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Volumn 76, Issue 24, 2002, Pages 12634-12645

Cytoplasmic trafficking of minute virus of mice: Low-pH requirement, routing to late endosomes, and proteasome interaction

Author keywords

[No Author keywords available]

Indexed keywords

ACLARUBICIN; BAFILOMYCIN A1; BREFELDIN A; EPOXOMICIN; LACTACYSTIN; PROTEASOME; TOSYLPHENYLALANYL CHLOROMETHYL KETONE;

EID: 0036891844     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.76.24.12634-12645.2002     Document Type: Article
Times cited : (76)

References (72)
  • 1
    • 0033998692 scopus 로고    scopus 로고
    • Infectious entry pathway of adeno-associated virus and adeno-associated virus vectors
    • Bartlett, J. S., R. Wilcher, and R. J. Samulski. 2000. Infectious entry pathway of adeno-associated virus and adeno-associated virus vectors. J. Virol. 74:2777-2785.
    • (2000) J. Virol. , vol.74 , pp. 2777-2785
    • Bartlett, J.S.1    Wilcher, R.2    Samulski, R.J.3
  • 2
    • 0026524911 scopus 로고
    • Infectious entry pathway for canine parvovirus
    • Basak, S., and H. Turner. 1992. Infectious entry pathway for canine parvovirus. Virology 186:368-376.
    • (1992) Virology , vol.186 , pp. 368-376
    • Basak, S.1    Turner, H.2
  • 3
    • 0031743946 scopus 로고    scopus 로고
    • Effect of bafilomycin A1 and nocodazole on endocytic transport in HeLa cells: Implications for viral uncoating and infection
    • Bayer, N., D. Schober, E. Prchla, R. F. Murphy, D. Blaas, and R. Fuchs. 1998. Effect of bafilomycin A1 and nocodazole on endocytic transport in HeLa cells: Implications for viral uncoating and infection. J. Virol. 72:9645-9655.
    • (1998) J. Virol. , vol.72 , pp. 9645-9655
    • Bayer, N.1    Schober, D.2    Prchla, E.3    Murphy, R.F.4    Blaas, D.5    Fuchs, R.6
  • 4
    • 0035137153 scopus 로고    scopus 로고
    • Polarity of human parainfluenza virus type 3 infection in polarized human lung epithelial A549 cells: Role of microfilament and microtubule
    • Bose, S., A. Malur, and A. K. Banerjee. 2001. Polarity of human parainfluenza virus type 3 infection in polarized human lung epithelial A549 cells: Role of microfilament and microtubule. J. Virol. 75:1984-1989.
    • (2001) J. Virol. , vol.75 , pp. 1984-1989
    • Bose, S.1    Malur, A.2    Banerjee, A.K.3
  • 5
    • 0011913143 scopus 로고
    • Bafilomycins: A class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells
    • Bowman, E. J., A. Siebers, and K. Altendorf. 1988. Bafilomycins: A class of inhibitors of membrane ATPases from microorganisms, animal cells, and plant cells. Proc. Natl. Acad. Sci. USA 85:7972-7976.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 7972-7976
    • Bowman, E.J.1    Siebers, A.2    Altendorf, K.3
  • 6
    • 0027686846 scopus 로고
    • Erythrocyte P antigen: Cellular receptor for B19 parvovirus
    • Brown, K. E., S. M. Anderson, and N. S. Young. 1993. Erythrocyte P antigen: Cellular receptor for B19 parvovirus. Science 262:114-117.
    • (1993) Science , vol.262 , pp. 114-117
    • Brown, K.E.1    Anderson, S.M.2    Young, N.S.3
  • 8
    • 0023857651 scopus 로고
    • The two transcription units of the autonomous parvovirus minute virus of mice are transcribed in a temporal order
    • Clemens, K. E., and D. J. Pintel. 1988. The two transcription units of the autonomous parvovirus minute virus of mice are transcribed in a temporal order. J. Virol. 62:1448-1451.
    • (1988) J. Virol. , vol.62 , pp. 1448-1451
    • Clemens, K.E.1    Pintel, D.J.2
  • 9
    • 0017200326 scopus 로고
    • The parvovirus MVM: A comparison of heavy and light particle infectivity and their density conversion in vitro
    • Clinton, G. M., and M. Hayashi. 1976. The parvovirus MVM: A comparison of heavy and light particle infectivity and their density conversion in vitro. Virology 74:57-63.
