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Volumn 78, Issue 6, 2004, Pages 2657-2665

Budding of PPxY-Containing Rhabdoviruses Is Not Dependent on Host Proteins TGS101 and VPS4A

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; PROTEIN; PROTEIN PPXY; PROTEIN TGS101; PROTEIN VPS4A; UBIQUITIN PROTEIN LIGASE NEDD4; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 1542377646     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/JVI.78.6.2657-2665.2004     Document Type: Article
Times cited : (98)

References (60)
  • 1
    • 0032101334 scopus 로고    scopus 로고
    • The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function
    • Babst, M., B. Wendland, E. J. Estepa, and S. D. Emr. 1998. The Vps4p AAA ATPase regulates membrane association of a Vps protein complex required for normal endosome function. EMBO J. 17:2982-2993.
    • (1998) EMBO J. , vol.17 , pp. 2982-2993
    • Babst, M.1    Wendland, B.2    Estepa, E.J.3    Emr, S.D.4
  • 2
    • 0036696804 scopus 로고    scopus 로고
    • Escrt-III: An endosome-associated heterooligomeric protein complex required for mvb sorting
    • Babst, M., D. J. Katzmann, E. J. Estepa-Sabal, T. Meerloo, and S. D. Emr. 2002. Escrt-III: an endosome-associated heterooligomeric protein complex required for mvb sorting. Dev. Cell 3:271-282.
    • (2002) Dev. Cell , vol.3 , pp. 271-282
    • Babst, M.1    Katzmann, D.J.2    Estepa-Sabal, E.J.3    Meerloo, T.4    Emr, S.D.5
  • 3
    • 0036697166 scopus 로고    scopus 로고
    • Endosome-associated complex. ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body
    • Babst, M., D. J. Katzmann, W. B. Snyder, B. Wendland, and S. D. Emr. 2002. Endosome-associated complex, ESCRT-II, recruits transport machinery for protein sorting at the multivesicular body. Dev. Cell 3:283-289.
    • (2002) Dev. Cell , vol.3 , pp. 283-289
    • Babst, M.1    Katzmann, D.J.2    Snyder, W.B.3    Wendland, B.4    Emr, S.D.5
  • 4
    • 0034157875 scopus 로고    scopus 로고
    • Mammalian tumor susceptibility gene 101 (TSG101) and the yeast homologue, Vps23p, both function in late endosomal trafficking
    • Babst, M., G. Odorizzi, E. J. Estepa, and S. D. Emr. 2000. Mammalian tumor susceptibility gene 101 (TSG101) and the yeast homologue, Vps23p, both function in late endosomal trafficking. Traffic 1:248-258.
    • (2000) Traffic , vol.1 , pp. 248-258
    • Babst, M.1    Odorizzi, G.2    Estepa, E.J.3    Emr, S.D.4
  • 5
    • 0030891524 scopus 로고    scopus 로고
    • Endosomal transport function in yeast requires a novel AAA-type ATPase, Vps4p
    • Babst, M., T. K. Sato, L. M. Banta, and S. D. Emr. 1997. Endosomal transport function in yeast requires a novel AAA-type ATPase, Vps4p. EMBO J. 16:1820-1831.
    • (1997) EMBO J. , vol.16 , pp. 1820-1831
    • Babst, M.1    Sato, T.K.2    Banta, L.M.3    Emr, S.D.4
  • 7
    • 0035853688 scopus 로고    scopus 로고
    • TSG101/mammalian VPS23 and mammalian VPS28 interact directly and are recruited to VPS4-induced endosomes
    • Bishop, N., and P. Woodman. 2000. TSG101/mammalian VPS23 and mammalian VPS28 interact directly and are recruited to VPS4-induced endosomes. J. Biol. Chem. 276:11735-11742.
    • (2000) J. Biol. Chem. , vol.276 , pp. 11735-11742
    • Bishop, N.1    Woodman, P.2
  • 8
    • 0037377710 scopus 로고    scopus 로고
    • Organization of the vesicular stomatitis virus glycoprotein into membrane microdomains occurs independently of intracellular viral components
    • Brown, E. L., and D. S. Lyles. 2003. Organization of the vesicular stomatitis virus glycoprotein into membrane microdomains occurs independently of intracellular viral components. J. Virol. 77:3985-3992.
