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Volumn 16, Issue 12, 1996, Pages 7054-7062

c-ABL tyrosine kinase activity is regulated by association with a novel SH3-domain-binding protein

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; CELL PROTEIN; ONCOPROTEIN; PROTEIN TYROSINE KINASE;

EID: 0029956391     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.16.12.7054     Document Type: Article
Times cited : (37)

References (49)
  • 2
    • 0026743906 scopus 로고
    • Identification of a protein that binds to the SH3 region of ABL and is similar to Bcr and GAP-rho
    • Cicchetti, P., B. J. Mayer, G. Thiel, and D. Baltimore. 1992. Identification of a protein that binds to the SH3 region of ABL and is similar to Bcr and GAP-rho. Science 257:803-806.
    • (1992) Science , vol.257 , pp. 803-806
    • Cicchetti, P.1    Mayer, B.J.2    Thiel, G.3    Baltimore, D.4
  • 3
    • 0028999836 scopus 로고
    • 3BP-1, an SH3 domain binding protein, has GAP activity for Rac and inhibits growth factor-induced membrane ruffling in fibroblasts
    • Cicchetti, P., A. J. Ridley, Y. Zheng, R. A. Cerione, and D. Baltimore. 1995. 3BP-1, an SH3 domain binding protein, has GAP activity for Rac and inhibits growth factor-induced membrane ruffling in fibroblasts. EMBO J. 14:3127-3135.
    • (1995) EMBO J. , vol.14 , pp. 3127-3135
    • Cicchetti, P.1    Ridley, A.J.2    Zheng, Y.3    Cerione, R.A.4    Baltimore, D.5
  • 4
    • 0027300619 scopus 로고
    • The when and how of Src regulation
    • Cooper, J. A., and B. Howell. 1993. The when and how of Src regulation. Cell 73:1051-1054.
    • (1993) Cell , vol.73 , pp. 1051-1054
    • Cooper, J.A.1    Howell, B.2
  • 5
    • 0017863403 scopus 로고
    • Studies on the properties and mode of action of the purified regulatory subunit of bovine heart adenosine 3′:5′-monophosphate-dependent protein kinase
    • Corbin, J. D. 1978. Studies on the properties and mode of action of the purified regulatory subunit of bovine heart adenosine 3′:5′-monophosphate-dependent protein kinase. J. Biol. Chem. 253:3997-4003.
    • (1978) J. Biol. Chem. , vol.253 , pp. 3997-4003
    • Corbin, J.D.1
  • 6
    • 0016430836 scopus 로고
    • The distribution and dissociation of cyclic adenosine 3′:5′-monophosphate-dependent protein kinases in adipose, cardiac, and other tissues
    • Corbin, J. D., S. L. Keely, and C. R. Park. 1975. The distribution and dissociation of cyclic adenosine 3′:5′-monophosphate-dependent protein kinases in adipose, cardiac, and other tissues. J. Biol. Chem. 250:218-225.
    • (1975) J. Biol. Chem. , vol.250 , pp. 218-225
    • Corbin, J.D.1    Keely, S.L.2    Park, C.R.3
  • 7
    • 11944275667 scopus 로고
    • ABI-2, a novel SH3-containing protein, interacts with the c-ABL tyrosine kinase and modulates c-ABL transforming activity
    • Dai, Z., and A. M. Pendergast. 1995. ABI-2, a novel SH3-containing protein, interacts with the c-ABL tyrosine kinase and modulates c-ABL transforming activity. Genes Dev. 9:2583-2597.
    • (1995) Genes Dev. , vol.9 , pp. 2583-2597
    • Dai, Z.1    Pendergast, A.M.2
  • 8
    • 0017406326 scopus 로고
    • Isolation and properties of the rabbit skeletal muscle protein inhibitor of adenosine 3′,5′-monophosphate dependent protein kinases
    • Demaillie, J. G., K. A. Peter, and E. H. Fischer. 1977. Isolation and properties of the rabbit skeletal muscle protein inhibitor of adenosine 3′,5′-monophosphate dependent protein kinases. Biochemistry 16:3080-3086.