    • (1976) Virology , vol.74 , pp. 57-63
    • Clinton, G.M.1    Hayashi, M.2
  • 10
    • 0023065751 scopus 로고
    • The autonomously replicating parvoviruses of vertebrates
    • Cotmore, S. F., and P. Tattersall. 1987. The autonomously replicating parvoviruses of vertebrates. Adv. Virus Res. 33:91-174.
    • (1987) Adv. Virus Res. , vol.33 , pp. 91-174
    • Cotmore, S.F.1    Tattersall, P.2
  • 11
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux, O., K. Tanaka, and A. L. Goldberg. 1996. Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65:801-847.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 12
    • 0031059493 scopus 로고    scopus 로고
    • Microtubules are involved in bafilomycin A1-induced tubulation and Rab5-dependent vacuolation of early endosomes
    • D'Arrigo, A., C. Bucci, B. H. Toh, and H. Stenmark. 1997. Microtubules are involved in bafilomycin A1-induced tubulation and Rab5-dependent vacuolation of early endosomes. Eur. J. Cell Biol. 72:95-103.
    • (1997) Eur. J. Cell Biol. , vol.72 , pp. 95-103
    • D'Arrigo, A.1    Bucci, C.2    Toh, B.H.3    Stenmark, H.4
  • 13
    • 0037036452 scopus 로고    scopus 로고
    • Proteasome inhibitors reduce luciferase and beta-galactosidase activity in tissue culture cells
    • Deroo, B. J., and T. K. Archer. 2002. Proteasome inhibitors reduce luciferase and beta-galactosidase activity in tissue culture cells. J. Biol. Chem. 277:20120-20123.
    • (2002) J. Biol. Chem. , vol.277 , pp. 20120-20123
    • Deroo, B.J.1    Archer, T.K.2
  • 15
    • 0035138205 scopus 로고    scopus 로고
    • Intracellular trafficking of adeno-associated virus vectors: Routing to the late endosomal compartment and proteasome degradation
    • Douar, A. M., K. Poulard, D. Stockholm, and O. Danos. 2001. Intracellular trafficking of adeno-associated virus vectors: Routing to the late endosomal compartment and proteasome degradation. J. Virol. 75:1824-1833.
    • (2001) J. Virol. , vol.75 , pp. 1824-1833
    • Douar, A.M.1    Poulard, K.2    Stockholm, D.3    Danos, O.4
  • 16
    • 0034091579 scopus 로고    scopus 로고
    • Endosomal processing limits gene transfer to polarized airway epithelia by adeno-associated virus
    • Duan, D., Y. Yue, Z. Yan, J. Yang, and J. F. Engelhardt. 2000. Endosomal processing limits gene transfer to polarized airway epithelia by adeno-associated virus. J. Clin. Investig. 105:1573-1587.
    • (2000) J. Clin. Investig. , vol.105 , pp. 1573-1587
    • Duan, D.1    Yue, Y.2    Yan, Z.3    Yang, J.4    Engelhardt, J.F.5
  • 17
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
    • Fenteany, G., R. F. Standaert, W. S. Lane, S. Choi, E. J. Corey, and S. L. Schreiber. 1995. Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science 268:726-731.
    • (1995) Science , vol.268 , pp. 726-731
    • Fenteany, G.1    Standaert, R.F.2    Lane, W.S.3    Choi, S.4    Corey, E.J.5    Schreiber, S.L.6
  • 18
    • 0030014641 scopus 로고    scopus 로고
    • The antitumor drug aclacinomycin A, which inhibits the degradation of ubiquitinated proteins, shows selectivity for the chymotrypsin-like activity of the bovine pituitary 20 S proteasome
    • Figueiredo-Pereira, M. E., W. E. Chen, J. Li, and O. Johdo. 1996. The antitumor drug aclacinomycin A, which inhibits the degradation of ubiquitinated proteins, shows selectivity for the chymotrypsin-like activity of the bovine pituitary 20 S proteasome. J. Biol. Chem. 271:16455-16459.
    • (1996) J. Biol. Chem. , vol.271 , pp. 16455-16459
    • Figueiredo-Pereira, M.E.1    Chen, W.E.2    Li, J.3    Johdo, O.4
  • 19
    • 0031057925 scopus 로고    scopus 로고
    • Rapid degradation of CD4 in cells expressing human immunodeficiency virus type 1 Env and Vpu is blocked by proteasome inhibitors
    • Fujita, K., S. Omura, and J. Silver. 1997. Rapid degradation of CD4 in cells expressing human immunodeficiency virus type 1 Env and Vpu is blocked by proteasome inhibitors. J. Gen. Virol. 78:619-625.
