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Volumn 31, Issue 21, 2012, Pages 4204-4220

Endocytic tubules regulated by Rab GTPases 5 and 11 are used for envelopment of herpes simplex virus

Author keywords

endocytosis; HSV1; Rab11; Rab5; trans Golgi network

Indexed keywords

DYNAMIN; RAB GTPASE 11; RAB GTPASE 5; RAB PROTEIN; TRANSFERRIN RECEPTOR; UNCLASSIFIED DRUG; VIRUS GLYCOPROTEIN;

EID: 84868587398     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/emboj.2012.262     Document Type: Article
Times cited : (119)

References (82)
  • 1
    • 0032889509 scopus 로고    scopus 로고
    • Intracellular traffic of herpes simplex virus glycoprotein gE: Characterization of the sorting signals required for its trans-Golgi network localization
    • Alconada A, Bauer U, Sodeik B, Hoflack B (1999) Intracellular traffic of herpes simplex virus glycoprotein gE: characterization of the sorting signals required for its trans-Golgi network localization. J Virol 73: 377-387 (Pubitemid 28565381)
    • (1999) Journal of Virology , vol.73 , Issue.1 , pp. 377-387
    • Alconada, A.1    Bauer, U.2    Sodeik, B.3    Hoflack, B.4
  • 2
    • 0031711867 scopus 로고    scopus 로고
    • African swine fever virus is enveloped by a two-membraned collapsed cisterna derived from the endoplasmic reticulum
    • Andres G, Garcia-Escudero R, Simon-Mateo C, Vinuela E (1998) African swine fever virus is enveloped by a two-membraned collapsed cisterna derived from the endoplasmic reticulum. J Virol 72: 8988-9001 (Pubitemid 28471843)
    • (1998) Journal of Virology , vol.72 , Issue.11 , pp. 8988-9001
    • Andres, G.1    Garcia-Escudero, R.2    Simon-Mateo, C.3    Vinuela, E.4
  • 3
    • 33750728629 scopus 로고    scopus 로고
    • Two modes of herpesvirus trafficking in neurons: Membrane acquisition directs motion
    • DOI 10.1128/JVI.01441-06
    • Antinone SE, Smith GA (2006) Two modes of herpesvirus trafficking in neurons: membrane acquisition directs motion. J Virol 80: 11235-11240 (Pubitemid 44706563)
    • (2006) Journal of Virology , vol.80 , Issue.22 , pp. 11235-11240
    • Antinone, S.E.1    Smith, G.A.2
  • 4
    • 33751168961 scopus 로고    scopus 로고
    • The formation of TGN-to-plasma-membrane transport carriers
    • Bard F, Malhotra V (2006) The formation of TGN-to-plasma-membrane transport carriers. Annu Rev Cell Dev Biol 22: 439-455
    • (2006) Annu Rev Cell Dev Biol , vol.22 , pp. 439-455
    • Bard, F.1    Malhotra, V.2
  • 5
    • 0034939645 scopus 로고    scopus 로고
    • Transport of viral proteins to the apical membranes and interaction of matrix protein with glycoproteins in the assembly of influenza viruses
    • DOI 10.1016/S0168-1702(01)00266-0, PII S0168170201002660
    • Barman S, Ali A, Hui EK, Adhikary L, Nayak DP (2001) Transport of viral proteins to the apical membranes and interaction of matrix protein with glycoproteins in the assembly of influenza viruses. Virus Res 77: 61-69 (Pubitemid 32622811)
    • (2001) Virus Research , vol.77 , Issue.1 , pp. 61-69
    • Barman, S.1    Ali, A.2    Hui, E.K.-W.3    Adhikary, L.4    Nayak, D.P.5
  • 6
    • 0345742558 scopus 로고    scopus 로고
    • Effects of mutations in the cytoplasmic domain of herpes simplex virus type 1 glycoprotein B on intracellular transport and infectivity
    • DOI 10.1128/JVI.78.3.1540-1551.2004
    • Beitia Ortiz de Zarate I, Kaelin K, Rozenberg F (2004) Effects of mutations in the cytoplasmic domain of herpes simplex virus type 1 glycoprotein B on intracellular transport and infectivity. J Virol 78: 1540-1551 (Pubitemid 38095863)
    • (2004) Journal of Virology , vol.78 , Issue.3 , pp. 1540-1551
    • Ortiz De Zarate, I.B.1    Kaelin, K.2    Rozenberg, F.3
  • 7
    • 0015518063 scopus 로고
    • Studies on the biogenesis of herpesvirus envelope
    • Ben-Porat T, Kaplan AS (1972) Studies on the biogenesis of herpesvirus envelope. Nature 235: 165-166
    • (1972) Nature , vol.235 , pp. 165-166
    • Ben-Porat, T.1    Kaplan, A.S.2
  • 9
    • 0001007022 scopus 로고
