메뉴 건너뛰기




Volumn 3, Issue 5-6, 2012, Pages 436-446

Structure, Regulation, Signaling, and Targeting of Abl Kinases in Cancer

Author keywords

Bcr Abl; kinase inhibitor; kinase structure; tyrosine kinase

Indexed keywords

ABELSON KINASE; ADAPTOR PROTEIN; ADENOSINE TRIPHOSPHATE; BCR ABL PROTEIN; HYBRID PROTEIN; IMATINIB; NILOTINIB; ONCOPROTEIN; PHOSPHOTYROSINE; PHOSPHOTYROSINE 177; PONATINIB; PROTEIN CRK; PROTEIN NUP214; PROTEIN SH2; PROTEIN SH3; REBASTINIB; STAT5 PROTEIN; UNCLASSIFIED DRUG;

EID: 84875515439     PISSN: 19476019     EISSN: 19476027     Source Type: Journal    
DOI: 10.1177/1947601912458584     Document Type: Article
Times cited : (114)

References (113)
  • 1
    • 0032937828 scopus 로고    scopus 로고
    • Cycling, stressed-out and nervous: cellular functions of c-Abl
    • Van Etten RA.Cycling, stressed-out and nervous: cellular functions of c-Abl.Trends Cell Biol. 1999;9:179-86.
    • (1999) Trends Cell Biol , vol.9 , pp. 179-186
    • van Etten, R.A.1
  • 2
    • 0036391801 scopus 로고    scopus 로고
    • The Abl family kinases: mechanisms of regulation and signaling
    • Pendergast AM.The Abl family kinases: mechanisms of regulation and signaling.Adv Cancer Res. 2002;85:51-100.
    • (2002) Adv Cancer Res , vol.85 , pp. 51-100
    • Pendergast, A.M.1
  • 3
    • 63749127483 scopus 로고    scopus 로고
    • Kinome signaling through regulated protein-protein interactions in normal and cancer cells
    • Pawson T,Kofler M.Kinome signaling through regulated protein-protein interactions in normal and cancer cells.Curr Opin Cell Biol. 2009;21:147-53.
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 147-153
    • Pawson, T.1    Kofler, M.2
  • 4
    • 0347132269 scopus 로고    scopus 로고
    • Regulation of the c-Abl and Bcr-Abl tyrosine kinases
    • Hantschel O,Superti-Furga G.Regulation of the c-Abl and Bcr-Abl tyrosine kinases.Nat Rev Mol Cell Biol. 2004;5:33-44.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 33-44
    • Hantschel, O.1    Superti-Furga, G.2
  • 5
    • 0028859279 scopus 로고
    • Protein modules and signalling networks
    • Pawson T.Protein modules and signalling networks.Nature. 1995;373:573-80.
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 6
    • 0028485085 scopus 로고
    • High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides
    • Musacchio A,Saraste M,Wilmanns M.High-resolution crystal structures of tyrosine kinase SH3 domains complexed with proline-rich peptides.Nat Struct Biol. 1994;1:546.
    • (1994) Nat Struct Biol , vol.1 , pp. 546
    • Musacchio, A.1    Saraste, M.2    Wilmanns, M.3
  • 7
    • 0026669472 scopus 로고
    • Three-dimensional solution structure of the src homology 2 domain of c-abl
    • Overduin M,Rios CB,Mayer BJ,Baltimore D,Cowburn D.Three-dimensional solution structure of the src homology 2 domain of c-abl.Cell. 1992;70:697-704.
    • (1992) Cell , vol.70 , pp. 697-704
    • Overduin, M.1    Rios, C.B.2    Mayer, B.J.3    Baltimore, D.4    Cowburn, D.5
  • 8
    • 0029645577 scopus 로고
    • The solution structure of Abl SH3, and its relationship to SH2 in the SH(32) construct
    • Gosser YQ,Zheng J,Overduin M,Mayer BJ,Cowburn D.The solution structure of Abl SH3, and its relationship to SH2 in the SH(32) construct.Structure. 1995;3:1075-86.
    • (1995) Structure , vol.3 , pp. 1075-1086
    • Gosser, Y.Q.1    Zheng, J.2    Overduin, M.3    Mayer, B.J.4    Cowburn, D.5
  • 10
    • 0031882251 scopus 로고    scopus 로고
    • An intramolecular SH3-domain interaction regulates c-Abl activity
    • Barilá D,Superti-Furga G.An intramolecular SH3-domain interaction regulates c-Abl activity.Nat Genet. 1998;18:280-2.
    • (1998) Nat Genet , vol.18 , pp. 280-282
    • Barilá, D.1    Superti-Furga, G.2
  • 11
    • 0037459341 scopus 로고    scopus 로고
    • Variation on an Src-like theme
    • Harrison SC.Variation on an Src-like theme.Cell. 2003;112:737-40.
    • (2003) Cell , vol.112 , pp. 737-740
    • Harrison, S.C.1
  • 12
    • 0031578579 scopus 로고    scopus 로고
    • The 2.35 A crystal structure of the inactivated form of chicken Src: a dynamic molecule with multiple regulatory interactions
    • Williams JC,Weijland A,Gonfloni S, et al.The 2.35 A crystal structure of the inactivated form of chicken Src: a dynamic molecule with multiple regulatory interactions.J Mol Biol. 1997;274:757-75.
    • (1997) J Mol Biol , vol.274 , pp. 757-775
    • Williams, J.C.1    Weijland, A.2    Gonfloni, S.3
  • 13
    • 0031034930 scopus 로고    scopus 로고
    • Crystal structure of the Src family tyrosine kinase Hck
    • Sicheri F,Moarefi I,Kuriyan J.Crystal structure of the Src family tyrosine kinase Hck.Nature. 1997;385:602-9.
    • (1997) Nature , vol.385 , pp. 602-609
    • Sicheri, F.1    Moarefi, I.2    Kuriyan, J.3
  • 14
    • 0031025991 scopus 로고    scopus 로고
    • Three-dimensional structure of the tyrosine kinase c-Src
    • Xu W,Harrison SC,Eck MJ.Three-dimensional structure of the tyrosine kinase c-Src.Nature. 1997;385:595-601.
    • (1997) Nature , vol.385 , pp. 595-601
    • Xu, W.1    Harrison, S.C.2    Eck, M.J.3
  • 15
    • 0026601293 scopus 로고
    • Point mutations in the abl SH2 domain coordinately impair phosphotyrosine binding in vitro and transforming activity in vivo
    • Mayer BJ,Jackson PK,Van Etten RA,Baltimore D.Point mutations in the abl SH2 domain coordinately impair phosphotyrosine binding in vitro and transforming activity in vivo.Mol Cell Biol. 1992;12:609-18.