    • (1997) J. Gen. Virol. , vol.78 , pp. 619-625
    • Fujita, K.1    Omura, S.2    Silver, J.3
  • 20
    • 0027787987 scopus 로고
    • +-ATPase, blocks lysosomal cholesterol trafficking in macrophages
    • +-ATPase, blocks lysosomal cholesterol trafficking in macrophages. J. Biol. Chem. 268:27345-27348.
    • (1993) J. Biol. Chem. , vol.268 , pp. 27345-27348
    • Furuchi, T.1    Aikawa, K.2    Arai, H.3    Inoue, K.4
  • 22
    • 0024517745 scopus 로고
    • Characterization of the early endosome and putative endocytic carrier vesicles in vivo and with an assay of vesicle fusion in vitro
    • Gruenberg, J., G. Griffiths, and K. E. Howell. 1989. Characterization of the early endosome and putative endocytic carrier vesicles in vivo and with an assay of vesicle fusion in vitro. J. Cell Biol. 108:1301-1316.
    • (1989) J. Cell Biol. , vol.108 , pp. 1301-1316
    • Gruenberg, J.1    Griffiths, G.2    Howell, K.E.3
  • 25
    • 0034957168 scopus 로고    scopus 로고
    • Adeno-associated virus serotype 4 (AAV4) and AAV5 both require sialic acid binding for hemagglutination and efficient transduction but differ in sialic acid linkage specificity
    • Kaludov, N., K. E. Brown, R. W. Walters, J. Zabner, and J. A. Chiorini. 2001. Adeno-associated virus serotype 4 (AAV4) and AAV5 both require sialic acid binding for hemagglutination and efficient transduction but differ in sialic acid linkage specificity. J. Virol. 75:6884-6893.
    • (2001) J. Virol. , vol.75 , pp. 6884-6893
    • Kaludov, N.1    Brown, K.E.2    Walters, R.W.3    Zabner, J.4    Chiorini, J.A.5
  • 26
    • 0031785929 scopus 로고    scopus 로고
    • How do animal DNA viruses get to the nucleus?
    • Kasamatsu, H., and A. Nakanishi. 1998. How do animal DNA viruses get to the nucleus? Annu. Rev. Microbiol. 52:627-686.
    • (1998) Annu. Rev. Microbiol. , vol.52 , pp. 627-686
    • Kasamatsu, H.1    Nakanishi, A.2
  • 27
    • 0025373110 scopus 로고
    • Mechanisms of enveloped virus entry into cells
    • Kielian, M., and S. Jungerwirth. 1990. Mechanisms of enveloped virus entry into cells. Mol. Biol. Med. 7:17-31.
    • (1990) Mol. Biol. Med. , vol.7 , pp. 17-31
    • Kielian, M.1    Jungerwirth, S.2
  • 28
    • 0033197542 scopus 로고    scopus 로고
    • Proteasome active sites allosterically regulate each other, suggesting a cyclical bite-chew mechanism for protein breakdown
    • Kisselev, A. F., T. N. Akopian, V. Castillo, and A. L. Goldberg. 1999. Proteasome active sites allosterically regulate each other, suggesting a cyclical bite-chew mechanism for protein breakdown. Mol. Cell 4:395-402.
    • (1999) Mol. Cell , vol.4 , pp. 395-402
    • Kisselev, A.F.1    Akopian, T.N.2    Castillo, V.3    Goldberg, A.L.4
  • 29
    • 0032487332 scopus 로고    scopus 로고
    • Mechanisms of enveloped virus entry into animal cells
    • Klasse, P. J., R. Bron, and M. Marsh. 1998. Mechanisms of enveloped virus entry into animal cells. Adv. Drug Delivery Rev. 34:65-91.
