메뉴 건너뛰기




Volumn 99, Issue 5, 2018, Pages 619-630

Coronavirus S protein-induced fusion is blocked prior to hemifusion by Abl kinase inhibitors

Author keywords

Abl kinase; Abl1; Abl2; Cell cell fusion; Coronavirus; GNF2; GNF5; IBV; Imatinib; MERS CoV; SARS CoV; Virus cell fusion

Indexed keywords

ABELSON KINASE; GNF 2; GNF 5; IMATINIB; PROTEIN TYROSINE KINASE INHIBITOR; UNCLASSIFIED DRUG; VIRUS RECEPTOR; VIRUS SPIKE PROTEIN; ANTIVIRUS AGENT; BENZAMIDE DERIVATIVE; CORONAVIRUS SPIKE GLYCOPROTEIN; GNF-2 COMPOUND; N-(2-HYDROXYETHYL)-3-(6-((4-(TRIFLUOROMETHOXY)PHENYL)AMINO)-4-PYRIMIDINYL)BENZAMIDE; PROTEIN KINASE INHIBITOR; PYRIMIDINE DERIVATIVE;

EID: 85046402518     PISSN: 00221317     EISSN: 14652099     Source Type: Journal    
DOI: 10.1099/jgv.0.001047     Document Type: Article
Times cited : (125)

References (59)
  • 1
    • 84923050027 scopus 로고    scopus 로고
    • Ebola virus and severe acute respiratory syndrome coronavirus display late cell entry kinetics: Evidence that transport to NPC1+ endolysosomes is a rate-defining step
    • Mingo RM, Simmons JA, Shoemaker CJ, Nelson EA, Schornberg KL et al. Ebola virus and severe acute respiratory syndrome coronavirus display late cell entry kinetics: evidence that transport to NPC1+ endolysosomes is a rate-defining step. J Virol 2015;89: 2931–2943.
    • (2015) J Virol , vol.89 , pp. 2931-2943
    • Mingo, R.M.1    Simmons, J.A.2    Shoemaker, C.J.3    Nelson, E.A.4    Schornberg, K.L.5
  • 2
    • 84908065761 scopus 로고    scopus 로고
    • Host cell entry of Middle East respiratory syndrome coronavirus after two-step, furin-mediated activation of the spike protein
    • Millet JK, Whittaker GR. Host cell entry of Middle East respiratory syndrome coronavirus after two-step, furin-mediated activation of the spike protein. Proc Natl Acad Sci USA 2014;111:15214–15219.
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 15214-15219
    • Millet, J.K.1    Whittaker, G.R.2
  • 3
    • 84912120721 scopus 로고    scopus 로고
    • Coronavirus cell entry occurs through the endo-/lysosomal pathway in a proteolysis-dependent manner
    • Burkard C, Verheije MH, Wicht O, van Kasteren SI, van Kuppeveld FJ et al. Coronavirus cell entry occurs through the endo-/lysosomal pathway in a proteolysis-dependent manner. PLoS Pathog 2014;10:e1004502.
    • (2014) Plos Pathog , pp. 10
    • Burkard, C.1    Verheije, M.H.2    Wicht, O.3    Van Kasteren, S.I.4    Van Kuppeveld, F.J.5
  • 4
    • 84930047858 scopus 로고    scopus 로고
    • Host cell proteases: Critical determinants of coronavirus tropism and pathogenesis
    • Millet JK, Whittaker GR. Host cell proteases: critical determinants of coronavirus tropism and pathogenesis. Virus Res 2015;202: 120–134.
    • (2015) Virus Res , vol.202 , pp. 120-134
    • Millet, J.K.1    Whittaker, G.R.2
  • 5
    • 84902176510 scopus 로고    scopus 로고
    • Repurposing of clinically developed drugs for treatment of Middle East respiratory syndrome coronavirus infection
    • Dyall J, Coleman CM, Hart BJ, Venkataraman T, Holbrook MR et al. Repurposing of clinically developed drugs for treatment of Middle East respiratory syndrome coronavirus infection. Antimicrob Agents Chemother 2014;58:4885–4893.