    • (1992) Mol Cell Biol , vol.12 , pp. 609-618
    • Mayer, B.J.1    Jackson, P.K.2    van Etten, R.A.3    Baltimore, D.4
  • 16
    • 0027520893 scopus 로고
    • En bloc substitution of the Src homology region 2 domain activates the transforming potential of the c-Abl protein tyrosine kinase
    • Muller AJ,Pendergast AM,Parmar K,Havlik MH,Rosenberg N,Witte ON.En bloc substitution of the Src homology region 2 domain activates the transforming potential of the c-Abl protein tyrosine kinase.Proc Natl Acad Sci U S A. 1993;90:3457-61.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 3457-3461
    • Muller, A.J.1    Pendergast, A.M.2    Parmar, K.3    Havlik, M.H.4    Rosenberg, N.5    Witte, O.N.6
  • 17
    • 0035166003 scopus 로고    scopus 로고
    • The Src homology 2 domain of Bcr/Abl is required for efficient induction of chronic myeloid leukemia-like disease in mice but not for lymphoid leukemogenesis or activation of phosphatidylinositol 3-kinase
    • Roumiantsev S,de Aos IE,Varticovski L,Ilaria RL,Van Etten RA.The Src homology 2 domain of Bcr/Abl is required for efficient induction of chronic myeloid leukemia-like disease in mice but not for lymphoid leukemogenesis or activation of phosphatidylinositol 3-kinase.Blood. 2001;97:4-13.
    • (2001) Blood , vol.97 , pp. 4-13
    • Roumiantsev, S.1    de Aos, I.E.2    Varticovski, L.3    Ilaria, R.L.4    van Etten, R.A.5
  • 18
    • 0344626926 scopus 로고    scopus 로고
    • Structural basis for the autoinhibition of c-Abl tyrosine kinase
    • Nagar B,Hantschel O,Young MA, et al.Structural basis for the autoinhibition of c-Abl tyrosine kinase.Cell. 2003;112:859-71.
    • (2003) Cell , vol.112 , pp. 859-871
    • Nagar, B.1    Hantschel, O.2    Young, M.A.3
  • 19
    • 0344626925 scopus 로고    scopus 로고
    • A myristoyl/phosphotyrosine switch regulates c-Abl
    • Hantschel O,Nagar B,Guettler S, et al.A myristoyl/phosphotyrosine switch regulates c-Abl.Cell. 2003;112:845-57.
    • (2003) Cell , vol.112 , pp. 845-857
    • Hantschel, O.1    Nagar, B.2    Guettler, S.3
  • 20
    • 77950502609 scopus 로고    scopus 로고
    • A potent and highly specific FN3 monobody inhibitor of the Abl SH2 domain
    • Wojcik J,Hantschel O,Grebien F, et al.A potent and highly specific FN3 monobody inhibitor of the Abl SH2 domain.Nat Struct Mol Biol. 2010;17:519-27.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 519-527
    • Wojcik, J.1    Hantschel, O.2    Grebien, F.3
  • 21
    • 0032875098 scopus 로고    scopus 로고
    • Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins
    • Resh MD.Fatty acylation of proteins: new insights into membrane targeting of myristoylated and palmitoylated proteins.Biochim Biophys Acta. 1999;1451:1-16.
    • (1999) Biochim Biophys Acta , vol.1451 , pp. 1-16
    • Resh, M.D.1
  • 22
    • 23744493479 scopus 로고    scopus 로고
    • Structural basis for the cytoskeletal association of Bcr-Abl/c-Abl
    • Hantschel O,Wiesner S,Guttler T, et al.Structural basis for the cytoskeletal association of Bcr-Abl/c-Abl.Mol Cell. 2005;19:461-73.
    • (2005) Mol Cell , vol.19 , pp. 461-473
    • Hantschel, O.1    Wiesner, S.2    Guttler, T.3
  • 23
    • 84856460186 scopus 로고    scopus 로고
    • Allosteric BCR-ABL inhibitors in Philadelphia chromosome-positive acute lymphoblastic leukemia: novel opportunities for drug combinations to overcome resistance
    • Hantschel O.Allosteric BCR-ABL inhibitors in Philadelphia chromosome-positive acute lymphoblastic leukemia: novel opportunities for drug combinations to overcome resistance.Haematologica. 2012;97:157-9.
    • (2012) Haematologica , vol.97 , pp. 157-159
    • Hantschel, O.1
  • 24
    • 0035819026 scopus 로고    scopus 로고
    • Phosphorylation and structure-based functional studies reveal a positive and a negative role for the activation loop of the c-Abl tyrosine kinase
    • Dorey K,Engen JR,Kretzschmar J, et al.Phosphorylation and structure-based functional studies reveal a positive and a negative role for the activation loop of the c-Abl tyrosine kinase.Oncogene. 2001;20:8075-84.
    • (2001) Oncogene , vol.20 , pp. 8075-8084
    • Dorey, K.1    Engen, J.R.2    Kretzschmar, J.3
  • 25
    • 0034634597 scopus 로고    scopus 로고
    • c-Abl has high intrinsic tyrosine kinase activity that is stimulated by mutation of the src homology 3 domain and by autophosphorylation at two distinct regulatory tyrosines
    • Brasher BB,Van Etten RA.c-Abl has high intrinsic tyrosine kinase activity that is stimulated by mutation of the src homology 3 domain and by autophosphorylation at two distinct regulatory tyrosines.J Biol Chem. 2000;275:35631-7.
    • (2000) J Biol Chem , vol.275 , pp. 35631-35637
    • Brasher, B.B.1    van Etten, R.A.2
  • 27
    • 0036682301 scopus 로고    scopus 로고
    • Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI-571)
    • Nagar B,Bornmann WG,Pellicena P, et al.Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI-571).Cancer Res. 2002;62:4236-43.
    • (2002) Cancer Res , vol.62 , pp. 4236-4243
    • Nagar, B.1    Bornmann, W.G.2    Pellicena, P.3
  • 28
    • 0035800507 scopus 로고    scopus 로고
    • Clinical resistance to STI-571 cancer therapy caused by BCR-ABL gene mutation or amplification
    • Gorre ME,Mohammed M,Ellwood K, et al.Clinical resistance to STI-571 cancer therapy caused by BCR-ABL gene mutation or amplification.Science. 2001;293:876-80.
    • (2001) Science , vol.293 , pp. 876-880
    • Gorre, M.E.1    Mohammed, M.2    Ellwood, K.3
  • 29
    • 33646755174 scopus 로고    scopus 로고
    • A Src-like inactive conformation in the abl tyrosine kinase domain
    • Levinson NM,Kuchment O,Shen K, et al.A Src-like inactive conformation in the abl tyrosine kinase domain.PLoS Biol. 2006;4:e144.