    • (1998) Adv. Drug Delivery Rev. , vol.34 , pp. 65-91
    • Klasse, P.J.1    Bron, R.2    Marsh, M.3
  • 30
    • 0035290730 scopus 로고    scopus 로고
    • Antigen processing by the proteasome
    • Kloetzel, P. M. 2001. Antigen processing by the proteasome. Nat. Rev. Mol. Cell Biol. 2:179-187.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 179-187
    • Kloetzel, P.M.1
  • 31
    • 0032189348 scopus 로고    scopus 로고
    • Proteasome inhibitors: Valuable new tools for cell biologists
    • Lee, D. H., and A. L. Goldberg. 1998. Proteasome inhibitors: Valuable new tools for cell biologists. Trends Cell Biol. 8:397-403.
    • (1998) Trends Cell Biol. , vol.8 , pp. 397-403
    • Lee, D.H.1    Goldberg, A.L.2
  • 32
    • 0034782919 scopus 로고    scopus 로고
    • Genome organization of the densovirus from Bombyx mori (BmDNV-1) and enzyme activity of its capsid
    • Li, Y., Z. Zadori, H. Bando, R. Dubuc, G. Fediere, J. Szelei, and P. Tijssen. 2001. Genome organization of the densovirus from Bombyx mori (BmDNV-1) and enzyme activity of its capsid. J. Gen. Virol. 82:2821-2825.
    • (2001) J. Gen. Virol. , vol.82 , pp. 2821-2825
    • Li, Y.1    Zadori, Z.2    Bando, H.3    Dubuc, R.4    Fediere, G.5    Szelei, J.6    Tijssen, P.7
  • 33
    • 0025940101 scopus 로고
    • Brefeldin A's effects on endosomes, lysosomes, and the TGN suggest a general mechanism for regulating organelle structure and membrane traffic
    • Lippincott-Schwartz, J., L. Yuan, C. Tipper, M. Amherdt, L. Orci, and R. Klausner. 1991. Brefeldin A's effects on endosomes, lysosomes, and the TGN suggest a general mechanism for regulating organelle structure and membrane traffic. Cell 67:601-616.
    • (1991) Cell , vol.67 , pp. 601-616
    • Lippincott-Schwartz, J.1    Yuan, L.2    Tipper, C.3    Amherdt, M.4    Orci, L.5    Klausner, R.6
  • 34
    • 0000653633 scopus 로고
    • Three degrees of guanylic acid-inosinic acid pyrophosphorylase deficiency in mouse fibroblasts
    • Littlefield, J. W. 1964. Three degrees of guanylic acid-inosinic acid pyrophosphorylase deficiency in mouse fibroblasts. Nature 203:1142-1144.
    • (1964) Nature , vol.203 , pp. 1142-1144
    • Littlefield, J.W.1
  • 35
    • 0034469913 scopus 로고    scopus 로고
    • Phosphorylation status of the parvovirus minute virus of mice particle: Mapping and biological relevance of the major phosphorylation sites
    • Maroto, B., J. C. Ramírez, and J. M. Almendral. 2000. Phosphorylation status of the parvovirus minute virus of mice particle: Mapping and biological relevance of the major phosphorylation sites. J. Virol. 74:10892-10902.
    • (2000) J. Virol. , vol.74 , pp. 10892-10902
    • Maroto, B.1    Ramírez, J.C.2    Almendral, J.M.3
  • 36
    • 0024534779 scopus 로고
    • Virus entry into animal cells
    • Marsh, M., and A. Helenius. 1989. Virus entry into animal cells. Adv. Virus Res. 36:107-151.
    • (1989) Adv. Virus Res. , vol.36 , pp. 107-151
    • Marsh, M.1    Helenius, A.2
  • 37
    • 0033621047 scopus 로고    scopus 로고
    • Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity
    • Meng, L., R. Mohan, B. H. Kwok, M. Elofsson, N. Sin, and C. M. Crews. 1999. Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity. Proc. Natl. Acad. Sci. USA 96:10403-10408.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 10403-10408
    • Meng, L.1    Mohan, R.2    Kwok, B.H.3    Elofsson, M.4    Sin, N.5    Crews, C.M.6
  • 38
    • 0035811841 scopus 로고    scopus 로고
    • The NS2 protein generated by the parvovirus minute virus of mice is degraded by the proteasome in a manner independent of ubiquitin chain elongation or activation
    • Miller, C. L., and D. J. Pintel. 2001. The NS2 protein generated by the parvovirus minute virus of mice is degraded by the proteasome in a manner independent of ubiquitin chain elongation or activation. Virology 285:346-355.
