
    • Butturini A, Gale RP. Allogeneic bone marrow transplantation for leukemia. Curr Opin Hematol 1994;1:402-5
    • (1994) Curr Opin Hematol , vol.1 , pp. 402-5
    • Butturini, A.1    Gale, R.P.2
  • 73
    • 0028964106 scopus 로고
    • Mismatched bone marrow transplantation
    • Henslee-Downey PJ. Mismatched bone marrow transplantation. Curr Opin Oncol 1995;7:115-21
    • (1995) Curr Opin Oncol , vol.7 , pp. 115-21
    • Henslee-Downey, P.J.1
  • 74
    • 0032605618 scopus 로고    scopus 로고
    • Long-term follow-up of patients who achieved complete remission after donor leukocyte infusions
    • Porter DL, Collins RH, Shpilberg O, et al. Long-term follow-up of patients who achieved complete remission after donor leukocyte infusions. Biol Blood Marrow Transplant 1999;5:253-61
    • (1999) Biol Blood Marrow Transplant , vol.5 , pp. 253-61
    • Porter, D.L.1    Collins, R.H.2    Shpilberg, O.3
  • 75
    • 0031879036 scopus 로고    scopus 로고
    • Graft-versus-leukemia is sufficient to induce remission in juvenile myelomonocytic leukemia
    • Orchard PJ, Miller JS, McGlennen R, et al. Graft-versus-leukemia is sufficient to induce remission in juvenile myelomonocytic leukemia. Bone MarrowTransplant 1998;22:201-3
    • (1998) Bone MarrowTransplant , vol.22 , pp. 201-3
    • Orchard, P.J.1    Miller, J.S.2    McGlennen, R.3
  • 76
    • 0034971850 scopus 로고    scopus 로고
    • Non-myeloablative allogeneic stem cell transplantation focusing on immunotherapy of life-threatening malignant and non-malignant diseases
    • Slavin S, Nagler A, Shapira M, et al. Non-myeloablative allogeneic stem cell transplantation focusing on immunotherapy of life-threatening malignant and non-malignant diseases. Crit Rev Oncol Hematol 2001;39:25-9
    • (2001) Crit Rev Oncol Hematol , vol.39 , pp. 25-9
    • Slavin, S.1    Nagler, A.2    Shapira, M.3
  • 77
    • 0033642531 scopus 로고    scopus 로고
    • Intentional induction of mixed chimerism and achievement of antitumor responses after nonmyeloablative conditioning therapy and HLA-matched donor bone marrow transplantation for refractory hematologic malignancies
    • Spitzer TR, McAfee S, Sackstein R, et al. Intentional induction of mixed chimerism and achievement of antitumor responses after nonmyeloablative conditioning therapy and HLA-matched donor bone marrow transplantation for refractory hematologic malignancies. Biol Blood Marrow Transplant 2000;6:309-20
    • (2000) Biol Blood Marrow Transplant , vol.6 , pp. 309-20
    • Spitzer, T.R.1    McAfee, S.2    Sackstein, R.3
  • 78
    • 4644313506 scopus 로고    scopus 로고
    • Dual targeting of Bruton's tyrosine kinase and Janus kinase 3 with rationally designed inhibitors prevents graft-versus-host disease (GVHD) in a murine allogeneic bone marrow transplantation model
    • Cetkovic-Cvrlje M, Uckun FM. Dual targeting of Bruton's tyrosine kinase and Janus kinase 3 with rationally designed inhibitors prevents graft-versus-host disease (GVHD) in a murine allogeneic bone marrow transplantation model. Br J Haematol 2004;126:821-7
    • (2004) Br J Haematol , vol.126 , pp. 821-7
    • Cetkovic-Cvrlje, M.1    Uckun, F.M.2
  • 80
    • 12844269949 scopus 로고    scopus 로고
    • Warfarin versus low-molecular-weight heparin therapy in cancer patients
