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Volumn 15, Issue 8, 2004, Pages 3520-3529

Enteropathogenic Escherichia coli use redundant tyrosine kinases to form actin pedestals

Author keywords

[No Author keywords available]

Indexed keywords

ABELSON KINASE; ACTIN; PROTEIN TYROSINE KINASE; PYRIDO[2,3 D]PYRIMIDINE DERIVATIVE;

EID: 3343010235     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E04-02-0093     Document Type: Article
Times cited : (98)

References (62)
  • 1
    • 0037425580 scopus 로고    scopus 로고
    • Fyn tyrosine kinase is a critical regulator of disabled-1 during brain development
    • Arnaud, L., Ballif, B.A., Foerster, E., and Cooper, J.A. (2003). Fyn tyrosine kinase is a critical regulator of disabled-1 during brain development. Curr. Biol. 13, 9-17.
    • (2003) Curr. Biol. , vol.13 , pp. 9-17
    • Arnaud, L.1    Ballif, B.A.2    Foerster, E.3    Cooper, J.A.4
  • 2
    • 0142041888 scopus 로고    scopus 로고
    • Abl tyrosine kinases are required for infection by Shigella flexneri
    • Burton, E.A., Plattner, R., and Pendergast, A.M. (2003). Abl tyrosine kinases are required for infection by Shigella flexneri. EMBO J. 22, 5471-5479.
    • (2003) EMBO J. , vol.22 , pp. 5471-5479
    • Burton, E.A.1    Plattner, R.2    Pendergast, A.M.3
  • 3
    • 0842309767 scopus 로고    scopus 로고
    • Clustering of Nck by a 12-residue Tir phosphopeptide is sufficient to trigger localized actin assembly
    • Campellone, K.G., Rankin, S., Pawson, T., Kirschner, M.W., Tipper, J., and Leong, J.M. (2004). Clustering of Nck by a 12-residue Tir phosphopeptide is sufficient to trigger localized actin assembly. J. Cell Biol. 164, 407-416.
    • (2004) J. Cell Biol. , vol.164 , pp. 407-416
    • Campellone, K.G.1    Rankin, S.2    Pawson, T.3    Kirschner, M.W.4    Tipper, J.5    Leong, J.M.6
  • 4
    • 0034254928 scopus 로고    scopus 로고
    • Molecular and cell biology aspects of plague
    • Cornelis, G.R. (2000). Molecular and cell biology aspects of plague. Proc. Natl. Acad. Sci. USA 97, 8778-8783.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 8778-8783
    • Cornelis, G.R.1
  • 6
    • 0027250343 scopus 로고
    • A second chromosomal gene necessary for intimate attachment of enteropathogenic Escherichia coli to epithelial cells
    • Donnenberg, M.S., Yu, J., and Kaper, J.B. (1993). A second chromosomal gene necessary for intimate attachment of enteropathogenic Escherichia coli to epithelial cells. J. Bacteriol. 175, 4670-4676.
    • (1993) J. Bacteriol. , vol.175 , pp. 4670-4676
    • Donnenberg, M.S.1    Yu, J.2    Kaper, J.B.3
  • 7
    • 0034095603 scopus 로고    scopus 로고
    • The pyrido[2,3-d]pyrimidine derivative PD180970 inhibits p210Bcr-Abl tyrosine kinase and induces apoptosis of K562 leukemic cells
    • Dorsey, J.F., Jove, R., Kraker, A.J., and Wu, J. (2000). The pyrido[2,3-d]pyrimidine derivative PD180970 inhibits p210Bcr-Abl tyrosine kinase and induces apoptosis of K562 leukemic cells. Cancer Res. 60, 3127-3131.
    • (2000) Cancer Res. , vol.60 , pp. 3127-3131
    • Dorsey, J.F.1    Jove, R.2    Kraker, A.J.3    Wu, J.4
  • 9
    • 0031024613 scopus 로고    scopus 로고
    • Crk is required for apoptosis in Xenopus egg extracts
    • Evans, E.K., Lu, W., Strum, S.L., Mayer, B.J., and Kornbluth, S. (1997). Crk is required for apoptosis in Xenopus egg extracts. EMBO J. 16, 230-241.
