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Volumn 88, Issue 17, 2014, Pages 9478-9489

Rewiring of cellular membrane homeostasis by picornaviruses

Author keywords

[No Author keywords available]

Indexed keywords

ANIMAL; CELL MEMBRANE; HOMEOSTASIS; HOST PATHOGEN INTERACTION; HUMAN; METABOLISM; PHYSIOLOGY; PICORNAVIRIDAE; VIROLOGY; VIRUS REPLICATION;

EID: 84907928930     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00922-14     Document Type: Short Survey
Times cited : (41)

References (108)
  • 2
    • 42349086670 scopus 로고    scopus 로고
    • Modification of intracellular membrane structures for virus replication
    • Miller S, Krijnse-Locker J. 2008. Modification of intracellular membrane structures for virus replication. Nat. Rev. Microbiol. 6:363-374. http://dx.doi.org/10.1038/nrmicro1890.
    • (2008) Nat. Rev. Microbiol , vol.6 , pp. 363-374
    • Miller, S.1    Krijnse-Locker, J.2
  • 3
    • 0022873377 scopus 로고
    • Poliovirus temperature-sensitive mutant containing a single nucleotide deletion in the 5=-noncoding region of the viral RNA
    • Racaniello VR, Meriam C. 1986. Poliovirus temperature-sensitive mutant containing a single nucleotide deletion in the 5=-noncoding region of the viral RNA. Virology 155:498-507. http://dx.doi.org/10.1016/0042-6822(86)90211-4.
    • (1986) Virology , vol.155 , pp. 498-507
    • Racaniello, V.R.1    Meriam, C.2
  • 4
    • 0013919693 scopus 로고
    • Differential inhibitory effects of actinomycin D among strains of poliovirus
    • Schaffer FL, Gordon M. 1966. Differential inhibitory effects of actinomycin D among strains of poliovirus. J. Bacteriol. 91:2309-2316.
    • (1966) J. Bacteriol , vol.91 , pp. 2309-2316
    • Schaffer, F.L.1    Gordon, M.2
  • 5
    • 84879513998 scopus 로고    scopus 로고
    • Increased long chain acyl-Coa synthetase activity and fatty acid import is linked to membrane synthesis for development of picornavirus replication organelles
    • Nchoutmboube JA, Viktorova EG, Scott AJ, Ford LA, Pei Z, Watkins PA, Ernst RK, Belov GA. 2013. Increased long chain acyl-Coa synthetase activity and fatty acid import is linked to membrane synthesis for development of picornavirus replication organelles. PLoS Pathog. 9:e1003401. http://dx.doi.org/10.1371/journal.ppat.1003401.
    • (2013) PLoS Pathog , vol.9
    • Nchoutmboube, J.A.1    Viktorova, E.G.2    Scott, A.J.3    Ford, L.A.4    Pei, Z.5    Watkins, P.A.6    Ernst, R.K.7    Belov, G.A.8
  • 6
    • 0020265917 scopus 로고
    • Inactivation of cap-binding proteins accompanies the shut-off of host protein synthesis by poliovirus
    • Lee KA, Sonenberg N. 1982. Inactivation of cap-binding proteins accompanies the shut-off of host protein synthesis by poliovirus. Proc. Natl. Acad. Sci. U. S. A. 79:3447-3451. http://dx.doi.org/10.1073/pnas.79.11.3447.
    • (1982) Proc. Natl. Acad. Sci. U. S. A , vol.79 , pp. 3447-3451
    • Lee, K.A.1    Sonenberg, N.2
  • 7
    • 84855939285 scopus 로고    scopus 로고
    • Complex dynamic development of poliovirus membranous replication complexes
    • Belov GA, Nair V, Hansen BT, Hoyt FH, Fischer ER, Ehrenfeld E. 2012. Complex dynamic development of poliovirus membranous replication complexes. J. Virol. 86:302-312. http://dx.doi.org/10.1128/JVI.05937-11.
    • (2012) J. Virol , vol.86 , pp. 302-312
    • Belov, G.A.1    Nair, V.2    Hansen, B.T.3    Hoyt, F.H.4    Fischer, E.R.5    Ehrenfeld, E.6
  • 9
    • 0021069227 scopus 로고
    • Intracellular distribution of poliovirus proteins and the induction of virus-specific cytoplasmic structures
    • Bienz K, Egger D, Rasser Y, Bossart W. 1983. Intracellular distribution of poliovirus proteins and the induction of virus-specific cytoplasmic structures. Virology 131:39-48. http://dx.doi.org/10.1016/0042-6822 (83)90531-7.
    • (1983) Virology , vol.131 , pp. 39-48
    • Bienz, K.1    Egger, D.2    Rasser, Y.3    Bossart, W.4
  • 10
    • 14744283953 scopus 로고    scopus 로고
    • Intracellular location and translocation of silent and active poliovirus replication complexes
    • Egger D, Bienz K. 2005. Intracellular location and translocation of silent and active poliovirus replication complexes. J. Gen. Virol. 86:707-718. http://dx.doi.org/10.1099/vir.0.80442-0.
    • (2005) J. Gen. Virol , vol.86 , pp. 707-718
    • Egger, D.1    Bienz, K.2
  • 11
    • 80455132064 scopus 로고    scopus 로고
    • The transformation of enterovirus replication structures: a three-dimensional study of single-and doublemembrane compartments
    • Limpens RW, van der Schaar HM, Kumar D, Koster AJ, Snijder EJ, van Kuppeveld FJ, Barcena M. 2011. The transformation of enterovirus replication structures: a three-dimensional study of single-and doublemembrane compartments. mBio 2(5):e00166-11. http://dx.doi.org/10.1128/mBio.00166-11.
    • (2011) mBio , vol.2 , Issue.5
    • Limpens, R.W.1    van der Schaar, H.M.2    Kumar, D.3    Koster, A.J.4    Snijder, E.J.5    van Kuppeveld, F.J.6    Barcena, M.7
  • 12
    • 0033798416 scopus 로고    scopus 로고
    • Remodeling the endoplasmic reticulum by poliovirus infection and by individual viral proteins: an autophagy-like origin for virus-induced vesicles
    • Suhy DA, Giddings TH, Jr, Kirkegaard K. 2000. Remodeling the endoplasmic reticulum by poliovirus infection and by individual viral proteins: an autophagy-like origin for virus-induced vesicles. J. Virol. 74: 8953-8965. http://dx.doi.org/10.1128/JVI.74.19.8953-8965.2000.
    • (2000) J. Virol , vol.74 , pp. 8953-8965
    • Suhy, D.A.1    Giddings, T.H.2    Kirkegaard, K.3
  • 14
    • 85011178750 scopus 로고
    • Fine structure of changes produced in cultured cells sampled at specified intervals during a single growth cycle of polio virus
    • Kallman F, Williams RC, Dulbecco R, Vogt M. 1958. Fine structure of changes produced in cultured cells sampled at specified intervals during a single growth cycle of polio virus. J. Biophys. Biochem. Cytol. 4:301-308. http://dx.doi.org/10.1083/jcb.4.3.301.