    • (2014) Antimicrob Agents Chemother , vol.58 , pp. 4885-4893
    • Dyall, J.1    Coleman, C.M.2    Hart, B.J.3    Venkataraman, T.4    Holbrook, M.R.5
  • 6
    • 84901321275 scopus 로고    scopus 로고
    • Oxidative stress-induced signaling pathways implicated in the pathogenesis of Parkinson’s disease
    • Gaki GS, Papavassiliou AG. Oxidative stress-induced signaling pathways implicated in the pathogenesis of Parkinson’s disease. Neuromolecular Med 2014;16:217–230.
    • (2014) Neuromolecular Med , vol.16 , pp. 217-230
    • Gaki, G.S.1    Papavassiliou, A.G.2
  • 7
    • 77956920417 scopus 로고    scopus 로고
    • ABL tyrosine kinases: Evolution of function, regulation, and specificity
    • Colicelli J. ABL tyrosine kinases: evolution of function, regulation, and specificity. Sci Signal 2010;3:re6.
    • (2010) Sci Signal , vol.3
    • Colicelli, J.1
  • 8
    • 0041690966 scopus 로고    scopus 로고
    • Werner syndrome protein phosphorylation by abl tyrosine kinase regulates its activity and distribution
    • Cheng WH, von Kobbe C, Opresko PL, Fields KM, Ren J et al. Werner syndrome protein phosphorylation by abl tyrosine kinase regulates its activity and distribution. Mol Cell Biol 2003;23:6385–6395.
    • (2003) Mol Cell Biol , vol.23 , pp. 6385-6395
    • Cheng, W.H.1    Von Kobbe, C.2    Opresko, P.L.3    Fields, K.M.4    Ren, J.5
  • 9
    • 84982106460 scopus 로고    scopus 로고
    • Abelson kinase acts as a robust, multifunctional scaffold in regulating embryonic morphogenesis
    • Rogers EM, Spracklen AJ, Bilancia CG, Sumigray KD, Allred SC et al. Abelson kinase acts as a robust, multifunctional scaffold in regulating embryonic morphogenesis. Mol Biol Cell 2016;27:2613–2631.
    • (2016) Mol Biol Cell , vol.27 , pp. 2613-2631
    • Rogers, E.M.1    Spracklen, A.J.2    Bilancia, C.G.3    Sumigray, K.D.4    Allred, S.C.5
  • 10
    • 84959019886 scopus 로고    scopus 로고
    • Multifunctional Abl kinases in health and disease
    • Khatri A, Wang J, Pendergast AM. Multifunctional Abl kinases in health and disease. J Cell Sci 2016;129:9–16.
    • (2016) J Cell Sci , vol.129 , pp. 9-16
    • Khatri, A.1    Wang, J.2    Pendergast, A.M.3
  • 11
    • 0030031766 scopus 로고    scopus 로고
    • Inhibition of the Abl protein-tyrosine kinase in vitro and in vivo by a 2-phenylaminopyrimidine derivative
    • Buchdunger E, Zimmermann J, Mett H, Meyer T, Müller M et al. Inhibition of the Abl protein-tyrosine kinase in vitro and in vivo by a 2-phenylaminopyrimidine derivative. Cancer Res 1996;56:100–104.
    • (1996) Cancer Res , vol.56 , pp. 100-104
    • Buchdunger, E.1    Zimmermann, J.2    Mett, H.3    Meyer, T.4    Müller, M.5
  • 12
    • 0015694748 scopus 로고
    • Letter: A new consistent chromosomal abnormality in chronic myelogenous leukaemia identified by quinacrine fluorescence and Giemsa staining
    • Rowley JD. Letter: a new consistent chromosomal abnormality in chronic myelogenous leukaemia identified by quinacrine fluorescence and Giemsa staining. Nature 1973;243:290–293.