    • Electron microscope observations of African swine fever virus in tissue culture cells
    • Breese Jr SS, DeBoer CJ (1966) Electron microscope observations of African swine fever virus in tissue culture cells. Virology 28: 420-428
    • (1966) Virology , vol.28 , pp. 420-428
    • Breese Jr., S.S.1    Deboer, C.J.2
  • 10
    • 77952719625 scopus 로고    scopus 로고
    • The Rab11 pathway is required for influenza A virus budding and filament formation
    • Bruce EA, Digard P, Stuart AD (2010) The Rab11 pathway is required for influenza A virus budding and filament formation. J Virol 84: 5848-5859
    • (2010) J Virol , vol.84 , pp. 5848-5859
    • Bruce, E.A.1    Digard, P.2    Stuart, A.D.3
  • 11
    • 9644260511 scopus 로고    scopus 로고
    • Envelopment of the hepatitis B virus nucleocapsid
    • DOI 10.1016/j.virusres.2004.08.016, PII S0168170204003272
    • Bruss V (2004) Envelopment of the hepatitis B virus nucleocapsid. Virus Res 106: 199-209 (Pubitemid 39572965)
    • (2004) Virus Research , vol.106 , Issue.2 SPEC. ISSUE , pp. 199-209
    • Bruss, V.1
  • 12
    • 33846502163 scopus 로고    scopus 로고
    • Hepatitis B virus morphogenesis
    • Bruss V (2007) Hepatitis B virus morphogenesis. World J Gastroenterol 13: 65-73 (Pubitemid 46165463)
    • (2007) World Journal of Gastroenterology , vol.13 , Issue.1 , pp. 65-73
    • Bruss, V.1
  • 15
  • 16
    • 80054758176 scopus 로고    scopus 로고
    • Involvement of members of the Rab family and related small GTPases in autophagosome formation and maturation
    • Chua CE, Gan BQ, Tang BL (2011) Involvement of members of the Rab family and related small GTPases in autophagosome formation and maturation. Cell Mol Life Sci 68: 3349-3358
    • (2011) Cell Mol Life Sci , vol.68 , pp. 3349-3358
    • Chua, C.E.1    Gan, B.Q.2    Tang, B.L.3
  • 17
    • 0029857253 scopus 로고    scopus 로고
    • Direct interaction between the envelope and matrix proteins of HIV-1
    • Cosson P (1996) Direct interaction between the envelope and matrix proteins of HIV-1. EMBO J 15: 5783-5788 (Pubitemid 26375499)
    • (1996) EMBO Journal , vol.15 , Issue.21 , pp. 5783-5788
    • Cosson, P.1
  • 18
    • 9944249048 scopus 로고    scopus 로고
    • Alphaherpesvirus glycoprotein M causes the relocalization of plasma membrane proteins
    • DOI 10.1099/vir.0.80361-0
    • Crump CM, Bruun B, Bell S, Pomeranz LE, Minson T, Browne HM (2004) Alphaherpesvirus glycoprotein M causes the relocalization of plasma membrane proteins. J Gen Virol 85: 3517-3527 (Pubitemid 39591859)
    • (2004) Journal of General Virology , vol.85 , Issue.12 , pp. 3517-3527
    • Crump, C.M.1    Bruun, B.2    Bell, S.3    Pomeranz, L.E.4    Minson, T.5    Browne, H.M.6
  • 19
    • 34447265020 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 cytoplasmic envelopment requires functional Vps4
    • DOI 10.1128/JVI.00222-07
    • Crump CM, Yates C, Minson T (2007) Herpes simplex virus type 1 cytoplasmic envelopment requires functional Vps4. J Virol 81: 7380-7387 (Pubitemid 47047827)
    • (2007) Journal of Virology , vol.81 , Issue.14 , pp. 7380-7387
    • Crump, C.M.1    Yates, C.2    Minson, T.3
  • 20
    • 0032498526 scopus 로고    scopus 로고
    • ARF6 targets recycling vesicles to the plasma membrane: Insights from an ultrastructural investigation
    • DOI 10.1083/jcb.140.3.603
    • D'Souza-Schorey C, van Donselaar E, Hsu VW, Yang C, Stahl PD, Peters PJ (1998) ARF6 targets recycling vesicles to the plasma membrane: insights from an ultrastructural investigation. J Cell Biol 140: 603-616 (Pubitemid 28134063)
    • (1998) Journal of Cell Biology , vol.140 , Issue.3 , pp. 603-616
    • D'Souza-Schorey, C.1    Van Donselaar, E.2    Hsu, V.W.3    Yang, C.4    Stahl, P.D.5    Peters, P.J.6
  • 21
    • 0001737927 scopus 로고
    • The structure and assembly of herpes viruses
    • Harris JR, Horne RW (eds) London Academic Press
    • Dargin D (1986) The structure and assembly of herpes viruses. In Electronmicroscopy of Proteins, Virus Structure, Harris JR, Horne RW (eds) Vol. 5, pp 359-437. London: Academic Press