    • Zacharski LR, Prandoni P, Monreal M. Warfarin versus low-molecular-weight heparin therapy in cancer patients. Oncologist 2005;10:72-9
    • (2005) Oncologist , vol.10 , pp. 72-9
    • Zacharski, L.R.1    Prandoni, P.2    Monreal, M.3
  • 81
    • 0033576522 scopus 로고    scopus 로고
    • The treatment of cerebrovascular disorders with anticoagulants and platelet aggregation inhibitors
    • Ameriso SF. The treatment of cerebrovascular disorders with anticoagulants and platelet aggregation inhibitors. RevNeurol 1999;29:1285-90
    • (1999) RevNeurol , vol.29 , pp. 1285-90
    • Ameriso, S.F.1
  • 82
    • 0030790042 scopus 로고    scopus 로고
    • Glycoprotein VI is the collagen receptor in platelets which underlies tyrosine phosphorylation of the Fc receptor gamma-chain
    • Gibbins JM, Okuma M, Farndale R, et al. Glycoprotein VI is the collagen receptor in platelets which underlies tyrosine phosphorylation of the Fc receptor gamma-chain. FEBS Lett 1997;413:255-9
    • (1997) FEBS Lett , vol.413 , pp. 255-9
    • Gibbins, J.M.1    Okuma, M.2    Farndale, R.3
  • 83
    • 0030742897 scopus 로고    scopus 로고
    • Platelet receptors for collagen
    • Moroi M, Jung SM. Platelet receptors for collagen. Thromb Haemost 1997;78:439-44
    • (1997) Thromb Haemost , vol.78 , pp. 439-44
    • Moroi, M.1    Jung, S.M.2
  • 84
    • 0030764155 scopus 로고    scopus 로고
    • A novel association of Fc receptor gamma-chain with glycoprotein VI and their co-expression as a collagen receptor in human platelets
    • Tsuji M, Ezumi Y, Arai M, Takayama H. A novel association of Fc receptor gamma-chain with glycoprotein VI and their co-expression as a collagen receptor in human platelets. J Biol Chem 1997;272:23528-31
    • (1997) J Biol Chem , vol.272 , pp. 23528-31
    • Tsuji, M.1    Ezumi, Y.2    Arai, M.3    Takayama, H.4
  • 85
    • 0032497629 scopus 로고    scopus 로고
    • A role for Bruton's tyrosine kinase (Btk) in platelet activation by collagen
    • Quek LS, Bolen J, Watson SP. A role for Bruton's tyrosine kinase (Btk) in platelet activation by collagen. CurrBiol 1998;8:1137-40
    • (1998) CurrBiol , vol.8 , pp. 1137-40
    • Quek, L.S.1    Bolen, J.2    Watson, S.P.3
  • 86
    • 17644442615 scopus 로고    scopus 로고
    • Rapid tyrosine phosphorylation and activation of Bruton's tyrosine/TEC kinases in platelets induced by collagen binding or CD32 cross-linking
    • Oda A, Ikeda Y, Ochs HD, et al. Rapid tyrosine phosphorylation and activation of Bruton's tyrosine/TEC kinases in platelets induced by collagen binding or CD32 cross-linking. Blood 2000;95:1663-70
    • (2000) Blood , vol.95 , pp. 1663-70
    • Oda, A.1    Ikeda, Y.2    Ochs, H.D.3
  • 87
    • 4444260266 scopus 로고    scopus 로고
    • Platelet adhesion signalling and the regulation of thrombus formation
    • Gibbins JM. Platelet adhesion signalling and the regulation of thrombus formation. J Cell Sci 2004;117:3415-25
    • (2004) J Cell Sci , vol.117 , pp. 3415-25
    • Gibbins, J.M.1
  • 88
    • 0032102098 scopus 로고    scopus 로고
    • Collagen receptor signalling in platelets:extending the role of the ITAM
    • Watson S. Collagen receptor signalling in platelets:extending the role of the ITAM. Immunol Today 1998;19:260-4
    • (1998) Immunol Today , vol.19 , pp. 260-4