    • (1977) Biochemistry , vol.16 , pp. 3080-3086
    • Demaillie, J.G.1    Peter, K.A.2    Fischer, E.H.3
  • 9
    • 0029980440 scopus 로고    scopus 로고
    • Molecular glue: Kinase anchoring and scaffold proteins
    • Faux, M. C., and J. D. Scott. 1996. Molecular glue: kinase anchoring and scaffold proteins. Cell 85:9-12.
    • (1996) Cell , vol.85 , pp. 9-12
    • Faux, M.C.1    Scott, J.D.2
  • 10
    • 0028243505 scopus 로고
    • c-ABL kinase regulates the protein binding activity of c-CRK
    • Feller, S. M., B. Knudsen, and H. Hanafusa. 1994. c-ABL kinase regulates the protein binding activity of c-CRK. EMBO J. 13:2341-2351.
    • (1994) EMBO J. , vol.13 , pp. 2341-2351
    • Feller, S.M.1    Knudsen, B.2    Hanafusa, H.3
  • 11
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • London
    • Fields, S., and O. Song. 1989. A novel genetic system to detect protein-protein interactions. Nature (London) 340:245-246.
    • (1989) Nature , vol.340 , pp. 245-246
    • Fields, S.1    Song, O.2
  • 12
    • 0024461553 scopus 로고
    • Deletion of an N-terminal regulatory domain of c-ABL tyrosire kinase activates its oncogenic potential
    • Franz, W. M., P. Berger, and J. Y. J. Wang. 1989. Deletion of an N-terminal regulatory domain of c-ABL tyrosire kinase activates its oncogenic potential. EMBO J. 8:137-147.
    • (1989) EMBO J. , vol.8 , pp. 137-147
    • Franz, W.M.1    Berger, P.2    Wang, J.Y.J.3
  • 13
    • 0028895654 scopus 로고
    • Modular binding domains in signal transduction proteins
    • George, B. C., R. Ren, and D. Baltimore. 1995. Modular binding domains in signal transduction proteins. Cell 80:237-248.
    • (1995) Cell , vol.80 , pp. 237-248
    • George, B.C.1    Ren, R.2    Baltimore, D.3
  • 14
    • 0026562884 scopus 로고
    • Improved method for high efficiency transformation of intact yeast cells
    • Gietz, S. A., A. St. Jean, R. A. Woods, and R. H. Schiestl. 1992. Improved method for high efficiency transformation of intact yeast cells. Nucleic Acids Res. 20:1425.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 1425
    • Gietz, S.A.1    St. Jean, A.2    Woods, R.A.3    Schiestl, R.H.4
  • 15
    • 0020538097 scopus 로고
    • Demonstration of permanent factor-dependent multipotential (erythroid/neutrophil/basophil) hematopoietic progenitor cell lines
    • Greenberger, J. S., M. A. Sakakeeny, M. A. Humphries, C. J. Eaves, and R. J. Eckner. 1983. Demonstration of permanent factor-dependent multipotential (erythroid/neutrophil/basophil) hematopoietic progenitor cell lines. Proc. Natl. Acad. Sci. USA 80:2931-2935.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 2931-2935
    • Greenberger, J.S.1    Sakakeeny, M.A.2    Humphries, M.A.3    Eaves, C.J.4    Eckner, R.J.5
  • 16
    • 0030061922 scopus 로고    scopus 로고
    • IRS-1-mediated inhibition of insulin receptor tyrosine kinase activity in TNF-alpha and obesity-induced insulin resistance
    • Homatmisligil, G. S., P. Peraldi, A. Budavari, R. Ellis, M. F. White, and B. M. Spiegelman. 1996. IRS-1-mediated inhibition of insulin receptor tyrosine kinase activity in TNF-alpha and obesity-induced insulin resistance. Science 271:665-668.