    • (1973) Nature , vol.243 , pp. 290-293
    • Rowley, J.D.1
  • 13
    • 0020972979 scopus 로고
    • Localization of the c-ab1 oncogene adjacent to a translocation break point in chronic myelocytic leukaemia
    • Heisterkamp N, Stephenson JR, Groffen J, Hansen PF, de Klein A et al. Localization of the c-ab1 oncogene adjacent to a translocation break point in chronic myelocytic leukaemia. Nature 1983; 306:239–242.
    • (1983) Nature , vol.306 , pp. 239-242
    • Heisterkamp, N.1    Stephenson, J.R.2    Groffen, J.3    Hansen, P.F.4    De Klein, A.5
  • 14
    • 0020972981 scopus 로고
    • Translocation of c-ab1 oncogene correlates with the presence of a Philadelphia chromosome in chronic myelocytic leukaemia
    • Bartram CR, de Klein A, Hagemeijer A, van Agthoven T, Geurts van Kessel A et al. Translocation of c-ab1 oncogene correlates with the presence of a Philadelphia chromosome in chronic myelocytic leukaemia. Nature 1983;306:277–280.
    • (1983) Nature , vol.306 , pp. 277-280
    • Bartram, C.R.1    De Klein, A.2    Hagemeijer, A.3    Van Agthoven, T.4    Geurts Van Kessel, A.5
  • 15
    • 84990252098 scopus 로고    scopus 로고
    • Abelson kinase inhibitors are potent inhibitors of severe acute respiratory syndrome coronavirus and middle east respiratory syndrome coronavirus fusion
    • Coleman CM, Sisk JM, Mingo RM, Nelson EA, White JM et al. Abelson kinase inhibitors are potent inhibitors of severe acute respiratory syndrome coronavirus and middle east respiratory syndrome coronavirus fusion. J Virol 2016;90:8924–8933.
    • (2016) J Virol , vol.90 , pp. 8924-8933
    • Coleman, C.M.1    Sisk, J.M.2    Mingo, R.M.3    Nelson, E.A.4    White, J.M.5
  • 16
    • 30344475861 scopus 로고    scopus 로고
    • Virus-induced Abl and Fyn kinase signals permit coxsackievirus entry through epithelial tight junctions
    • Coyne CB, Bergelson JM. Virus-induced Abl and Fyn kinase signals permit coxsackievirus entry through epithelial tight junctions. Cell 2006;124:119–131.
    • (2006) Cell , vol.124 , pp. 119-131
    • Coyne, C.B.1    Bergelson, J.M.2
  • 17
    • 32944461681 scopus 로고    scopus 로고
    • Abl collaborates with Src family kinases to stimulate actin-based motility of vaccinia virus
    • Newsome TP, Weisswange I, Frischknecht F, Way M. Abl collaborates with Src family kinases to stimulate actin-based motility of vaccinia virus. Cell Microbiol 2006;8:233–241.
    • (2006) Cell Microbiol , vol.8 , pp. 233-241
    • Newsome, T.P.1    Weisswange, I.2    Frischknecht, F.3    Way, M.4
  • 18
    • 77954666282 scopus 로고    scopus 로고
    • Role of Abl kinase and the Wave2 signaling complex in HIV-1 entry at a post-hemifusion step
    • Harmon B, Campbell N, Ratner L. Role of Abl kinase and the Wave2 signaling complex in HIV-1 entry at a post-hemifusion step. PLoS Pathog 2010;6:e1000956.
    • (2010) Plos Pathog , pp. 6
    • Harmon, B.1    Campbell, N.2    Ratner, L.3
  • 19
    • 84938099466 scopus 로고    scopus 로고
    • Involvement of the Rac1-IRSp53-Wave2- Arp2/3 signaling pathway in HIV-1 gag particle release in CD4 T cells
    • Thomas A, Mariani-Floderer C, López-Huertas MR, Gros N, Hamard-P_eron E et al. Involvement of the Rac1-IRSp53-Wave2- Arp2/3 signaling pathway in HIV-1 gag particle release in CD4 T cells. J Virol 2015;89:8162–8181.