    • (2001) Virology , vol.285 , pp. 346-355
    • Miller, C.L.1    Pintel, D.J.2
  • 39
    • 0034967925 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway and proteasome inhibitors
    • Myung, J., K. B. Kim, and C. M. Crews. 2001. The ubiquitin-proteasome pathway and proteasome inhibitors. Med. Res. Rev. 21:245-273.
    • (2001) Med. Res. Rev. , vol.21 , pp. 245-273
    • Myung, J.1    Kim, K.B.2    Crews, C.M.3
  • 40
    • 0027980321 scopus 로고
    • The ubiquitin-proteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB
    • Palombella, V. J., O. J. Rando, A. L. Goldberg, and T. Maniatis. 1994. The ubiquitin-proteasome pathway is required for processing the NF-κB1 precursor protein and the activation of NF-κB. Cell 78:773-785.
    • (1994) Cell , vol.78 , pp. 773-785
    • Palombella, V.J.1    Rando, O.J.2    Goldberg, A.L.3    Maniatis, T.4
  • 41
    • 0019468712 scopus 로고
    • Infectious process of the parvovirus H-1: Correlation of protein content, particle density and viral infectivity
    • Paradiso, P. R. 1981. Infectious process of the parvovirus H-1: Correlation of protein content, particle density and viral infectivity. Virology 39:800-807.
    • (1981) Virology , vol.39 , pp. 800-807
    • Paradiso, P.R.1
  • 42
    • 0033937284 scopus 로고    scopus 로고
    • Cellular uptake and infection by canine parvovirus involves rapid dynamin-regulated clathrin-mediated endocytosis, followed by slower intracellular trafficking
    • Parker, J. S., and C. R. Parrish. 2000. Cellular uptake and infection by canine parvovirus involves rapid dynamin-regulated clathrin-mediated endocytosis, followed by slower intracellular trafficking. J. Virol. 74:1919-1930.
    • (2000) J. Virol. , vol.74 , pp. 1919-1930
    • Parker, J.S.1    Parrish, C.R.2
  • 43
    • 0035085754 scopus 로고    scopus 로고
    • Canine and feline parvoviruses can use human or feline transferrin receptors to bind, enter, and infect cells
    • Parker, J. S., W. J. Murphy, D. Wang, S. J. O'Brien, and C. R. Parrish. 2001. Canine and feline parvoviruses can use human or feline transferrin receptors to bind, enter, and infect cells. J. Virol. 75:3896-3902.
    • (2001) J. Virol. , vol.75 , pp. 3896-3902
    • Parker, J.S.1    Murphy, W.J.2    Wang, D.3    O'Brien, S.J.4    Parrish, C.R.5
  • 44
    • 0030610528 scopus 로고    scopus 로고
    • Bafilomycin A1 treatment retards transferrin receptor recycling more than bulk membrane recycling
    • Presley, J. F., S. Mayor, T. E. McGraw, K. W. Dunn, and F. R. Maxfield. 1997. Bafilomycin A1 treatment retards transferrin receptor recycling more than bulk membrane recycling. J. Biol. Chem. 272:13929-13936.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13929-13936
    • Presley, J.F.1    Mayor, S.2    McGraw, T.E.3    Dunn, K.W.4    Maxfield, F.R.5
  • 45
    • 0030823339 scopus 로고    scopus 로고
    • Growth of the parvovirus minute virus of mice MVMp3 in EL4 lymphocytes is restricted after cell entry and before viral DNA amplification: Cell-specific differences in virus uncoating in vitro
    • Previsani, N., S. Fontana, B. Hirt, and P. Beard. 1997. Growth of the parvovirus minute virus of mice MVMp3 in EL4 lymphocytes is restricted after cell entry and before viral DNA amplification: Cell-specific differences in virus uncoating in vitro. J. Virol. 71:7769-7780.
    • (1997) J. Virol. , vol.71 , pp. 7769-7780
    • Previsani, N.1    Fontana, S.2    Hirt, B.3    Beard, P.4
  • 46
  • 47
    • 0033799367 scopus 로고    scopus 로고
    • Endocytosis and nuclear trafficking of adeno-associated virus type 2 are controlled by Rac1 and phosphatidylinositol-3 kinase activation
    • Sanlioglu, S., P. K. Benson, J. Yang, E. M. Atkinson, T. Reynolds, and J. F. Engelhardt. 2000. Endocytosis and nuclear trafficking of adeno-associated virus type 2 are controlled by Rac1 and phosphatidylinositol-3 kinase activation. J. Virol. 74:9184-9196.