    • (2006) PLoS Biol , vol.4
    • Levinson, N.M.1    Kuchment, O.2    Shen, K.3
  • 30
    • 33847659183 scopus 로고    scopus 로고
    • c-Src binds to the cancer drug imatinib with an inactive Abl/c-Kit conformation and a distributed thermodynamic penalty
    • Seeliger MA,Nagar B,Frank F,Cao X,Henderson MN,Kuriyan J.c-Src binds to the cancer drug imatinib with an inactive Abl/c-Kit conformation and a distributed thermodynamic penalty.Structure. 2007;15:299-311.
    • (2007) Structure , vol.15 , pp. 299-311
    • Seeliger, M.A.1    Nagar, B.2    Frank, F.3    Cao, X.4    Henderson, M.N.5    Kuriyan, J.6
  • 31
    • 33644871166 scopus 로고    scopus 로고
    • Organization of the SH3-SH2 unit in active and inactive forms of the c-Abl tyrosine kinase
    • Nagar B,Hantschel O,Seeliger M, et al.Organization of the SH3-SH2 unit in active and inactive forms of the c-Abl tyrosine kinase.Mol Cell. 2006;21:787-98.
    • (2006) Mol Cell , vol.21 , pp. 787-798
    • Nagar, B.1    Hantschel, O.2    Seeliger, M.3
  • 32
    • 50249132542 scopus 로고    scopus 로고
    • Structural coupling of SH2-kinase domains links Fes and Abl substrate recognition and kinase activation
    • Filippakopoulos P,Kofler M,Hantschel O, et al.Structural coupling of SH2-kinase domains links Fes and Abl substrate recognition and kinase activation.Cell. 2008;134:793-803.
    • (2008) Cell , vol.134 , pp. 793-803
    • Filippakopoulos, P.1    Kofler, M.2    Hantschel, O.3
  • 33
    • 80054690374 scopus 로고    scopus 로고
    • Targeting the SH2-kinase interface in Bcr-Abl inhibits leukemogenesis
    • Grebien F,Hantschel O,Wojcik J, et al.Targeting the SH2-kinase interface in Bcr-Abl inhibits leukemogenesis.Cell. 2011;147:306-19.
    • (2011) Cell , vol.147 , pp. 306-319
    • Grebien, F.1    Hantschel, O.2    Wojcik, J.3
  • 34
    • 0029257493 scopus 로고
    • Evidence that the SH2 domains promote processive phosphorylation by protein-tyrosine kinases
    • Mayer BJ,Hirai H,Sakai R.Evidence that the SH2 domains promote processive phosphorylation by protein-tyrosine kinases.Curr Biol. 1995;5:296-305.
    • (1995) Curr Biol , vol.5 , pp. 296-305
    • Mayer, B.J.1    Hirai, H.2    Sakai, R.3
  • 35
    • 0028938721 scopus 로고
    • Catalytic specificity of protein-tyrosine kinases is critical for selective signalling
    • Zhou S,Carraway KL,Eck MJ, et al.Catalytic specificity of protein-tyrosine kinases is critical for selective signalling.Nature. 1995;373:536-9.
    • (1995) Nature , vol.373 , pp. 536-539
    • Zhou, S.1    Carraway, K.L.2    Eck, M.J.3
  • 36
    • 0020158951 scopus 로고
    • In vivo tyrosine phosphorylations of the Abelson virus transforming protein are absent in its normal cellular homolog
    • Ponticelli AS,Whitlock CA,Rosenberg N,Witte ON.In vivo tyrosine phosphorylations of the Abelson virus transforming protein are absent in its normal cellular homolog.Cell. 1982;29:953-60.
    • (1982) Cell , vol.29 , pp. 953-960
    • Ponticelli, A.S.1    Whitlock, C.A.2    Rosenberg, N.3    Witte, O.N.4
  • 37
    • 0035968166 scopus 로고    scopus 로고
    • Activation of c-Abl kinase activity and transformation by a chemical inducer of dimerization
    • Smith KM,Van Etten RA.Activation of c-Abl kinase activity and transformation by a chemical inducer of dimerization.J Biol Chem. 2001;276:24372-9.
    • (2001) J Biol Chem , vol.276 , pp. 24372-24379
    • Smith, K.M.1    van Etten, R.A.2
  • 38
    • 0000286732 scopus 로고
    • Minute chromosome in human chronic granulocytic leukemia
    • Nowell PC,Hungerford DA.Minute chromosome in human chronic granulocytic leukemia.Science. 1960;132:1497.
    • (1960) Science , vol.132 , pp. 1497
    • Nowell, P.C.1    Hungerford, D.A.2
  • 39
    • 55249116841 scopus 로고    scopus 로고
    • Chromosomal translocations: revisited yet again
    • Rowley JD.Chromosomal translocations: revisited yet again.Blood. 2008;112:2183-9.
    • (2008) Blood , vol.112 , pp. 2183-2189
    • Rowley, J.D.1
  • 40
    • 0034670036 scopus 로고    scopus 로고
    • The molecular biology of chronic myeloid leukemia
    • Deininger MW,Goldman JM,Melo JV.The molecular biology of chronic myeloid leukemia.Blood. 2000;96:3343-56.
    • (2000) Blood , vol.96 , pp. 3343-3356
    • Deininger, M.W.1    Goldman, J.M.2    Melo, J.V.3
  • 41
    • 2542441665 scopus 로고    scopus 로고
    • The BCR-ABL story: bench to bedside and back
    • Wong S,Witte ON.The BCR-ABL story: bench to bedside and back.Annu Rev Immunol. 2004;22:247-306.
    • (2004) Annu Rev Immunol , vol.22 , pp. 247-306
    • Wong, S.1    Witte, O.N.2
  • 42
    • 0029060662 scopus 로고
    • Establishment and molecular characterization of a novel leukemic cell line with Philadelphia chromosome expressing p230 BCR/ABL fusion protein
    • Wada H,Mizutani S,Nishimura J, et al.Establishment and molecular characterization of a novel leukemic cell line with Philadelphia chromosome expressing p230 BCR/ABL fusion protein.Cancer Res. 1995;55:3192-6.
    • (1995) Cancer Res , vol.55 , pp. 3192-3196
    • Wada, H.1    Mizutani, S.2    Nishimura, J.3
  • 43
    • 66149095910 scopus 로고    scopus 로고
    • Charting the molecular network of the drug target Bcr-Abl
    • Brehme M,Hantschel O,Colinge J, et al.Charting the molecular network of the drug target Bcr-Abl.Proc Natl Acad Sci U S A. 2009;106:7414-9.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 7414-7419
    • Brehme, M.1    Hantschel, O.2    Colinge, J.3
  • 44
    • 0027422977 scopus 로고
    • A coiled-coil oligomerization domain of Bcr is essential for the transforming function of Bcr-Abl oncoproteins
    • McWhirter JR,Galasso DL,Wang JY.A coiled-coil oligomerization domain of Bcr is essential for the transforming function of Bcr-Abl oncoproteins.Mol Cell Biol. 1993;13:7587-95.