    • (2015) J Virol , vol.89 , pp. 8162-8181
    • Thomas, A.1    Mariani-Floderer, C.2    López-Huertas, M.R.3    Gros, N.4    Hamard, E.5
  • 20
    • 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
    • Reeves PM, Smith SK, Olson VA, Thorne SH, Bornmann W et al. Variola and monkeypox viruses utilize conserved mechanisms of virion motility and release that depend on abl and SRC family tyrosine kinases. J Virol 2011;85:21–31.
    • (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
  • 21
    • 84857693882 scopus 로고    scopus 로고
    • Productive replication of Ebola virus is regulated by the c-Abl1 tyrosine kinase
    • García M, Cooper A, Shi W, Bornmann W, Carrion R et al. Productive replication of Ebola virus is regulated by the c-Abl1 tyrosine kinase. Sci Transl Med 2012 4:123ra24.
    • (2012) Sci Transl Med , vol.4 , pp. 123
    • García, M.1    Cooper, A.2    Shi, W.3    Bornmann, W.4    Carrion, R.5
  • 22
    • 84924964870 scopus 로고    scopus 로고
    • Identification of 53 compounds that block Ebola virus-like particle entry via a repurposing screen of approved drugs
    • Kouznetsova J, Sun W, Martínez-Romero C, Tawa G, Shinn P et al. Identification of 53 compounds that block Ebola virus-like particle entry via a repurposing screen of approved drugs. Emerg Microbes Infect 2014;3:e84.
    • (2014) Emerg Microbes Infect , vol.3
    • Kouznetsova, J.1    Sun, W.2    Martínez-Romero, C.3    Tawa, G.4    Shinn, P.5
  • 23
    • 84941309509 scopus 로고    scopus 로고
    • Hepatitis C virus particle assembly involves phosphorylation of NS5A by the c-Abl tyrosine kinase
    • Yamauchi S, Takeuchi K, Chihara K, Sun X, Honjoh C et al. Hepatitis C virus particle assembly involves phosphorylation of NS5A by the c-Abl tyrosine kinase. J Biol Chem 2015;290:21857–21864.
    • (2015) J Biol Chem , vol.290 , pp. 21857-21864
    • Yamauchi, S.1    Takeuchi, K.2    Chihara, K.3    Sun, X.4    Honjoh, C.5
  • 24
    • 0030782261 scopus 로고    scopus 로고
    • Heterogeneous distribution of the unusual phospholipid semilysobisphosphatidic acid through the Golgi complex
    • Cluett EB, Kuismanen E, Machamer CE. Heterogeneous distribution of the unusual phospholipid semilysobisphosphatidic acid through the Golgi complex. Mol Biol Cell 1997;8:2233–2240.
    • (1997) Mol Biol Cell , vol.8 , pp. 2233-2240
    • Cluett, E.B.1    Kuismanen, E.2    Machamer, C.E.3
  • 26
    • 0034665713 scopus 로고    scopus 로고
    • Structural mechanism for STI-571 inhibition of abelson tyrosine kinase
    • Schindler T, Bornmann W, Pellicena P, Miller WT, Clarkson B et al. Structural mechanism for STI-571 inhibition of abelson tyrosine kinase. Science 2000;289:1938–1942.
    • (2000) Science , vol.289 , pp. 1938-1942
    • Schindler, T.1    Bornmann, W.2    Pellicena, P.3    Miller, W.T.4    Clarkson, B.5
  • 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, Schindler T, Veach DR 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;62:4236–4243.
    • (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
  • 28
    • 75749146563 scopus 로고    scopus 로고
    • Targeting Bcr-Abl by combining allosteric with ATP-bindingsite inhibitors
    • Zhang J, Adri_an FJ, Jahnke W, Cowan-Jacob SW, Li AG, Ag L et al. Targeting Bcr-Abl by combining allosteric with ATP-bindingsite inhibitors. Nature 2010;463:501–506.