    • (1986) Electronmicroscopy of Proteins, Virus Structure , vol.5 , pp. 359-437
    • Dargin, D.1
  • 24
    • 0036112453 scopus 로고    scopus 로고
    • Localization of HCMV UL33 and US27 in endocytic compartments and viral membranes
    • DOI 10.1034/j.1600-0854.2002.030307.x
    • Fraile-Ramos A, Pelchen-Matthews A, Kledal TN, Browne H, Schwartz TW, Marsh M (2002) Localization of HCMV UL33 and US27 in endocytic compartments and viral membranes. Traffic 3: 218-232 (Pubitemid 34555479)
    • (2002) Traffic , vol.3 , Issue.3 , pp. 218-232
    • Fraile-Ramos, A.1    Pelchen-Matthews, A.2    Kledal, T.N.3    Browne, H.4    Schwartz, T.W.5    Marsh, M.6
  • 25
    • 0032563568 scopus 로고    scopus 로고
    • An endocytosed TGN38 chimeric protein is delivered to the TGN after trafficking through the endocytic recycling compartment in CHO cells
    • DOI 10.1083/jcb.142.4.923
    • Ghosh RN, Mallet WG, Soe TT, McGraw TE, Maxfield FR (1998) An endocytosed TGN38 chimeric protein is delivered to the TGN after trafficking through the endocytic recycling compartment in CHO cells. J Cell Biol 142: 923-936 (Pubitemid 28402049)
    • (1998) Journal of Cell Biology , vol.142 , Issue.4 , pp. 923-936
    • Ghosh, R.N.1    Mallet, W.G.2    Soe, T.T.3    McGraw, T.E.4    Maxfield, F.R.5
  • 26
    • 0019295460 scopus 로고
    • Pathways involved in fluid phase and adsorptive endocytosis in neuroblastoma
    • DOI 10.1083/jcb.87.3.579
    • Gonatas J, Stieber A, Olsnes S, Gonatas NK (1980) Pathways involved in fluid phase and adsorptive endocytosis in neuroblastoma. J Cell Biol 87: 579-588 (Pubitemid 11161788)
    • (1980) Journal of Cell Biology , vol.87 , Issue.3 , pp. 579-588
    • Gonatas, J.1    Stieber, A.2    Olsnes, S.3    Gonatas, N.K.4
  • 28
    • 0024787848 scopus 로고
    • A quantitative analysis of the endocytic pathway in baby hamster kidney cells
    • DOI 10.1083/jcb.109.6.2703
    • Griffiths G, Back R, Marsh M (1989) A quantitative analysis of the endocytic pathway in baby hamster kidney cells. J Cell Biol 109: 2703-2720 (Pubitemid 20011898)
    • (1989) Journal of Cell Biology , vol.109 , Issue.6 , pp. 2703-2720
    • Griffiths, G.1    Back, R.2    Marsh, M.3
  • 29
    • 0030812588 scopus 로고    scopus 로고
    • Functional dissection of COP-I subunits in the biogenesis of multivesicular endosomes
    • DOI 10.1083/jcb.139.5.1183
    • Gu F, Aniento F, Parton RG, Gruenberg J (1997) Functional dissection of COP-I subunits in the biogenesis of multivesicular endosomes. J Cell Biol 139: 1183-1195 (Pubitemid 27523206)
    • (1997) Journal of Cell Biology , vol.139 , Issue.5 , pp. 1183-1195
    • Gu, F.1    Aniento, F.2    Parton, R.G.3    Gruenberg, J.4
  • 30
    • 80052233389 scopus 로고    scopus 로고
    • Endosome maturation
    • Huotari J, Helenius A (2011) Endosome maturation. EMBO J 30: 3481-3500
    • (2011) EMBO J , vol.30 , pp. 3481-3500
    • Huotari, J.1    Helenius, A.2
  • 31
    • 0026525542 scopus 로고
    • A novel herpes simplex virus glycoprotein, gL, forms a complex with glycoprotein H (gH) and affects normal folding and surface expression of gH
    • Hutchinson L, Browne H, Wargent V, Davis-Poynter N, Primorac S, Goldsmith K, Minson AC, Johnson DC (1992) A novel herpes simplex virus glycoprotein, gL, forms a complex with glycoprotein H (gH) and affects normal folding and surface expression of gH. J Virol 66: 2240-2250
    • (1992) J Virol , vol.66 , pp. 2240-2250
    • Hutchinson, L.1    Browne, H.2    Wargent, V.3    Davis-Poynter, N.4    Primorac, S.5    Goldsmith, K.6    Minson, A.C.7    Johnson, D.C.8
  • 32
    • 79954599465 scopus 로고    scopus 로고
    • Herpesviruses remodel host membranes for virus egress
    • Johnson DC, Baines JD (2011) Herpesviruses remodel host membranes for virus egress. Nat Rev Microbiol 9: 382-394
    • (2011) Nat Rev Microbiol , vol.9 , pp. 382-394
    • Johnson, D.C.1    Baines, J.D.2
  • 34
    • 74749099537 scopus 로고    scopus 로고
    • The early endosome: A busy sorting station for proteins at the crossroads