    • (1958) J. Biophys. Biochem. Cytol , vol.4 , pp. 301-308
    • Kallman, F.1    Williams, R.C.2    Dulbecco, R.3    Vogt, M.4
  • 15
    • 0029794678 scopus 로고    scopus 로고
    • Cellular origin and ultrastructure of membranes induced during poliovirus infection
    • Schlegel A, Giddings TH, Ladinsky MS, Kirkegaard K. 1996. Cellular origin and ultrastructure of membranes induced during poliovirus infection. J. Virol. 70:6576-6588.
    • (1996) J. Virol , vol.70 , pp. 6576-6588
    • Schlegel, A.1    Giddings, T.H.2    Ladinsky, M.S.3    Kirkegaard, K.4
  • 16
    • 33846594517 scopus 로고    scopus 로고
    • Topology of double-membraned vesicles and the opportunity for non-lytic release of cytoplasm
    • Kirkegaard K, Jackson WT. 2005. Topology of double-membraned vesicles and the opportunity for non-lytic release of cytoplasm. Autophagy 1:182-184. http://dx.doi.org/10.4161/auto.1.3.2065.
    • (2005) Autophagy , vol.1 , pp. 182-184
    • Kirkegaard, K.1    Jackson, W.T.2
  • 17
    • 84870776595 scopus 로고    scopus 로고
    • Intracellular vesicle acidification promotes maturation of infectious poliovirus particles
    • Richards AL, Jackson WT. 2012. Intracellular vesicle acidification promotes maturation of infectious poliovirus particles. PLoS Pathog. 8:e1003046. http://dx.doi.org/10.1371/journal.ppat.1003046.
    • (2012) PLoS Pathog , vol.8
    • Richards, A.L.1    Jackson, W.T.2
  • 18
    • 80054729346 scopus 로고    scopus 로고
    • COPII and COPI traffic at the ER-Golgi interface
    • Szul T, Sztul E. 2011. COPII and COPI traffic at the ER-Golgi interface. Physiology (Bethesda) 26:348-364. http://dx.doi.org/10.1152/physiol.00017.2011.
    • (2011) Physiology (Bethesda) , vol.26 , pp. 348-364
    • Szul, T.1    Sztul, E.2
  • 19
    • 0038726917 scopus 로고    scopus 로고
    • ER-to-Golgi transport: COPI and COPII function (review)
    • Duden R. 2003. ER-to-Golgi transport: COPI and COPII function (review). Mol. Membr. Biol. 20:197-207. http://dx.doi.org/10.1080/09687 68031000122548.
    • (2003) Mol. Membr. Biol , vol.20 , pp. 197-207
    • Duden, R.1
  • 21
    • 84866184330 scopus 로고    scopus 로고
    • Poliovirus infection transiently increases COPII vesicle budding
    • Trahey M, Oh HS, Cameron CE, Hay JC. 2012. Poliovirus infection transiently increases COPII vesicle budding. J. Virol. 86:9675-9682. http://dx.doi.org/10.1128/JVI.01159-12.
    • (2012) J. Virol , vol.86 , pp. 9675-9682
    • Trahey, M.1    Oh, H.S.2    Cameron, C.E.3    Hay, J.C.4
  • 22
    • 0034802046 scopus 로고    scopus 로고
    • Cellular COPII proteins are involved in production of the vesicles that form the poliovirus replication complex
    • Rust RC, Landmann L, Gosert R, Tang BL, Hong W, Hauri HP, Egger D, Bienz K. 2001. Cellular COPII proteins are involved in production of the vesicles that form the poliovirus replication complex. J. Virol. 75: 9808-9818. http://dx.doi.org/10.1128/JVI.75.20.9808-9818.2001.
    • (2001) J. Virol , vol.75 , pp. 9808-9818
    • Rust, R.C.1    Landmann, L.2    Gosert, R.3    Tang, B.L.4    Hong, W.5    Hauri, H.P.6    Egger, D.7    Bienz, K.8
  • 23
    • 33750459353 scopus 로고    scopus 로고
    • COPI activity coupled with fatty acid biosynthesis is required for viral replication
    • Cherry S, Kunte A, Wang H, Coyne C, Rawson RB, Perrimon N. 2006. COPI activity coupled with fatty acid biosynthesis is required for viral replication. PLoS Pathog. 2:900-912. http://dx.doi.org/10.1371/journal.ppat.0020102.
    • (2006) PLoS Pathog , vol.2 , pp. 900-912
    • Cherry, S.1    Kunte, A.2    Wang, H.3    Coyne, C.4    Rawson, R.B.5    Perrimon, N.6
  • 24
    • 0036838235 scopus 로고    scopus 로고
    • Differential requirements for COPI coats in formation of replication complexes among three genera of Picornaviridae
    • Gazina EV, Mackenzie JM, Gorrell RJ, Anderson DA. 2002. Differential requirements for COPI coats in formation of replication complexes among three genera of Picornaviridae. J. Virol. 76:11113-11122. http://dx.doi.org/10.1128/JVI.76.21.11113-11122.2002.
    • (2002) J. Virol , vol.76 , pp. 11113-11122
    • Gazina, E.V.1    Mackenzie, J.M.2    Gorrell, R.J.3    Anderson, D.A.4
  • 26
    • 0000115806 scopus 로고
    • Electron microscopic study of the formation of poliovirus
    • Dales S, Eggers HJ, Tamm I, Palade GE. 1965. Electron microscopic study of the formation of poliovirus. Virology 26:379-389. http://dx.doi.org/10.1016/0042-6822(65)90001-2.
    • (1965) Virology , vol.26 , pp. 379-389
    • Dales, S.1    Eggers, H.J.2    Tamm, I.3    Palade, G.E.4
  • 27
    • 0014346786 scopus 로고
    • Cytoplasmic membranebound vesicles in echovirus 12-infected cells
    • Skinner MS, Halperen S, Harkin JC. 1968. Cytoplasmic membranebound vesicles in echovirus 12-infected cells. Virology 36:241-253. http://dx.doi.org/10.1016/0042-6822(68)90141-4.
    • (1968) Virology , vol.36 , pp. 241-253
    • Skinner, M.S.1    Halperen, S.2    Harkin, J.C.3
  • 28
    • 0014094726 scopus 로고
    • Cytopathology of mengovirus infection. II. Proliferation of membranous cisternae
    • Amako K, Dales S. 1967. Cytopathology of mengovirus infection. II. Proliferation of membranous cisternae. Virology 32:201-215.