    • (1993) Mol Cell Biol , vol.13 , pp. 7587-7595
    • McWhirter, J.R.1    Galasso, D.L.2    Wang, J.Y.3
  • 46
    • 28944446279 scopus 로고    scopus 로고
    • Orientation and oligomerization specificity of the Bcr coiled-coil oligomerization domain
    • Taylor CM,Keating AE.Orientation and oligomerization specificity of the Bcr coiled-coil oligomerization domain.Biochemistry. 2005;44:16246-56.
    • (2005) Biochemistry , vol.44 , pp. 16246-16256
    • Taylor, C.M.1    Keating, A.E.2
  • 47
    • 43049136596 scopus 로고    scopus 로고
    • Targeting of the N-terminal coiled coil oligomerization interface by a helix-2 peptide inhibits unmutated and imatinib-resistant BCR/ABL
    • Beissert T,Hundertmark A,Kaburova V, et al.Targeting of the N-terminal coiled coil oligomerization interface by a helix-2 peptide inhibits unmutated and imatinib-resistant BCR/ABL.Int J Cancer. 2008;122:2744-52.
    • (2008) Int J Cancer , vol.122 , pp. 2744-2752
    • Beissert, T.1    Hundertmark, A.2    Kaburova, V.3
  • 48
    • 74049164212 scopus 로고    scopus 로고
    • Oligomerization inhibition, combined with allosteric inhibition, abrogates the transformation potential of T315I-positive BCR/ABL
    • Mian AA,Oancea C,Zhao Z,Ottmann OG,Ruthardt M.Oligomerization inhibition, combined with allosteric inhibition, abrogates the transformation potential of T315I-positive BCR/ABL.Leukemia. 2009;23:2242-7.
    • (2009) Leukemia , vol.23 , pp. 2242-2247
    • Mian, A.A.1    Oancea, C.2    Zhao, Z.3    Ottmann, O.G.4    Ruthardt, M.5
  • 49
    • 0027368352 scopus 로고
    • BCR-ABL-induced oncogenesis is mediated by direct interaction with the SH2 domain of the GRB-2 adaptor protein
    • Pendergast AM,Quilliam LA,Cripe LD, et al.BCR-ABL-induced oncogenesis is mediated by direct interaction with the SH2 domain of the GRB-2 adaptor protein.Cell. 1993;75:175-85.
    • (1993) Cell , vol.75 , pp. 175-185
    • Pendergast, A.M.1    Quilliam, L.A.2    Cripe, L.D.3
  • 50
    • 0034661522 scopus 로고    scopus 로고
    • The Grb2 binding site is required for the induction of chronic myeloid leukemia-like disease in mice by the Bcr/Abl tyrosine kinase
    • Million RP,Van Etten RA.The Grb2 binding site is required for the induction of chronic myeloid leukemia-like disease in mice by the Bcr/Abl tyrosine kinase.Blood. 2000;96:664-70.
    • (2000) Blood , vol.96 , pp. 664-670
    • Million, R.P.1    van Etten, R.A.2
  • 51
    • 33745083714 scopus 로고    scopus 로고
    • A common phosphotyrosine signature for the Bcr-Abl kinase
    • Goss VL,Lee KA,Moritz A, et al.A common phosphotyrosine signature for the Bcr-Abl kinase.Blood. 2006;107:4888-97.
    • (2006) Blood , vol.107 , pp. 4888-4897
    • Goss, V.L.1    Lee, K.A.2    Moritz, A.3
  • 53
    • 0037333264 scopus 로고    scopus 로고
    • The "Gab" in signal transduction
    • Gu H,Neel BG.The "Gab" in signal transduction.Trends Cell Biol. 2003;13:122-30.
    • (2003) Trends Cell Biol , vol.13 , pp. 122-130
    • Gu, H.1    Neel, B.G.2
  • 54
    • 19044372472 scopus 로고    scopus 로고
    • Critical role for Gab2 in transformation by BCR/ABL
    • Sattler M,Mohi MG,Pride YB, et al.Critical role for Gab2 in transformation by BCR/ABL.Cancer Cell. 2002;1:479-92.
    • (2002) Cancer Cell , vol.1 , pp. 479-492
    • Sattler, M.1    Mohi, M.G.2    Pride, Y.B.3
  • 55
    • 14644425319 scopus 로고    scopus 로고
    • Mechanisms of BCR-ABL in the pathogenesis of chronic myelogenous leukaemia
    • Ren R.Mechanisms of BCR-ABL in the pathogenesis of chronic myelogenous leukaemia.Nat Rev Cancer. 2005;5:172-83.
    • (2005) Nat Rev Cancer , vol.5 , pp. 172-183
    • Ren, R.1
  • 56
    • 0037082489 scopus 로고    scopus 로고
    • Regulation of the Erk2-Elk1 signaling pathway and megakaryocytic differentiation of Bcr-Abl(+) K562 leukemic cells by Gab2
    • Dorsey JF,Cunnick JM,Mane SM,Wu J.Regulation of the Erk2-Elk1 signaling pathway and megakaryocytic differentiation of Bcr-Abl(+) K562 leukemic cells by Gab2.Blood. 2002;99:1388-97.
    • (2002) Blood , vol.99 , pp. 1388-1397
    • Dorsey, J.F.1    Cunnick, J.M.2    Mane, S.M.3    Wu, J.4
  • 57
    • 23944477884 scopus 로고    scopus 로고
    • Activated STAT5 proteins induce activation of the PI 3-kinase/Akt and Ras/MAPK pathways via the Gab2 scaffolding adapter
    • Nyga R,Pecquet C,Harir N, et al.Activated STAT5 proteins induce activation of the PI 3-kinase/Akt and Ras/MAPK pathways via the Gab2 scaffolding adapter.Biochem J. 2005;390:359-66.
    • (2005) Biochem J , vol.390 , pp. 359-366
    • Nyga, R.1    Pecquet, C.2    Harir, N.3
  • 58
    • 33846927933 scopus 로고    scopus 로고
    • Constitutive activation of Stat5 promotes its cytoplasmic localization and association with PI3-kinase in myeloid leukemias
    • Harir N,Pecquet C,Kerenyi M, et al.Constitutive activation of Stat5 promotes its cytoplasmic localization and association with PI3-kinase in myeloid leukemias.Blood. 2007;109:1678-86.
    • (2007) Blood , vol.109 , pp. 1678-1686
    • Harir, N.1    Pecquet, C.2    Kerenyi, M.3
  • 59
    • 43049090771 scopus 로고    scopus 로고
    • The cytotoxicity of a Grb2-SH3 inhibitor in Bcr-Abl positive K562 cells
    • Ye YB,Lin JY,Chen Q, et al.The cytotoxicity of a Grb2-SH3 inhibitor in Bcr-Abl positive K562 cells.Biochem Pharmacol. 2008;75:2080-91.
