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Volumn 112, Issue 6, 2003, Pages 845-857

A myristoyl/phosphotyrosine switch regulates c-Abl

Author keywords

[No Author keywords available]

Indexed keywords

IMATINIB; ONCOPROTEIN; PHOSPHOTYROSINE; PROTEIN TYROSINE KINASE;

EID: 0344626925     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(03)00191-0     Document Type: Article
Times cited : (391)

References (63)
  • 1
    • 0037459344 scopus 로고    scopus 로고
    • Mechanisms of autoinhibition and STI-157/imatinib resistance revealed by mutagenesis of BCR-ABL
    • this issue,
    • Azam M., Latek R.R., Daley G.Q. Mechanisms of autoinhibition and STI-157/imatinib resistance revealed by mutagenesis of BCR-ABL. Cell. 112:2003;831-843. this issue,
    • (2003) Cell , vol.112 , pp. 831-843
    • Azam, M.1    Latek, R.R.2    Daley, G.Q.3
  • 2
    • 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. 18:1998;280-282.
    • (1998) Nat. Genet. , vol.18 , pp. 280-282
    • Barilá, D.1    Superti-Furga, G.2
  • 4
    • 0035902180 scopus 로고    scopus 로고
    • Oncogenic kinase signaling
    • Blume-Jensen P., Hunter T. Oncogenic kinase signaling. Nature. 411:2001;355-365.
    • (2001) Nature , vol.411 , pp. 355-365
    • Blume-Jensen, P.1    Hunter, T.2
  • 5
    • 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 B.B., Van Etten R.A. 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. 275:2000;35631-35637.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35631-35637
    • Brasher, B.B.1    Van Etten, R.A.2
  • 6
    • 0035935998 scopus 로고    scopus 로고
    • Mutational analysis of the regulatory function of the c-Abl Src homology 3 domain
    • Brasher B.B., Roumiantsev S., Van Etten R.A. Mutational analysis of the regulatory function of the c-Abl Src homology 3 domain. Oncogene. 20:2001;7744-7752.
    • (2001) Oncogene , vol.20 , pp. 7744-7752
    • Brasher, B.B.1    Roumiantsev, S.2    Van Etten, R.A.3
  • 7
    • 0034510155 scopus 로고    scopus 로고
    • Cytoskeletal protein PSTPIP1 directs the PEST-type protein tyrosine phosphatase to the c-Abl kinase to mediate Abl dephosphorylation
    • Cong F., Spencer S., Cote J.F., Wu Y., Tremblay M.L., Lasky L.A., Goff S.P. Cytoskeletal protein PSTPIP1 directs the PEST-type protein tyrosine phosphatase to the c-Abl kinase to mediate Abl dephosphorylation. Mol. Cell. 6:2000;1413-1423.
    • (2000) Mol. Cell , vol.6 , pp. 1413-1423
    • Cong, F.1    Spencer, S.2    Cote, J.F.3    Wu, Y.4    Tremblay, M.L.5    Lasky, L.A.6    Goff, S.P.7
  • 10
    • 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 J.R., Kretzschmar J., Wilm M., Neubauer G., Schindler T., Superti-Furga G. Phosphorylation and structure-based functional studies reveal a positive and a negative role for the activation loop of the c-Abl tyrosine kinase. Oncogene. 20:2001;8075-8084.
    • (2001) Oncogene , vol.20 , pp. 8075-8084
    • Dorey, K.1    Engen, J.R.2    Kretzschmar, J.3    Wilm, M.4    Neubauer, G.5    Schindler, T.6    Superti-Furga, G.7
  • 12
    • 0027940655 scopus 로고
    • SH2 and SH3 domains as molecular adhesives: The interactions of Crk and Abl
    • Feller S.M., Ren R., Hanafusa H., Baltimore D. SH2 and SH3 domains as molecular adhesives. the interactions of Crk and Abl Trends Biochem. Sci. 19:1994;453-458.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 453-458
    • Feller, S.M.1    Ren, R.2    Hanafusa, H.3    Baltimore, D.4
  • 13
    • 0037084333 scopus 로고    scopus 로고
    • C-Abl is an effector of Src for growth factor-induced c-myc expression and DNA synthesis
    • Furstoss O., Dorey K., Simon V., Barila D., Superti-Furga G., Roche S. c-Abl is an effector of Src for growth factor-induced c-myc expression and DNA synthesis. EMBO J. 21:2002;514-524.