    • (2010) Nature , vol.463 , pp. 501-506
    • Zhang, J.1    Adri, F.J.2    Jahnke, W.3    Cowan-Jacob, S.W.4    Li, A.G.5    Ag, L.6
  • 29
  • 30
    • 84875518820 scopus 로고    scopus 로고
    • The ins and outs of bcr-abl inhibition
    • Reddy EP, Aggarwal AK. The ins and outs of bcr-abl inhibition. Genes Cancer 2012;3:447–454.
    • (2012) Genes Cancer , vol.3 , pp. 447-454
    • Reddy, E.P.1    Aggarwal, A.K.2
  • 31
    • 34147135956 scopus 로고    scopus 로고
    • The intracellular sites of early replication and budding of SARScoronavirus
    • Stertz S, Reichelt M, Spiegel M, Kuri T, Martínez-Sobrido L et al. The intracellular sites of early replication and budding of SARScoronavirus. Virology 2007;361:304–315.
    • (2007) Virology , vol.361 , pp. 304-315
    • Stertz, S.1    Reichelt, M.2    Spiegel, M.3    Kuri, T.4    Martínez-Sobrido, L.5
  • 32
    • 2442647673 scopus 로고    scopus 로고
    • Intracellular targeting signals contribute to localization of coronavirus spike proteins near the virus assembly site
    • Lontok E, Corse E, Machamer CE. Intracellular targeting signals contribute to localization of coronavirus spike proteins near the virus assembly site. J Virol 2004;78:5913–5922.
    • (2004) J Virol , vol.78 , pp. 5913-5922
    • Lontok, E.1    Corse, E.2    Machamer, C.E.3
  • 33
    • 70350379633 scopus 로고    scopus 로고
    • Regulation of cell migration and morphogenesis by Abl-family kinases: Emerging mechanisms and physiological contexts
    • Bradley WD, Koleske AJ. Regulation of cell migration and morphogenesis by Abl-family kinases: emerging mechanisms and physiological contexts. J Cell Sci 2009;122:3441–3454.
    • (2009) J Cell Sci , vol.122 , pp. 3441-3454
    • Bradley, W.D.1    Koleske, A.J.2
  • 34
    • 47249127287 scopus 로고    scopus 로고
    • The c- Abl tyrosine kinase regulates actin remodeling at the immune synapse
    • Huang Y, Comiskey EO, Dupree RS, Li S, Koleske AJ et al. The c- Abl tyrosine kinase regulates actin remodeling at the immune synapse. Blood 2008;112:111–119.
    • (2008) Blood , vol.112 , pp. 111-119
    • Huang, Y.1    Comiskey, E.O.2    Dupree, R.S.3    Li, S.4    Koleske, A.J.5
  • 35
    • 84864135309 scopus 로고    scopus 로고
    • Abl family kinases modulate T cell-mediated inflammation and chemokine-induced migration through the adaptor HEF1 and the GTPase Rap1
    • Gu JJ, Lavau CP, Pugacheva E, Soderblom EJ, Moseley MA et al. Abl family kinases modulate T cell-mediated inflammation and chemokine-induced migration through the adaptor HEF1 and the GTPase Rap1. Sci Signal 2012;5:ra51.
    • (2012) Sci Signal , vol.5 , pp. 51
    • Gu, J.J.1    Lavau, C.P.2    Pugacheva, E.3    Soderblom, E.J.4    Moseley, M.A.5
  • 36
    • 0032439213 scopus 로고    scopus 로고
    • Essential roles for the Abl and Arg tyrosine kinases in neurulation
    • Koleske AJ, Gifford AM, Scott ML, Nee M, Bronson RT et al. Essential roles for the Abl and Arg tyrosine kinases in neurulation. Neuron 1998;21:1259–1272.
    • (1998) Neuron , vol.21 , pp. 1259-1272
    • Koleske, A.J.1    Gifford, A.M.2    Scott, M.L.3    Nee, M.4    Bronson, R.T.5
  • 37
    • 78650043640 scopus 로고    scopus 로고
    • Abl kinases are required for invadopodia formation and chemokine- induced invasion
    • Smith-Pearson PS, Greuber EK, Yogalingam G, Pendergast AM. Abl kinases are required for invadopodia formation and chemokine- induced invasion. J Biol Chem 2010;285:40201–40211.