    • (2000) J. Virol. , vol.74 , pp. 9184-9196
    • Sanlioglu, S.1    Benson, P.K.2    Yang, J.3    Atkinson, E.M.4    Reynolds, T.5    Engelhardt, J.F.6
  • 48
    • 0031935031 scopus 로고    scopus 로고
    • CD4 glyprotein degradation induced by human immunodeficiency virus type 1 Vpu protein requires the function of proteasomes and the ubiquitin-conjugating pathway
    • Schubert, U., L. C. Anton, I. Bacik, J. H. Cox, S. Bour, J. R. Bennink, M. Orlowski, K. Strebel, and J. W. Yewdell. 1998. CD4 glyprotein degradation induced by human immunodeficiency virus type 1 Vpu protein requires the function of proteasomes and the ubiquitin-conjugating pathway. J. Virol. 72:2280-2288.
    • (1998) J. Virol. , vol.72 , pp. 2280-2288
    • Schubert, U.1    Anton, L.C.2    Bacik, I.3    Cox, J.H.4    Bour, S.5    Bennink, J.R.6    Orlowski, M.7    Strebel, K.8    Yewdell, J.W.9
  • 50
    • 2642670312 scopus 로고    scopus 로고
    • Antiviral activity of the proteasome on incoming human immunodeficiency virus type 1
    • Schwartz, O., V. Marechal, B. Friguet, F. Arenzana-Seisdedos, and J. M. Heard. 1998. Antiviral activity of the proteasome on incoming human immunodeficiency virus type 1. J. Virol. 72:3845-3850.
    • (1998) J. Virol. , vol.72 , pp. 3845-3850
    • Schwartz, O.1    Marechal, V.2    Friguet, B.3    Arenzana-Seisdedos, F.4    Heard, J.M.5
  • 51
    • 0034659804 scopus 로고    scopus 로고
    • The selective proteasome inhibitors lactacystin and epoxomicin can be used to either up- or down-regulate antigen presentation at nontoxic doses
    • Schwarz, K., R. de Giuli, G. Schmidtke, S. Kostka, M. van den Broek, K. B. Kim, C. M. Crews, R. Kraft, and M. Groettrup. 2000. The selective proteasome inhibitors lactacystin and epoxomicin can be used to either up- or down-regulate antigen presentation at nontoxic doses. J. Immunol. 164:6147-6157.
    • (2000) J. Immunol. , vol.164 , pp. 6147-6157
    • Schwarz, K.1    De Giuli, R.2    Schmidtke, G.3    Kostka, S.4    Van den Broek, M.5    Kim, K.B.6    Crews, C.M.7    Kraft, R.8    Groettrup, M.9
  • 52
    • 0018763480 scopus 로고
    • Inhibition of the lysosomal pathway of protein degradation in isolated rat hepatocytes by ammonia, methylamine, chloroquine and leupeptin
    • Seglen, P. O., B. Grinde, and A. E. Solheim. 1979. Inhibition of the lysosomal pathway of protein degradation in isolated rat hepatocytes by ammonia, methylamine, chloroquine and leupeptin. Eur. J. Biochem. 95:215-225.
    • (1979) Eur. J. Biochem. , vol.95 , pp. 215-225
    • Seglen, P.O.1    Grinde, B.2    Solheim, A.E.3
  • 53
    • 0035976603 scopus 로고    scopus 로고
    • Real-time single-molecule imaging of the infection pathway of an adeno-associated virus
    • Seisenberger, G., M. U. Ried, T. Endress, H. Buning, M. Hallek, and C. Brauchle. 2001. Real-time single-molecule imaging of the infection pathway of an adeno-associated virus. Science 294:1929-1932.
    • (2001) Science , vol.294 , pp. 1929-1932
    • Seisenberger, G.1    Ried, M.U.2    Endress, T.3    Buning, H.4    Hallek, M.5    Brauchle, C.6
  • 54
    • 0034307164 scopus 로고    scopus 로고
    • Mechanisms of viral transport in the cytoplasm
    • Sodeik, B. 2000. Mechanisms of viral transport in the cytoplasm. Trends Microbiol. 8:465-472.