    • (2002) EMBO J. , vol.21 , pp. 514-524
    • Furstoss, O.1    Dorey, K.2    Simon, V.3    Barila, D.4    Superti-Furga, G.5    Roche, S.6
  • 14
    • 0031464009 scopus 로고    scopus 로고
    • The role of the linker between the SH2 domain and catalytic domain in the regulation and function of Src
    • Gonfloni S., Williams J.C., Hattula K., Weijland A., Wierenga R.K., Superti-Furga G. The role of the linker between the SH2 domain and catalytic domain in the regulation and function of Src. EMBO J. 16:1997;7261-7271.
    • (1997) EMBO J. , vol.16 , pp. 7261-7271
    • Gonfloni, S.1    Williams, J.C.2    Hattula, K.3    Weijland, A.4    Wierenga, R.K.5    Superti-Furga, G.6
  • 15
    • 0032769397 scopus 로고    scopus 로고
    • Leucine 255 of Src couples intramolecular interactions to inhibition of catalysis
    • Gonfloni S., Frischknecht F., Way M., Superti-Furga G. Leucine 255 of Src couples intramolecular interactions to inhibition of catalysis. Nat. Struct. Biol. 6:1999;760-764.
    • (1999) Nat. Struct. Biol. , vol.6 , pp. 760-764
    • Gonfloni, S.1    Frischknecht, F.2    Way, M.3    Superti-Furga, G.4
  • 16
    • 0034072765 scopus 로고    scopus 로고
    • Crosstalk between the catalytic and regulatory domains allows bidirectional regulation of Src
    • Gonfloni S., Weijland A., Kretzschmar J., Superti-Furga G. Crosstalk between the catalytic and regulatory domains allows bidirectional regulation of Src. Nat. Struct. Biol. 7:2000;281-286.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 281-286
    • Gonfloni, S.1    Weijland, A.2    Kretzschmar, J.3    Superti-Furga, G.4
  • 17
    • 0029991686 scopus 로고    scopus 로고
    • Transgenes encoding both type I and type IV c-abl proteins rescue the lethality of c-abl mutant mice
    • Hardin J.D., Boast S., Mendelsohn M., de los Santos K., Goff S.P. Transgenes encoding both type I and type IV c-abl proteins rescue the lethality of c-abl mutant mice. Oncogene. 12:1996;2669-2677.
    • (1996) Oncogene , vol.12 , pp. 2669-2677
    • Hardin, J.D.1    Boast, S.2    Mendelsohn, M.3    De los Santos, K.4    Goff, S.P.5
  • 18
    • 0032925147 scopus 로고    scopus 로고
    • Structural analysis of receptor tyrosine kinases
    • Hubbard S.R. Structural analysis of receptor tyrosine kinases. Prog. Biophys. Mol. Biol. 71:1999;343-358.
    • (1999) Prog. Biophys. Mol. Biol. , vol.71 , pp. 343-358
    • Hubbard, S.R.1
  • 19
    • 0036909260 scopus 로고    scopus 로고
    • Protein tyrosine kinases: Autoregulation and small-molecule inhibition
    • Hubbard S.R. Protein tyrosine kinases. autoregulation and small-molecule inhibition Curr. Opin. Struct. Biol. 12:2002;735-741.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 735-741
    • Hubbard, S.R.1
  • 20
    • 0033786922 scopus 로고    scopus 로고
    • Protein tyrosine kinase structure and function
    • Hubbard S.R., Till J.H. Protein tyrosine kinase structure and function. Annu. Rev. Biochem. 69:2000;373-398.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 373-398
    • Hubbard, S.R.1    Till, J.H.2
  • 21
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • Huse M., Kuriyan J. The conformational plasticity of protein kinases. Cell. 109:2002;275-282.