    • Watson, S.1
  • 89
    • 0032785842 scopus 로고    scopus 로고
    • Regulation and function of WASp in platelets by the collagen receptor, glycoprotein VI
    • Gross BS, Wilde JI, Quek L, et al. Regulation and function of WASp in platelets by the collagen receptor, glycoprotein VI. Blood 1999;94:4166-76
    • (1999) Blood , vol.94 , pp. 4166-76
    • Gross, B.S.1    Wilde, J.I.2    Quek, L.3
  • 90
    • 0036247866 scopus 로고    scopus 로고
    • A dual function anti-leukemic agent with anti-thrombotic activity
    • Tibbles H, Vassilev A, Uckun FM. A dual function anti-leukemic agent with anti-thrombotic activity. Leuk Lymphoma 2002;43:1121-7
    • (2002) Leuk Lymphoma , vol.43 , pp. 1121-7
    • Tibbles, H.1    Vassilev, A.2    Uckun, F.M.3
  • 91
    • 0038235827 scopus 로고    scopus 로고
    • The Anti-leukemic Bruton's tyrosine kinase inhibitor LFM-A13 prevents fatal thromboembolism
    • Uckun FM, VassilevAO, Bartell S, et al. The Anti-leukemic Bruton's tyrosine kinase inhibitor LFM-A13 prevents fatal thromboembolism. Leuk Lymphoma 2003;44:1569-77
    • (2003) Leuk Lymphoma , vol.44 , pp. 1569-77
    • Uckun, F.M.1    Vassilev, A.O.2    Bartell, S.3
  • 92
    • 3042739756 scopus 로고    scopus 로고
    • In vivo toxicity and antithrombotic profile of the oral formulation of the antileukemic agent, LFM-A13-F
    • Tibbles HE, Samuel P, Erbeck D, et al. In vivo toxicity and antithrombotic profile of the oral formulation of the antileukemic agent, LFM-A13-F. Arzneimittelforschung Drug Res 2004;54:330-9
    • (2004) Arzneimittelforschung Drug Res , vol.54 , pp. 330-9
    • Tibbles, H.E.1    Samuel, P.2    Erbeck, D.3
  • 93
    • 0023800081 scopus 로고
    • Sequelae of thrombotic or hemorrhagic complications following L-asparaginase therapy for childhood lymphoblastic leukemia
    • Ott N, Ramsay NK, Priest JR, et al. Sequelae of thrombotic or hemorrhagic complications following L-asparaginase therapy for childhood lymphoblastic leukemia. Am J Pediatr Hematol Oncol 1988;10:191-5
    • (1988) Am J Pediatr Hematol Oncol , vol.10 , pp. 191-5
    • Ott, N.1    Ramsay, N.K.2    Priest, J.R.3
  • 94
    • 13144254208 scopus 로고    scopus 로고
    • Genetic analysis of patients with defects in early B-cell development
    • Conley ME, Broides A, Hernandez-Trujillo V, et al. Genetic analysis of patients with defects in early B-cell development. Immunol Rev 2005;203:216-34
    • (2005) Immunol Rev , vol.203 , pp. 216-34
    • Conley, M.E.1    Broides, A.2    Hernandez-Trujillo, V.3
  • 95
    • 19944434293 scopus 로고    scopus 로고
    • Bruton's tyrosine kinase: Cell biology, sequence conservation, mutation spectrum, siRNA modifications, and expression profiling
    • Lindvall JM, Blomberg KE, Valiaho J, et al. Bruton's tyrosine kinase: cell biology, sequence conservation, mutation spectrum, siRNA modifications, and expression profiling. Immunol Rev 2005;203:200-15
    • (2005) Immunol Rev , vol.203 , pp. 200-15
    • Lindvall, J.M.1    Blomberg, K.E.2    Valiaho, J.3
  • 96
    • 21344468850 scopus 로고    scopus 로고
    • X linked agammaglobulinaemia and rheumatoid arthritis
    • Verbruggen G, De Backer S, Deforce D, et al. X linked agammaglobulinaemia and rheumatoid arthritis. Ann Rheum Dis 2005;64:1075-8
    • (2005) Ann Rheum Dis , vol.64 , pp. 1075-8