    • (2008) Biochem Pharmacol , vol.75 , pp. 2080-2091
    • Ye, Y.B.1    Lin, J.Y.2    Chen, Q.3
  • 60
    • 42449146501 scopus 로고    scopus 로고
    • Targeting survival cascades induced by activation of Ras/Raf/MEK/ERK, PI3K/PTEN/Akt/mTOR and Jak/STAT pathways for effective leukemia therapy
    • McCubrey JA,Steelman LS,Abrams SL, et al.Targeting survival cascades induced by activation of Ras/Raf/MEK/ERK, PI3K/PTEN/Akt/mTOR and Jak/STAT pathways for effective leukemia therapy.Leukemia. 2008;22:708-22.
    • (2008) Leukemia , vol.22 , pp. 708-722
    • McCubrey, J.A.1    Steelman, L.S.2    Abrams, S.L.3
  • 61
    • 77954977940 scopus 로고    scopus 로고
    • Chronic myeloid leukemia: mechanisms of blastic transformation
    • Perrotti D,Jamieson C,Goldman J,Skorski T.Chronic myeloid leukemia: mechanisms of blastic transformation.J Clin Invest. 2010;120:2254-64.
    • (2010) J Clin Invest , vol.120 , pp. 2254-2264
    • Perrotti, D.1    Jamieson, C.2    Goldman, J.3    Skorski, T.4
  • 62
    • 0026788001 scopus 로고
    • Dominant negative MYC blocks transformation by ABL oncogenes
    • Sawyers CL,Callahan W,Witte ON.Dominant negative MYC blocks transformation by ABL oncogenes.Cell. 1992;70:901-10.
    • (1992) Cell , vol.70 , pp. 901-910
    • Sawyers, C.L.1    Callahan, W.2    Witte, O.N.3
  • 63
    • 0028116526 scopus 로고
    • Identification of CRKL as the constitutively phosphorylated 39-kD tyrosine phosphoprotein in chronic myelogenous leukemia cells
    • Nichols GL,Raines MA,Vera JC,Lacomis L,Tempst P,Golde DW.Identification of CRKL as the constitutively phosphorylated 39-kD tyrosine phosphoprotein in chronic myelogenous leukemia cells.Blood. 1994;84:2912-8.
    • (1994) Blood , vol.84 , pp. 2912-2918
    • Nichols, G.L.1    Raines, M.A.2    Vera, J.C.3    Lacomis, L.4    Tempst, P.5    Golde, D.W.6
  • 64
    • 0035475308 scopus 로고    scopus 로고
    • Crk family adaptors-signalling complex formation and biological roles
    • Feller SM.Crk family adaptors-signalling complex formation and biological roles.Oncogene. 2001;20:6348-71.
    • (2001) Oncogene , vol.20 , pp. 6348-6371
    • Feller, S.M.1
  • 65
    • 0029790791 scopus 로고    scopus 로고
    • The CRKL adaptor protein transforms fibroblasts and functions in transformation by the BCR-ABL oncogene
    • Senechal K,Halpern J,Sawyers CL.The CRKL adaptor protein transforms fibroblasts and functions in transformation by the BCR-ABL oncogene.J Biol Chem. 1996;271:23255-61.
    • (1996) J Biol Chem , vol.271 , pp. 23255-23261
    • Senechal, K.1    Halpern, J.2    Sawyers, C.L.3
  • 67
    • 0029810923 scopus 로고    scopus 로고
    • Constitutive activation of STAT5 by the BCR-ABL oncogene in chronic myelogenous leukemia
    • Shuai K,Halpern J,ten Hoeve J,Rao X,Sawyers CL.Constitutive activation of STAT5 by the BCR-ABL oncogene in chronic myelogenous leukemia.Oncogene. 1996;13:247-54.
    • (1996) Oncogene , vol.13 , pp. 247-254
    • Shuai, K.1    Halpern, J.2    ten Hoeve, J.3    Rao, X.4    Sawyers, C.L.5
  • 68
    • 0033583530 scopus 로고    scopus 로고
    • Signal transducer and activator of transcription (STAT)5 activation by BCR/ABL is dependent on intact Src homology (SH)3 and SH2 domains of BCR/ABL and is required for leukemogenesis
    • Nieborowska-Skorska M,Wasik MA,Slupianek A, et al.Signal transducer and activator of transcription (STAT)5 activation by BCR/ABL is dependent on intact Src homology (SH)3 and SH2 domains of BCR/ABL and is required for leukemogenesis.J Exp Med. 1999;189:1229-42.
    • (1999) J Exp Med , vol.189 , pp. 1229-1242
    • Nieborowska-Skorska, M.1    Wasik, M.A.2    Slupianek, A.3
  • 69
    • 33745111882 scopus 로고    scopus 로고
    • Clarifying the role of Stat5 in lymphoid development and Abelson-induced transformation
    • Hoelbl A,Kovacic B,Kerenyi MA, et al.Clarifying the role of Stat5 in lymphoid development and Abelson-induced transformation.Blood. 2006;107:4898-906.
    • (2006) Blood , vol.107 , pp. 4898-4906
    • Hoelbl, A.1    Kovacic, B.2    Kerenyi, M.A.3
  • 70
    • 77953667590 scopus 로고    scopus 로고
    • Stat5 is indispensable for the maintenance of bcr/abl-positive leukaemia
    • Hoelbl A,Schuster C,Kovacic B, et al.Stat5 is indispensable for the maintenance of bcr/abl-positive leukaemia.EMBO Mol Med. 2010;2:98-110.
    • (2010) EMBO Mol Med , vol.2 , pp. 98-110
    • Hoelbl, A.1    Schuster, C.2    Kovacic, B.3
  • 71
    • 79953113891 scopus 로고    scopus 로고
    • High STAT5 levels mediate imatinib resistance and indicate disease progression in chronic myeloid leukemia
    • Warsch W,Kollmann K,Eckelhart E, et al.High STAT5 levels mediate imatinib resistance and indicate disease progression in chronic myeloid leukemia.Blood. 2011;117:3409-20.
    • (2011) Blood , vol.117 , pp. 3409-3420
    • Warsch, W.1    Kollmann, K.2    Eckelhart, E.3
  • 72
    • 84857143671 scopus 로고    scopus 로고
    • BCR-ABL uncouples canonical JAK2-STAT5 signaling in chronic myeloid leukemia
    • Hantschel O,Warsch W,Eckelhart E, et al.BCR-ABL uncouples canonical JAK2-STAT5 signaling in chronic myeloid leukemia.Nat Chem Biol. 2012;8:285-93.