    • (1997) EMBO J. , vol.16 , pp. 230-241
    • Evans, E.K.1    Lu, W.2    Strum, S.L.3    Mayer, B.J.4    Kornbluth, S.5
  • 10
    • 0028283880 scopus 로고
    • The eaeB gene of enteropathogenic Escherichia coli is necessary for signal transduction in epithelial cells
    • Foubister, V., Rosenshine, I., Donnenberg, M.S., and Finlay, B.B. (1994). The eaeB gene of enteropathogenic Escherichia coli is necessary for signal transduction in epithelial cells. Infect. Immun. 62, 3038-3040.
    • (1994) Infect. Immun. , vol.62 , pp. 3038-3040
    • Foubister, V.1    Rosenshine, I.2    Donnenberg, M.S.3    Finlay, B.B.4
  • 13
    • 0035496899 scopus 로고    scopus 로고
    • Chronic myeloid leukemia: Current treatment options
    • Goldman, J.M., and Druker, B.J. (2001). Chronic myeloid leukemia: current treatment options. Blood 98, 2039-2042.
    • (2001) Blood , vol.98 , pp. 2039-2042
    • Goldman, J.M.1    Druker, B.J.2
  • 14
    • 0035059331 scopus 로고    scopus 로고
    • Recruitment of cytoskeletal and signaling proteins to enteropathogenic and enterohemorrhagic Escherichia coli pedestals
    • Goosney, D.L., DeVinney, R., and Finlay, B.B. (2001). Recruitment of cytoskeletal and signaling proteins to enteropathogenic and enterohemorrhagic Escherichia coli pedestals. Infect. Immun. 69, 3315-3333.
    • (2001) Infect. Immun. , vol.69 , pp. 3315-3333
    • Goosney, D.L.1    DeVinney, R.2    Finlay, B.B.3
  • 15
    • 0034518342 scopus 로고    scopus 로고
    • Gut feelings: Enteropathogenic E. coli (EPEC) interactions with the host
    • Goosney, D.L., Gruenheid, S., and Finlay, B.B. (2000). Gut feelings: enteropathogenic E. coli (EPEC) interactions with the host. Annu. Rev. Cell Dev. Biol. 16, 173-189.
    • (2000) Annu. Rev. Cell Dev. Biol. , vol.16 , pp. 173-189
    • Goosney, D.L.1    Gruenheid, S.2    Finlay, B.B.3
  • 16
    • 0035800507 scopus 로고    scopus 로고
    • Clinical resistance to STI-571 cancer therapy caused by BCR-ABL gene mutation or amplification
    • Gorre, M.E., Mohammed, M., Ellwood, K., Hsu, N., Paquette, R., Rao, P.N., and Sawyers, C.L. (2001). Clinical resistance to STI-571 cancer therapy caused by BCR-ABL gene mutation or amplification. Science 293, 876-880.
    • (2001) Science , vol.293 , pp. 876-880
    • Gorre, M.E.1    Mohammed, M.2    Ellwood, K.3    Hsu, N.4    Paquette, R.5    Rao, P.N.6    Sawyers, C.L.7
  • 18
    • 85047697990 scopus 로고    scopus 로고
    • Cell transformation by the middle T-antigen of polyoma virus
    • Ichaso, N., and Dilworth, S.M. (2001). Cell transformation by the middle T-antigen of polyoma virus. Oncogene. 20, 7908-7916.
    • (2001) Oncogene , vol.20 , pp. 7908-7916
    • Ichaso, N.1    Dilworth, S.M.2
  • 19
    • 0028038920 scopus 로고
    • Genetics of signal transduction: Tales from the mouse
    • Imamoto, A., Soriano, P., and Stein, P.L. (1994). Genetics of signal transduction: tales from the mouse. Curr. Opin. Genet. Dev. 4, 40-46.
    • (1994) Curr. Opin. Genet. Dev. , vol.4 , pp. 40-46
    • Imamoto, A.1    Soriano, P.2    Stein, P.L.3
  • 20
    • 0029099975 scopus 로고
    • Enteropathogenic Escherichia coli contains a putative type III secretion system necessary for the export of proteins involved in attaching and effacing lesion formation
    • Jarvis, K.G., Giron, J.A., Jerse, A.E., McDaniel, T.K., Donnenberg, M.S., and Kaper, J.B. (1995). Enteropathogenic Escherichia coli contains a putative type III secretion system necessary for the export of proteins involved in attaching and effacing lesion formation. Proc. Natl. Acad. Sci. USA 92, 7996-8000.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7996-8000
    • Jarvis, K.G.1    Giron, J.A.2    Jerse, A.E.3    McDaniel, T.K.4    Donnenberg, M.S.5    Kaper, J.B.6
  • 23
    • 0033002855 scopus 로고    scopus 로고
    • Phosphorylation of tyrosine 474 of the enteropathogenic Escherichia coli (EPEC) Tir receptor molecule is essential for actin nucleating activity and is preceded by additional host modifications
    • Kenny, B. (1999). Phosphorylation of tyrosine 474 of the enteropathogenic Escherichia coli (EPEC) Tir receptor molecule is essential for actin nucleating activity and is preceded by additional host modifications. Mol. Microbiol. 31, 1229-1241.