    • (2003) J. Virol. , vol.77 , pp. 3985-3992
    • Brown, E.L.1    Lyles, D.S.2
  • 9
    • 0036672208 scopus 로고    scopus 로고
    • An ESCRT into the endosome
    • Conibear, E. 2002. An ESCRT into the endosome. Mol. Cell 10:215-216.
    • (2002) Mol. Cell , vol.10 , pp. 215-216
    • Conibear, E.1
  • 10
    • 0033050343 scopus 로고    scopus 로고
    • Late domain function identified in the vesicular stomatitis virus M protein by use of rhabdovirus-retrovirus chimeras
    • Craven, R. C., R. N. Harty, J. Paragas, P. Palese, and J. W. Wills. 1999. Late domain function identified in the vesicular stomatitis virus M protein by use of rhabdovirus-retrovirus chimeras. J. Virol. 73:3359-3365.
    • (1999) J. Virol. , vol.73 , pp. 3359-3365
    • Craven, R.C.1    Harty, R.N.2    Paragas, J.3    Palese, P.4    Wills, J.W.5
  • 11
    • 0036133283 scopus 로고    scopus 로고
    • The late domain of human immunodeficiency virus type 1 p6 promotes virus release in a cell type-dependent manner
    • Demirov, D. G., J. M. Orenstein, and E. O. Freed. 2002. The late domain of human immunodeficiency virus type 1 p6 promotes virus release in a cell type-dependent manner. J. Virol. 76:105-117.
    • (2002) J. Virol. , vol.76 , pp. 105-117
    • Demirov, D.G.1    Orenstein, J.M.2    Freed, E.O.3
  • 12
    • 0036239363 scopus 로고    scopus 로고
    • Viral late domains
    • Freed, E. O. 2002. Viral late domains. J. Virol. 76:4679-4687.
    • (2002) J. Virol. , vol.76 , pp. 4679-4687
    • Freed, E.O.1
  • 14
    • 0037688240 scopus 로고    scopus 로고
    • Defects in human immunodeficiency virus budding and endosomal sorting induced by TSG101 overexpression
    • Goila-Gaur, R., D. G. Demirov, J. M. Orenstein, A. Ono, and E. O. Freed. 2003. Defects in human immunodeficiency virus budding and endosomal sorting induced by TSG101 overexpression. J. Virol. 77:6507-6519.
    • (2003) J. Virol. , vol.77 , pp. 6507-6519
    • Goila-Gaur, R.1    Demirov, D.G.2    Orenstein, J.M.3    Ono, A.4    Freed, E.O.5
  • 15
    • 0042389562 scopus 로고    scopus 로고
    • The Mason-Pfizer monkey virus PPPY and PSAP motifs both contribute to virus release
    • Gottwein, E., J. Bodem, B. Muller, A. Schmechel, H. Zentgraf, and H. G. Krausslich. 2003. The Mason-Pfizer monkey virus PPPY and PSAP motifs both contribute to virus release. J. Virol. 77:9474-9485.
    • (2003) J. Virol. , vol.77 , pp. 9474-9485
    • Gottwein, E.1    Bodem, J.2    Muller, B.3    Schmechel, A.4    Zentgraf, H.5    Krausslich, H.G.6
  • 16
    • 0033050750 scopus 로고    scopus 로고
    • A proline-rich motif within the matrix protein of vesicular stomatitis virus and rabies virus interacts with WW domains of cellular proteins: Implications for viral budding
    • Harty, R. N., J. Paragas, M. Sudol, and P. Palese. 1999. A proline-rich motif within the matrix protein of vesicular stomatitis virus and rabies virus interacts with WW domains of cellular proteins: implications for viral budding. J. Virol. 73:2921-2929.
    • (1999) J. Virol. , vol.73 , pp. 2921-2929
    • Harty, R.N.1    Paragas, J.2    Sudol, M.3    Palese, P.4
  • 17
    • 0034610295 scopus 로고    scopus 로고
    • A PPxY motif within the VP40 protein of Ebola virus interacts physically and functionally with a ubiquitin ligase: Implication for filovirus budding
    • Harty, R. N., M. E. Brown, G. Wang, J. Huibregtse, and F. P. Hayes. 2000. A PPxY motif within the VP40 protein of Ebola virus interacts physically and functionally with a ubiquitin ligase: implication for filovirus budding. Proc. Natl. Acad. Sci. USA 97:13871-13876.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13871-13876
    • Harty, R.N.1    Brown, M.E.2    Wang, G.3    Huibregtse, J.4    Hayes, F.P.5
  • 19
    • 0028971135 scopus 로고
    • p6Gag is required for particle production from full-length human immunodeficiency virus type 1 molecular clones expression protease
    • Huang, M., J. M. Orenstein, M. A. Martin, and E. O. Freed. 1995. p6Gag is required for particle production from full-length human immunodeficiency virus type 1 molecular clones expression protease. J. Virol. 69:6810-6818.