    • (1967) Virology , vol.32 , pp. 201-215
    • Amako, K.1    Dales, S.2
  • 29
    • 1842854071 scopus 로고    scopus 로고
    • The ultrastructure of the developing replication site in foot-and-mouth disease virus-infected BHK-38 cells
    • Monaghan P, Cook H, Jackson T, Ryan M, Wileman T. 2004. The ultrastructure of the developing replication site in foot-and-mouth disease virus-infected BHK-38 cells. J. Gen. Virol. 85:933-946. http://dx.doi.org/10.1099/vir.0.19408-0.
    • (2004) J. Gen. Virol , vol.85 , pp. 933-946
    • Monaghan, P.1    Cook, H.2    Jackson, T.3    Ryan, M.4    Wileman, T.5
  • 31
    • 0031926171 scopus 로고    scopus 로고
    • Brefeldin A inhibits cell-free, de novo synthesis of poliovirus
    • Cuconati A, Molla A, Wimmer E. 1998. Brefeldin A inhibits cell-free, de novo synthesis of poliovirus. J. Virol. 72:6456-6464.
    • (1998) J. Virol , vol.72 , pp. 6456-6464
    • Cuconati, A.1    Molla, A.2    Wimmer, E.3
  • 32
    • 0028309941 scopus 로고
    • Secretory pathway function, but not cytoskeletal integrity, is required in poliovirus infection
    • Doedens J, Maynell LA, Klymkowsky MW, Kirkegaard K. 1994. Secretory pathway function, but not cytoskeletal integrity, is required in poliovirus infection. Arch. Virol. Suppl. 9:159-172.
    • (1994) Arch. Virol. Suppl , vol.9 , pp. 159-172
    • Doedens, J.1    Maynell, L.A.2    Klymkowsky, M.W.3    Kirkegaard, K.4
  • 33
    • 0026794415 scopus 로고
    • Involvement of membrane traffic in the replication of poliovirus genomes: effects of brefeldin A
    • Irurzun A, Perez L, Carrasco L. 1992. Involvement of membrane traffic in the replication of poliovirus genomes: effects of brefeldin A. Virology 191:166-175. http://dx.doi.org/10.1016/0042-6822(92)90178-R.
    • (1992) Virology , vol.191 , pp. 166-175
    • Irurzun, A.1    Perez, L.2    Carrasco, L.3
  • 34
    • 0026533754 scopus 로고
    • Inhibition of poliovirus RNA synthesis by brefeldin A
    • Maynell LA, Kirkegaard K, Klymkowsky MW. 1992. Inhibition of poliovirus RNA synthesis by brefeldin A. J. Virol. 66:1985-1994.
    • (1992) J. Virol , vol.66 , pp. 1985-1994
    • Maynell, L.A.1    Kirkegaard, K.2    Klymkowsky, M.W.3
  • 35
    • 0002955384 scopus 로고    scopus 로고
    • Brefeldin A acts to stabilize an abortive ARF-GDP-Sec7 domain protein complex: involvement of specific residues of the Sec7 domain
    • Peyroche A, Antonny B, Robineau S, Acker J, Cherfils J, Jackson CL. 1999. Brefeldin A acts to stabilize an abortive ARF-GDP-Sec7 domain protein complex: involvement of specific residues of the Sec7 domain. Mol. Cell 3:275-285. http://dx.doi.org/10.1016/S1097-27 65(00)80455-4.
    • (1999) Mol. Cell , vol.3 , pp. 275-285
    • Peyroche, A.1    Antonny, B.2    Robineau, S.3    Acker, J.4    Cherfils, J.5    Jackson, C.L.6
  • 36
    • 0348047597 scopus 로고    scopus 로고
    • Crystal structure of ARF1*Sec7 complexed with brefeldin A and its implications for the guanine nucleotide exchange mechanism
    • Mossessova E, Corpina RA, Goldberg J. 2003. Crystal structure of ARF1*Sec7 complexed with brefeldin A and its implications for the guanine nucleotide exchange mechanism. Mol. Cell 12:1403-1411. http://dx.doi.org/10.1016/S1097-2765(03)00475-1.
    • (2003) Mol. Cell , vol.12 , pp. 1403-1411
    • Mossessova, E.1    Corpina, R.A.2    Goldberg, J.3
  • 37
    • 0346243924 scopus 로고    scopus 로고
    • Structural snapshots of the mechanism and inhibition of a guanine nucleotide exchange factor
    • Renault L, Guibert B, Cherfils J. 2003. Structural snapshots of the mechanism and inhibition of a guanine nucleotide exchange factor. Nature 426:525-530. http://dx.doi.org/10.1038/nature02197.
    • (2003) Nature , vol.426 , pp. 525-530
    • Renault, L.1    Guibert, B.2    Cherfils, J.3
  • 38
    • 70350070478 scopus 로고    scopus 로고
    • Large Arf1 guanine nucleotide exchange factors: evolution, domain structure, and roles in membrane trafficking and human disease
    • Bui QT, Golinelli-Cohen MP, Jackson CL. 2009. Large Arf1 guanine nucleotide exchange factors: evolution, domain structure, and roles in membrane trafficking and human disease. Mol. Genet. Genomics 282: 329-350. http://dx.doi.org/10.1007/s00438-009-0473-3.
    • (2009) Mol. Genet. Genomics , vol.282 , pp. 329-350
    • Bui, Q.T.1    Golinelli-Cohen, M.P.2    Jackson, C.L.3
  • 39
    • 57149096870 scopus 로고    scopus 로고
    • A critical role of a cellular membrane traffic protein in poliovirus RNA replication
    • Belov GA, Feng Q, Nikovics K, Jackson CL, Ehrenfeld E. 2008. A critical role of a cellular membrane traffic protein in poliovirus RNA replication. PLoS Pathog. 4:e1000216. http://dx.doi.org/10.1371/journal.ppat.1000216.
    • (2008) PLoS Pathog , vol.4
    • Belov, G.A.1    Feng, Q.2    Nikovics, K.3    Jackson, C.L.4    Ehrenfeld, E.5
  • 40
    • 77954506478 scopus 로고    scopus 로고
    • Differential effects of the putative GBF1 inhibitors golgicide A and AG1478 on enterovirus replication
    • van der Linden L, van der Schaar HM, Lanke KH, Neyts J, van Kuppeveld FJ. 2010. Differential effects of the putative GBF1 inhibitors golgicide A and AG1478 on enterovirus replication. J. Virol. 84:7535-7542. http://dx.doi.org/10.1128/JVI.02684-09.
    • (2010) J. Virol , vol.84 , pp. 7535-7542
    • van der Linden, L.1    van der Schaar, H.M.2    Lanke, K.H.3    Neyts, J.4    van Kuppeveld, F.J.5
  • 42
    • 34248345508 scopus 로고    scopus 로고
    • Molecular determinants of the interaction between coxsackievirus protein 3A and guanine nucleotide exchange factor GBF1
    • Wessels E, Duijsings D, Lanke KH, Melchers WJ, Jackson CL, van Kuppeveld FJ. 2007. Molecular determinants of the interaction between coxsackievirus protein 3A and guanine nucleotide exchange factor GBF1. J. Virol. 81:5238-5245. http://dx.doi.org/10.1128/JVI.02680-06.