    • (1996) Science , vol.271 , pp. 665-668
    • Homatmisligil, G.S.1    Peraldi, P.2    Budavari, A.3    Ellis, R.4    White, M.F.5    Spiegelman, B.M.6
  • 17
    • 0028287635 scopus 로고
    • Insights into autoregulation from the crystal structure of twitchin kinase
    • London
    • Hu, S. H. 1994. Insights into autoregulation from the crystal structure of twitchin kinase. Nature (London) 369:581-584.
    • (1994) Nature , vol.369 , pp. 581-584
    • Hu, S.H.1
  • 18
    • 0024343691 scopus 로고
    • N-terminal mutation activates the leukemogenic potential of the myristoylated form of c-ABL
    • Jackson, P., and D. Baltimore. 1989. N-terminal mutation activates the leukemogenic potential of the myristoylated form of c-ABL. EMBO J. 8:449-456.
    • (1989) EMBO J. , vol.8 , pp. 449-456
    • Jackson, P.1    Baltimore, D.2
  • 19
    • 0028333768 scopus 로고
    • Sequential protein kinase reactions controlling cell growth and differentiation
    • Johnson, G. L., and R. R. Vaillancourt. 1994. Sequential protein kinase reactions controlling cell growth and differentiation. Curr. Opin. Cell Biol. 6:230-238.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 230-238
    • Johnson, G.L.1    Vaillancourt, R.R.2
  • 20
    • 0028251408 scopus 로고
    • Substrate and pseudosubstrate interactions with protein kinases: Determinants of specificity
    • Kemp, B. E., M. W. Parker, S. Hu, T. Tiganis, and C. House. 1994. Substrate and pseudosubstrate interactions with protein kinases: determinants of specificity. Trends Biochem. Sci. 19:440-444.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 440-444
    • Kemp, B.E.1    Parker, M.W.2    Hu, S.3    Tiganis, T.4    House, C.5
  • 21
    • 0025158107 scopus 로고
    • Protein kinase recognition sequence
    • Kemp, B. E., and R. B. Pearson. 1990. Protein kinase recognition sequence. Trends Biochem. Sci. 15:342-346.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 342-346
    • Kemp, B.E.1    Pearson, R.B.2
  • 22
    • 0023664006 scopus 로고
    • The calmodulin binding domain of chicken smooth muscle myosin light chain kinase contains a pseudosubstrate sequence
    • Kemp, B. E., R. B. Pearson, V. Guerriero, J. C. Bagchi, and A. R. Means. 1987. The calmodulin binding domain of chicken smooth muscle myosin light chain kinase contains a pseudosubstrate sequence. J. Biol. Chem. 262:2542-2548.
    • (1987) J. Biol. Chem. , vol.262 , pp. 2542-2548
    • Kemp, B.E.1    Pearson, R.B.2    Guerriero, V.3    Bagchi, J.C.4    Means, A.R.5
  • 23
    • 0029072131 scopus 로고
    • Intrasteric regulation of myosin light chain kinase
    • Krueger, J. K., R. C. Padre, and J. T. Stull. 1995. Intrasteric regulation of myosin light chain kinase. J. Biol. Chem. 270:16848-16853.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16848-16853
    • Krueger, J.K.1    Padre, R.C.2    Stull, J.T.3
  • 24
    • 0026686182 scopus 로고
    • Two species of human CRK cDNA encode proteins with distinct biological activities
    • Matsuda, M., S. Tanaka, S. Nagata, A. Kojima, T. Kurata, and M. Shibuta. 1992. Two species of human CRK cDNA encode proteins with distinct biological activities. Mol. Cell. Biol. 12:3482-3489.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3482-3489
    • Matsuda, M.1    Tanaka, S.2    Nagata, S.3    Kojima, A.4    Kurata, T.5    Shibuta, M.6
  • 25
    • 0027943714 scopus 로고
    • Activation of cyclin-dependent kinase 4 (cdk4) by mouse MO15-associated kinase
    • Matsuoka, M., J.-Y. Kato, R. P. Fisher, D. O. Morgan, and C. J. Sherr. 1994. Activation of cyclin-dependent kinase 4 (cdk4) by mouse MO15-associated kinase. Mol. Cell. Biol. 14:7265-7275.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7265-7275
    • Matsuoka, M.1    Kato, J.-Y.2    Fisher, R.P.3    Morgan, D.O.4    Sherr, C.J.5
  • 26
    • 0028212411 scopus 로고
    • Mutagenic analysis of the roles of SH2 and SH3 domains in regulation of the Abl tyrosine kinase
    • Mayer, B. J., and D. Baltimore. 1994. Mutagenic analysis of the roles of SH2 and SH3 domains in regulation of the Abl tyrosine kinase. Mol. Cell. Biol. 14:2883-2894.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 2883-2894
    • Mayer, B.J.1    Baltimore, D.2
  • 27
    • 0029257493 scopus 로고
    • Evidence that SH2 domains promote processive phosphorylation by protein tyrosine kinases
    • Mayer, B. J., H. Hirai, and R. Sakai. 1995. Evidence that SH2 domains promote processive phosphorylation by protein tyrosine kinases. Curr. Biol. 5:296-305.