    • (2010) J Biol Chem , vol.285 , pp. 40201-40211
    • Smith-Pearson, P.S.1    Greuber, E.K.2    Yogalingam, G.3    Pendergast, A.M.4
  • 38
    • 79952203229 scopus 로고    scopus 로고
    • An EGFR-Src-Arg-cortactin pathway mediates functional maturation of invadopodia and breast cancer cell invasion
    • Mader CC, Oser M, Magalhaes MA, Bravo-Cordero JJ, Condeelis J et al. An EGFR-Src-Arg-cortactin pathway mediates functional maturation of invadopodia and breast cancer cell invasion. Cancer Res 2011;71:1730–1741.
    • (2011) Cancer Res , vol.71 , pp. 1730-1741
    • Mader, C.C.1    Oser, M.2    Magalhaes, M.A.3    Bravo-Cordero, J.J.4    Condeelis, J.5
  • 39
    • 65649119024 scopus 로고    scopus 로고
    • Arg interacts with cortactin to promote adhesion-dependent cell edge protrusion
    • Lapetina S, Mader CC, Machida K, Mayer BJ, Koleske AJ. Arg interacts with cortactin to promote adhesion-dependent cell edge protrusion. J Cell Biol 2009;185:503–519.
    • (2009) J Cell Biol , vol.185 , pp. 503-519
    • Lapetina, S.1    Mader, C.C.2    Machida, K.3    Mayer, B.J.4    Koleske, A.J.5
  • 40
    • 84865425266 scopus 로고    scopus 로고
    • Arg/Abl2 modulates the affinity and stoichiometry of binding of cortactin to F-actin
    • MacGrath SM, Koleske AJ. Arg/Abl2 modulates the affinity and stoichiometry of binding of cortactin to F-actin. Biochemistry 2012; 51:6644–6653.
    • (2012) Biochemistry , vol.51 , pp. 6644-6653
    • Macgrath, S.M.1    Koleske, A.J.2
  • 41
    • 84873045444 scopus 로고    scopus 로고
    • Abl2/Arg controls dendritic spine and dendrite arbor stability via distinct cytoskeletal control pathways
    • Lin YC, Yeckel MF, Koleske AJ. Abl2/Arg controls dendritic spine and dendrite arbor stability via distinct cytoskeletal control pathways. J Neurosci 2013;33:1846–1857.
    • (2013) J Neurosci , vol.33 , pp. 1846-1857
    • Lin, Y.C.1    Yeckel, M.F.2    Koleske, A.J.3
  • 42
    • 84922809107 scopus 로고    scopus 로고
    • Abl2/Abl-related gene stabilizes actin filaments, stimulates actin branching by actin-related protein 2/3 complex, and promotes actin filament severing by cofilin
    • Courtemanche N, Gifford SM, Simpson MA, Pollard TD, Koleske AJ. Abl2/Abl-related gene stabilizes actin filaments, stimulates actin branching by actin-related protein 2/3 complex, and promotes actin filament severing by cofilin. J Biol Chem 2015;290: 4038–4046.
    • (2015) J Biol Chem , vol.290 , pp. 4038-4046
    • Courtemanche, N.1    Gifford, S.M.2    Simpson, M.A.3    Pollard, T.D.4    Koleske, A.J.5
  • 43
    • 0035920195 scopus 로고    scopus 로고
    • Inhibition of c-Abl tyrosine kinase activity by filamentous actin
    • Woodring PJ, Hunter T, Wang JY. Inhibition of c-Abl tyrosine kinase activity by filamentous actin. J Biol Chem 2001;276:27104–27110.