    • (1999) Mol. Microbiol. , vol.31 , pp. 1229-1241
    • Kenny, B.1
  • 24
    • 0030701868 scopus 로고    scopus 로고
    • Enteropathogenic E. coli (EPEC) transfers its receptor for intimate adherence into mammalian cells
    • Kenny, B., DeVinney, R., Stein, M., Reinscheid, D.J., Frey, E.A., and Finlay, B.B. (1997). Enteropathogenic E. coli (EPEC) transfers its receptor for intimate adherence into mammalian cells. Cell 91, 511-520.
    • (1997) Cell , vol.91 , pp. 511-520
    • Kenny, B.1    DeVinney, R.2    Stein, M.3    Reinscheid, D.J.4    Frey, E.A.5    Finlay, B.B.6
  • 25
    • 0030701868 scopus 로고    scopus 로고
    • Enteropathogenic E. coli (EPEC) transfers its receptor for intimate adherence into mammalian cells
    • Kenny, B., Devinney, R., Stein, M., Reinscheid, D.J., Frey, E.A., and Finlay, B.B. (1999). Enteropathogenic E. coli (EPEC) transfers its receptor for intimate adherence into mammalian cells. Cell 91, 511-520.
    • (1999) Cell , vol.91 , pp. 511-520
    • Kenny, B.1    Devinney, R.2    Stein, M.3    Reinscheid, D.J.4    Frey, E.A.5    Finlay, B.B.6
  • 26
    • 0035106689 scopus 로고    scopus 로고
    • The two PDGF receptors maintain conserved signaling in vivo despite divergent embryological functions
    • Klinghoffer, R.A., Mueting-Nelsen, P.F., Faerman, A., Shani, M., and Soriano, P. (2001). The two PDGF receptors maintain conserved signaling in vivo despite divergent embryological functions. Mol. Cell 7, 343-354.
    • (2001) Mol. Cell , vol.7 , pp. 343-354
    • Klinghoffer, R.A.1    Mueting-Nelsen, P.F.2    Faerman, A.3    Shani, M.4    Soriano, P.5
  • 29
    • 0034308176 scopus 로고    scopus 로고
    • Biochemical and cellular effects of c-Src kinase-selective pyrido[2,3-d]pyrimidine tyrosine kinase inhibitors
    • Kraker, A.J., Hartl, B.C., Amar, A.M., Barvian, M.R., Showalter, H.D., and Moore, C.W. (2000). Biochemical and cellular effects of c-Src kinase-selective pyrido[2,3-d]pyrimidine tyrosine kinase inhibitors. Biochem. Pharmacol. 60, 885-898.
    • (2000) Biochem. Pharmacol. , vol.60 , pp. 885-898
    • Kraker, A.J.1    Hartl, B.C.2    Amar, A.M.3    Barvian, M.R.4    Showalter, H.D.5    Moore, C.W.6
  • 30
    • 0029348008 scopus 로고
    • Abl tyrosine protein kinase
    • Laneuville, P. (1995). Abl tyrosine protein kinase. Semin. Immunol. 7, 255-266.
    • (1995) Semin. Immunol. , vol.7 , pp. 255-266
    • Laneuville, P.1
  • 31
    • 0033983099 scopus 로고    scopus 로고
    • From Abl to actin: Abl tyrosine kinase and associated proteins in growth cone morility
    • Lanier, L.M., and Gertler, F.B. (2000). From Abl to actin: Abl tyrosine kinase and associated proteins in growth cone morility. Curr. Opin. Neurobiol. 10, 80-87.
    • (2000) Curr. Opin. Neurobiol. , vol.10 , pp. 80-87
    • Lanier, L.M.1    Gertler, F.B.2
  • 32
    • 0036839579 scopus 로고    scopus 로고
    • Chemoattractant-stimulated Rac activation in wild-type and Rac2-deficient murine neutrophils: Preferential activation of Rac2 and Rac2 gene dosage effect on neutrophil functions
    • Li, S., Yamauchi, A., Marchal, C.C., Molitoris, J.K., Quilliam, L.A., and Dinauer, M.C. (2002). Chemoattractant-stimulated Rac activation in wild-type and Rac2-deficient murine neutrophils: preferential activation of Rac2 and Rac2 gene dosage effect on neutrophil functions. J. Immunol. 169, 5043-5051.