    • (2007) J. Virol , vol.81 , pp. 5238-5245
    • Wessels, E.1    Duijsings, D.2    Lanke, K.H.3    Melchers, W.J.4    Jackson, C.L.5    van Kuppeveld, F.J.6
  • 43
    • 79955398622 scopus 로고    scopus 로고
    • Analysis of poliovirus protein 3A interactions with viral and cellular proteins in infected cells
    • Teterina NL, Pinto Y, Weaver JD, Jensen KS, Ehrenfeld E. 2011. Analysis of poliovirus protein 3A interactions with viral and cellular proteins in infected cells. J. Virol. 85:4284-4296. http://dx.doi.org/10.1128/JVI.02398-10.
    • (2011) J. Virol , vol.85 , pp. 4284-4296
    • Teterina, N.L.1    Pinto, Y.2    Weaver, J.D.3    Jensen, K.S.4    Ehrenfeld, E.5
  • 47
    • 0033549576 scopus 로고    scopus 로고
    • GBF1: A novel Golgiassociated BFA-resistant guanine nucleotide exchange factor that displays specificity for ADP-ribosylation factor 5
    • Claude A, Zhao BP, Kuziemsky CE, Dahan S, Berger SJ, Yan JP, Armold AD, Sullivan EM, Melancon P. 1999. GBF1: A novel Golgiassociated BFA-resistant guanine nucleotide exchange factor that displays specificity for ADP-ribosylation factor 5. J. Cell Biol. 146:71-84. http://dx.doi.org/10.1083/jcb.146.999.71.
    • (1999) J. Cell Biol , vol.146 , pp. 71-84
    • Claude, A.1    Zhao, B.P.2    Kuziemsky, C.E.3    Dahan, S.4    Berger, S.J.5    Yan, J.P.6    Armold, A.D.7    Sullivan, E.M.8    Melancon, P.9
  • 48
    • 37249041571 scopus 로고    scopus 로고
    • Dissecting the role of the ARF guanine nucleotide exchange factor GBF1 in Golgi biogenesis and protein trafficking
    • Szul T, Grabski R, Lyons S, Morohashi Y, Shestopal S, Lowe M, Sztul E. 2007. Dissecting the role of the ARF guanine nucleotide exchange factor GBF1 in Golgi biogenesis and protein trafficking. J. Cell Sci. 120: 3929-3940. http://dx.doi.org/10.1242/jcs.010769.
    • (2007) J. Cell Sci , vol.120 , pp. 3929-3940
    • Szul, T.1    Grabski, R.2    Lyons, S.3    Morohashi, Y.4    Shestopal, S.5    Lowe, M.6    Sztul, E.7
  • 49
    • 18744386949 scopus 로고    scopus 로고
    • Poliovirus proteins induce membrane association of GTPase ADP-ribosylation factor
    • Belov GA, Fogg MH, Ehrenfeld E. 2005. Poliovirus proteins induce membrane association of GTPase ADP-ribosylation factor. J. Virol. 79: 7207-7216. http://dx.doi.org/10.1128/JVI.79.11.7207-7216.2005.
    • (2005) J. Virol , vol.79 , pp. 7207-7216
    • Belov, G.A.1    Fogg, M.H.2    Ehrenfeld, E.3
  • 50
    • 33846569842 scopus 로고    scopus 로고
    • Involvement of cellular membrane traffic proteins in poliovirus replication
    • Belov GA, Ehrenfeld E. 2007. Involvement of cellular membrane traffic proteins in poliovirus replication. Cell Cycle 6:36-38. http://dx.doi.org/10.4161/cc.6.1.3683.
    • (2007) Cell Cycle , vol.6 , pp. 36-38
    • Belov, G.A.1    Ehrenfeld, E.2
  • 51
    • 1842562401 scopus 로고    scopus 로고
    • The poliovirus replication machinery can escape inhibition by an antiviral drug that targets a host cell protein
    • Crotty S, Saleh MC, Gitlin L, Beske O, Andino R. 2004. The poliovirus replication machinery can escape inhibition by an antiviral drug that targets a host cell protein. J. Virol. 78:3378-3386. http://dx.doi.org/10.1128/JVI.78.7.3378-3386.2004.
    • (2004) J. Virol , vol.78 , pp. 3378-3386
    • Crotty, S.1    Saleh, M.C.2    Gitlin, L.3    Beske, O.4    Andino, R.5
  • 52
    • 78249237877 scopus 로고    scopus 로고
    • Poliovirus replication requires the N-terminus but not the catalytic Sec7 domain of ArfGEF GBF1
    • Belov GA, Kovtunovych G, Jackson CL, Ehrenfeld E. 2010. Poliovirus replication requires the N-terminus but not the catalytic Sec7 domain of ArfGEF GBF1. Cell. Microbiol. 12:1463-1479. http://dx.doi.org/10.1111/j.1462-5822.2010.01482.x.
    • (2010) Cell. Microbiol , vol.12 , pp. 1463-1479
    • Belov, G.A.1    Kovtunovych, G.2    Jackson, C.L.3    Ehrenfeld, E.4
  • 53
    • 84859594211 scopus 로고    scopus 로고
    • The 3A protein from multiple picornaviruses utilizes the Golgi adaptor proteinACBD3to recruit PI4KIIIβ
    • Greninger AL, Knudsen GM, Betegon M, Burlingame AL, Derisi JL. 2012. The 3A protein from multiple picornaviruses utilizes the Golgi adaptor proteinACBD3to recruit PI4KIIIβ. J. Virol. 86:3605-3616. http://dx.doi.org/10.1128/JVI.06778-11.
    • (2012) J. Virol , vol.86 , pp. 3605-3616
    • Greninger, A.L.1    Knudsen, G.M.2    Betegon, M.3    Burlingame, A.L.4    Derisi, J.L.5
  • 54
    • 17444409335 scopus 로고    scopus 로고
    • Dissection of membrane dynamics of the ARF-guanine nucleotide exchange factor GBF1
    • Szul T, Garcia-Mata R, Brandon E, Shestopal S, Alvarez C, Sztul E. 2005. Dissection of membrane dynamics of the ARF-guanine nucleotide exchange factor GBF1. Traffic 6:374-385. http://dx.doi.org/10.1111/j.1600-0854.2005.00282.x.