    • Jovic M, Sharma M, Rahajeng J, Caplan S (2010) The early endosome: a busy sorting station for proteins at the crossroads. Histol Histopathol 25: 99-112
    • (2010) Histol Histopathol , vol.25 , pp. 99-112
    • Jovic, M.1    Sharma, M.2    Rahajeng, J.3    Caplan, S.4
  • 35
    • 33646168140 scopus 로고    scopus 로고
    • Reconstitution of herpes simplex virus microtubule-dependent trafficking in vitro
    • Lee GE, Murray JW, Wolkoff AW, Wilson DW (2006) Reconstitution of herpes simplex virus microtubule-dependent trafficking in vitro. J Virol 80: 4264-4275
    • (2006) J Virol , vol.80 , pp. 4264-4275
    • Lee, G.E.1    Murray, J.W.2    Wolkoff, A.W.3    Wilson, D.W.4
  • 37
    • 0027398577 scopus 로고
    • Rab9 functions in transport between late endosomes and the trans Golgi network
    • Lombardi D, Soldati T, Riederer MA, Goda Y, Zerial M, Pfeffer SR (1993) Rab9 functions in transport between late endosomes and the trans Golgi network. EMBO J 12: 677-682 (Pubitemid 23073715)
    • (1993) EMBO Journal , vol.12 , Issue.2 , pp. 677-682
    • Lombardi, D.1    Soldati, T.2    Riederer, M.A.3    Goda, Y.4    Zerial, M.5    Pfeffer, S.R.6
  • 38
    • 50149119228 scopus 로고    scopus 로고
    • Comprehensive characterization of extracellular herpes simplex virus type 1 virions
    • Loret S, Guay G, Lippe R (2008) Comprehensive characterization of extracellular herpes simplex virus type 1 virions. J Virol 82: 8605-8618
    • (2008) J Virol , vol.82 , pp. 8605-8618
    • Loret, S.1    Guay, G.2    Lippe, R.3
  • 40
    • 76049106065 scopus 로고    scopus 로고
    • Endocytic Rab proteins are required for hepatitis C virus replication complex formation
    • Manna D, Aligo J, Xu C, Park WS, Koc H, Heo WD, Konan KV (2010) Endocytic Rab proteins are required for hepatitis C virus replication complex formation. Virology 398: 21-37
    • (2010) Virology , vol.398 , pp. 21-37
    • Manna, D.1    Aligo, J.2    Xu, C.3    Park, W.S.4    Koc, H.5    Heo, W.D.6    Konan, K.V.7
  • 41
    • 11144234329 scopus 로고    scopus 로고
    • Incorporation of three endocytosed varicella-zoster virus glycoproteins, gE, gH, and gB, into the virion envelope
    • DOI 10.1128/JVI.79.2.997-1007.2005
    • Maresova L, Pasieka TJ, Homan E, Gerday E, Grose C (2005) Incorporation of three endocytosed varicella-zoster virus glycoproteins, gE, gH, and gB, into the virion envelope. J Virol 79: 997-1007 (Pubitemid 40053883)
    • (2005) Journal of Virology , vol.79 , Issue.2 , pp. 997-1007
    • Maresova, L.1    Pasieka, T.J.2    Homan, E.3    Gerday, E.4    Grose, C.5
  • 42
    • 34547114456 scopus 로고    scopus 로고
    • Pathways of clathrin-independent endocytosis
    • DOI 10.1038/nrm2216, PII NRM2216
    • Mayor S, Pagano RE (2007) Pathways of clathrin-independent endocytosis. Nat Rev Mol Cell Biol 8: 603-612 (Pubitemid 47106613)
    • (2007) Nature Reviews Molecular Cell Biology , vol.8 , Issue.8 , pp. 603-612
    • Mayor, S.1    Pagano, R.E.2
  • 43
    • 0035138826 scopus 로고    scopus 로고
    • Cytoplasmic domain of herpes simplex virus gE causes accumulation in the trans-Golgi network, a site of virus envelopment and sorting of virions to cell junctions
    • DOI 10.1128/JVI.75.4.1928-1940.2001
    • McMillan TN, Johnson DC (2001) Cytoplasmic domain of herpes simplex virus gE causes accumulation in the trans-Golgi network, a site of virus envelopment and sorting of virions to cell junctions. J Virol 75: 1928-1940 (Pubitemid 32110183)
    • (2001) Journal of Virology , vol.75 , Issue.4 , pp. 1928-1940
    • McMillan, T.N.1    Johnson, D.C.2
  • 44
    • 33644637789 scopus 로고    scopus 로고
    • Intriguing interplay between viral proteins during herpesvirus assembly or: The herpesvirus assembly puzzle
    • DOI 10.1016/j.vetmic.2005.11.040, PII S0378113505003639
    • Mettenleiter TC (2006) Intriguing interplay between viral proteins during herpesvirus assembly or: the herpesvirus assembly puzzle. Vet Microbiol 113: 163-169 (Pubitemid 43326212)