    • (2002) J. Immunol. , vol.169 , pp. 5043-5051
    • Li, S.1    Yamauchi, A.2    Marchal, C.C.3    Molitoris, J.K.4    Quilliam, L.A.5    Dinauer, M.C.6
  • 34
    • 0034769365 scopus 로고    scopus 로고
    • Actin pedestal formation by enteropathogenic Escherichia coli and intracellular motility of Shigella flexneri are abolished in N-WASP-defective cells
    • Lommel, S., Benesch, S., Rottner, K., Franz, T., Wehland, J., and Kuhn, R. (2001). Actin pedestal formation by enteropathogenic Escherichia coli and intracellular motility of Shigella flexneri are abolished in N-WASP-defective cells. EMBO Rep. 2, 850-857.
    • (2001) EMBO Rep. , vol.2 , pp. 850-857
    • Lommel, S.1    Benesch, S.2    Rottner, K.3    Franz, T.4    Wehland, J.5    Kuhn, R.6
  • 36
    • 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., and Kuriyan, J. (2002). Crystal structures of the kinase domain of c-Abl in complex with the small molecule inhibitors PD173955 and imatinib (STI-571). Cancer Res. 62, 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
  • 37
    • 0036391801 scopus 로고    scopus 로고
    • The Abl family kinases: Mechanisms of regulation and signaling
    • Pendergast, A.M. (2002). The Abl family kinases: mechanisms of regulation and signaling. Adv. Cancer Res. 85, 51-100.
    • (2002) Adv. Cancer Res. , vol.85 , pp. 51-100
    • Pendergast, A.M.1
  • 38
    • 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., and Pendergast, A.M. (1999). c-Abl is activated by growth factors and Src family kinases and has a role in the cellular response to PDGF. Genes Dev. 13, 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
  • 39
    • 0037169351 scopus 로고    scopus 로고
    • Autoinhibition of c-Abl
    • Pluk, H., Dorey, K., and Superti-Furga, G. (2002). Autoinhibition of c-Abl. Cell. 108, 247-259.
    • (2002) Cell , vol.108 , pp. 247-259
    • Pluk, H.1    Dorey, K.2    Superti-Furga, G.3
  • 40
    • 0031561479 scopus 로고    scopus 로고
    • Signal transduction by wild-type and leukemogenic Abl proteins
    • Raitano, A.B., Whang, Y.E., and Sawyers, C.L. (1997). Signal transduction by wild-type and leukemogenic Abl proteins. Biochim. Biophys. Acta 1333, F201-F216.
    • (1997) Biochim. Biophys. Acta , vol.1333
    • Raitano, A.B.1    Whang, Y.E.2    Sawyers, C.L.3
  • 41
    • 0028181873 scopus 로고
    • Abl protein-tyrosine kinase selects the Crk adapter as a substrate using SH3-binding sites
    • Ren, R., Ye, Z.S., and Baltimore, D. (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
  • 42
    • 0020647208 scopus 로고
    • Hemorrhagic colitis associated with a rare Escherichia coli serotype
    • Riley, L.W., et al. (1983). Hemorrhagic colitis associated with a rare Escherichia coli serotype. N. Engl. J. Med. 308, 681-685.
    • (1983) N. Engl. J. Med. , vol.308 , pp. 681-685
    • Riley, L.W.1
  • 43
    • 0034693799 scopus 로고    scopus 로고
    • The protein tyrosine kinase family of the human genome
    • Robinson, D.R., Wu, Y.M., and Lin, S.F. (2000). The protein tyrosine kinase family of the human genome. Oncogene 19, 5548-5557.
    • (2000) Oncogene , vol.19 , pp. 5548-5557
    • Robinson, D.R.1    Wu, Y.M.2    Lin, S.F.3
  • 44
    • 0033574722 scopus 로고    scopus 로고
    • The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly
    • Rohatgi, R., Ma, L., Miki, H., Lopez, M., Kirchhausen, T., Takenawa, T., and Kirschner, M.W. (1999). The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly. Cell 97, 221-231.