    • (1995) J. Virol. , vol.69 , pp. 6810-6818
    • Huang, M.1    Orenstein, J.M.2    Martin, M.A.3    Freed, E.O.4
  • 20
    • 0038618682 scopus 로고    scopus 로고
    • Basic residues of the helix six domain of influenza virus M1 involved in nuclear translocation of M1 can be replaced by PTAP and YPDL late assembly domain motif
    • Hui, E. K., S. Barman, T. Y. Yang, and D. P. Nayak. 2003. Basic residues of the helix six domain of influenza virus M1 involved in nuclear translocation of M1 can be replaced by PTAP and YPDL late assembly domain motif. J. Virol. 77:7078-7092.
    • (2003) J. Virol. , vol.77 , pp. 7078-7092
    • Hui, E.K.1    Barman, S.2    Yang, T.Y.3    Nayak, D.P.4
  • 21
    • 0035031534 scopus 로고    scopus 로고
    • Ebola virus VP40-induced particle formation and association with the lipid bilayer
    • Jasenosky, L. D., G. Neumann, I. Lukashevich, and Y. Kawaoka. 2001. Ebola virus VP40-induced particle formation and association with the lipid bilayer. J. Virol. 75:5205-5214.
    • (2001) J. Virol. , vol.75 , pp. 5205-5214
    • Jasenosky, L.D.1    Neumann, G.2    Lukashevich, I.3    Kawaoka, Y.4
  • 22
    • 0033775605 scopus 로고    scopus 로고
    • Mutations in the PPPY motif of vesicular stomatitis virus matrix protein reduce virus budding by inhibiting a late step in virion release
    • Jayakar, H. R., K. G. Murti, and M. A. Whitt. 2000. Mutations in the PPPY motif of vesicular stomatitis virus matrix protein reduce virus budding by inhibiting a late step in virion release. J. Virol. 74:9818-9827.
    • (2000) J. Virol. , vol.74 , pp. 9818-9827
    • Jayakar, H.R.1    Murti, K.G.2    Whitt, M.A.3
  • 23
    • 0028987484 scopus 로고
    • Membrane vesiculation function and exocytosis of wild-type and mutant matrix proteins of vesicular stomatitis virus
    • Justice, P. A., W. Sun, Y. Li, Z. Ye, P. R. Grigera, and R. R. Wagner. 1995. Membrane vesiculation function and exocytosis of wild-type and mutant matrix proteins of vesicular stomatitis virus. J. Virol. 69:3156-3160.
    • (1995) J. Virol. , vol.69 , pp. 3156-3160
    • Justice, P.A.1    Sun, W.2    Li, Y.3    Ye, Z.4    Grigera, P.R.5    Wagner, R.R.6
  • 24
    • 0035958546 scopus 로고    scopus 로고
    • Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I
    • Katzmann, D. J., M. Babst, and S. D. Emr. 2001. Ubiquitin-dependent sorting into the multivesicular body pathway requires the function of a conserved endosomal protein sorting complex, ESCRT-I. Cell 106:145-155.
    • (2001) Cell , vol.106 , pp. 145-155
    • Katzmann, D.J.1    Babst, M.2    Emr, S.D.3
  • 25
    • 0035949489 scopus 로고    scopus 로고
    • Proteins related to the Nedd4 family of ubiquitin protein ligases interact with the L domain of Rous sarcoma virus and are required for gag budding from cells
    • Kikonyogo, A., F. Bouamr, M. L. Vana, Y. Xiang, A. Aiyar, C. Carter, and J. Leis. 2001. Proteins related to the Nedd4 family of ubiquitin protein ligases interact with the L domain of Rous sarcoma virus and are required for gag budding from cells. Proc. Natl. Acad. Sci. USA 98:11199-11204.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11199-11204
    • Kikonyogo, A.1    Bouamr, F.2    Vana, M.L.3    Xiang, Y.4    Aiyar, A.5    Carter, C.6    Leis, J.7
  • 26
    • 0036776607 scopus 로고    scopus 로고
    • The PPPY motif of human T-cell leukemia virus type 1 Gag protein is required early in the budding process
    • Le Blanc, I., M. C. Prevost, M. C. Dokhelar, and A. R. Rosenberg. 2002. The PPPY motif of human T-cell leukemia virus type 1 Gag protein is required early in the budding process. J. Virol. 76:10024-10029.