    • (1995) Curr. Biol. , vol.5 , pp. 296-305
    • Mayer, B.J.1    Hirai, H.2    Sakai, R.3
  • 28
    • 0027422977 scopus 로고
    • A coiled-coil oligomerization domain of Bcr is essential for the transforming function of Bcr-Abl oncoproteins
    • McWhirter, J. R., D. L. Galasso, and J. Y. J. Wang. 1993. A coiled-coil oligomerization domain of Bcr is essential for the transforming function of Bcr-Abl oncoproteins. Mol. Cell. Biol. 13:7587-7597.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7587-7597
    • McWhirter, J.R.1    Galasso, D.L.2    Wang, J.Y.J.3
  • 29
    • 0025924674 scopus 로고
    • Activation of tyrosine kinase and microfilament-binding functions of c-abl by bcr sequences in bcr/abl fusion proteins
    • McWhirter, J. R., and J. Y. J. Wang. 1991. Activation of tyrosine kinase and microfilament-binding functions of c-abl by bcr sequences in bcr/abl fusion proteins. Mol. Cell. Biol. 11:1553-1565.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 1553-1565
    • McWhirter, J.R.1    Wang, J.Y.J.2
  • 30
    • 0025959660 scopus 로고
    • BCR first exon sequences specifically activate the BCRIABL tyrosine kinase oncogene of Philadelphia chromosome-positive human leukemias
    • Muller, A. J., J. C. Young, A.-M. Pendergast, M. Pondel, N. R. Landau, D. R. Littman, and O. N. Witte. 1991. BCR first exon sequences specifically activate the BCRIABL tyrosine kinase oncogene of Philadelphia chromosome-positive human leukemias. Mol. Cell. Biol. 11:1785-1792.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 1785-1792
    • Muller, A.J.1    Young, J.C.2    Pendergast, A.-M.3    Pondel, M.4    Landau, N.R.5    Littman, D.R.6    Witte, O.N.7
  • 31
    • 0023571161 scopus 로고
    • Nucleotide sequence of testis-derived c-ABL cDNAs: Implications for testis-specific transcription and ABL oncogene activation
    • Oppi, C., S. K. Shore, and E. P. Reddy. 1987. Nucleotide sequence of testis-derived c-ABL cDNAs: implications for testis-specific transcription and ABL oncogene activation. Proc. Natl. Acad. Sci. USA 84:8200-8204.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 8200-8204
    • Oppi, C.1    Shore, S.K.2    Reddy, E.P.3
  • 32
    • 0023932685 scopus 로고
    • Calcium/calmodulin-dependent protein kinase. II. Characterization of distinct calmodulin binding and inhibitory domains
    • Payne, M. E. 1988. Calcium/calmodulin-dependent protein kinase. II. Characterization of distinct calmodulin binding and inhibitory domains. J. Biol. Chem. 263:7190-7195.
