메뉴 건너뛰기




Volumn 4, Issue 123, 2012, Pages

Productive replication of ebola virus is regulated by the c-Abl1 tyrosine kinase

Author keywords

[No Author keywords available]

Indexed keywords

ABELSON KINASE; ALANINE; IMATINIB; NILOTINIB; PROTEIN KINASE INHIBITOR; PROTEIN VP40; SMALL INTERFERING RNA; 4 METHYL N (3 (4 METHYLIMIDAZOL 1 YL) 5 (TRIFLUOROMETHYL)PHENYL) 3 ((4 PYRIDIN 3 YLPYRIMIDIN 2 YL)AMINO)BENZAMIDE; 4-METHYL-N-(3-(4-METHYLIMIDAZOL-1-YL)-5-(TRIFLUOROMETHYL)PHENYL)-3-((4-PYRIDIN-3-YLPYRIMIDIN-2-YL)AMINO)BENZAMIDE; ANTIVIRUS AGENT; CORE PROTEIN; NUCLEOPROTEIN; NUCLEOPROTEIN VP40, EBOLA VIRUS; PYRIMIDINE DERIVATIVE; TYROSINE; VIRUS PROTEIN;

EID: 84857693882     PISSN: 19466234     EISSN: 19466242     Source Type: Journal    
DOI: 10.1126/scitranslmed.3003500     Document Type: Article
Times cited : (111)

References (58)
  • 1
    • 0036670360 scopus 로고    scopus 로고
    • The assembly of Ebola virus nucleocapsid requires virion-associated proteins 35 and 24 and posttranslational modification of nucleoprotein
    • Y. Huang, L. Xu, Y. Sun, G. J. Nabel, The assembly of Ebola virus nucleocapsid requires virion-associated proteins 35 and 24 and posttranslational modification of nucleoprotein. Mol. Cell 10, 307-316 (2002).
    • (2002) Mol. Cell , vol.10 , pp. 307-316
    • Huang, Y.1    Xu, L.2    Sun, Y.3    Nabel, G.J.4
  • 5
    • 0142041888 scopus 로고    scopus 로고
    • Abl tyrosine kinases are required for infection by Shigella flexneri
    • E. A. Burton, R. Plattner, A. M. Pendergast, Abl tyrosine kinases are required for infection by Shigella flexneri. EMBO J. 22, 5471-5479 (2003).
    • (2003) EMBO J. , vol.22 , pp. 5471-5479
    • Burton, E.A.1    Plattner, R.2    Pendergast, A.M.3
  • 8
    • 77950824613 scopus 로고    scopus 로고
    • Abl family tyrosine kinases regulate sialylated ganglioside receptors for polyomavirus
    • A. I. Swimm, W. Bornmann, M. Jiang, M. J. Imperiale, A. E. Lukacher, D. Kalman, Abl family tyrosine kinases regulate sialylated ganglioside receptors for polyomavirus. J. Virol. 84, 4243-4251 (2010).
    • (2010) J. Virol. , vol.84 , pp. 4243-4251
    • Swimm, A.I.1    Bornmann, W.2    Jiang, M.3    Imperiale, M.J.4    Lukacher, A.E.5    Kalman, D.6
  • 9
    • 78650053134 scopus 로고    scopus 로고
    • Variola and monkeypox viruses utilize conserved mechanisms of virion motility and release that depend on Abl and Src family tyrosine kinases
    • P. M. Reeves, S. K. Smith, V. A. Olson, S. H. Thorne, W. Bornmann, I. K. Damon, D. Kalman, Variola and monkeypox viruses utilize conserved mechanisms of virion motility and release that depend on Abl and Src family tyrosine kinases. J. Virol. 85, 21-31 (2011).
    • (2011) J. Virol. , vol.85 , pp. 21-31
    • Reeves, P.M.1    Smith, S.K.2    Olson, V.A.3    Thorne, S.H.4    Bornmann, W.5    Damon, I.K.6    Kalman, D.7
  • 10
    • 0033614446 scopus 로고    scopus 로고
    • Chronic myeloid leukemia
    • C. L. Sawyers, Chronic myeloid leukemia. N. Engl. J. Med. 340, 1330-1340 (1999).
    • (1999) N. Engl. J. Med. , vol.340 , pp. 1330-1340
    • Sawyers, C.L.1
  • 11
    • 0035496899 scopus 로고    scopus 로고
    • Chronic myeloid leukemia: Current treatment options
    • J. M. Goldman, B. J. Druker, Chronic myeloid leukemia: Current treatment options. Blood 98, 2039-2042 (2001).