    • (2012) Nat Chem Biol , vol.8 , pp. 285-293
    • Hantschel, O.1    Warsch, W.2    Eckelhart, E.3
  • 73
    • 79953109597 scopus 로고    scopus 로고
    • The STAT5 inhibitor pimozide decreases survival of chronic myelogenous leukemia cells resistant to kinase inhibitors
    • Nelson EA,Walker SR,Weisberg E, et al.The STAT5 inhibitor pimozide decreases survival of chronic myelogenous leukemia cells resistant to kinase inhibitors.Blood. 2011;117:3421-9.
    • (2011) Blood , vol.117 , pp. 3421-3429
    • Nelson, E.A.1    Walker, S.R.2    Weisberg, E.3
  • 74
    • 6944252248 scopus 로고    scopus 로고
    • Fusion of NUP214 to ABL1 on amplified episomes in T-cell acute lymphoblastic leukemia
    • Graux C,Cools J,Melotte C, et al.Fusion of NUP214 to ABL1 on amplified episomes in T-cell acute lymphoblastic leukemia.Nat Genet. 2004;36:1084-9.
    • (2004) Nat Genet , vol.36 , pp. 1084-1089
    • Graux, C.1    Cools, J.2    Melotte, C.3
  • 75
    • 46149106112 scopus 로고    scopus 로고
    • Kinase activation and transformation by NUP214-ABL1 is dependent on the context of the nuclear pore
    • De Keersmaecker K,Rocnik JL,Bernad R, et al.Kinase activation and transformation by NUP214-ABL1 is dependent on the context of the nuclear pore.Mol Cell. 2008;31:134-42.
    • (2008) Mol Cell , vol.31 , pp. 134-142
    • de Keersmaecker, K.1    Rocnik, J.L.2    Bernad, R.3
  • 76
    • 57849108906 scopus 로고    scopus 로고
    • Intrinsic differences between the catalytic properties of the oncogenic NUP214-ABL1 and BCR-ABL1 fusion protein kinases
    • De Keersmaecker K,Versele M,Cools J,Superti-Furga G,Hantschel O.Intrinsic differences between the catalytic properties of the oncogenic NUP214-ABL1 and BCR-ABL1 fusion protein kinases.Leukemia. 2008;22:2208-16.
    • (2008) Leukemia , vol.22 , pp. 2208-2216
    • de Keersmaecker, K.1    Versele, M.2    Cools, J.3    Superti-Furga, G.4    Hantschel, O.5
  • 77
    • 45149096506 scopus 로고    scopus 로고
    • Activity of tyrosine kinase inhibitors against human NUP214-ABL1-positive T cell malignancies
    • Quintas-Cardama A,Tong W,Manshouri T, et al.Activity of tyrosine kinase inhibitors against human NUP214-ABL1-positive T cell malignancies.Leukemia. 2008;22:1117-24.
    • (2008) Leukemia , vol.22 , pp. 1117-1124
    • Quintas-Cardama, A.1    Tong, W.2    Manshouri, T.3
  • 78
    • 79954414959 scopus 로고    scopus 로고
    • ABL1 fusion genes in hematological malignancies: a review
    • De Braekeleer E,Douet-Guilbert N,Rowe D, et al.ABL1 fusion genes in hematological malignancies: a review.Eur J Haematol. 2011;86:361-71.
    • (2011) Eur J Haematol , vol.86 , pp. 361-371
    • de Braekeleer, E.1    Douet-Guilbert, N.2    Rowe, D.3
  • 79
    • 0032778537 scopus 로고    scopus 로고
    • The tyrosine kinase abl-related gene ARG is fused to ETV6 in an AML-M4Eo patient with a t(1;12)(q25;p13): molecular cloning of both reciprocal transcripts
    • Cazzaniga G,Tosi S,Aloisi A, et al.The tyrosine kinase abl-related gene ARG is fused to ETV6 in an AML-M4Eo patient with a t(1;12)(q25;p13): molecular cloning of both reciprocal transcripts.Blood. 1999;94:4370-3.
    • (1999) Blood , vol.94 , pp. 4370-4373
    • Cazzaniga, G.1    Tosi, S.2    Aloisi, A.3
  • 80
    • 2442707893 scopus 로고    scopus 로고
    • A direct binding site for Grb2 contributes to transformation and leukemogenesis by the Tel-Abl (ETV6-Abl) tyrosine kinase
    • Million RP,Harakawa N,Roumiantsev S,Varticovski L,Van Etten RA.A direct binding site for Grb2 contributes to transformation and leukemogenesis by the Tel-Abl (ETV6-Abl) tyrosine kinase.Mol Cell Biol. 2004;24:4685-95.
    • (2004) Mol Cell Biol , vol.24 , pp. 4685-4695
    • Million, R.P.1    Harakawa, N.2    Roumiantsev, S.3    Varticovski, L.4    van Etten, R.A.5
  • 81
    • 58149398623 scopus 로고    scopus 로고
    • Translation of the Philadelphia chromosome into therapy for CML
    • Druker BJ.Translation of the Philadelphia chromosome into therapy for CML.Blood. 2008;112:4808-17.
    • (2008) Blood , vol.112 , pp. 4808-4817
    • Druker, B.J.1
  • 82
    • 84856509534 scopus 로고    scopus 로고
    • FDA drug approvals
    • Mullard A.FDA drug approvals.Nat Rev Drug Discov. 2011 2012;11:91-4.
    • (2011) Nat Rev Drug Discov , vol.11 , pp. 91-94
    • Mullard, A.1
  • 83
    • 37049014938 scopus 로고    scopus 로고
    • Chemical proteomic profiles of the BCR-ABL inhibitors imatinib, nilotinib and dasatinib reveal novel kinase and non-kinase targets
    • Rix U,Hantschel O,Durnberger G, et al.Chemical proteomic profiles of the BCR-ABL inhibitors imatinib, nilotinib and dasatinib reveal novel kinase and non-kinase targets.Blood. 2007;110:4055-63.
    • (2007) Blood , vol.110 , pp. 4055-4063
    • Rix, U.1    Hantschel, O.2    Durnberger, G.3
  • 84
    • 67349233062 scopus 로고    scopus 로고
    • Six-year follow-up of patients receiving imatinib for the first-line treatment of chronic myeloid leukemia
    • Hochhaus A,O'Brien SG,Guilhot F, et al.Six-year follow-up of patients receiving imatinib for the first-line treatment of chronic myeloid leukemia.Leukemia. 2009;23:1054-61.