    • Verbruggen, G.1    De Backer, S.2    Deforce, D.3
  • 97
    • 33846246989 scopus 로고    scopus 로고
    • Bruton's tyrosine kinase together with PI 3-kinase are part of Toll-like receptor 2 multiprotein complex and mediate LTA induced Toll-like receptor 2 responses in macrophages
    • Liljeroos M, Vuolteenaho R, Morath S, et al. Bruton's tyrosine kinase together with PI 3-kinase are part of Toll-like receptor 2 multiprotein complex and mediate LTA induced Toll-like receptor 2 responses in macrophages. Cell Signal 2006;19:625-33
    • (2006) Cell Signal , vol.19 , pp. 625-33
    • Liljeroos, M.1    Vuolteenaho, R.2    Morath, S.3
  • 98
    • 33644844972 scopus 로고    scopus 로고
    • Bruton's tyrosine kinase is required for TLR2 and TLR4-induced TNF, but not IL-6, production
    • Horwood NJ, Page TH, McDaid JP, et al. Bruton's tyrosine kinase is required for TLR2 and TLR4-induced TNF, but not IL-6, production. J Immunol 2006;176:3635-41
    • (2006) J Immunol , vol.176 , pp. 3635-41
    • Horwood, N.J.1    Page, T.H.2    McDaid, J.P.3
  • 99
    • 0038544296 scopus 로고    scopus 로고
    • Bruton's tyrosine kinase is required for lipopolysaccharide-induced tumor necrosis factor {alpha} production
    • Horwood NJ, Mahon T, McDaid JP, et al. Bruton's tyrosine kinase is required for lipopolysaccharide-induced tumor necrosis factor {alpha} production. J Exp Med 2003;197:1603-11
    • (2003) J Exp Med , vol.197 , pp. 1603-11
    • Horwood, N.J.1    Mahon, T.2    McDaid, J.P.3
  • 100
    • 33646566560 scopus 로고    scopus 로고
    • Roles for phosphoinositide 3-kinases, Bruton's tyrosine kinase, and Jun kinases in B lymphocyte chemotaxis and homing
    • Ortolano S, Hwang IY, Han SB, Kehrl JH. Roles for phosphoinositide 3-kinases, Bruton's tyrosine kinase, and Jun kinases in B lymphocyte chemotaxis and homing. Eur J Immunol 2006;36:1285-95
    • (2006) Eur J Immunol , vol.36 , pp. 1285-95
    • Ortolano, S.1    Hwang, I.Y.2    Han, S.B.3    Kehrl, J.H.4
  • 101
    • 0038221378 scopus 로고    scopus 로고
    • Chemotactic factor-induced recruitment and activation of TEC family kinases in human neutrophils. II. Effects of LFM-A13, a specific Btk inhibitor
    • Gilbert C, Levasseur S, Desaulniers P, et al. Chemotactic factor-induced recruitment and activation of TEC family kinases in human neutrophils. II. Effects of LFM-A13, a specific Btk inhibitor. J Immunol 2003;170:5235-43
    • (2003) J Immunol , vol.170 , pp. 5235-43
    • Gilbert, C.1    Levasseur, S.2    Desaulniers, P.3
  • 102
    • 23044513194 scopus 로고    scopus 로고
    • Signaling through CD16b in human neutrophils involves the TEC family of tyrosine kinases
    • Fernandes MJ, Lachance G, Pare G, et al. Signaling through CD16b in human neutrophils involves the TEC family of tyrosine kinases. J Leukoc Biol 2005;78:524-32
    • (2005) J Leukoc Biol , vol.78 , pp. 524-32
    • Fernandes, M.J.1    Lachance, G.2    Pare, G.3
  • 103
    • 33745119045 scopus 로고    scopus 로고
    • Analysis of amphotericin B-induced cell signaling with chemical inhibitors of signaling molecules
    • Matsuo K, Hotokezaka H, Ohara N, et al. Analysis of amphotericin B-induced cell signaling with chemical inhibitors of signaling molecules. Microbiol Immunol 2006;50:337-47