    • (2006) Veterinary Microbiology , vol.113 , Issue.3-4 SPEC. ISSUE , pp. 163-169
    • Mettenleiter, T.C.1
  • 45
    • 33746318034 scopus 로고    scopus 로고
    • Herpesvirus assembly: A tale of two membranes
    • DOI 10.1016/j.mib.2006.06.013, PII S1369527406000968
    • Mettenleiter TC, Klupp BG, Granzow H (2006) Herpesvirus assembly: a tale of two membranes. Curr Opin Microbiol 9: 423-429 (Pubitemid 44108724)
    • (2006) Current Opinion in Microbiology , vol.9 , Issue.4 , pp. 423-429
    • Mettenleiter, T.C.1    Klupp, B.G.2    Granzow, H.3
  • 46
    • 31144448686 scopus 로고    scopus 로고
    • Egress of alphaherpesviruses
    • Mettenleiter TC, Minson T (2006) Egress of alphaherpesviruses. J Virol 80: 1610-1611
    • (2006) J Virol , vol.80 , pp. 1610-1611
    • Mettenleiter, T.C.1    Minson, T.2
  • 47
    • 63149090485 scopus 로고    scopus 로고
    • Herpes simplex virus utilizes the large secretory vesicle pathway for anterograde transport of tegument and envelope proteins and for viral exocytosis from growth cones of human fetal axons
    • author reply 1611-1612
    • author reply 1611-1612 Miranda-Saksena M, Boadle RA, Aggarwal A, Tijono B, Rixon FJ, Diefenbach R, Cunningham AL (2009) Herpes simplex virus utilizes the large secretory vesicle pathway for anterograde transport of tegument and envelope proteins and for viral exocytosis from growth cones of human fetal axons. J Virol 83: 3187-3199
    • (2009) J Virol , vol.83 , pp. 3187-3199
    • Miranda-Saksena, M.1    Boadle, R.A.2    Aggarwal, A.3    Tijono, B.4    Rixon, F.J.5    Diefenbach, R.6    Cunningham, A.L.7
  • 48
    • 9644283009 scopus 로고    scopus 로고
    • Assembly and budding of influenza virus
    • DOI 10.1016/j.virusres.2004.08.012, PII S0168170204003235
    • Nayak DP, Hui EK, Barman S (2004) Assembly and budding of influenza virus. Virus Res 106: 147-165 (Pubitemid 39572961)
    • (2004) Virus Research , vol.106 , Issue.2 SPEC. ISSUE , pp. 147-165
    • Nayak, D.P.1    Hui, E.K.-W.2    Barman, S.3
  • 49
    • 78649438708 scopus 로고    scopus 로고
    • Ultrastructural analysis of virion formation and intraaxonal transport of herpes simplex virus type 1 in primary rat neurons
    • Negatsch A, Granzow H, Maresch C, Klupp BG, Fuchs W, Teifke JP, Mettenleiter TC (2010) Ultrastructural analysis of virion formation and intraaxonal transport of herpes simplex virus type 1 in primary rat neurons. J Virol 84: 13031-13035
    • (2010) J Virol , vol.84 , pp. 13031-13035
    • Negatsch, A.1    Granzow, H.2    Maresch, C.3    Klupp, B.G.4    Fuchs, W.5    Teifke, J.P.6    Mettenleiter, T.C.7
  • 50
    • 0014282895 scopus 로고
    • Electron microscopy of herpes simplex virus. II. Sequence of development
    • Nii S, Morgan C, Rose HM (1968) Electron microscopy of herpes simplex virus. II. Sequence of development. J Virol 2: 517-536
    • (1968) J Virol , vol.2 , pp. 517-536
    • Nii, S.1    Morgan, C.2    Rose, H.M.3
  • 51
    • 0024541206 scopus 로고
    • Internalization of horseradish peroxidase isozymes by pancreatic acinar cells in vitro
    • Oliver C, Tolbert CL, Waters JF (1989) Internalization of horseradish peroxidase isozymes by pancreatic acinar cells in vitro. J Histochem Cytochem 37: 49-56 (Pubitemid 19016541)
    • (1989) Journal of Histochemistry and Cytochemistry , vol.37 , Issue.1 , pp. 49-56
    • Oliver, C.1    Tolbert, C.L.2    Waters, J.F.3
  • 52
    • 0022773447 scopus 로고
    • Transport of horseradish peroxidase from the cell surface to the Golgi in insulin-secreting cells: Preferential labelling of cisternae located in an intermediate position in the stack
    • Orci L, Ravazzola M, Amherdt M, Brown D, Perrelet A (1986) Transport of horseradish peroxidase from the cell surface to the Golgi in insulin-secreting cells: preferential labelling of cisternae located in an intermediate position in the stack. EMBO J 5: 2097-2101
    • (1986) EMBO J , vol.5 , pp. 2097-2101
    • Orci, L.1    Ravazzola, M.2    Amherdt, M.3    Brown, D.4    Perrelet, A.5
  • 53