    • (2009) Leukemia , vol.23 , pp. 1054-1061
    • Hochhaus, A.1    O'Brien, S.G.2    Guilhot, F.3
  • 85
    • 80051573352 scopus 로고    scopus 로고
    • BCR-ABL kinase domain mutation analysis in chronic myeloid leukemia patients treated with tyrosine kinase inhibitors: recommendations from an expert panel on behalf of European LeukemiaNet
    • Soverini S,Hochhaus A,Nicolini FE, et al.BCR-ABL kinase domain mutation analysis in chronic myeloid leukemia patients treated with tyrosine kinase inhibitors: recommendations from an expert panel on behalf of European LeukemiaNet.Blood. 2011;118:1208-15.
    • (2011) Blood , vol.118 , pp. 1208-1215
    • Soverini, S.1    Hochhaus, A.2    Nicolini, F.E.3
  • 86
    • 13844251975 scopus 로고    scopus 로고
    • Characterization of AMN107, a selective inhibitor of native and mutant Bcr-Abl
    • Weisberg E,Manley PW,Breitenstein W, et al.Characterization of AMN107, a selective inhibitor of native and mutant Bcr-Abl.Cancer Cell. 2005;7:129-41.
    • (2005) Cancer Cell , vol.7 , pp. 129-141
    • Weisberg, E.1    Manley, P.W.2    Breitenstein, W.3
  • 89
    • 49649108911 scopus 로고    scopus 로고
    • Solution conformations and dynamics of ABL kinase-inhibitor complexes determined by NMR substantiate the different binding modes of imatinib/nilotinib and dasatinib
    • Vajpai N,Strauss A,Fendrich G, et al.Solution conformations and dynamics of ABL kinase-inhibitor complexes determined by NMR substantiate the different binding modes of imatinib/nilotinib and dasatinib.J Biol Chem. 2008;283:18292-302.
    • (2008) J Biol Chem , vol.283 , pp. 18292-18302
    • Vajpai, N.1    Strauss, A.2    Fendrich, G.3
  • 90
    • 34548097263 scopus 로고    scopus 로고
    • The Btk tyrosine kinase is a major target of the Bcr-Abl inhibitor dasatinib
    • Hantschel O,Rix U,Schmidt U, et al.The Btk tyrosine kinase is a major target of the Bcr-Abl inhibitor dasatinib.Proc Natl Acad Sci U S A. 2007;104:13283-8.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 13283-13288
    • Hantschel, O.1    Rix, U.2    Schmidt, U.3
  • 91
    • 42049123098 scopus 로고    scopus 로고
    • Target spectrum of the BCR-ABL inhibitors imatinib, nilotinib and dasatinib
    • Hantschel O,Rix U,Superti-Furga G.Target spectrum of the BCR-ABL inhibitors imatinib, nilotinib and dasatinib.Leuk Lymphoma. 2008;49:615-9.
    • (2008) Leuk Lymphoma , vol.49 , pp. 615-619
    • Hantschel, O.1    Rix, U.2    Superti-Furga, G.3
  • 92
    • 77953691179 scopus 로고    scopus 로고
    • Nilotinib versus imatinib for newly diagnosed chronic myeloid leukemia
    • Saglio G,Kim D-W,Issaragrisil S, et al.Nilotinib versus imatinib for newly diagnosed chronic myeloid leukemia.N Engl J Med. 2010;362:2251-9.
    • (2010) N Engl J Med , vol.362 , pp. 2251-2259
    • Saglio, G.1    Kim, D.-W.2    Issaragrisil, S.3
  • 93
    • 77953725855 scopus 로고    scopus 로고
    • Dasatinib versus imatinib in newly diagnosed chronic-phase chronic myeloid leukemia
    • Kantarjian H,Shah NP,Hochhaus A, et al.Dasatinib versus imatinib in newly diagnosed chronic-phase chronic myeloid leukemia.N Engl J Med. 2010;362:2260-70.
    • (2010) N Engl J Med , vol.362 , pp. 2260-2270
    • Kantarjian, H.1    Shah, N.P.2    Hochhaus, A.3
  • 94
    • 51649120694 scopus 로고    scopus 로고
    • Therapeutic options against BCR-ABL1 T315I-positive chronic myelogenous leukemia
    • Quintas-Cardama A,Cortes J.Therapeutic options against BCR-ABL1 T315I-positive chronic myelogenous leukemia.Clin Cancer Res. 2008;14:4392-9.
    • (2008) Clin Cancer Res , vol.14 , pp. 4392-4399
    • Quintas-Cardama, A.1    Cortes, J.2
  • 95
    • 70350507997 scopus 로고    scopus 로고
    • AP24534, a pan-BCR-ABL inhibitor for chronic myeloid leukemia, potently inhibits the T315I mutant and overcomes mutation-based resistance
    • O'Hare T,Shakespeare WC,Zhu X, et al.AP24534, a pan-BCR-ABL inhibitor for chronic myeloid leukemia, potently inhibits the T315I mutant and overcomes mutation-based resistance.Cancer Cell. 2009;16:401-12.
    • (2009) Cancer Cell , vol.16 , pp. 401-412
    • O'Hare, T.1    Shakespeare, W.C.2    Zhu, X.3
  • 96
    • 79953765304 scopus 로고    scopus 로고
    • Conformational control inhibition of the BCR-ABL1 tyrosine kinase, including the gatekeeper T315I mutant, by the switch-control inhibitor DCC-2036
    • Chan WW,Wise SC,Kaufman MD, et al.Conformational control inhibition of the BCR-ABL1 tyrosine kinase, including the gatekeeper T315I mutant, by the switch-control inhibitor DCC-2036.Cancer Cell. 2011;19:556-68.
    • (2011) Cancer Cell , vol.19 , pp. 556-568
    • Chan, W.W.1    Wise, S.C.2    Kaufman, M.D.3
  • 97
    • 84860841611 scopus 로고    scopus 로고
    • Initial findings from the PACE trial: a pivotal phase 2 study of ponatinib in patients with CML and Ph+ ALL resistant or intolerant to dasatinib or nilotinib, or with the T315I mutation
    • Cortes JE,Kim D-W,Pinilla-Ibarz J, et al.Initial findings from the PACE trial: a pivotal phase 2 study of ponatinib in patients with CML and Ph+ ALL resistant or intolerant to dasatinib or nilotinib, or with the T315I mutation.Blood. 2011;118:109.
    • (2011) Blood , vol.118 , pp. 109
    • Cortes, J.E.1    Kim, D.-W.2    Pinilla-Ibarz, J.3
  • 98
    • 33644889108 scopus 로고    scopus 로고
    • Allosteric inhibitors of Bcr-abl-dependent cell proliferation
    • Adrian FJ,Ding Q,Sim T, et al.Allosteric inhibitors of Bcr-abl-dependent cell proliferation.Nat Chem Biol. 2006;2:95-102.