    • (2002) Cell , vol.109 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 22
    • 0024343691 scopus 로고
    • N-terminal mutations activate the leukemogenic potential of the myristoylated form of c-abl
    • Jackson P., Baltimore D. N-terminal mutations activate the leukemogenic potential of the myristoylated form of c-abl. EMBO J. 8:1989;449-456.
    • (1989) EMBO J. , vol.8 , pp. 449-456
    • Jackson, P.1    Baltimore, D.2
  • 26
    • 0026601293 scopus 로고
    • Point mutations in the abl SH2 domain coordinately impair phosphotyrosine binding in vitro and transforming activity in vivo
    • Mayer B.J., Jackson P.K., Van Etten R.A., Baltimore D. Point mutations in the abl SH2 domain coordinately impair phosphotyrosine binding in vitro and transforming activity in vivo. Mol. Cell. Biol. 12:1992;609-618.
    • (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
  • 27
    • 0027422977 scopus 로고
    • A coiled-coil oligomerization domain of Bcr is essential for the transforming function of Bcr-Abl oncoproteins
    • McWhirter J.R., Galasso D.L., Wang J.Y. A coiled-coil oligomerization domain of Bcr is essential for the transforming function of Bcr-Abl oncoproteins. Mol. Cell. Biol. 13:1993;7587-7595.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7587-7595
    • McWhirter, J.R.1    Galasso, D.L.2    Wang, J.Y.3
  • 29
    • 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. 1:1994;546-551.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 546-551
    • Musacchio, A.1    Saraste, M.2    Wilmanns, M.3
  • 30
    • 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 W.G., Pellicena P., Schindler T., Veach D.R., Miller W.T., Clarkson B., Kuriyan J. Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI-571). Cancer Res. 62:2002;4236-4243.
    • (2002) Cancer Res. , vol.62 , pp. 4236-4243
    • Nagar, B.1    Bornmann, W.G.2    Pellicena, P.3    Schindler, T.4    Veach, D.R.5    Miller, W.T.6    Clarkson, B.7    Kuriyan, J.8
  • 32
    • 0036391801 scopus 로고    scopus 로고
    • The Abl family kinases: Mechanisms of regulation and signaling
    • Pendergast A.M. The Abl family kinases. mechanisms of regulation and signaling Adv. Cancer Res. 85:2002;51-100.
    • (2002) Adv. Cancer Res. , vol.85 , pp. 51-100
    • Pendergast, A.M.1
  • 33
    • 0033568349 scopus 로고    scopus 로고
    • C-Abl is activated by growth factors and src family kinases and has a role in the cellular response to PDGF
    • Plattner R., Kadlec L., DeMali K.A., Kazlauskas A., Pendergast A.M. c-Abl is activated by growth factors and src family kinases and has a role in the cellular response to PDGF. Genes Dev. 13:1999;2400-2411.
    • (1999) Genes Dev. , vol.13 , pp. 2400-2411
    • Plattner, R.1    Kadlec, L.2    DeMali, K.A.3    Kazlauskas, A.4    Pendergast, A.M.5
  • 34
  • 35
    • 0034723419 scopus 로고    scopus 로고
    • Reciprocal regulation of Hck activity by phosphorylation of Tyr(527) and Tyr(416). Effect of introducing a high affinity intramolecular SH2 ligand
    • Porter M., Schindler T., Kuriyan J., Miller W.T. Reciprocal regulation of Hck activity by phosphorylation of Tyr(527) and Tyr(416). Effect of introducing a high affinity intramolecular SH2 ligand. J. Biol. Chem. 275:2000;2721-2726.