    • 70350322311 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 production requires a functional ESCRT-III complex but is independent of TSG101 and ALIX expression
    • Pawliczek T, Crump CM (2009) Herpes simplex virus type 1 production requires a functional ESCRT-III complex but is independent of TSG101 and ALIX expression. J Virol 83: 11254-11264
    • (2009) J Virol , vol.83 , pp. 11254-11264
    • Pawliczek, T.1    Crump, C.M.2
  • 54
    • 70450223884 scopus 로고    scopus 로고
    • Multiple routes of protein transport from endosomes to the trans Golgi network
    • Pfeffer SR (2009) Multiple routes of protein transport from endosomes to the trans Golgi network. FEBS Lett 583: 3811-3816
    • (2009) FEBS Lett , vol.583 , pp. 3811-3816
    • Pfeffer, S.R.1
  • 58
    • 67649891816 scopus 로고    scopus 로고
    • Protein kinase D-dependent trafficking of the large Herpes simplex virus type 1 capsids from the TGN to plasma membrane
    • Remillard-Labrosse G, Mihai C, Duron J, Guay G, Lippe R (2009) Protein kinase D-dependent trafficking of the large Herpes simplex virus type 1 capsids from the TGN to plasma membrane. Traffic 10: 1074-1083
    • (2009) Traffic , vol.10 , pp. 1074-1083
    • Remillard-Labrosse, G.1    Mihai, C.2    Duron, J.3    Guay, G.4    Lippe, R.5
  • 59
    • 24144442691 scopus 로고    scopus 로고
    • Rab conversion as a mechanism of progression from early to late endosomes
    • DOI 10.1016/j.cell.2005.06.043, PII S0092867405006975
    • Rink J, Ghigo E, Kalaidzidis Y, Zerial M (2005) Rab conversion as a mechanism of progression from early to late endosomes. Cell 122: 735-749 (Pubitemid 41242638)
    • (2005) Cell , vol.122 , Issue.5 , pp. 735-749
    • Rink, J.1    Ghigo, E.2    Kalaidzidis, Y.3    Zerial, M.4
  • 60
    • 53049097995 scopus 로고    scopus 로고
    • Vaccinia virus morphogenesis and dissemination
    • Roberts KL, Smith GL (2008) Vaccinia virus morphogenesis and dissemination. Trends Microbiol 16: 472-479
    • (2008) Trends Microbiol , vol.16 , pp. 472-479
    • Roberts, K.L.1    Smith, G.L.2
  • 62
    • 50249107793 scopus 로고    scopus 로고
    • Hepatitis C virus budding at lipid droplet-associated ER membrane visualized by 3D electron microscopy
    • Roingeard P, Hourioux C, Blanchard E, Prensier G (2008) Hepatitis C virus budding at lipid droplet-associated ER membrane visualized by 3D electron microscopy. Histochem Cell Biol 130: 561-566
    • (2008) Histochem Cell Biol , vol.130 , pp. 561-566
    • Roingeard, P.1    Hourioux, C.2    Blanchard, E.3    Prensier, G.4
  • 63
    • 0028097957 scopus 로고
    • Assembly of vaccinia virus: The second wrapping cisterna is derived from the trans Golgi network
    • Schmelz M, Sodeik B, Ericsson M, Wolffe EJ, Shida H, Hiller G, Griffiths G (1994) Assembly of vaccinia virus: the second wrapping cisterna is derived from the trans Golgi network. J Virol 68: 130-147
    • (1994) J Virol , vol.68 , pp. 130-147
    • Schmelz, M.1    Sodeik, B.2    Ericsson, M.3    Wolffe, E.J.4    Shida, H.5    Hiller, G.6    Griffiths, G.7
  • 64
    • 0021806048 scopus 로고
    • A new method of preparing gold probes for multiple-labeling cytochemistry
    • Slot JW, Geuze HJ (1985) A new method of preparing gold probes for multiple-labeling cytochemistry. Eur J Cell Biol 38: 87-93 (Pubitemid 15045723)
    • (1985) European Journal of Cell Biology , vol.38 , Issue.1 , pp. 87-93
    • Slot, J.W.1    Geuze, H.J.2
  • 65
    • 33750742492 scopus 로고    scopus 로고
    • Herpes simplex virus capsids are transported in neuronal axons without an envelope containing the viral glycoproteins
    • DOI 10.1128/JVI.01107-06
    • Snyder A, Wisner TW, Johnson DC (2006) Herpes simplex virus capsids are transported in neuronal axons without an envelope containing the viral glycoproteins. J Virol 80: 11165-11177 (Pubitemid 44706556)
    • (2006) Journal of Virology , vol.80 , Issue.22 , pp. 11165-11177
    • Snyder, A.1    Wisner, T.W.2    Johnson, D.C.3
  • 66
    • 68049105101 scopus 로고    scopus 로고
    • Rab GTPases as coordinators of vesicle traffic