    • (2002) J. Virol. , vol.76 , pp. 10024-10029
    • Le Blanc, I.1    Prevost, M.C.2    Dokhelar, M.C.3    Rosenberg, A.R.4
  • 27
    • 0036148338 scopus 로고    scopus 로고
    • Functional replacement and positional dependence of homologous and heterologous L domains in equine infectious anemia virus replication
    • Li, F., C. Chen, B. A. Puffer, and R. C. Montelaro. 2002. Functional replacement and positional dependence of homologous and heterologous L domains in equine infectious anemia virus replication. J. Virol. 76:1569-1577.
    • (2002) J. Virol. , vol.76 , pp. 1569-1577
    • Li, F.1    Chen, C.2    Puffer, B.A.3    Montelaro, R.C.4
  • 28
    • 0027299296 scopus 로고
    • Viral liposomes released from insect cells infected with recombinant baculovirus expressing the matrix protein of vesicular stomatitis virus
    • Li, Y., L. Luo, M. Schubert, R. R. Wagner, and C. Y. Kang. 1993. Viral liposomes released from insect cells infected with recombinant baculovirus expressing the matrix protein of vesicular stomatitis virus. J. Virol. 67:4415-4420.
    • (1993) J. Virol. , vol.67 , pp. 4415-4420
    • Li, Y.1    Luo, L.2    Schubert, M.3    Wagner, R.R.4    Kang, C.Y.5
  • 29
    • 0037303193 scopus 로고    scopus 로고
    • Overlapping motifs (PTAP and PPEY) within the Ebola virus VP40 protein function independently as late budding domains: Involvement of host proteins TSG101 and VPS-4
    • Licata J. M., M. Simpson-Holley, N. T. Wright, Z. Han, J. Paragas, and R. N. Harty. 2003. Overlapping motifs (PTAP and PPEY) within the Ebola virus VP40 protein function independently as late budding domains: involvement of host proteins TSG101 and VPS-4. J. Virol. 77:1812-1819.
    • (2003) J. Virol. , vol.77 , pp. 1812-1819
    • Licata, J.M.1    Simpson-Holley, M.2    Wright, N.T.3    Han, Z.4    Paragas, J.5    Harty, R.N.6
  • 30
    • 0142123069 scopus 로고    scopus 로고
    • Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor protein
    • a. Martin-Serrano, J., A. Yaravoy, D. Perez-Caballero, and P. D. Bieniasz. 2003. Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor protein. Proc. Natl. Acad. Sci. USA 100:12414-12419.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 12414-12419
    • Martin-Serrano, J.1    Yaravoy, A.2    Perez-Caballero, D.3    Bieniasz, P.D.4
  • 31
    • 0035658023 scopus 로고    scopus 로고
    • HIV-1 and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress
    • Martin-Serrano, J., T. Zang, and P. D. Bieniasz. 2001. HIV-1 and Ebola virus encode small peptide motifs that recruit Tsg101 to sites of particle assembly to facilitate egress. Nat. Med. 7:1313-1319.
    • (2001) Nat. Med. , vol.7 , pp. 1313-1319
    • Martin-Serrano, J.1    Zang, T.2    Bieniasz, P.D.3
  • 32
    • 0037383128 scopus 로고    scopus 로고
    • Role of ESCRT-I in retroviral budding
    • Martin-Serrano, J., T. Zang, and P. D. Bieniasz. 2003. Role of ESCRT-I in retroviral budding. J. Virol. 77:4794-4804.
    • (2003) J. Virol. , vol.77 , pp. 4794-4804
    • Martin-Serrano, J.1    Zang, T.2    Bieniasz, P.D.3
  • 33
    • 0034881154 scopus 로고    scopus 로고
    • Expression and immunogenicity of human immunodeficiency virus type 1 Gag expressed by a replication-competent rhabdovirus-based vaccine vector
    • McGettigan, J. P., S. Sarma, J. M. Orenstein, R. J. Pomerantz, and M. J. Schnell. 2001. Expression and immunogenicity of human immunodeficiency virus type 1 Gag expressed by a replication-competent rhabdovirus-based vaccine vector. J. Virol. 75:8724-8732.