    • (2001) J Biol Chem , vol.276 , pp. 27104-27110
    • Woodring, P.J.1    Hunter, T.2    Wang, J.Y.3
  • 45
    • 16244370694 scopus 로고    scopus 로고
    • Cortactin: An Achilles’ heel of the actin cytoskeleton targeted by pathogens
    • Selbach M, Backert S. Cortactin: an Achilles’ heel of the actin cytoskeleton targeted by pathogens. Trends Microbiol 2005;13: 181–189.
    • (2005) Trends Microbiol , vol.13 , pp. 181-189
    • Selbach, M.1    Backert, S.2
  • 46
    • 79956141898 scopus 로고    scopus 로고
    • Subversion of the actin cytoskeleton during viral infection
    • Taylor MP, Koyuncu OO, Enquist LW. Subversion of the actin cytoskeleton during viral infection. Nat Rev Microbiol 2011;9:427–439.
    • (2011) Nat Rev Microbiol , vol.9 , pp. 427-439
    • Taylor, M.P.1    Koyuncu, O.O.2    Enquist, L.W.3
  • 47
    • 78650727309 scopus 로고    scopus 로고
    • Abl family of tyrosine kinases and microbial pathogenesis
    • Wessler S, Backert S. Abl family of tyrosine kinases and microbial pathogenesis. Int Rev Cell Mol Biol 2011;286:271–300.
    • (2011) Int Rev Cell Mol Biol , vol.286 , pp. 271-300
    • Wessler, S.1    Backert, S.2
  • 48
    • 79961005771 scopus 로고    scopus 로고
    • 3BP2-deficient mice are osteoporotic with impaired osteoblast and osteoclast functions
    • Levaot N, Simoncic PD, Dimitriou ID, Scotter A, La Rose J et al. 3BP2-deficient mice are osteoporotic with impaired osteoblast and osteoclast functions. J Clin Invest 2011;121:3244–3257.
    • (2011) J Clin Invest , vol.121 , pp. 3244-3257
    • Levaot, N.1    Simoncic, P.D.2    Dimitriou, I.D.3    Scotter, A.4    La Rose, J.5
  • 49
    • 84876827016 scopus 로고    scopus 로고
    • Signaling mechanisms in mammalian myoblast fusion
    • Hindi SM, Tajrishi MM, Kumar A. Signaling mechanisms in mammalian myoblast fusion. Sci Signal 2013;6:re2.
    • (2013) Sci Signal , vol.6
    • Hindi, S.M.1    Tajrishi, M.M.2    Kumar, A.3
  • 50
    • 84930944871 scopus 로고    scopus 로고
    • Mechanisms of myoblast fusion during muscle development
    • Kim JH, Jin P, Duan R, Chen EH. Mechanisms of myoblast fusion during muscle development. Curr Opin Genet Dev 2015;32:162–170.
    • (2015) Curr Opin Genet Dev , vol.32 , pp. 162-170
    • Kim, J.H.1    Jin, P.2    Duan, R.3    Chen, E.H.4
  • 51
    • 84876323868 scopus 로고    scopus 로고
    • Actin-propelled invasive membrane protrusions promote fusogenic protein engagement during cell-cell fusion
    • Shilagardi K, Li S, Luo F, Marikar F, Duan R et al. Actin-propelled invasive membrane protrusions promote fusogenic protein engagement during cell-cell fusion. Science 2013;340:359–363.
    • (2013) Science , vol.340 , pp. 359-363
    • Shilagardi, K.1    Li, S.2    Luo, F.3    Marikar, F.4    Duan, R.5
  • 52
    • 84901422239 scopus 로고    scopus 로고
    • Podosome organization drives osteoclast-mediated bone resorption
    • Georgess D, Machuca-Gayet I, Blangy A, Jurdic P. Podosome organization drives osteoclast-mediated bone resorption. Cell Adh Migr 2014;8:192–204.
    • (2014) Cell Adh Migr , vol.8 , pp. 192-204
    • Georgess, D.1    Machuca-Gayet, I.2    Blangy, A.3    Jurdic, P.4
  • 53
    • 27144511135 scopus 로고    scopus 로고
    • Contribution of trafficking signals in the cytoplasmic tail of the infectious bronchitis virus spike protein to virus infection
    • Youn S, Collisson EW, Machamer CE. Contribution of trafficking signals in the cytoplasmic tail of the infectious bronchitis virus spike protein to virus infection. J Virol 2005;79:13209–13217.