    • (2001) Blood , vol.98 , pp. 2039-2042
    • Goldman, J.M.1    Druker, B.J.2
  • 15
    • 58149398623 scopus 로고    scopus 로고
    • Translation of the Philadelphia chromosome into therapy for CML
    • B. J. Druker, Translation of the Philadelphia chromosome into therapy for CML. Blood 112, 4808-4817 (2008).
    • (2008) Blood , vol.112 , pp. 4808-4817
    • Druker, B.J.1
  • 16
    • 3142710288 scopus 로고    scopus 로고
    • Contribution of Ebola virus glycoprotein, nucleoprotein, and VP24 to budding of VP40 virus-like particles
    • J. M. Licata, R. F. Johnson, Z. Han, R. N. Harty, Contribution of Ebola virus glycoprotein, nucleoprotein, and VP24 to budding of VP40 virus-like particles. J. Virol. 78, 7344-7351 (2004).
    • (2004) J. Virol. , vol.78 , pp. 7344-7351
    • Licata, J.M.1    Johnson, R.F.2    Han, Z.3    Harty, R.N.4
  • 17
    • 33947210792 scopus 로고    scopus 로고
    • Enteropathogenic Escherichia coli Tir is an SH2/3 ligand that recruits and activates tyrosine kinases required for pedestal formation
    • B. Bommarius, D. Maxwell, A. Swimm, S. Leung, A. Corbett, W. Bornmann, D. Kalman, Enteropathogenic Escherichia coli Tir is an SH2/3 ligand that recruits and activates tyrosine kinases required for pedestal formation. Mol. Microbiol. 63, 1748-1768 (2007).
    • (2007) Mol. Microbiol. , vol.63 , pp. 1748-1768
    • Bommarius, B.1    Maxwell, D.2    Swimm, A.3    Leung, S.4    Corbett, A.5    Bornmann, W.6    Kalman, D.7
  • 18
    • 29144487064 scopus 로고    scopus 로고
    • Filovirus assembly and budding
    • B. Hartlieb, W. Weissenhorn, Filovirus assembly and budding. Virology 344, 64-70 (2006).
    • (2006) Virology , vol.344 , pp. 64-70
    • Hartlieb, B.1    Weissenhorn, W.2
  • 19
    • 0034610295 scopus 로고    scopus 로고
    • A PPxY motif within the VP40 protein of Ebola virus interacts physically and functionally with a ubiquitin ligase: Implications for filovirus budding
    • R. N. Harty, M. E. Brown, G. Wang, J. Huibregtse, F. P. Hayes, A PPxY motif within the VP40 protein of Ebola virus interacts physically and functionally with a ubiquitin ligase: Implications for filovirus budding. Proc. Natl. Acad. Sci. U.S.A. 97, 13871-13876 (2000).
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 13871-13876
    • Harty, R.N.1    Brown, M.E.2    Wang, G.3    Huibregtse, J.4    Hayes, F.P.5
  • 21
    • 35549005397 scopus 로고    scopus 로고
    • Immunopathology of highly virulent pathogens: Insights from Ebola virus
    • C. A. Zampieri, N. J. Sullivan, G. J. Nabel, Immunopathology of highly virulent pathogens: Insights from Ebola virus. Nat. Immunol. 8, 1159-1164 (2007).
    • (2007) Nat. Immunol. , vol.8 , pp. 1159-1164
    • Zampieri, C.A.1    Sullivan, N.J.2    Nabel, G.J.3
  • 22
    • 0036235725 scopus 로고    scopus 로고
    • Ebola virus VP40 drives the formation of virus-like filamentous particles along with GP
    • T. Noda, H. Sagara, E. Suzuki, A. Takada, H. Kida, Y. Kawaoka, Ebola virus VP40 drives the formation of virus-like filamentous particles along with GP. J. Virol. 76, 4855-4865 (2002).
    • (2002) J. Virol. , vol.76 , pp. 4855-4865
    • Noda, T.1    Sagara, H.2    Suzuki, E.3    Takada, A.4    Kida, H.5    Kawaoka, Y.6
  • 24
    • 77953742423 scopus 로고    scopus 로고
    • Oligomerization of Ebola virus VP40 is essential for particle morphogenesis and regulation of viral transcription
    • T. Hoenen, N. Biedenkopf, F. Zielecki, S. Jung, A. Groseth, H. Feldmann, S. Becker, Oligomerization of Ebola virus VP40 is essential for particle morphogenesis and regulation of viral transcription. J. Virol. 84, 7053-7063 (2010).