    • (2000) J. Biol. Chem. , vol.275 , pp. 2721-2726
    • Porter, M.1    Schindler, T.2    Kuriyan, J.3    Miller, W.T.4
  • 36
    • 0031561479 scopus 로고    scopus 로고
    • Signal transduction by wild-type and leukemogenic Abl proteins
    • Raitano A.B., Whang Y.E., Sawyers C.L. Signal transduction by wild-type and leukemogenic Abl proteins. Biochim. Biophys. Acta. 1333:1997;F201-F216.
    • (1997) Biochim. Biophys. Acta , vol.1333
    • Raitano, A.B.1    Whang, Y.E.2    Sawyers, C.L.3
  • 37
    • 0023774753 scopus 로고
    • Differential expression of type-specific c-abl mRNAs in mouse tissues and cell lines
    • Renshaw M.W., Capozza M.A., Wang J.Y. Differential expression of type-specific c-abl mRNAs in mouse tissues and cell lines. Mol. Cell. Biol. 8:1988;4547-4551.
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 4547-4551
    • Renshaw, M.W.1    Capozza, M.A.2    Wang, J.Y.3
  • 38
    • 0028173679 scopus 로고
    • Myristylation and palmitylation of Src family members: The fats of the matter
    • Resh M.D. Myristylation and palmitylation of Src family members. the fats of the matter Cell. 76:1994;411-413.
    • (1994) Cell , vol.76 , pp. 411-413
    • Resh, M.D.1
  • 39
    • 0032875098 scopus 로고    scopus 로고
    • Fatty acylation of proteins: New insights into membrane targeting of myristoylated and palmitoylated proteins
    • Resh M.D. Fatty acylation of proteins. new insights into membrane targeting of myristoylated and palmitoylated proteins Biochim. Biophys. Acta. 1451:1999;1-16.
    • (1999) Biochim. Biophys. Acta , vol.1451 , pp. 1-16
    • Resh, M.D.1
  • 40
    • 0036678472 scopus 로고    scopus 로고
    • Clinical resistance to the kinase inhibitor STI-571 in chronic myeloid leukemia by mutation of Tyr-253 in the Abl kinase domain P-loop
    • Roumiantsev S., Shah N.P., Gorre M.E., Nicoll J., Brasher B.B., Sawyers C.L., Van Etten R.A. Clinical resistance to the kinase inhibitor STI-571 in chronic myeloid leukemia by mutation of Tyr-253 in the Abl kinase domain P-loop. Proc. Natl. Acad. Sci. USA. 99:2002;10700-10705.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 10700-10705
    • Roumiantsev, S.1    Shah, N.P.2    Gorre, M.E.3    Nicoll, J.4    Brasher, B.B.5    Sawyers, C.L.6    Van Etten, R.A.7
  • 41
    • 0025719212 scopus 로고
    • Selective binding of activated pp60c-src by an immobilized synthetic phosphopeptide modeled on the carboxyl terminus of pp60c-src
    • Roussel R.R., Brodeur S.R., Shalloway D., Laudano A.P. Selective binding of activated pp60c-src by an immobilized synthetic phosphopeptide modeled on the carboxyl terminus of pp60c-src. Proc. Natl. Acad. Sci. USA. 88:1991;10696-10700.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10696-10700
    • Roussel, R.R.1    Brodeur, S.R.2    Shalloway, D.3    Laudano, A.P.4
  • 42
    • 0036463987 scopus 로고    scopus 로고
    • Disabling Abl-perspectives on Abl kinase regulation and cancer therapeutics
    • Sawyers C.L. Disabling Abl-perspectives on Abl kinase regulation and cancer therapeutics. Cancer Cell. 1:2002;13-15.
    • (2002) Cancer Cell , vol.1 , pp. 13-15
    • Sawyers, C.L.1
  • 44
    • 0034644539 scopus 로고    scopus 로고
    • Cell signaling by receptor tyrosine kinases
    • Schlessinger J. Cell signaling by receptor tyrosine kinases. Cell. 103:2000;211-225.
    • (2000) Cell , vol.103 , pp. 211-225
    • Schlessinger, J.1
  • 46
    • 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. 385:1997;602-609.