    • (2005) J Virol , vol.79 , pp. 13209-13217
    • Youn, S.1    Collisson, E.W.2    Machamer, C.E.3
  • 54
    • 33847218615 scopus 로고    scopus 로고
    • The cytoplasmic tail of the severe acute respiratory syndrome coronavirus spike protein contains a novel endoplasmic reticulum retrieval signal that binds COPI and promotes interaction with membrane protein
    • McBride CE, Li J, Machamer CE. The cytoplasmic tail of the severe acute respiratory syndrome coronavirus spike protein contains a novel endoplasmic reticulum retrieval signal that binds COPI and promotes interaction with membrane protein. J Virol 2007;81: 2418–2428.
    • (2007) J Virol , vol.81 , pp. 2418-2428
    • McBride, C.E.1    Li, J.2    Machamer, C.E.3
  • 55
    • 75449088413 scopus 로고    scopus 로고
    • A single tyrosine in the severe acute respiratory syndrome coronavirus membrane protein cytoplasmic tail is important for efficient interaction with spike protein
    • McBride CE, Machamer CE. A single tyrosine in the severe acute respiratory syndrome coronavirus membrane protein cytoplasmic tail is important for efficient interaction with spike protein. J Virol 2010;84:1891–1901.
    • (2010) J Virol , vol.84 , pp. 1891-1901
    • McBride, C.E.1    Machamer, C.E.2
  • 56
    • 80052297532 scopus 로고    scopus 로고
    • Binding of avian coronavirus spike proteins to host factors reflects virus tropism and pathogenicity
    • Wickramasinghe IN, de Vries RP, Gröne A, de Haan CA, Verheije MH. Binding of avian coronavirus spike proteins to host factors reflects virus tropism and pathogenicity. J Virol 2011;85:8903–8912.
    • (2011) J Virol , vol.85 , pp. 8903-8912
    • Wickramasinghe, I.N.1    De Vries, R.P.2    Gröne, A.3    De Haan, C.A.4    Verheije, M.H.5
  • 57
    • 84885318384 scopus 로고    scopus 로고
    • Contributions of the S2 spike ectodomain to attachment and host range of infectious bronchitis virus
    • Promkuntod N, Wickramasinghe IN, de Vrieze G, Gröne A, Verheije MH. Contributions of the S2 spike ectodomain to attachment and host range of infectious bronchitis virus. Virus Res 2013;177:127–137.
    • (2013) Virus Res , vol.177 , pp. 127-137
    • Promkuntod, N.1    Wickramasinghe, I.N.2    De Vrieze, G.3    Gröne, A.4    Verheije, M.H.5
  • 58
    • 0029177467 scopus 로고
    • A highly conserved epitope on the spike protein of infectious bronchitis virus
    • Wang L, Parr RL, King DJ, Collisson EW. A highly conserved epitope on the spike protein of infectious bronchitis virus. Arch Virol 1995;140:2201–2213.
    • (1995) Arch Virol , vol.140 , pp. 2201-2213
    • Wang, L.1    Parr, R.L.2    King, D.J.3    Collisson, E.W.4
  • 59
    • 1642488368 scopus 로고    scopus 로고
    • Characterization of severe acute respiratory syndromeassociated coronavirus (SARS-CoV) spike glycoprotein-mediated viral entry
    • Simmons G, Reeves JD, Rennekamp AJ, Amberg SM, Piefer AJ et al. Characterization of severe acute respiratory syndromeassociated coronavirus (SARS-CoV) spike glycoprotein-mediated viral entry. Proc Natl Acad Sci USA 2004;101:4240–4245.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 4240-4245
    • Simmons, G.1    Reeves, J.D.2    Rennekamp, A.J.3    Amberg, S.M.4    Piefer, A.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.