    • (2010) J. Virol. , vol.84 , pp. 7053-7063
    • Hoenen, T.1    Biedenkopf, N.2    Zielecki, F.3    Jung, S.4    Groseth, A.5    Feldmann, H.6    Becker, S.7
  • 25
    • 33746029728 scopus 로고    scopus 로고
    • Effect of Ebola virus proteins GP, NP and VP35 on VP40 VLP morphology
    • R. F. Johnson, P. Bell, R. N. Harty, Effect of Ebola virus proteins GP, NP and VP35 on VP40 VLP morphology. Virol. J. 3, 31 (2006).
    • (2006) Virol. J. , vol.3 , pp. 31
    • Johnson, R.F.1    Bell, P.2    Harty, R.N.3
  • 26
    • 77649220531 scopus 로고    scopus 로고
    • Conserved motifs within Ebola and Marburg virus VP40 proteins are important for stability, localization, and subsequent budding of virus-like particles
    • Y. Liu, L. Cocka, A. Okumura, Y. A. Zhang, J. O. Sunyer, R. N. Harty, Conserved motifs within Ebola and Marburg virus VP40 proteins are important for stability, localization, and subsequent budding of virus-like particles. J. Virol. 84, 2294-2303 (2010).
    • (2010) J. Virol. , vol.84 , pp. 2294-2303
    • Liu, Y.1    Cocka, L.2    Okumura, A.3    Zhang, Y.A.4    Sunyer, J.O.5    Harty, R.N.6
  • 27
    • 0036371220 scopus 로고    scopus 로고
    • Abl: Mechanisms of regulation and activation
    • J. M. Smith, B. J. Mayer, Abl: Mechanisms of regulation and activation. Front. Biosci. 7, d31-d42 (2002).
    • (2002) Front. Biosci. , vol.7
    • Smith, J.M.1    Mayer, B.J.2
  • 28
    • 0141757323 scopus 로고    scopus 로고
    • Reprogramming control of an allosteric signaling switch through modular recombination
    • J. E. Dueber, B. J. Yeh, K. Chak, W. A. Lim, Reprogramming control of an allosteric signaling switch through modular recombination. Science 301, 1904-1908 (2003).
    • (2003) Science , vol.301 , pp. 1904-1908
    • Dueber, J.E.1    Yeh, B.J.2    Chak, K.3    Lim, W.A.4
  • 29
    • 9944220618 scopus 로고    scopus 로고
    • Rewiring cell signaling: The logic and plasticity of eukaryotic protein circuitry
    • J. E. Dueber, B. J. Yeh, R. P. Bhattacharyya, W. A. Lim, Rewiring cell signaling: The logic and plasticity of eukaryotic protein circuitry. Curr. Opin. Struct. Biol. 14, 690-699 (2004).
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 690-699
    • Dueber, J.E.1    Yeh, B.J.2    Bhattacharyya, R.P.3    Lim, W.A.4
  • 31
    • 4644276702 scopus 로고    scopus 로고
    • Imatinib targets other than bcr/abl and their clinical relevance in myeloid disorders
    • A. Pardanani, A. Tefferi, Imatinib targets other than bcr/abl and their clinical relevance in myeloid disorders. Blood 104, 1931-1939 (2004).
    • (2004) Blood , vol.104 , pp. 1931-1939
    • Pardanani, A.1    Tefferi, A.2
  • 32
    • 70350103708 scopus 로고    scopus 로고
    • Class effects of tyrosine kinase inhibitors in the treatment of chronic myeloid leukemia
    • F. J. Giles, M. O'Dwyer, R. Swords, Class effects of tyrosine kinase inhibitors in the treatment of chronic myeloid leukemia. Leukemia 23, 1698-1707 (2009).
    • (2009) Leukemia , vol.23 , pp. 1698-1707
    • Giles, F.J.1    O'Dwyer, M.2    Swords, R.3
  • 34
    • 2442670346 scopus 로고    scopus 로고
    • Context-dependent effects of L domains and ubiquitination on viral budding
    • J. Martin-Serrano, D. Perez-Caballero, P. D. Bieniasz, Context-dependent effects of L domains and ubiquitination on viral budding. J. Virol. 78, 5554-5563 (2004).