    • (2000) Trends Microbiol. , vol.8 , pp. 465-472
    • Sodeik, B.1
  • 56
    • 0031906147 scopus 로고    scopus 로고
    • Membrane-associated heparan sulfate proteoglycan is a receptor for adeno-associated virus type 2 virions
    • Summerford, C., and R. J. Samulski. 1998. Membrane-associated heparan sulfate proteoglycan is a receptor for adeno-associated virus type 2 virions. J. Virol. 72:1438-1445.
    • (1998) J. Virol. , vol.72 , pp. 1438-1445
    • Summerford, C.1    Samulski, R.J.2
  • 57
    • 0024542678 scopus 로고
    • Direct evidence for nuclear and cytoplasmic colocalization of proteasomes (multiprotease complexes) in liver
    • Tanaka, K., A. Kumatori, K. Ii, and A. Ichihara. 1989. Direct evidence for nuclear and cytoplasmic colocalization of proteasomes (multiprotease complexes) in liver. J. Cell. Physiol. 139:34-41.
    • (1989) J. Cell. Physiol. , vol.139 , pp. 34-41
    • Tanaka, K.1    Kumatori, A.2    Ii, K.3    Ichihara, A.4
  • 58
    • 0017353812 scopus 로고
    • Sequence homology between the structural polypeptides of minute virus of mice
    • Tattersall, P., A. J. Shatkin, and D. C. Ward. 1977. Sequence homology between the structural polypeptides of minute virus of mice. J. Mol. Biol. 111:375-394.
    • (1977) J. Mol. Biol. , vol.111 , pp. 375-394
    • Tattersall, P.1    Shatkin, A.J.2    Ward, D.C.3
  • 59
    • 0020523002 scopus 로고
    • Reciprocal productive and restrictive virus-cell interactions of immunosuppressive and prototype strains of minute virus of mice
    • Tattersall, P., and J. Bratton. 1983. Reciprocal productive and restrictive virus-cell interactions of immunosuppressive and prototype strains of minute virus of mice. J. Virol. 46:944-955.
    • (1983) J. Virol. , vol.46 , pp. 944-955
    • Tattersall, P.1    Bratton, J.2
  • 60
    • 0031692540 scopus 로고    scopus 로고
    • Binding of bovine parvovirus to erythrocyte membrane sialylglyproteins
    • Thacker, T. C., and F. B. Johnson. 1998. Binding of bovine parvovirus to erythrocyte membrane sialylglyproteins. J. Gen. Virol. 79:2163-2169.
    • (1998) J. Gen. Virol. , vol.79 , pp. 2163-2169
    • Thacker, T.C.1    Johnson, F.B.2
  • 61
    • 0027070506 scopus 로고
    • The trypsin-sensitive RVER domain in the capsid proteins of minute virus of mice is required for efficient cell binding and viral infection but not for proteolytic processing in vivo
    • Tullis, G. E., L. R. Burger, and D. J. Pintel. 1992. The trypsin-sensitive RVER domain in the capsid proteins of minute virus of mice is required for efficient cell binding and viral infection but not for proteolytic processing in vivo. Virology 191:846-857.
    • (1992) Virology , vol.191 , pp. 846-857
    • Tullis, G.E.1    Burger, L.R.2    Pintel, D.J.3
  • 62
    • 0027458466 scopus 로고
    • The minor capsid protein VP1 of the autonomous parvovirus minute virus of mice is dispensable for encapsidation of progeny single-stranded DNA but is required for infectivity
    • Tullis, G. E., L. R. Burger, and D. J. Pintel. 1993. The minor capsid protein VP1 of the autonomous parvovirus minute virus of mice is dispensable for encapsidation of progeny single-stranded DNA but is required for infectivity. J. Virol. 67:131-141.
    • (1993) J. Virol. , vol.67 , pp. 131-141
    • Tullis, G.E.1    Burger, L.R.2    Pintel, D.J.3
  • 63
    • 0029160297 scopus 로고
    • Transport from late endosomes to lysosomes, but not sorting of integral membrane proteins in endosomes, depends on the vacuolar proton pump
    • van Weert, A. W., K. W. Dunn, H. J. Gueze, F. R. Maxfield, and W. Stoorvogel. 1995. Transport from late endosomes to lysosomes, but not sorting of integral membrane proteins in endosomes, depends on the vacuolar proton pump. J. Cell Biol. 130:821-834.