    • (1999) Cell , vol.97 , pp. 221-231
    • Rohatgi, R.1    Ma, L.2    Miki, H.3    Lopez, M.4    Kirchhausen, T.5    Takenawa, T.6    Kirschner, M.W.7
  • 45
    • 0026733626 scopus 로고
    • Signal transduction between enteropathogenic Escherichia coli (EPEC) and epithelial cells: EPEC induces tyrosine phosphorylation of host cell proteins to initiate cytoskeletal rearrangement and bacterial uptake
    • Rosenshine, I., Donnenberg, M.S., Kaper, J.B., and Finlay, B.B. (1992). Signal transduction between enteropathogenic Escherichia coli (EPEC) and epithelial cells: EPEC induces tyrosine phosphorylation of host cell proteins to initiate cytoskeletal rearrangement and bacterial uptake. EMBO J. 11, 3551-3560.
    • (1992) EMBO J. , vol.11 , pp. 3551-3560
    • Rosenshine, I.1    Donnenberg, M.S.2    Kaper, J.B.3    Finlay, B.B.4
  • 46
    • 3342909864 scopus 로고
    • Enteropathogenic Escherichia coli Epec activates protein tyrosine kinase Tpk in infected epithelial cells characterization of the major Tpk substrate
    • Rosenshine, I., and Finlay, B.B. (1993). Enteropathogenic Escherichia coli Epec activates protein tyrosine kinase Tpk in infected epithelial cells characterization of the major Tpk substrate. Abstr. Gen. Meet. Am. Soc. Microbiol. 93, 73.
    • (1993) Abstr. Gen. Meet. Am. Soc. Microbiol. , vol.93 , pp. 73
    • Rosenshine, I.1    Finlay, B.B.2
  • 47
    • 0029933731 scopus 로고    scopus 로고
    • A pathogenic bacterium triggers epithelial signals to form a functional bacterial receptor that mediates actin pseudopod formation
    • Rosenshine, I., Ruschkowski, S., Stein, M., Reinscheid, D.J., Mills, S.D., and Finlay, B.B. (1996). A pathogenic bacterium triggers epithelial signals to form a functional bacterial receptor that mediates actin pseudopod formation. EMBO J. 15, 2613-2624.
    • (1996) EMBO J. , vol.15 , pp. 2613-2624
    • Rosenshine, I.1    Ruschkowski, S.2    Stein, M.3    Reinscheid, D.J.4    Mills, S.D.5    Finlay, B.B.6
  • 50
    • 0037169481 scopus 로고    scopus 로고
    • Cell surface-localized nucleolin is a eukaryotic receptor for the adhesin intimin-gamma of enterohemorrhagic Escherichia coli O 157, H7
    • Sinclair, J.F., and O'Brien, A.D. (2002). Cell surface-localized nucleolin is a eukaryotic receptor for the adhesin intimin-gamma of enterohemorrhagic Escherichia coli O 157, H7. J. Biol. Chem. 277, 2876-2885.
    • (2002) J. Biol. Chem. , vol.277 , pp. 2876-2885
    • Sinclair, J.F.1    O'Brien, A.D.2
  • 51
    • 0033600837 scopus 로고    scopus 로고
    • Activation of the Abl tyrosine kinase in vivo by Src homology 3 domains from the SrSrc homology 2/SrSrc homology 3 adaptor Nck
    • Smith, J.M., Katz, S., and Mayer, B.J. (1999). Activation of the Abl tyrosine kinase in vivo by Src homology 3 domains from the SrSrc homology 2/SrSrc homology 3 adaptor Nck. J. Biol. Chem. 274, 27956-27962.
    • (1999) J. Biol. Chem. , vol.274 , pp. 27956-27962
    • Smith, J.M.1    Katz, S.2    Mayer, B.J.3
  • 52
    • 0036371220 scopus 로고    scopus 로고
    • Abl: Mechanisms of regulation and activation
    • Smith, J.M., and Mayer, B.J. (2002). Abl: mechanisms of regulation and activation. Front. Biosci. 7, d31-d42.
    • (2002) Front. Biosci. , vol.7
    • Smith, J.M.1    Mayer, B.J.2
  • 53
    • 0028170518 scopus 로고
    • Combined deficiencies of SrSrc, Fyn, and Yes tyrosine kinases in mutant mice
    • Stein, P.L., Vogel, H., and Soriano, P. (1994). Combined deficiencies of SrSrc, Fyn, and Yes tyrosine kinases in mutant mice. Genes Dev. 8, 1999-2007.