    • (1997) Nature , vol.385 , pp. 602-609
    • Sicheri, F.1    Moarefi, I.2    Kuriyan, J.3
  • 47
    • 0036371220 scopus 로고    scopus 로고
    • Abl: Mechanisms of regulation and activation
    • Smith J.M., Mayer B.J. Abl. mechanisms of regulation and activation Front. Biosci. 7:2002;d31-d42.
    • (2002) Front. Biosci. , vol.7
    • Smith, J.M.1    Mayer, B.J.2
  • 48
    • 0029278886 scopus 로고
    • Structure-function relationships in Src family and related protein tyrosine kinases
    • Superti-Furga G., Courtneidge S.A. Structure-function relationships in Src family and related protein tyrosine kinases. Bioessays. 17:1995;321-330.
    • (1995) Bioessays , vol.17 , pp. 321-330
    • Superti-Furga, G.1    Courtneidge, S.A.2
  • 50
    • 0033552652 scopus 로고    scopus 로고
    • Protein myristoylation in protein-lipid and protein-protein interactions
    • Taniguchi H. Protein myristoylation in protein-lipid and protein-protein interactions. Biophys. Chem. 82:1999;129-137.
    • (1999) Biophys. Chem. , vol.82 , pp. 129-137
    • Taniguchi, H.1
  • 51
    • 0031197185 scopus 로고    scopus 로고
    • Protein kinase inhibition: Natural and synthetic variations on a theme
    • Taylor S.S., Radzio-Andzelm E. Protein kinase inhibition. natural and synthetic variations on a theme Curr. Opin. Chem. Biol. 1:1997;219-226.
    • (1997) Curr. Opin. Chem. Biol. , vol.1 , pp. 219-226
    • Taylor, S.S.1    Radzio-Andzelm, E.2
  • 52
    • 0025780879 scopus 로고
    • Neonatal lethality and lymphopenia in mice with a homozygous disruption of the c-abl proto-oncogene
    • Tybulewicz V.L.J., Crawford C.E., Jackson P.K., Bronson R.T., Mulligan R.C. Neonatal lethality and lymphopenia in mice with a homozygous disruption of the c-abl proto-oncogene. Cell. 65:1991;1153-1163.
    • (1991) Cell , vol.65 , pp. 1153-1163
    • Tybulewicz, V.L.J.1    Crawford, C.E.2    Jackson, P.K.3    Bronson, R.T.4    Mulligan, R.C.5
  • 53
    • 0032937828 scopus 로고    scopus 로고
    • Cycling, stressed-out and nervous: Cellular functions of c-Abl
    • Van Etten R.A. Cycling, stressed-out and nervous. cellular functions of c-Abl Trends Cell Biol. 9:1999;179-186.
    • (1999) Trends Cell Biol. , vol.9 , pp. 179-186
    • Van Etten, R.A.1
  • 54
    • 0028084328 scopus 로고
    • The COOH terminus of the c-Abl tyrosine kinase contains distinct F- and G-actin binding domains with bundling activity
    • Van Etten R.A., Jackson P.K., Baltimore D., Sanders M.C., Matsudaira P.T., Janmey P.A. The COOH terminus of the c-Abl tyrosine kinase contains distinct F- and G-actin binding domains with bundling activity. J. Cell Biol. 124:1994;325-340.
    • (1994) J. Cell Biol. , vol.124 , pp. 325-340
    • Van Etten, R.A.1    Jackson, P.K.2    Baltimore, D.3    Sanders, M.C.4    Matsudaira, P.T.5    Janmey, P.A.6
  • 56
    • 0037018155 scopus 로고    scopus 로고
    • Modulation of the F-actin cytoskeleton by c-Abl tyrosine kinase in cell spreading and neurite extension
    • Woodring P.J., Litwack E.D., O'Leary D.D., Lucero G.R., Wang J.Y., Hunter T. Modulation of the F-actin cytoskeleton by c-Abl tyrosine kinase in cell spreading and neurite extension. J. Cell Biol. 156:2002;879-892.