    • (1988) J. Biol. Chem. , vol.263 , pp. 7190-7195
    • Payne, M.E.1
  • 34
    • 0025766195 scopus 로고
    • BCR sequences essential for transformation by the BCR-ABL oncogene bind to the ABL SH2 regulatory domain in a non-phosphotyrosine-dependent manner
    • Pendergast, A. M., A. J. Muller, M. H. Havlik, Y. Maru, and O. N. Witte. 1991. BCR sequences essential for transformation by the BCR-ABL oncogene bind to the ABL SH2 regulatory domain in a non-phosphotyrosine-dependent manner. Cell 66:161-171.
    • (1991) Cell , vol.66 , pp. 161-171
    • Pendergast, A.M.1    Muller, A.J.2    Havlik, M.H.3    Maru, Y.4    Witte, O.N.5
  • 35
    • 0028329787 scopus 로고
    • Arresting developments in cell cycle control
    • Pine, J. 1994. Arresting developments in cell cycle control. Trends Biochem. Sci. 19:143-145.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 143-145
    • Pine, J.1
  • 36
    • 0020770310 scopus 로고
    • Nucleotide sequence of Abelson murine leukemia virus genome: Structural similarity of its transforming gene product to other oncogene products with tyrosine-specific kinase activity
    • Reddy, E. P., M. J. Smith, and A. Sirnivasan. 1983. Nucleotide sequence of Abelson murine leukemia virus genome: structural similarity of its transforming gene product to other oncogene products with tyrosine-specific kinase activity. Proc. Natl. Acad. Sci. USA 80:3623-3627.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 3623-3627
    • Reddy, E.P.1    Smith, M.J.2    Sirnivasan, A.3
  • 37
    • 0027408247 scopus 로고
    • Identification of a ten-amino acid proline-rich SH3 binding site
    • Ren, R., Z. Ye, and D. Baltimore. 1993. Identification of a ten-amino acid proline-rich SH3 binding site. Science 259:1157-1161.
    • (1993) Science , vol.259 , pp. 1157-1161
    • Ren, R.1    Ye, Z.2    Baltimore, D.3
  • 38
    • 0028181873 scopus 로고
    • ABL protein-tyrosine kinase selects the CRK adapter as a substrate using SH3-binding sites
    • Ren, R., Z. S. Ye, and D. Baltimore. 1994. ABL protein-tyrosine kinase selects the CRK adapter as a substrate using SH3-binding sites. Genes Dev. 8:783-795.
    • (1994) Genes Dev. , vol.8 , pp. 783-795
    • Ren, R.1    Ye, Z.S.2    Baltimore, D.3
  • 39
    • 0022971952 scopus 로고
    • Amino acid sequences common to rapidly degraded proteins: The PEST hypothesis
    • Rogers, S. R., R. Wells, and M. Rechsteiner. 1986. Amino acid sequences common to rapidly degraded proteins: the PEST hypothesis. Science 234: 364-368.
    • (1986) Science , vol.234 , pp. 364-368
    • Rogers, S.R.1    Wells, R.2    Rechsteiner, M.3
  • 40
    • 0028844631 scopus 로고
    • ABL-interactor-1, a novel SH3 protein binding to the carboxy-terminal portion of the ABL protein, suppresses v-ABL transforming activity
    • Shi, Y., K. Ålin, and S. P. Goff. 1995. ABL-interactor-1, a novel SH3 protein binding to the carboxy-terminal portion of the ABL protein, suppresses v-ABL transforming activity. Genes Dev. 9:2583-2597.
    • (1995) Genes Dev. , vol.9 , pp. 2583-2597
    • Shi, Y.1    Ålin, K.2    Goff, S.P.3
  • 41
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith, D. B., and G. L. Long. 1988. Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene 67:31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Long, G.L.2
  • 42
    • 0028149381 scopus 로고
    • The coordinated action of protein tyrosine phosphatases and kinases in cell signaling
    • Sun, T., and N. K. Tonks. 1994. The coordinated action of protein tyrosine phosphatases and kinases in cell signaling. Trends Biochem. Sci. 19:480-484.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 480-484
    • Sun, T.1    Tonks, N.K.2
  • 43
    • 0029072404 scopus 로고
    • Introduction of a loss-of-function point mutation from the SH3 region of the Caenorhabditis elegans sem-5 gene activates the transforming ability of c-ABL in vivo and abolishes binding of proline-rich ligands in vitro
    • Van Etten, R. A., J. Debnath, H. Zhou, and J. M. Casasnovas. 1995. Introduction of a loss-of-function point mutation from the SH3 region of the Caenorhabditis elegans sem-5 gene activates the transforming ability of c-ABL in vivo and abolishes binding of proline-rich ligands in vitro. Oncogene 10:1977-1988.