    • (2001) J. Virol. , vol.75 , pp. 8724-8732
    • McGettigan, J.P.1    Sarma, S.2    Orenstein, J.M.3    Pomerantz, R.J.4    Schnell, M.J.5
  • 34
    • 0034015604 scopus 로고    scopus 로고
    • Evidence for budding of human immunodeficiency virus type 1 selectively from glycolipid-enriched membrane lipid rafts
    • Nguyen, D. H., and J. E. Hildreth. 2000. Evidence for budding of human immunodeficiency virus type 1 selectively from glycolipid-enriched membrane lipid rafts. J. Virol. 74:3264-3272.
    • (2000) J. Virol. , vol.74 , pp. 3264-3272
    • Nguyen, D.H.1    Hildreth, J.E.2
  • 37
    • 0037334391 scopus 로고    scopus 로고
    • Retroviruses have differing requirements for proteasome function in the budding process
    • Ott, D. E., L. V. Coren, R. C. Sowder, Jr., J. Adams, and U. Schubert. 2003. Retroviruses have differing requirements for proteasome function in the budding process. J. Virol. 77:3384-3393.
    • (2003) J. Virol. , vol.77 , pp. 3384-3393
    • Ott, D.E.1    Coren, L.V.2    Sowder Jr., R.C.3    Adams, J.4    Schubert, U.5
  • 38
    • 0031900144 scopus 로고    scopus 로고
    • Ubiquitin is covalently attached to the p6Gag proteins of human immunodeficiency virus type 1 and simian immunodeficiency virus and to the p12Gag protein of Moloney murine leukemia virus
    • Ott, D. E., L. V. Coren, T. D. Copeland, B. P. Kane, D. G. Johnson, R. C. Sowder, Jr., Y. Yoshinaka, S. Oroszlan, L. O. Arthur, and L. E. Henderson. 1998. Ubiquitin is covalently attached to the p6Gag proteins of human immunodeficiency virus type 1 and simian immunodeficiency virus and to the p12Gag protein of Moloney murine leukemia virus. J. Virol. 72:2962-2968.
    • (1998) J. Virol. , vol.72 , pp. 2962-2968
    • Ott, D.E.1    Coren, L.V.2    Copeland, T.D.3    Kane, B.P.4    Johnson, D.G.5    Sowder Jr., R.C.6    Yoshinaka, Y.7    Oroszlan, S.8    Arthur, L.O.9    Henderson, L.E.10
  • 39
    • 0034700146 scopus 로고    scopus 로고
    • Ubiquitin is part of the retrovirus budding machinery
    • Patnaik, A., V. Chau, and J. W. Wills. 2000. Ubiquitin is part of the retrovirus budding machinery. Proc. Natl. Acad. Sci. USA 97:13069-13074.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13069-13074
    • Patnaik, A.1    Chau, V.2    Wills, J.W.3
  • 40
    • 0036829172 scopus 로고    scopus 로고
    • Structure of the Tsg101 UEV domain in complex with the PTAP motif of the HIV-1 p6 protein
    • Pornillos, O., S. L. Alam, D. R. Davis, and W. I. Sundquist. 2002. Structure of the Tsg101 UEV domain in complex with the PTAP motif of the HIV-1 p6 protein. Nat. Struct. Biol. 9:812-817.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 812-817
    • Pornillos, O.1    Alam, S.L.2    Davis, D.R.3    Sundquist, W.I.4
  • 41
    • 0030858622 scopus 로고    scopus 로고
    • Equine infectious anemia virus utilizes a YXXL motif within the late assembly domain of the Gag p9 protein
    • Puffer, B. A., L. J. Parent, J. W. Wills, and R. C. Montelaro. 1997. Equine infectious anemia virus utilizes a YXXL motif within the late assembly domain of the Gag p9 protein. J. Virol. 71:6541-6546
    • (1997) J. Virol. , vol.71 , pp. 6541-6546
    • Puffer, B.A.1    Parent, L.J.2    Wills, J.W.3    Montelaro, R.C.4
  • 42
    • 0031797730 scopus 로고    scopus 로고
    • Equine infectious anemia virus Gag polyprotein late domain specifically recruits cellular AP-2 adapter protein complexes during virion assembly
    • Puffer, B. A., S. C. Watkins, and R. C. Montelaro. 1998. Equine infectious anemia virus Gag polyprotein late domain specifically recruits cellular AP-2 adapter protein complexes during virion assembly. J. Virol. 72:10218-10221.