    • (2004) J. Virol. , vol.78 , pp. 5554-5563
    • Martin-Serrano, J.1    Perez-Caballero, D.2    Bieniasz, P.D.3
  • 35
    • 0141570508 scopus 로고    scopus 로고
    • Nedd4 regulates egress of Ebola virus-like particles from host cells
    • J. Yasuda, M. Nakao, Y. Kawaoka, H. Shida, Nedd4 regulates egress of Ebola virus-like particles from host cells. J. Virol. 77, 9987-9992 (2003).
    • (2003) J. Virol. , vol.77 , pp. 9987-9992
    • Yasuda, J.1    Nakao, M.2    Kawaoka, Y.3    Shida, H.4
  • 36
    • 0026696360 scopus 로고
    • Mitogen-activated protein kinases: Versatile transducers for cell signaling
    • S. L. Pelech, J. S. Sanghera, Mitogen-activated protein kinases: Versatile transducers for cell signaling. Trends Biochem. Sci. 17, 233-238 (1992).
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 233-238
    • Pelech, S.L.1    Sanghera, J.S.2
  • 38
    • 0022375091 scopus 로고
    • Descriptive analysis of Ebola virus proteins
    • L. H. Elliott, M. P. Kiley, J. B. McCormick, Descriptive analysis of Ebola virus proteins. Virology 147, 169-176 (1985).
    • (1985) Virology , vol.147 , pp. 169-176
    • Elliott, L.H.1    Kiley, M.P.2    McCormick, J.B.3
  • 39
    • 0028220763 scopus 로고
    • The nucleoprotein of Marburg virus is phosphorylated
    • S. Becker, S. Huppertz, H. D. Klenk, H. Feldmann, The nucleoprotein of Marburg virus is phosphorylated. J. Gen. Virol. 75 (Pt. 4), 809-818 (1994).
    • (1994) J. Gen. Virol. , vol.75 , Issue.PART. 4 , pp. 809-818
    • Becker, S.1    Huppertz, S.2    Klenk, H.D.3    Feldmann, H.4
  • 41
    • 0036060893 scopus 로고    scopus 로고
    • The Marburg virus surface protein GP is phosphorylated at its ectodomain
    • C. Sänger, E. Mühlberger, B. Lötfering, H. D. Klenk, S. Becker, The Marburg virus surface protein GP is phosphorylated at its ectodomain. Virology 295, 20-29 (2002).
    • (2002) Virology , vol.295 , pp. 20-29
    • Sänger, C.1    Mühlberger, E.2    Lötfering, B.3    Klenk, H.D.4    Becker, S.5
  • 43
    • 63149113399 scopus 로고    scopus 로고
    • Ebola virus protein VP35 impairs the function of interferon regulatory factor-activating kinases IKKe and TBK-1
    • K. C. Prins, W. B. Cárdenas, C. F. Basler, Ebola virus protein VP35 impairs the function of interferon regulatory factor-activating kinases IKKe and TBK-1. J. Virol. 83, 3069-3077 (2009).
    • (2009) J. Virol. , vol.83 , pp. 3069-3077
    • Prins, K.C.1    Cárdenas, W.B.2    Basler, C.F.3
  • 44
    • 35548931639 scopus 로고    scopus 로고
    • Influence of calcium/calmodulin on budding of Ebola VLPs: Implications for the involvement of the Ras/Raf/MEK/ERK pathway
    • Z. Han, R. N. Harty, Influence of calcium/calmodulin on budding of Ebola VLPs: Implications for the involvement of the Ras/Raf/MEK/ERK pathway. Virus Genes 35, 511-520 (2007).
    • (2007) Virus Genes , vol.35 , pp. 511-520
    • Han, Z.1    Harty, R.N.2
  • 46
    • 32944461681 scopus 로고    scopus 로고
    • Abl collaborates with Src family kinases to stimulate actin-based motility of vaccinia virus
    • T. P. Newsome, I. Weisswange, F. Frischknecht, M.Way, Abl collaborates with Src family kinases to stimulate actin-based motility of vaccinia virus. Cell. Microbiol. 8, 233-241 (2006).