    • (2006) Microbiol Immunol , vol.50 , pp. 337-47
    • Matsuo, K.1    Hotokezaka, H.2    Ohara, N.3
  • 104
    • 21244503601 scopus 로고    scopus 로고
    • Bruton's tyrosine kinase is involved in p65-mediated transactivation and phosphorylation of p65 on serine 536 during NFkappaB activation by lipopolysaccharide
    • Doyle SL, Jefferies CA, O'Neill LA. Bruton's tyrosine kinase is involved in p65-mediated transactivation and phosphorylation of p65 on serine 536 during NFkappaB activation by lipopolysaccharide. J Biol Chem 2005;280:23496-501
    • (2005) J Biol Chem , vol.280 , pp. 23496-501
    • Doyle, S.L.1    Jefferies, C.A.2    O'Neill, L.A.3
  • 105
    • 33745125425 scopus 로고    scopus 로고
    • Sundler R Different roles for non-receptor tyrosine kinases in arachidonate release induced by zymosan and Staphylococcus aureus in macrophages
    • Olsson S, Sundler R Different roles for non-receptor tyrosine kinases in arachidonate release induced by zymosan and Staphylococcus aureus in macrophages. J Inflamm (Lond) 2006;3:8-15
    • (2006) J Inflamm (Lond) , vol.3 , pp. 8-15
    • Olsson, S.1
  • 106
    • 77958483166 scopus 로고    scopus 로고
    • MedicineNet.com Asthma information. Available from
    • MedicineNet.com Asthma information. Available from: http://www. medicinenet.com/asthma/page2.htm
  • 108
    • 30944443047 scopus 로고    scopus 로고
    • Antisense-and RNA interference-based therapeutic strategies in allergy
    • Popescu, FD. Antisense-and RNA interference-based therapeutic strategies in allergy. J Cell Mol Med 2005;9:840-53
    • (2005) J Cell Mol Med , vol.9 , pp. 840-53
    • Popescu, F.D.1
  • 109
    • 0037063364 scopus 로고    scopus 로고
    • Silencing of Bruton's tyrosine kinase (Btk) using short interfering RNA duplexes (siRNA)
    • Heinonen JE, Smith CI, Nore BF. Silencing of Bruton's tyrosine kinase (Btk) using short interfering RNA duplexes (siRNA). FEBS Lett 2002;527:274-8
    • (2002) FEBS Lett , vol.527 , pp. 274-8
    • Heinonen, J.E.1    Smith, C.I.2    Nore, B.F.3
  • 110
    • 38149122052 scopus 로고    scopus 로고
    • Chemosensitizing anti-cancer activity of LFM-A13, a leflunomide metabolite analog targeting polo-like kinases
    • Uckun FM. Chemosensitizing anti-cancer activity of LFM-A13, a leflunomide metabolite analog targeting polo-like kinases. Cell Cycle 2007;6:3021-6
    • (2007) Cell Cycle , vol.6 , pp. 3021-6
    • Uckun, F.M.1
  • 111
    • 7644232049 scopus 로고    scopus 로고
    • Mechanism of B-cell receptor-induced phosphorylation and activation of phospholipase C-gamma2
    • Kim YJ, Sekiya F, Poulin B, et al. Mechanism of B-cell receptor-induced phosphorylation and activation of phospholipase C-gamma2. Mol Cell Biol 2004;24:9986-99
    • (2004) Mol Cell Biol , vol.24 , pp. 9986-99
    • Kim, Y.J.1    Sekiya, F.2    Poulin, B.3
  • 112
    • 0037063364 scopus 로고    scopus 로고
    • Silencing of Bruton's tyrosine kinase (Btk) using short interfering RNA duplexes (siRNA)
    • Heinonen JE, Smith CI, Nore BF. Silencing of Bruton's tyrosine kinase (Btk) using short interfering RNA duplexes (siRNA). FEBS Lett 2002;527:274-8
    • (2002) FEBS Lett , vol.527 , pp. 274-8
    • Heinonen, J.E.1    Smith, C.I.2    Nore, B.F.3
  • 113
    • 0035253352 scopus 로고    scopus 로고