    • (1998) J. Virol. , vol.72 , pp. 10218-10221
    • Puffer, B.A.1    Watkins, S.C.2    Montelaro, R.C.3
  • 44
    • 0031720833 scopus 로고    scopus 로고
    • Molecular events in the assembly of retrovirus particles
    • Sakalian, M., and E. Hunter. 1998. Molecular events in the assembly of retrovirus particles. Adv. Exp. Med. Biol. 440:329-339.
    • (1998) Adv. Exp. Med. Biol. , vol.440 , pp. 329-339
    • Sakalian, M.1    Hunter, E.2
  • 45
    • 0033593321 scopus 로고    scopus 로고
    • Influenza viruses select ordered lipid domains during budding from the plasma membrane
    • Scheiffele, P., A. Rietveld, T. Wilk, and K. Simons. 1999. Influenza viruses select ordered lipid domains during budding from the plasma membrane. J. Biol. Chem. 274:2038-2044.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2038-2044
    • Scheiffele, P.1    Rietveld, A.2    Wilk, T.3    Simons, K.4
  • 49
    • 0141844660 scopus 로고    scopus 로고
    • AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding
    • a. Strack, B., A. Calistri, S. Craig, E. Popova, and H. G. Gottlinger. 2003. AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding. Cell 114:689-699.
    • (2003) Cell , vol.114 , pp. 689-699
    • Strack, B.1    Calistri, A.2    Craig, S.3    Popova, E.4    Gottlinger, H.G.5
  • 51
    • 0037770225 scopus 로고    scopus 로고
    • Equine infectious anemia virus utilizes host vesicular protein sorting machinery during particle release
    • Tanzi, G. O., A. J. Piefer, and P. Bates. 2003. Equine infectious anemia virus utilizes host vesicular protein sorting machinery during particle release. J. Virol. 77:8440-8447.
    • (2003) J. Virol. , vol.77 , pp. 8440-8447
    • Tanzi, G.O.1    Piefer, A.J.2    Bates, P.3
  • 57
    • 0036023945 scopus 로고    scopus 로고
    • Functional involvement of a novel Nedd4-like ubiquitin Iigase on retrovirus budding
    • Yasuda, J., E. Hunter, M. Nakao, and H. Shida. 2002. Functional involvement of a novel Nedd4-like ubiquitin Iigase on retrovirus budding. EMBO Rep. 3:636-640.
    • (2002) EMBO Rep. , vol.3 , pp. 636-640
    • Yasuda, J.1    Hunter, E.2    Nakao, M.3    Shida, H.4
  • 58
    • 0141570508 scopus 로고    scopus 로고
    • Nedd4 regulates egress of Ebola virus-like particles from host cells
    • Yasuda, J., M. Nakao, Y. Kawaoka, and H. Shida. 2003. Nedd4 regulates egress of Ebola virus-like particles from host cells. J. Virol. 77:9987-9992.
    • (2003) J. Virol. , vol.77 , pp. 9987-9992
    • Yasuda, J.1    Nakao, M.2    Kawaoka, Y.3    Shida, H.4
  • 59
    • 0033854158 scopus 로고    scopus 로고
    • Infectivity of Moloney murine leukemia virus defective in late assembly events is restored by late assembly domains of other retroviruses
    • Yuan, B., S. Campbell, E. Bacharach, A. Rein, and S. P. Goff. 2000. Infectivity of Moloney murine leukemia virus defective in late assembly events is restored by late assembly domains of other retroviruses. J. Virol. 74:7250-7260.
    • (2000) J. Virol. , vol.74 , pp. 7250-7260
    • Yuan, B.1    Campbell, S.2    Bacharach, E.3    Rein, A.4    Goff, S.P.5
  • 60
    • 0344035661 scopus 로고    scopus 로고
    • Mutations altering the Moloney murine leukemia virus p12 Gag protein affect virion production and early events of the virus life cycle
    • Yuan, B., X. Li, and S. P. Goff. 1999. Mutations altering the Moloney murine leukemia virus p12 Gag protein affect virion production and early events of the virus life cycle. EMBO J. 18:4700-4710.
    • (1999) EMBO J. , vol.18 , pp. 4700-4710
    • Yuan, B.1    Li, X.2    Goff, S.P.3


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