    • (2006) Nat Chem Biol , vol.2 , pp. 95-102
    • Adrian, F.J.1    Ding, Q.2    Sim, T.3
  • 99
    • 75749146563 scopus 로고    scopus 로고
    • Targeting Bcr-Abl by combining allosteric with ATP-binding-site inhibitors
    • Zhang J,Adrián FJ,Jahnke W, et al.Targeting Bcr-Abl by combining allosteric with ATP-binding-site inhibitors.Nature. 2010;463:501-6.
    • (2010) Nature , vol.463 , pp. 501-506
    • Zhang, J.1    Adrián, F.J.2    Jahnke, W.3
  • 102
    • 78149470597 scopus 로고    scopus 로고
    • Insights into the stem cells of chronic myeloid leukemia
    • Sloma I,Jiang X,Eaves AC,Eaves CJ.Insights into the stem cells of chronic myeloid leukemia.Leukemia. 2010;24:1823-33.
    • (2010) Leukemia , vol.24 , pp. 1823-1833
    • Sloma, I.1    Jiang, X.2    Eaves, A.C.3    Eaves, C.J.4
  • 103
    • 2442465000 scopus 로고    scopus 로고
    • Requirement of Src kinases Lyn, Hck and Fgr for BCR-ABL1-induced B-lymphoblastic leukemia but not chronic myeloid leukemia
    • Hu Y,Liu Y,Pelletier S, et al.Requirement of Src kinases Lyn, Hck and Fgr for BCR-ABL1-induced B-lymphoblastic leukemia but not chronic myeloid leukemia.Nat Genet. 2004;36:453-61.
    • (2004) Nat Genet , vol.36 , pp. 453-461
    • Hu, Y.1    Liu, Y.2    Pelletier, S.3
  • 104
    • 0037438640 scopus 로고    scopus 로고
    • BCR-ABL independence and LYN kinase overexpression in chronic myelogenous leukemia cells selected for resistance to STI571
    • Donato NJ,Wu JY,Stapley J, et al.BCR-ABL independence and LYN kinase overexpression in chronic myelogenous leukemia cells selected for resistance to STI571.Blood. 2003;101:690-8.
    • (2003) Blood , vol.101 , pp. 690-698
    • Donato, N.J.1    Wu, J.Y.2    Stapley, J.3
  • 105
    • 46849114097 scopus 로고    scopus 로고
    • Association between imatinib-resistant BCR-ABL mutation-negative leukemia and persistent activation of LYN kinase
    • Wu J,Meng F,Kong LY, et al.Association between imatinib-resistant BCR-ABL mutation-negative leukemia and persistent activation of LYN kinase.J Natl Cancer Inst. 2008;100:926-39.
    • (2008) J Natl Cancer Inst , vol.100 , pp. 926-939
    • Wu, J.1    Meng, F.2    Kong, L.Y.3
  • 106
    • 0031455168 scopus 로고    scopus 로고
    • The Src family kinase Hck interacts with Bcr-Abl by a kinase-independent mechanism and phosphorylates the Grb2-binding site of Bcr
    • Warmuth M,Bergmann M,Priess A,Hauslmann K,Emmerich B,Hallek M.The Src family kinase Hck interacts with Bcr-Abl by a kinase-independent mechanism and phosphorylates the Grb2-binding site of Bcr.J Biol Chem. 1997;272:33260-70.
    • (1997) J Biol Chem , vol.272 , pp. 33260-33270
    • Warmuth, M.1    Bergmann, M.2    Priess, A.3    Hauslmann, K.4    Emmerich, B.5    Hallek, M.6
  • 107
    • 79952437988 scopus 로고    scopus 로고
    • Janus kinase 2 regulates Bcr-Abl signaling in chronic myeloid leukemia
    • Samanta A,Perazzona B,Chakraborty S, et al.Janus kinase 2 regulates Bcr-Abl signaling in chronic myeloid leukemia.Leukemia. 2011;25:463-72.
    • (2011) Leukemia , vol.25 , pp. 463-472
    • Samanta, A.1    Perazzona, B.2    Chakraborty, S.3
  • 108
    • 84860726170 scopus 로고    scopus 로고
    • Blockade of JAK2-mediated extrinsic survival signals restores sensitivity of CML cells to ABL inhibitors
    • Traer E,Mackenzie R,Snead J, et al.Blockade of JAK2-mediated extrinsic survival signals restores sensitivity of CML cells to ABL inhibitors.Leukemia. 2012;26:1140-3.
    • (2012) Leukemia , vol.26 , pp. 1140-1143
    • Traer, E.1    Mackenzie, R.2    Snead, J.3
  • 109
    • 0346999590 scopus 로고    scopus 로고
    • Phosphotyrosine mapping in Bcr/Abl oncoprotein using phosphotyrosine-specific immonium ion scanning
    • Steen H,Fernandez M,Ghaffari S,Pandey A,Mann M.Phosphotyrosine mapping in Bcr/Abl oncoprotein using phosphotyrosine-specific immonium ion scanning.Mol Cell Proteomics. 2003;2:138-45.
    • (2003) Mol Cell Proteomics , vol.2 , pp. 138-145
    • Steen, H.1    Fernandez, M.2    Ghaffari, S.3    Pandey, A.4    Mann, M.5
  • 110
    • 21144458164 scopus 로고    scopus 로고
    • Immunoaffinity profiling of tyrosine phosphorylation in cancer cells
    • Rush J,Moritz A,Lee KA, et al.Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.Nat Biotechnol. 2005;23:94-101.
    • (2005) Nat Biotechnol , vol.23 , pp. 94-101
    • Rush, J.1    Moritz, A.2    Lee, K.A.3
  • 111
    • 78149469721 scopus 로고    scopus 로고
    • The proximal signaling network of the BCR-ABL1 oncogene shows a modular organization
    • Titz B,Low T,Komisopoulou E,Chen SS,Rubbi L,Graeber TG.The proximal signaling network of the BCR-ABL1 oncogene shows a modular organization.Oncogene. 2010;29:5895-910.
    • (2010) Oncogene , vol.29 , pp. 5895-5910
    • Titz, B.1    Low, T.2    Komisopoulou, E.3    Chen, S.S.4    Rubbi, L.5    Graeber, T.G.6
  • 112
    • 84863124648 scopus 로고    scopus 로고
    • Chronic myeloid leukemia stem cells are not dependent on Bcr-Abl kinase activity for their survival
    • Hamilton A,Helgason GV,Schemionek M, et al.Chronic myeloid leukemia stem cells are not dependent on Bcr-Abl kinase activity for their survival.Blood. 2012;119:1501-10.
    • (2012) Blood , vol.119 , pp. 1501-1510
    • Hamilton, A.1    Helgason, G.V.2    Schemionek, M.3
  • 113
    • 78149463193 scopus 로고    scopus 로고
    • CML: how low can you go?
    • Schiffer CA.CML: how low can you go?.Blood. 2010;116:3686-7.
    • (2010) Blood , vol.116 , pp. 3686-3687
    • Schiffer, C.A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.