    • (1994) Genes Dev. , vol.8 , pp. 1999-2007
    • Stein, P.L.1    Vogel, H.2    Soriano, P.3
  • 54
    • 0002757927 scopus 로고    scopus 로고
    • Deconvolution in optical microscopy
    • ed. P.A. Jansson, San Diego: Academic Press
    • Swedlow, J.R., Sedat, J.W., and Agard, D.A. (1997). Deconvolution in optical microscopy. In: Deconvolution of Images and Spectra, ed. P.A. Jansson, San Diego: Academic Press, 284-307.
    • (1997) Deconvolution of Images and Spectra , pp. 284-307
    • Swedlow, J.R.1    Sedat, J.W.2    Agard, D.A.3
  • 55
    • 0028789982 scopus 로고
    • Differential inhibition of signaling pathways by dominant-negative SH2/SH3 adapter proteins
    • Tanaka, M., Gupta, R., and Mayer, B.J. (1995). Differential inhibition of signaling pathways by dominant-negative SH2/SH3 adapter proteins. Mol. Cell Biol. 15, 6829-6837.
    • (1995) Mol. Cell Biol. , vol.15 , pp. 6829-6837
    • Tanaka, M.1    Gupta, R.2    Mayer, B.J.3
  • 56
    • 0038813693 scopus 로고    scopus 로고
    • The SrSrc-selective kinase inhibitor PP1 also inhibits Kit and Bcr-Abl tyrosine kinases
    • Tatton, L., Morley, G.M., Chopra, R., and Khwaja, A. (2003). The SrSrc-selective kinase inhibitor PP1 also inhibits Kit and Bcr-Abl tyrosine kinases. J. Biol. Chem. 278, 4847-4853.
    • (2003) J. Biol. Chem. , vol.278 , pp. 4847-4853
    • Tatton, L.1    Morley, G.M.2    Chopra, R.3    Khwaja, A.4
  • 57
    • 0035909994 scopus 로고    scopus 로고
    • Genetically encoded fluorescent reporters of protein tyrosine kinase activities in living cells
    • Ting, A.Y., Kain, K.H., Klemke, R.L., and Tsien, R.Y. (2001). Genetically encoded fluorescent reporters of protein tyrosine kinase activities in living cells. Proc. Natl. Acad. Sci. USA 98, 15003-15008.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 15003-15008
    • Ting, A.Y.1    Kain, K.H.2    Klemke, R.L.3    Tsien, R.Y.4
  • 58
    • 0025780879 scopus 로고
    • Neonatal lethality and lymphopenia in mice with a homozygous disruption of the c-abl proto-oncogene
    • Tybulewicz, V.L., Crawford, C.E., Jackson, P.K., Bronson, R.T., and Mulligan, R.C. (1991). Neonatal lethality and lymphopenia in mice with a homozygous disruption of the c-abl proto-oncogene. Cell 65, 1153-1163.
    • (1991) Cell , vol.65 , pp. 1153-1163
    • Tybulewicz, V.L.1    Crawford, C.E.2    Jackson, P.K.3    Bronson, R.T.4    Mulligan, R.C.5
  • 59
    • 0024218250 scopus 로고
    • Negative regulation of c-abl tyrosine kinase by its variable N-terminal amino acids
    • Wang, J.Y. (1988). Negative regulation of c-abl tyrosine kinase by its variable N-terminal amino acids. Oncogene Res. 3, 293-298.
    • (1988) Oncogene Res. , vol.3 , pp. 293-298
    • Wang, J.Y.1
  • 60
    • 0036682230 scopus 로고    scopus 로고
    • Characterization of potent inhibitors of the Bcr-Abl and the c-kit receptor tyrosine kinases
    • Wisniewski, D., et al. (2002). Characterization of potent inhibitors of the Bcr-Abl and the c-kit receptor tyrosine kinases. Cancer Res. 62, 4244-4255.
    • (2002) Cancer Res. , vol.62 , pp. 4244-4255
    • Wisniewski, D.1
  • 61
    • 0035920195 scopus 로고    scopus 로고
    • Inhibition of c-Abl tyrosine kinase activity by filamentous actin
    • Woodring, P.J., Hunter, T., and Wang, J.Y. (2001). Inhibition of c-Abl tyrosine kinase activity by filamentous actin. J. Biol. Chem. 276, 27104-27110.
    • (2001) J. Biol. Chem. , vol.276 , pp. 27104-27110
    • Woodring, P.J.1    Hunter, T.2    Wang, J.Y.3
  • 62
    • 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., and Hunter, T. (2002). Modulation of the F-actin cytoskeleton by c-Abl tyrosine kinase in cell spreading and neurite extension. J. Cell Biol. 156, 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.