    • (2005) Traffic , vol.6 , pp. 374-385
    • Szul, T.1    Garcia-Mata, R.2    Brandon, E.3    Shestopal, S.4    Alvarez, C.5    Sztul, E.6
  • 55
    • 14844333247 scopus 로고    scopus 로고
    • Dynamics of GBF1, a brefeldin A-sensitive Arf1 exchange factor at the Golgi
    • Niu TK, Pfeifer AC, Lippincott-Schwartz J, Jackson CL. 2005. Dynamics of GBF1, a brefeldin A-sensitive Arf1 exchange factor at the Golgi. Mol. Biol. Cell 16:1213-1222. http://dx.doi.org/10.1091/mbc.E04-07-0599.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 1213-1222
    • Niu, T.K.1    Pfeifer, A.C.2    Lippincott-Schwartz, J.3    Jackson, C.L.4
  • 56
    • 34347386746 scopus 로고    scopus 로고
    • Rab1b interacts with GBF1 and modulates both ARF1 dynamics and COPI association
    • Monetta P, Slavin I, Romero N, Alvarez C. 2007. Rab1b interacts with GBF1 and modulates both ARF1 dynamics and COPI association. Mol. Biol. Cell 18:2400-2410. http://dx.doi.org/10.1091/mbc.E06-11-1005.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 2400-2410
    • Monetta, P.1    Slavin, I.2    Romero, N.3    Alvarez, C.4
  • 57
    • 80051785915 scopus 로고    scopus 로고
    • Mislocalization of large ARF-GEFs as a potential mechanism for BFA resistance in COG-deficient cells
    • Flanagan-Steet H, Johnson S, Smith RD, Bangiyeva J, Lupashin V, Steet R. 2011. Mislocalization of large ARF-GEFs as a potential mechanism for BFA resistance in COG-deficient cells. Exp. Cell Res. 317:2342-2352. http://dx.doi.org/10.1016/j.yexcr.2011.06.005.
    • (2011) Exp. Cell Res , vol.317 , pp. 2342-2352
    • Flanagan-Steet, H.1    Johnson, S.2    Smith, R.D.3    Bangiyeva, J.4    Lupashin, V.5    Steet, R.6
  • 58
    • 0242417632 scopus 로고    scopus 로고
    • The membrane-tethering protein p115 interacts with GBF1, an ARF guanine-nucleotide-exchange factor
    • García-Mata R, Sztul E. 2003. The membrane-tethering protein p115 interacts with GBF1, an ARF guanine-nucleotide-exchange factor. EMBO Rep. 4:320-325. http://dx.doi.org/10.1038/sj.embor.embor762.
    • (2003) EMBO Rep , vol.4 , pp. 320-325
    • García-Mata, R.1    Sztul, E.2
  • 59
    • 34548552643 scopus 로고    scopus 로고
    • The Arf GEF GBF1 is required for GGA recruitment to Golgi membranes
    • Lefrançois P, McCormick PJ. 2007. The Arf GEF GBF1 is required for GGA recruitment to Golgi membranes. Traffic 8:1440-1451. http://dx.doi.org/10.1111/j.1600-0854.2007.00623.x.
    • (2007) Traffic , vol.8 , pp. 1440-1451
    • Lefrançois, P.1    McCormick, P.J.2
  • 60
    • 58049099709 scopus 로고    scopus 로고
    • A COPI coat subunit interacts directly with an early-Golgi localized Arf exchange factor
    • Deng Y, Golinelli-Cohen MP, Smirnova E, Jackson CL. 2009. A COPI coat subunit interacts directly with an early-Golgi localized Arf exchange factor. EMBO Rep. 10:58-64. http://dx.doi.org/10.1038/embor.2008.221.
    • (2009) EMBO Rep , vol.10 , pp. 58-64
    • Deng, Y.1    Golinelli-Cohen, M.P.2    Smirnova, E.3    Jackson, C.L.4
  • 62
    • 0037632878 scopus 로고    scopus 로고
    • A novel Golgi membrane protein is a partner of the ARF exchange factors Gealp and Gea2p
    • Chantalat S, Courbeyrette R, Senic-Matuglia F, Jackson CL, Goud B, Peyroche A. 2003. A novel Golgi membrane protein is a partner of the ARF exchange factors Gealp and Gea2p. Mol. Biol. Cell 14:2357-2371. http://dx.doi.org/10.1091/mbc.E02-10-0693.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 2357-2371
    • Chantalat, S.1    Courbeyrette, R.2    Senic-Matuglia, F.3    Jackson, C.L.4    Goud, B.5    Peyroche, A.6
  • 63
    • 80053353907 scopus 로고    scopus 로고
    • Trs65p, a subunit of the Ypt1p GEF TRAPPII, interacts with the Arf1p exchange factor Gea2p to facilitate COPI-mediated vesicle traffic
    • Chen SL, Cai HQ, Park SK, Menon S, Jackson CL, Ferro-Novick S. 2011. Trs65p, a subunit of the Ypt1p GEF TRAPPII, interacts with the Arf1p exchange factor Gea2p to facilitate COPI-mediated vesicle traffic. Mol. Biol. Cell 22:3634-3644. http://dx.doi.org/10.1091/mbc.E11-03-0197.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 3634-3644
    • Chen, S.L.1    Cai, H.Q.2    Park, S.K.3    Menon, S.4    Jackson, C.L.5    Ferro-Novick, S.6
  • 66
    • 20544455617 scopus 로고    scopus 로고
    • Golgins and GTPases, giving identity and structure to the Golgi apparatus
    • Short B, Haas A, Barr FA. 2005. Golgins and GTPases, giving identity and structure to the Golgi apparatus. Biochim. Biophys. Acta 1744:383-395. http://dx.doi.org/10.1016/j.bbamcr.2005.02.001.
    • (2005) Biochim. Biophys. Acta , vol.1744 , pp. 383-395
    • Short, B.1    Haas, A.2    Barr, F.A.3
  • 67
    • 84863115228 scopus 로고    scopus 로고
    • ARF1 and GBF1 generate a PI4P-enriched environment supportive of hepatitis C virus replication
    • Zhang L, Hong Z, Lin W, Shao RX, Goto K, Hsu VW, Chung RT. 2012. ARF1 and GBF1 generate a PI4P-enriched environment supportive of hepatitis C virus replication. PLoS One 7:e32135. http://dx.doi.org/10.1371/journal.pone.0032135.
    • (2012) PLoS One , vol.7
    • Zhang, L.1    Hong, Z.2    Lin, W.3    Shao, R.X.4    Goto, K.5    Hsu, V.W.6    Chung, R.T.7
  • 69
    • 34548172905 scopus 로고    scopus 로고
    • Activation of cellular Arf GTPases by poliovirus protein 3CD correlates with virus replication
    • Belov GA, Habbersett C, Franco D, Ehrenfeld E. 2007. Activation of cellular Arf GTPases by poliovirus protein 3CD correlates with virus replication. J. Virol. 81:9259-9267. http://dx.doi.org/10.1128/JVI.00840-07.