    • (1995) J. Cell Biol. , vol.130 , pp. 821-834
    • Van Weert, A.W.1    Dunn, K.W.2    Gueze, H.J.3    Maxfield, F.R.4    Stoorvogel, W.5
  • 64
    • 0031464535 scopus 로고    scopus 로고
    • Characterization of a nuclear localization signal of canine parvovirus capsid proteins
    • Vihinen-Ranta, M., L. Kakkola, A. Kalela, P. Vilja, and M. Vuento. 1997. Characterization of a nuclear localization signal of canine parvovirus capsid proteins. Eur. J. Biochem. 250:389-394.
    • (1997) Eur. J. Biochem. , vol.250 , pp. 389-394
    • Vihinen-Ranta, M.1    Kakkola, L.2    Kalela, A.3    Vilja, P.4    Vuento, M.5
  • 66
    • 0034000922 scopus 로고    scopus 로고
    • Cytoplasmic trafficking of the canine parvovirus capsid and its role in infection and nuclear transport
    • Vihinen-Ranta, M., W. Yuan, and C. R. Parrish. 2000. Cytoplasmic trafficking of the canine parvovirus capsid and its role in infection and nuclear transport. J. Virol. 74:4853-4859.
    • (2000) J. Virol. , vol.74 , pp. 4853-4859
    • Vihinen-Ranta, M.1    Yuan, W.2    Parrish, C.R.3
  • 67
    • 0036149891 scopus 로고    scopus 로고
    • The VP1 N-terminal sequence of canine parvovirus affects nuclear transport of capsids and efficient cell infection
    • Vihinen-Ranta, M., D. Wang, W. S. Weichert, and C. R. Parrish. 2002. The VP1 N-terminal sequence of canine parvovirus affects nuclear transport of capsids and efficient cell infection. J. Virol. 76:1884-1891.
    • (2002) J. Virol. , vol.76 , pp. 1884-1891
    • Vihinen-Ranta, M.1    Wang, D.2    Weichert, W.S.3    Parrish, C.R.4
  • 68
    • 0035827546 scopus 로고    scopus 로고
    • Binding of adeno-associated virus type 5 to 2,3-linked sialic acid is required for gene transfer
    • Walters, R. W., S. M. Yi, S. Keshavjee, K. E. Brown, M. J. Welsh, J. A. Chiorini, and J. Zabner. 2001. Binding of adeno-associated virus type 5 to 2,3-linked sialic acid is required for gene transfer. J. Biol. Chem. 276:20610-20616.
    • (2001) J. Biol. Chem. , vol.276 , pp. 20610-20616
    • Walters, R.W.1    Yi, S.M.2    Keshavjee, S.3    Brown, K.E.4    Welsh, M.J.5    Chiorini, J.A.6    Zabner, J.7
  • 69
    • 0032505630 scopus 로고    scopus 로고
    • Assaying for structural variation in the parvovirus capsid and its role in infection
    • Weichert, W. S., J. S. Parker, A. T. Wahid, S. F. Chang, E. Meier, and C. R. Parrish. 1998. Assaying for structural variation in the parvovirus capsid and its role in infection. Virology 250:106-117.
    • (1998) Virology , vol.250 , pp. 106-117
    • Weichert, W.S.1    Parker, J.S.2    Wahid, A.T.3    Chang, S.F.4    Meier, E.5    Parrish, C.R.6
  • 70
    • 0020752797 scopus 로고
    • Membrane fusion proteins of enveloped viruses
    • White, J., M. Kielian, and A. Helenius. 1983. Membrane fusion proteins of enveloped viruses. Q. Rev. Biophys. 16:151-195.
    • (1983) Q. Rev. Biophys. , vol.16 , pp. 151-195
    • White, J.1    Kielian, M.2    Helenius, A.3
  • 71
    • 0036171821 scopus 로고    scopus 로고
    • Ubiquitination of both adeno-associated virus type 2 and 5 capsid proteins affects the transduction efficiency of recombinant vectors
    • Yan, Z., R. Zak, G. W. Luxton, T. C. Ritchie, U. Bantel-Schaal, and J. F. Engelhardt. 2002. Ubiquitination of both adeno-associated virus type 2 and 5 capsid proteins affects the transduction efficiency of recombinant vectors. J. Virol. 76:2043-2053.
    • (2002) J. Virol. , vol.76 , pp. 2043-2053
    • Yan, Z.1    Zak, R.2    Luxton, G.W.3    Ritchie, T.C.4    Bantel-Schaal, U.5    Engelhardt, J.F.6


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