    • Stat5 and Sp1 regulate transcription of the cyclin D2 gene in response to IL-2
    • Martino A, Holmes JH, Lord JD, et al. Stat5 and Sp1 regulate transcription of the cyclin D2 gene in response to IL-2. J Immunol 2001;166:1723-9
    • (2001) J Immunol , vol.166 , pp. 1723-9
    • Martino, A.1    Holmes, J.H.2    Lord, J.D.3
  • 114
    • 7644244868 scopus 로고    scopus 로고
    • FoxO3a and BCR-ABL regulate cyclin D2 transcription through a STAT5/BCL6-dependent mechanism
    • Fernandez deMattos S, Essafi A, Soeiro I, et al. FoxO3a and BCR-ABL regulate cyclin D2 transcription through a STAT5/BCL6-dependent mechanism. Mol Cell Biol. 2004, 24:10058-71
    • (2004) Mol Cell Biol , vol.24 , pp. 10058-71
    • Fernandez De Mattos, S.1    Essafi, A.2    Soeiro, I.3
  • 122
  • 141
    • 38049084406 scopus 로고    scopus 로고
    • Discovery of slective irreversible inhibitors of Bruton's tyrosine kinase
    • Pan Z, Scheerens H, Li SJ, et al. Discovery of slective irreversible inhibitors of Bruton's tyrosine kinase. ChemMedChem 2007;2:58-61
    • (2007) ChemMedChem , vol.2 , pp. 58-61
    • Pan, Z.1    Scheerens, H.2    Li, S.J.3
  • 142
    • 77955625479 scopus 로고    scopus 로고
    • The Bruton tyrosine kinase inhibitor PCI-32765 blocks B-cell activation and is efficacious in models of autoimmune disease and B-cell malignancy
    • Honigberg LA, Smith AM, Sirisawad M, et al. The Bruton tyrosine kinase inhibitor PCI-32765 blocks B-cell activation and is efficacious in models of autoimmune disease and B-cell malignancy. Proc Natl Acad Sci USA 2010;107:13075-80
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 13075-80
    • Honigberg, L.A.1    Smith, A.M.2    Sirisawad, M.3
  • 144
    • 77958481737 scopus 로고    scopus 로고
    • A novel platform-based approach to silence oncoproteins using small molecule therapeutics-Application to Bruton's tyrosine kinase [abstract 3739]
    • Evans E, Tester R, Aslanian S, et al. A novel platform-based approach to silence oncoproteins using small molecule therapeutics-Application to Bruton's tyrosine kinase [abstract 3739]. Proc. AACR Symp. Denver, CO; 2009
    • (2009) Proc. AACR Symp. Denver CO
    • Evans, E.1    Tester, R.2    Aslanian, S.3
  • 145
    • 77249095150 scopus 로고    scopus 로고
    • Structures of human Bruton's tyrosine kinase in active and inactive conformations suggest a mechanism of activation for TEC family kinases
    • Marcotte DJ, Liu YT, Arduini RM, et al. Structures of human Bruton's tyrosine kinase in active and inactive conformations suggest a mechanism of activation for TEC family kinases. Protein Sci 2010;19:429-39
    • (2010) Protein Sci , vol.19 , pp. 429-39
    • Marcotte, D.J.1    Liu, Y.T.2    Arduini, R.M.3
  • 146
    • 0035798646 scopus 로고    scopus 로고
    • Crystal structure of Bruton's tyrosine kinase domain suggests a novel pathway for activation and provides insights into the molecular basis of X-linked agammaglobulinemia
    • Mao C, Zhou M, Uckun FM. Crystal structure of Bruton's tyrosine kinase domain suggests a novel pathway for activation and provides insights into the molecular basis of X-linked agammaglobulinemia. J Biol Chem 2001;276:41435-43
    • (2001) J Biol Chem , vol.276 , pp. 41435-43
    • Mao, C.1    Zhou, M.2    Uckun, F.M.3


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