    • (2007) J. Virol , vol.81 , pp. 9259-9267
    • Belov, G.A.1    Habbersett, C.2    Franco, D.3    Ehrenfeld, E.4
  • 70
    • 80052186347 scopus 로고    scopus 로고
    • Membrane-trafficking sorting hubs: cooperation between PI4P and small GTPases at the trans-Golgi network
    • Santiago-Tirado FH, Bretscher A. 2011. Membrane-trafficking sorting hubs: cooperation between PI4P and small GTPases at the trans-Golgi network. Trends Cell Biol. 21:515-525. http://dx.doi.org/10.1016/j.tcb.2011.05.005.
    • (2011) Trends Cell Biol , vol.21 , pp. 515-525
    • Santiago-Tirado, F.H.1    Bretscher, A.2
  • 71
    • 0033194151 scopus 로고    scopus 로고
    • ARF mediates recruitment of PtdIns-4-OH kinase-beta and stimulates synthesis of PtdIns(4, 5)P2 on the Golgi complex
    • Godi A, Pertile P, Meyers R, Marra P, Di Tullio G, Iurisci C, Luini A, Corda D, De Matteis MA. 1999. ARF mediates recruitment of PtdIns-4-OH kinase-beta and stimulates synthesis of PtdIns(4, 5)P2 on the Golgi complex. Nat. Cell Biol. 1:280-287. http://dx.doi.org/10.1038/12993.
    • (1999) Nat. Cell Biol , vol.1 , pp. 280-287
    • Godi, A.1    Pertile, P.2    Meyers, R.3    Marra, P.4    Di Tullio, G.5    Iurisci, C.6    Luini, A.7    Corda, D.8    De Matteis, M.A.9
  • 72
    • 84856501318 scopus 로고    scopus 로고
    • ACBD3-mediated recruitment of PI4KB to picornavirus RNA replication sites
    • Sasaki J, Ishikawa K, Arita M, Taniguchi K. 2012. ACBD3-mediated recruitment of PI4KB to picornavirus RNA replication sites. EMBO J. 31:754-766. http://dx.doi.org/10.1038/emboj.2011.429.
    • (2012) EMBO J , vol.31 , pp. 754-766
    • Sasaki, J.1    Ishikawa, K.2    Arita, M.3    Taniguchi, K.4
  • 74
    • 84897380301 scopus 로고    scopus 로고
    • Phosphatidylinositol-4 kinase III beta and oxysterolbinding protein accumulate unesterified cholesterol on poliovirusinduced membrane structure
    • Arita M. 2014. Phosphatidylinositol-4 kinase III beta and oxysterolbinding protein accumulate unesterified cholesterol on poliovirusinduced membrane structure. Microbiol. Immunol. 58:239-256. http://dx.doi.org/10.1111/1348-0421.12144.
    • (2014) Microbiol. Immunol , vol.58 , pp. 239-256
    • Arita, M.1
  • 77
    • 79551707738 scopus 로고    scopus 로고
    • Phosphatidylinositol 4-kinase III beta is a target of enviroxime-like compounds for antipoliovirus activity
    • Arita M, Kojima H, Nagano T, Okabe T, Wakita T, Shimizu H. 2011. Phosphatidylinositol 4-kinase III beta is a target of enviroxime-like compounds for antipoliovirus activity. J. Virol. 85:2364-2372. http://dx.doi.org/10.1128/JVI.02249-10.
    • (2011) J. Virol , vol.85 , pp. 2364-2372
    • Arita, M.1    Kojima, H.2    Nagano, T.3    Okabe, T.4    Wakita, T.5    Shimizu, H.6
  • 78
    • 28444439900 scopus 로고    scopus 로고
    • Organelle identity and the signposts for membrane traffic
    • Behnia R, Munro S. 2005. Organelle identity and the signposts for membrane traffic. Nature 438:597-604. http://dx.doi.org/10.1038/nature04397.
    • (2005) Nature , vol.438 , pp. 597-604
    • Behnia, R.1    Munro, S.2
  • 79
    • 84880962133 scopus 로고    scopus 로고
    • Phosphoinositides: tiny lipids with giant impact on cell regulation
    • Balla T. 2013. Phosphoinositides: tiny lipids with giant impact on cell regulation. Physiol. Rev. 93:1019-1137. http://dx.doi.org/10.1152/physrev.00 028.2012.
    • (2013) Physiol. Rev , vol.93 , pp. 1019-1137
    • Balla, T.1
  • 81
    • 84896700191 scopus 로고    scopus 로고
    • Fitness and virulence of a coxsackievirus mutant that can circumnavigate the need for phosphatidylinositol 4-kinase class III beta
    • Thibaut HJ, van der Schaar HM, Lanke KH, Verbeken E, Andrews M, Leyssen P, Neyts J, van Kuppeveld FJ. 2014. Fitness and virulence of a coxsackievirus mutant that can circumnavigate the need for phosphatidylinositol 4-kinase class III beta. J. Virol. 88:3048-3051. http://dx.doi.org/10.1128/JVI.03177-13.
    • (2014) J. Virol , vol.88 , pp. 3048-3051
    • Thibaut, H.J.1    van der Schaar, H.M.2    Lanke, K.H.3    Verbeken, E.4    Andrews, M.5    Leyssen, P.6    Neyts, J.7    van Kuppeveld, F.J.8
  • 82
    • 69449107491 scopus 로고    scopus 로고
    • Cellular kinase inhibitors that suppress enterovirus replication have a conserved target in viral protein 3A similar to that of enviroxime
    • Arita M, Wakita T, Shimizu H. 2009. Cellular kinase inhibitors that suppress enterovirus replication have a conserved target in viral protein 3A similar to that of enviroxime. J. Gen. Virol. 90:1869-1879. http://dx.doi.org/10.1099/vir.0.012096-0.
    • (2009) J. Gen. Virol , vol.90 , pp. 1869-1879
    • Arita, M.1    Wakita, T.2    Shimizu, H.3
  • 83
    • 0018844239 scopus 로고
    • Inhibition of rhinovirus replication in organ culture by a potential antiviral drug
    • DeLong DC, Reed SE. 1980. Inhibition of rhinovirus replication in organ culture by a potential antiviral drug. J. Infect. Dis. 141:87-91. http://dx.doi.org/10.1093/infdis/141.1.87.
    • (1980) J. Infect. Dis , vol.141 , pp. 87-91
    • DeLong, D.C.1    Reed, S.E.2
  • 84
    • 84875776334 scopus 로고    scopus 로고
    • Oxysterol-binding protein family I is the target of minor enviroxime-like compounds
    • Arita M, Kojima H, Nagano T, Okabe T, Wakita T, Shimizu H. 2013. Oxysterol-binding protein family I is the target of minor enviroxime-like compounds. J. Virol. 87:4252-4260. http://dx.doi.org/10.1128/JVI.03546-12.