    • (1995) Oncogene , vol.10 , pp. 1977-1988
    • Van Etten, R.A.1    Debnath, J.2    Zhou, H.3    Casasnovas, J.M.4
  • 44
    • 0026009187 scopus 로고
    • Utilization of the inhibitor protein of adenosine cyclic monophosphate-dependent protein kinase, and peptides derived from it, as tools to study adenosine cyclic monophosphate-mcdiated cellular processes
    • Walsh, D. A., and D. B. Galss. 1991. Utilization of the inhibitor protein of adenosine cyclic monophosphate-dependent protein kinase, and peptides derived from it, as tools to study adenosine cyclic monophosphate-mcdiated cellular processes. Methods Enzymol. 201:304-316.
    • (1991) Methods Enzymol. , vol.201 , pp. 304-316
    • Walsh, D.A.1    Galss, D.B.2
  • 45
    • 0027406462 scopus 로고
    • ABL tyrosine kinase in signal transduction and cell-cycle regulation
    • Wang, J. Y. J. 1993. ABL tyrosine kinase in signal transduction and cell-cycle regulation. Curr. Opin. Genet. Dev. 3:35-43.
    • (1993) Curr. Opin. Genet. Dev. , vol.3 , pp. 35-43
    • Wang, J.Y.J.1
  • 46
    • 0027429964 scopus 로고
    • A C-terminal protein-binding domain in the retinoblastoma protein regulates nuclear C-ABL tyrosine kinase in the cell cycle
    • Welch, P. J., and J. Y. J. Wang. 1993. A C-terminal protein-binding domain in the retinoblastoma protein regulates nuclear C-ABL tyrosine kinase in the cell cycle. Cell 75:779-790.
    • (1993) Cell , vol.75 , pp. 779-790
    • Welch, P.J.1    Wang, J.Y.J.2
  • 47
    • 0016804632 scopus 로고
    • Bovine brain adenosine 3′,5′-monophosphate dependent protein kinase. Mechanism of regulatory subunit inhibition of the catalytic subunit
    • Witt, J. J., and R. J. Roskoski. 1975. Bovine brain adenosine 3′,5′-monophosphate dependent protein kinase. Mechanism of regulatory subunit inhibition of the catalytic subunit. Biochemistry 14:4503-4507.
    • (1975) Biochemistry , vol.14 , pp. 4503-4507
    • Witt, J.J.1    Roskoski, R.J.2
  • 48
    • 0024316095 scopus 로고
    • Cloning of the murine c-FGR protooncogene cDNA and induction of c-FGR expression by proliferation and activation factors in normal bone marrow-derived monocytic cells
    • Yi, T., and C. L. Willman. 1989. Cloning of the murine c-FGR protooncogene cDNA and induction of c-FGR expression by proliferation and activation factors in normal bone marrow-derived monocytic cells. Oncogene 4:1081-1087.
    • (1989) Oncogene , vol.4 , pp. 1081-1087
    • Yi, T.1    Willman, C.L.2
  • 49
    • 0029880874 scopus 로고    scopus 로고
    • Activated ABL oncogenes and apoptosis: Differing responses of transformed mycloid progenitor cell lines
    • Zhu, J., P. N. Nabissa, B. Hoffman, D. A. Liebermann, and S. K. Shore. 1996. Activated ABL oncogenes and apoptosis: differing responses of transformed mycloid progenitor cell lines. Blood 87:4368-4375.
    • (1996) Blood , vol.87 , pp. 4368-4375
    • Zhu, J.1    Nabissa, P.N.2    Hoffman, B.3    Liebermann, D.A.4    Shore, S.K.5


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