    • (2006) Cell. Microbiol. , vol.8 , pp. 233-241
    • Newsome, T.P.1    Weisswange, I.2    Frischknecht, F.3    Way, M.4
  • 49
    • 77954936778 scopus 로고    scopus 로고
    • Viral and host proteins that modulate filovirus budding
    • Y. Liu, R. N. Harty, Viral and host proteins that modulate filovirus budding. Future Virol. 5, 481-491 (2010).
    • (2010) Future Virol. , vol.5 , pp. 481-491
    • Liu, Y.1    Harty, R.N.2
  • 50
    • 34249848879 scopus 로고    scopus 로고
    • Overview of second-generation tyrosine kinase inhibitors for patients with imatinib-resistant chronic myelogenous leukemia
    • P. Ault, Overview of second-generation tyrosine kinase inhibitors for patients with imatinib-resistant chronic myelogenous leukemia. Clin. J. Oncol. Nurs. 11, 125-129 (2007).
    • (2007) Clin. J. Oncol. Nurs. , vol.11 , pp. 125-129
    • Ault, P.1
  • 52
    • 79952279792 scopus 로고    scopus 로고
    • Uncommon or delayed adverse events associated with imatinib treatment for chronic myeloid leukemia
    • R. Salie, R. T. Silver, Uncommon or delayed adverse events associated with imatinib treatment for chronic myeloid leukemia. Clin. Lymphoma Myeloma Leuk. 10, 331-335 (2010).
    • (2010) Clin. Lymphoma Myeloma Leuk. , vol.10 , pp. 331-335
    • Salie, R.1    Silver, R.T.2
  • 53
    • 79952095377 scopus 로고    scopus 로고
    • Cardiotoxicity associated with targeting kinase pathways in cancer
    • H. R. Mellor, A. R. Bell, J. P. Valentin, R. R. A. Roberts, Cardiotoxicity associated with targeting kinase pathways in cancer. Toxicol. Sci. 120, 14-32 (2011).
    • (2011) Toxicol. Sci. , vol.120 , pp. 14-32
    • Mellor, H.R.1    Bell, A.R.2    Valentin, J.P.3    Roberts, R.R.A.4
  • 55
    • 0033600240 scopus 로고    scopus 로고
    • Interaction of c-Abl and p73a and their collaboration to induce apoptosis
    • R. Agami, G. Blandino, M. Oren, Y. Shaul, Interaction of c-Abl and p73a and their collaboration to induce apoptosis. Nature 399, 809-813 (1999).
    • (1999) Nature , vol.399 , pp. 809-813
    • Agami, R.1    Blandino, G.2    Oren, M.3    Shaul, Y.4
  • 56
    • 2442691605 scopus 로고    scopus 로고
    • pH-dependent entry of severe acute respiratory syndrome coronavirus is mediated by the spike glycoprotein and enhanced by dendritic cell transfer through DC-SIGN
    • Z. Y. Yang, Y. Huang, L. Ganesh, K. Leung, W. P. Kong, O. Schwartz, K. Subbarao, G. J. Nabel, pH-dependent entry of severe acute respiratory syndrome coronavirus is mediated by the spike glycoprotein and enhanced by dendritic cell transfer through DC-SIGN. J. Virol. 78, 5642-5650 (2004).
    • (2004) J. Virol. , vol.78 , pp. 5642-5650
    • Yang, Z.Y.1    Huang, Y.2    Ganesh, L.3    Leung, K.4    Kong, W.P.5    Schwartz, O.6    Subbarao, K.7    Nabel, G.J.8
  • 57
    • 33745158157 scopus 로고
    • A simple method of estimating fifty per cent endpoints
    • L. J. Reed, H. Muench, A simple method of estimating fifty per cent endpoints. Am. J. Hygiene 27, 493-497 (1938).
    • (1938) Am. J. Hygiene , vol.27 , pp. 493-497
    • Reed, L.J.1    Muench, H.2
  • 58
    • 0032961627 scopus 로고    scopus 로고
    • Mass spectrometric identification of proteins from silver-stained polyacrylamide gel: A method for the removal of silver ions to enhance sensitivity
    • F. Gharahdaghi, C. R. Weinberg, D. A. Meagher, B. S. Imai, S. M. Mische, Mass spectrometric identification of proteins from silver-stained polyacrylamide gel: A method for the removal of silver ions to enhance sensitivity. Electrophoresis 20, 601-605 (1999).
    • (1999) Electrophoresis , vol.20 , pp. 601-605
    • Gharahdaghi, F.1    Weinberg, C.R.2    Meagher, D.A.3    Imai, B.S.4    Mische, S.M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.