    • (2013) J. Virol , vol.87 , pp. 4252-4260
    • Arita, M.1    Kojima, H.2    Nagano, T.3    Okabe, T.4    Wakita, T.5    Shimizu, H.6
  • 85
    • 55549111249 scopus 로고    scopus 로고
    • Coordinated lipid transfer between the endoplasmic reticulum and the Golgi complex requires the VAP proteins and is essential for Golgi-mediated transport
    • Peretti D, Dahan N, Shimoni E, Hirschberg K, Lev S. 2008. Coordinated lipid transfer between the endoplasmic reticulum and the Golgi complex requires the VAP proteins and is essential for Golgi-mediated transport. Mol. Biol. Cell 19:3871-3884. http://dx.doi.org/10.1091/mbc.E08-05-0498.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 3871-3884
    • Peretti, D.1    Dahan, N.2    Shimoni, E.3    Hirschberg, K.4    Lev, S.5
  • 86
    • 84866434896 scopus 로고    scopus 로고
    • Multisite phosphorylation of oxysterol-binding protein regulates sterol binding and activation of sphingomyelin synthesis
    • Goto A, Liu X, Robinson CA, Ridgway ND. 2012. Multisite phosphorylation of oxysterol-binding protein regulates sterol binding and activation of sphingomyelin synthesis. Mol. Biol. Cell 23:3624-3635. http://dx.doi.org/10.1091/mbc.E12-04-0283.
    • (2012) Mol. Biol. Cell , vol.23 , pp. 3624-3635
    • Goto, A.1    Liu, X.2    Robinson, C.A.3    Ridgway, N.D.4
  • 87
    • 78650123509 scopus 로고    scopus 로고
    • Oxysterol binding protein-dependent activation of sphingomyelin synthesis in the Golgi apparatus requires phosphatidylinositol 4-kinase IIalpha
    • Banerji S, Ngo M, Lane CF, Robinson CA, Minogue S, Ridgway ND. 2010. Oxysterol binding protein-dependent activation of sphingomyelin synthesis in the Golgi apparatus requires phosphatidylinositol 4-kinase IIalpha. Mol. Biol. Cell 21:4141-4150. http://dx.doi.org/10.1091/mbc.E10-05-0424.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 4141-4150
    • Banerji, S.1    Ngo, M.2    Lane, C.F.3    Robinson, C.A.4    Minogue, S.5    Ridgway, N.D.6
  • 88
    • 84887957821 scopus 로고    scopus 로고
    • A four-step cycle driven by PI(4)P hydrolysis directs sterol/PI(4)P exchange by the ER-Golgi tether OSBP
    • Mesmin B, Bigay J, von Filseck JM, Lacas-Gervais S, Drin G, Antonny B. 2013. A four-step cycle driven by PI(4)P hydrolysis directs sterol/PI(4)P exchange by the ER-Golgi tether OSBP. Cell 155:830-843. http://dx.doi.org/10.1016/j.cell.2013.09.056.
    • (2013) Cell , vol.155 , pp. 830-843
    • Mesmin, B.1    Bigay, J.2    von Filseck, J.M.3    Lacas-Gervais, S.4    Drin, G.5    Antonny, B.6
  • 89
    • 84898981360 scopus 로고    scopus 로고
    • Oxysterol-binding protein is a phosphatidylinositol 4-kinase effector required for HCV replication membrane integrity and cholesterol trafficking
    • Wang H, Perry JW, Lauring AS, Neddermann P, De Francesco R, Tai AW. 2014. Oxysterol-binding protein is a phosphatidylinositol 4-kinase effector required for HCV replication membrane integrity and cholesterol trafficking. Gastroenterology 146:1373-1385.e1311. http://dx.doi.org/10.1053/j.gastro.2014.02.002.
    • (2014) Gastroenterology , vol.146 , pp. 1373.e1311-1385.e1311
    • Wang, H.1    Perry, J.W.2    Lauring, A.S.3    Neddermann, P.4    De Francesco, R.5    Tai, A.W.6
  • 90
    • 0018830280 scopus 로고
    • Poliovirus increases phosphatidylcholine biosynthesis in HeLa cells by stimulation of the rate-limiting reaction catalyzed by CTP: phosphocholine cytidylyltransferase
    • Vance DE, Trip EM, Paddon HB. 1980. Poliovirus increases phosphatidylcholine biosynthesis in HeLa cells by stimulation of the rate-limiting reaction catalyzed by CTP: phosphocholine cytidylyltransferase. J. Biol. Chem. 255:1064-1069.
    • (1980) J. Biol. Chem , vol.255 , pp. 1064-1069
    • Vance, D.E.1    Trip, E.M.2    Paddon, H.B.3
  • 91
    • 0015251797 scopus 로고
    • Incorporation of lipid precursors into cytoplasmic membranes of poliovirus-infected Hela cells
    • Mosser AG, Caliguiri LA, Tamm I. 1972. Incorporation of lipid precursors into cytoplasmic membranes of poliovirus-infected Hela cells. Virology 47:39-47. http://dx.doi.org/10.1016/0042-6822(72)90236-X.
    • (1972) Virology , vol.47 , pp. 39-47
    • Mosser, A.G.1    Caliguiri, L.A.2    Tamm, I.3
  • 92
    • 0023153244 scopus 로고
    • The effect of mengovirus infection on lipid synthesis in cultured Ehrlich ascites tumor cells
    • Schimmel H, Traub P. 1987. The effect of mengovirus infection on lipid synthesis in cultured Ehrlich ascites tumor cells. Lipids 22:95-103. http://dx.doi.org/10.1007/BF02534860.
    • (1987) Lipids , vol.22 , pp. 95-103
    • Schimmel, H.1    Traub, P.2
  • 93
    • 2342572271 scopus 로고    scopus 로고
    • Phospholipid biosynthesis in mammalian cells
    • Vance JE, Vance DE. 2004. Phospholipid biosynthesis in mammalian cells. Biochem. Cell Biol. 82:113-128. http://dx.doi.org/10.1139/o03-073.
    • (2004) Biochem. Cell Biol , vol.82 , pp. 113-128
    • Vance, J.E.1    Vance, D.E.2
  • 94
    • 38549173564 scopus 로고    scopus 로고
    • Membrane lipids: where they are and how they behave
    • van Meer G, Voelker DR, Feigenson GW. 2008. Membrane lipids: where they are and how they behave. Nat. Rev. Mol. Cell Biol. 9:112-124. http://dx.doi.org/10.1038/nrm2330.
    • (2008) Nat. Rev. Mol. Cell Biol , vol.9 , pp. 112-124
    • van Meer, G.1    Voelker, D.R.2    Feigenson, G.W.3
  • 95
    • 0027439285 scopus 로고
    • Movement of fatty acids, fatty acid analogues, and bile acids across phospholipid bilayers
    • Kamp F, Hamilton JA, Westerhoff HV. 1993. Movement of fatty acids, fatty acid analogues, and bile acids across phospholipid bilayers. Biochemistry 32:11074-11086. http://dx.doi.org/10.1021/bi00092a017.