    • (2002) J. Cell Biol. , vol.156 , pp. 879-892
    • Woodring, P.J.1    Litwack, E.D.2    O'Leary, D.D.3    Lucero, G.R.4    Wang, J.Y.5    Hunter, T.6
  • 57
    • 0031025991 scopus 로고    scopus 로고
    • Three-dimensional structure of the tyrosine kinase c-Src
    • Xu W., Harrison S.C., Eck M.J. Three-dimensional structure of the tyrosine kinase c-Src. Nature. 385:1997;595-601.
    • (1997) Nature , vol.385 , pp. 595-601
    • Xu, W.1    Harrison, S.C.2    Eck, M.J.3
  • 58
    • 0034141280 scopus 로고    scopus 로고
    • Association of the Abl tyrosine kinase with the Trk nerve growth factor receptor
    • Yano H., Cong F., Birge R.B., Goff S.P., Chao M.V. Association of the Abl tyrosine kinase with the Trk nerve growth factor receptor. J. Neurosci. Res. 59:2000;356-364.
    • (2000) J. Neurosci. Res. , vol.59 , pp. 356-364
    • Yano, H.1    Cong, F.2    Birge, R.B.3    Goff, S.P.4    Chao, M.V.5
  • 59
    • 0035815288 scopus 로고    scopus 로고
    • Dynamic coupling between the SH2 and SH3 domains of c-Src and Hck underlies their inactivation by C-terminal tyrosine phosphorylation
    • Young M.A., Gonfloni S., Superti-Furga G., Roux B., Kuriyan J. Dynamic coupling between the SH2 and SH3 domains of c-Src and Hck underlies their inactivation by C-terminal tyrosine phosphorylation. Cell. 105:2001;115-126.
    • (2001) Cell , vol.105 , pp. 115-126
    • Young, M.A.1    Gonfloni, S.2    Superti-Furga, G.3    Roux, B.4    Kuriyan, J.5
  • 60
    • 0035811562 scopus 로고    scopus 로고
    • Multiple signaling interactions of Abl and Arg kinases with the EphB2 receptor
    • Yu H.H., Zisch A.H., Dodelet V.C., Pasquale E.B. Multiple signaling interactions of Abl and Arg kinases with the EphB2 receptor. Oncogene. 20:2001;3995-4006.
    • (2001) Oncogene , vol.20 , pp. 3995-4006
    • Yu, H.H.1    Zisch, A.H.2    Dodelet, V.C.3    Pasquale, E.B.4
  • 62
    • 0028265638 scopus 로고
    • Sequence specificity in the recognition of the epidermal growth factor receptor by the abl Src homology 2 domain
    • Zhu G., Decker S.J., Maclean D., McNamara D.J., Singh J., Sawyer T.K., Saltiel A.R. Sequence specificity in the recognition of the epidermal growth factor receptor by the abl Src homology 2 domain. Oncogene. 9:1994;1379-1385.
    • (1994) Oncogene , vol.9 , pp. 1379-1385
    • Zhu, G.1    Decker, S.J.2    Maclean, D.3    McNamara, D.J.4    Singh, J.5    Sawyer, T.K.6    Saltiel, A.R.7
  • 63
    • 0034671627 scopus 로고    scopus 로고
    • The c-Abl tyrosine kinase is regulated downstream of the B cell antigen receptor and interacts with CD19
    • Zipfel P.A., Grove M., Blackburn K., Fujimoto M., Tedder T.F., Pendergast A.M. The c-Abl tyrosine kinase is regulated downstream of the B cell antigen receptor and interacts with CD19. J. Immunol. 165:2000;6872-6879.
    • (2000) J. Immunol. , vol.165 , pp. 6872-6879
    • Zipfel, P.A.1    Grove, M.2    Blackburn, K.3    Fujimoto, M.4    Tedder, T.F.5    Pendergast, A.M.6


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