    • Stenmark H (2009) Rab GTPases as coordinators of vesicle traffic. Nat Rev Mol Cell Biol 10: 513-525
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 513-525
    • Stenmark, H.1
  • 67
    • 43949089146 scopus 로고    scopus 로고
    • Simultaneous tracking of capsid, tegument, and envelope protein localization in living cells infected with triply fluorescent herpes simplex virus 1
    • DOI 10.1128/JVI.02681-07
    • Sugimoto K, Uema M, Sagara H, Tanaka M, Sata T, Hashimoto Y, Kawaguchi Y (2008) Simultaneous tracking of capsid, tegument, and envelope protein localization in living cells infected with triply fluorescent herpes simplex virus 1. J Virol 82: 5198-5211 (Pubitemid 351705229)
    • (2008) Journal of Virology , vol.82 , Issue.11 , pp. 5198-5211
    • Sugimoto, K.1    Uema, M.2    Sagara, H.3    Tanaka, M.4    Sata, T.5    Hashimoto, Y.6    Kawaguchi, Y.7
  • 68
    • 9644281042 scopus 로고    scopus 로고
    • Molecular mechanism of paramyxovirus budding
    • DOI 10.1016/j.virusres.2004.08.010, PII S0168170204003211
    • Takimoto T, Portner A (2004) Molecular mechanism of paramyxovirus budding. Virus Res 106: 133-145 (Pubitemid 39572960)
    • (2004) Virus Research , vol.106 , Issue.2 SPEC. ISSUE , pp. 133-145
    • Takimoto, T.1    Portner, A.2
  • 69
    • 0031901313 scopus 로고    scopus 로고
    • Role of envelope protein gE endocytosis in the pseudorabies virus life cycle
    • Tirabassi RS, Enquist LW (1998) Role of envelope protein gE endocytosis in the pseudorabies virus life cycle. J Virol 72: 4571-4579 (Pubitemid 28215631)
    • (1998) Journal of Virology , vol.72 , Issue.6 , pp. 4571-4579
    • Tirabassi, R.S.1    Enquist, L.W.2
  • 70
    • 0032976556 scopus 로고    scopus 로고
    • Mutation of the YXXL endocytosis motif in the cytoplasmic tail of pseudorabies virus gE
    • Tirabassi RS, Enquist LW (1999) Mutation of the YXXL endocytosis motif in the cytoplasmic tail of pseudorabies virus gE. J Virol 73: 2717-2728 (Pubitemid 29135657)
    • (1999) Journal of Virology , vol.73 , Issue.4 , pp. 2717-2728
    • Tirabassi, R.S.1    Enquist, L.W.2
  • 71
    • 0019042936 scopus 로고
    • Immunochemistry on ultrathin frozen sections
    • Tokuyasu KT (1980) Immunochemistry on ultrathin frozen sections. Histochem J 12: 381-403
    • (1980) Histochem J , vol.12 , pp. 381-403
    • Tokuyasu, K.T.1
  • 72
    • 0027530255 scopus 로고
    • Progeny vaccinia and human cytomegalovirus particles utilize early endosomal cisternae for their envelopes
    • Tooze J, Hollinshead M, Reis B, Radsak K, Kern H (1993) Progeny vaccinia and human cytomegalovirus particles utilize early endosomal cisternae for their envelopes. Eur J Cell Biol 60: 163-178 (Pubitemid 23092674)
    • (1993) European Journal of Cell Biology , vol.60 , Issue.1 , pp. 163-178
    • Tooze, J.1    Hollinshead, M.2    Reis, B.3    Radsak, K.4    Kern, H.5
  • 73
    • 0033379104 scopus 로고    scopus 로고
    • Biochemical analysis of distinct Rab5- and Rab11-positive endosomes along the transferrin pathway
    • Trischler M, Stoorvogel W, Ullrich O (1999) Biochemical analysis of distinct Rab5-and Rab11-positive endosomes along the transferrin pathway. J Cell Sci 112(Part 24): 4773-4783 (Pubitemid 30034824)
    • (1999) Journal of Cell Science , vol.112 , Issue.24 , pp. 4773-4783
    • Trischler, M.1    Stoorvogel, W.2    Ullrich, O.3
  • 74
    • 21644443202 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 capsids transit by the trans-Golgi network, where viral glycoproteins accumulate independently of capsid egress
    • DOI 10.1128/JVI.79.14.8847-8860.2005
    • Turcotte S, Letellier J, Lippe R (2005) Herpes simplex virus type 1 capsids transit by the trans-Golgi network, where viral glycoproteins accumulate independently of capsid egress. J Virol 79: 8847-8860 (Pubitemid 40934795)
    • (2005) Journal of Virology , vol.79 , Issue.14 , pp. 8847-8860
    • Turcotte, S.1    Letellier, J.2    Lippe, R.3
  • 75
    • 0029850677 scopus 로고    scopus 로고