    • (1993) Biochemistry , vol.32 , pp. 11074-11086
    • Kamp, F.1    Hamilton, J.A.2    Westerhoff, H.V.3
  • 96
    • 0026007057 scopus 로고
    • Effects of fatty acids on lipid synthesis and viralRNAreplication in poliovirus-infected cells
    • Guinea R, Carrasco L. 1991. Effects of fatty acids on lipid synthesis and viralRNAreplication in poliovirus-infected cells. Virology 185:473-476. http://dx.doi.org/10.1016/0042-6822(91)90802-I.
    • (1991) Virology , vol.185 , pp. 473-476
    • Guinea, R.1    Carrasco, L.2
  • 97
    • 0025328822 scopus 로고
    • Phospholipid biosynthesis and poliovirus genome replication, two coupled phenomena
    • Guinea R, Carrasco L. 1990. Phospholipid biosynthesis and poliovirus genome replication, two coupled phenomena. EMBO J. 9:2011-2016.
    • (1990) EMBO J , vol.9 , pp. 2011-2016
    • Guinea, R.1    Carrasco, L.2
  • 98
    • 34548610648 scopus 로고    scopus 로고
    • The human fatty acid synthase: a new therapeutic target for coxsackievirus B3-induced diseases?
    • Rassmann A, Henke A, Jarasch N, Lottspeich F, Saluz HP, Munder T. 2007. The human fatty acid synthase: a new therapeutic target for coxsackievirus B3-induced diseases? Antiviral Res. 76:150-158. http://dx.doi.org/10.1016/j.antiviral.2007.06.011.
    • (2007) Antiviral Res , vol.76 , pp. 150-158
    • Rassmann, A.1    Henke, A.2    Jarasch, N.3    Lottspeich, F.4    Saluz, H.P.5    Munder, T.6
  • 99
    • 77958100661 scopus 로고    scopus 로고
    • Dengue virus nonstructural protein 3 redistributes fatty acid synthase to sites of viral replication and increases cellular fatty acid synthesis
    • Heaton NS, Perera R, Berger KL, Khadka S, Lacount DJ, Kuhn RJ, Randall G. 2010. Dengue virus nonstructural protein 3 redistributes fatty acid synthase to sites of viral replication and increases cellular fatty acid synthesis. Proc. Natl. Acad. Sci. U. S. A. 107:17345-17350. http://dx.doi.org/10.1073/pnas.1010811107.
    • (2010) Proc. Natl. Acad. Sci. U. S. A , vol.107 , pp. 17345-17350
    • Heaton, N.S.1    Perera, R.2    Berger, K.L.3    Khadka, S.4    Lacount, D.J.5    Kuhn, R.J.6    Randall, G.7
  • 100
    • 84876461949 scopus 로고    scopus 로고
    • Modulation of fatty acid synthase enzyme activity and expression during hepatitis C virus replication
    • Nasheri N, Joyce M, Rouleau Y, Yang P, Yao S, Tyrrell DL, Pezacki JP. 2013. Modulation of fatty acid synthase enzyme activity and expression during hepatitis C virus replication. Chem. Biol. 20:570-582. http://dx.doi.org/10.1016/j.chembiol.2013.03.014.
    • (2013) Chem. Biol , vol.20 , pp. 570-582
    • Nasheri, N.1    Joyce, M.2    Rouleau, Y.3    Yang, P.4    Yao, S.5    Tyrrell, D.L.6    Pezacki, J.P.7
  • 101
    • 14744294236 scopus 로고    scopus 로고
    • Maintenance of the diacylglycerol level in the Golgi apparatus by the Nir2 protein is critical for Golgi secretory function
    • Litvak V, Dahan N, Ramachandran S, Sabanay H, Lev S. 2005. Maintenance of the diacylglycerol level in the Golgi apparatus by the Nir2 protein is critical for Golgi secretory function. Nat. Cell Biol. 7:225-234. http://dx.doi.org/10.1038/ncb1221.
    • (2005) Nat. Cell Biol , vol.7 , pp. 225-234
    • Litvak, V.1    Dahan, N.2    Ramachandran, S.3    Sabanay, H.4    Lev, S.5
  • 102
    • 80051505725 scopus 로고    scopus 로고
    • Phospholipid synthesis participates in the regulation of diacylglycerol required for membrane trafficking at the Golgi complex
    • Sarri E, Sicart A, Lazaro-Dieguez F, Egea G. 2011. Phospholipid synthesis participates in the regulation of diacylglycerol required for membrane trafficking at the Golgi complex. J. Biol. Chem. 286:28632-28643. http://dx.doi.org/10.1074/jbc.M111.267534.
    • (2011) J. Biol. Chem , vol.286 , pp. 28632-28643
    • Sarri, E.1    Sicart, A.2    Lazaro-Dieguez, F.3    Egea, G.4
  • 104
    • 0036734611 scopus 로고    scopus 로고
    • The major sites of cellular phospholipid synthesis and molecular determinants of fatty acid and lipid head group specificity
    • Henneberry AL, Wright MM, McMaster CR. 2002. The major sites of cellular phospholipid synthesis and molecular determinants of fatty acid and lipid head group specificity. Mol. Biol. Cell 13:3148-3161. http://dx.doi.org/10.1091/mbc.01-11-0540.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3148-3161
    • Henneberry, A.L.1    Wright, M.M.2    McMaster, C.R.3
  • 105
    • 0026519212 scopus 로고
    • Structural and functional characterization of the poliovirus replication complex
    • Bienz K, Egger D, Pfister T, Troxler M. 1992. Structural and functional characterization of the poliovirus replication complex. J. Virol. 66:2740-2747.
    • (1992) J. Virol , vol.66 , pp. 2740-2747
    • Bienz, K.1    Egger, D.2    Pfister, T.3    Troxler, M.4
  • 106
    • 27844552576 scopus 로고    scopus 로고
    • Confined multilamellae prefer cylindrical morphology. A theory of myelin formation
    • Huang JR, Zou LN, Witten TA. 2005. Confined multilamellae prefer cylindrical morphology. A theory of myelin formation. Eur. Phys. J. E Soft Matter 18:279-285. http://dx.doi.org/10.1140/epje/e2005-00035-8.
    • (2005) Eur. Phys. J. E Soft Matter , vol.18 , pp. 279-285
    • Huang, J.R.1    Zou, L.N.2    Witten, T.A.3
  • 108
    • 56349152646 scopus 로고    scopus 로고
    • The Big Bang of picorna-like virus evolution antedates the radiation of eukaryotic supergroups
    • Koonin EV, Wolf YI, Nagasaki K, Dolja VV. 2008. The Big Bang of picorna-like virus evolution antedates the radiation of eukaryotic supergroups. Nat. Rev. Microbiol. 6:925-939. http://dx.doi.org/10.1038/nrmicro2030.
    • (2008) Nat. Rev. Microbiol , vol.6 , pp. 925-939
    • Koonin, E.V.1    Wolf, Y.I.2    Nagasaki, K.3    Dolja, V.V.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.