    • Rab11 regulates recycling through the pericentriolar recycling endosome
    • Ullrich O, Reinsch S, Urbe S, Zerial M, Parton RG (1996) Rab11 regulates recycling through the pericentriolar recycling endosome. J Cell Biol 135: 913-924 (Pubitemid 26403768)
    • (1996) Journal of Cell Biology , vol.135 , Issue.4 , pp. 913-924
    • Ullrich, O.1    Reinsch, S.2    Urbe, S.3    Zerial, M.4    Parton, R.G.5
  • 76
    • 0036153898 scopus 로고    scopus 로고
    • Dynamin-dependent transferrin receptor recycling by endosome-derived clathrin-coated vesicles
    • DOI 10.1091/mbc.01-07-0380
    • van Dam EM, Stoorvogel W (2002) Dynamin-dependent transferrin receptor recycling by endosome-derived clathrin-coated vesicles. Mol Biol Cell 13: 169-182 (Pubitemid 34106067)
    • (2002) Molecular Biology of the Cell , vol.13 , Issue.1 , pp. 169-182
    • Van Dam, E.M.1    Stoorvogel, W.2
  • 77
    • 0037073739 scopus 로고    scopus 로고
    • Endocytosed transferrin receptors recycle via distinct dynamin and phosphatidylinositol 3-kinase-dependent pathways
    • DOI 10.1074/jbc.M206271200
    • van Dam EM, Ten Broeke T, Jansen K, Spijkers P, Stoorvogel W (2002) Endocytosed transferrin receptors recycle via distinct dynamin and phosphatidylinositol 3-kinase-dependent pathways. J Biol Chem 277: 48876-48883 (Pubitemid 35470856)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.50 , pp. 48876-48883
    • Van Dam, E.M.1    Ten Broeke, T.2    Jansen, K.3    Spijkers, P.4    Stoorvogel, W.5
  • 78
    • 66449123730 scopus 로고    scopus 로고
    • Rab7 regulates late endocytic trafficking downstream of multivesicular body biogenesis and cargo sequestration
    • Vanlandingham PA, Ceresa BP (2009) Rab7 regulates late endocytic trafficking downstream of multivesicular body biogenesis and cargo sequestration. J Biol Chem 284: 12110-12124
    • (2009) J Biol Chem , vol.284 , pp. 12110-12124
    • Vanlandingham, P.A.1    Ceresa, B.P.2
  • 79
    • 0032829388 scopus 로고    scopus 로고
    • Effects of targeting herpes simplex virus type 1 gD to the endoplasmic reticulum and trans-Golgi network
    • Whiteley A, Bruun B, Minson T, Browne H (1999) Effects of targeting herpes simplex virus type 1 gD to the endoplasmic reticulum and trans-Golgi network. J Virol 73: 9515-9520 (Pubitemid 29487107)
    • (1999) Journal of Virology , vol.73 , Issue.11 , pp. 9515-9520
    • Whiteley, A.1    Bruun, B.2    Minson, T.3    Browne, H.4
  • 80
    • 6344243522 scopus 로고    scopus 로고
    • Redistribution of cellular and herpes simplex virus proteins from the trans-Golgi network to cell junctions without enveloped capsids
    • DOI 10.1128/JVI.78.21.11519-11535.2004
    • Wisner TW, Johnson DC (2004) Redistribution of cellular and herpes simplex virus proteins from the trans-golgi network to cell junctions without enveloped capsids. J Virol 78: 11519-11535 (Pubitemid 39390738)
    • (2004) Journal of Virology , vol.78 , Issue.21 , pp. 11519-11535
    • Wisner, T.W.1    Johnson, D.C.2
  • 81
    • 79954571251 scopus 로고    scopus 로고
    • Anterograde transport of herpes simplex virus capsids in neurons by both separate and married mechanisms
    • Wisner TW, Sugimoto K, Howard PW, Kawaguchi Y, Johnson DC (2011) Anterograde transport of herpes simplex virus capsids in neurons by both separate and married mechanisms. J Virol 85: 5919-5928
    • (2011) J Virol , vol.85 , pp. 5919-5928
    • Wisner, T.W.1    Sugimoto, K.2    Howard, P.W.3    Kawaguchi, Y.4    Johnson, D.C.5
  • 82
    • 79961195618 scopus 로고    scopus 로고
    • Analysis of Rab GTPase-activating proteins indicates that Rab1a/b and Rab43 are important for herpes simplex virus 1 secondary envelopment
    • Zenner HL, Yoshimura S, Barr FA, Crump CM (2011) Analysis of Rab GTPase-activating proteins indicates that Rab1a/b and Rab43 are important for herpes simplex virus 1 secondary envelopment. J Virol 85: 8012-8021
    • (2011) J Virol , vol.85 , pp. 8012-8021
    • Zenner, H.L.1    Yoshimura, S.2    Barr, F.A.3    Crump, C.M.4


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