메뉴 건너뛰기




Volumn 106, Issue 2 SPEC.ISS., 2004, Pages 103-116

Budding of alphaviruses

Author keywords

Alphaviruses; Glycoprotein; T = 4 icosahedral symmetry

Indexed keywords

COAT PROTEIN; GAG PROTEIN; GLYCOPROTEIN; LEUCINE; STRUCTURAL PROTEIN; TYROSINE; VIRUS PROTEIN; VIRUS RNA;

EID: 9644260512     PISSN: 01681702     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.virusres.2004.08.008     Document Type: Article
Times cited : (79)

References (120)
  • 1
    • 0014089129 scopus 로고
    • Replication of Semliki Forest virus: An electron microscopic study
    • N.H. Acheson, and I. Tamm Replication of Semliki Forest virus: an electron microscopic study Virology 32 1967 128 143
    • (1967) Virology , vol.32 , pp. 128-143
    • Acheson, N.H.1    Tamm, I.2
  • 2
    • 0018126813 scopus 로고
    • Evidence for an autoprotease activity of Sindbis virus capsid protein
    • G. Aliperti, and M.J. Schlesinger Evidence for an autoprotease activity of Sindbis virus capsid protein Virology 90 1978 366 369
    • (1978) Virology , vol.90 , pp. 366-369
    • Aliperti, G.1    Schlesinger, M.J.2
  • 3
    • 0035823046 scopus 로고    scopus 로고
    • Inhibition of the membrane fusion machinery prevents exit from the TGN and proteolytic processing by furin
    • A.M. Band, J. Maatta, L. Kaariainen, and E. Kuismanen Inhibition of the membrane fusion machinery prevents exit from the TGN and proteolytic processing by furin FEBS Lett. 505 2001 118 124
    • (2001) FEBS Lett. , vol.505 , pp. 118-124
    • Band, A.M.1    Maatta, J.2    Kaariainen, L.3    Kuismanen, E.4
  • 4
    • 0026476307 scopus 로고
    • Alphavirus assembly and entry: Role of the cytoplasmic tail of the E1 spike subunit
    • B.U. Barth, M. Suomalainen, P. Liljestrom, and H. Garoff Alphavirus assembly and entry: role of the cytoplasmic tail of the E1 spike subunit J. Virol. 66 1992 7560 7564
    • (1992) J. Virol. , vol.66 , pp. 7560-7564
    • Barth, B.U.1    Suomalainen, M.2    Liljestrom, P.3    Garoff, H.4
  • 5
    • 0028912679 scopus 로고
    • The oligomerization reaction of the Semliki Forest virus membrane protein subunits
    • B.U. Barth, J.M. Wahlberg, and H. Garoff The oligomerization reaction of the Semliki Forest virus membrane protein subunits J. Cell Biol. 128 1995 283 291
    • (1995) J. Cell Biol. , vol.128 , pp. 283-291
    • Barth, B.U.1    Wahlberg, J.M.2    Garoff, H.3
  • 6
    • 0038009933 scopus 로고    scopus 로고
    • Retroviral genomic RNAs are transported to the plasma membrane by endosomal vesicles
    • E. Basyuk, T. Galli, M. Mougel, J.M. Blanchard, M. Sitbon, and E. Bertrand Retroviral genomic RNAs are transported to the plasma membrane by endosomal vesicles Dev. Cell. 5 2003 161 174
    • (2003) Dev. Cell. , vol.5 , pp. 161-174
    • Basyuk, E.1    Galli, T.2    Mougel, M.3    Blanchard, J.M.4    Sitbon, M.5    Bertrand, E.6
  • 7
    • 0015776481 scopus 로고
    • Replication of Sindbis virus. 3. An electron microscopic study of virus maturation using the surface replica technique
    • C.R. Birdwell, E.G. Strauss, and J.H. Strauss Replication of Sindbis virus. 3. An electron microscopic study of virus maturation using the surface replica technique Virology 56 1973 420 438
    • (1973) Virology , vol.56 , pp. 420-438
    • Birdwell, C.R.1    Strauss, E.G.2    Strauss, J.H.3
  • 12
    • 0026419333 scopus 로고
    • Structure of Sindbis virus core protein reveals a chymotrypsin-like serine proteinase and the organization of the virion
    • H.K. Choi, L. Tong, W. Minor, P. Dumas, U. Boege, M.G. Rossmann, and G. Wengler Structure of Sindbis virus core protein reveals a chymotrypsin-like serine proteinase and the organization of the virion Nature 354 1991 37 43
    • (1991) Nature , vol.354 , pp. 37-43
    • Choi, H.K.1    Tong, L.2    Minor, W.3    Dumas, P.4    Boege, U.5    Rossmann, M.G.6    Wengler, G.7
  • 13
    • 0023775458 scopus 로고
    • Dissection of Semliki Forest virus glycoprotein delivery from the trans-Golgi network to the cell surface in permeabilized BHK cells
    • I. de Curtis, and K. Simons Dissection of Semliki Forest virus glycoprotein delivery from the trans-Golgi network to the cell surface in permeabilized BHK cells Proc. Natl. Acad. Sci. U.S.A. 85 1988 8052 8056
    • (1988) Proc. Natl. Acad. Sci. U.S.A. , vol.85 , pp. 8052-8056
    • De Curtis, I.1    Simons, K.2
  • 14
    • 0028935439 scopus 로고
    • Mutations in the putative fusion peptide of Semliki Forest virus affect spike protein oligomerization and virus assembly
    • W.A. Duffus, P. Levy-Mintz, M.R. Klimjack, and M. Kielian Mutations in the putative fusion peptide of Semliki Forest virus affect spike protein oligomerization and virus assembly J. Virol. 69 1995 2471 2479
    • (1995) J. Virol. , vol.69 , pp. 2471-2479
    • Duffus, W.A.1    Levy-Mintz, P.2    Klimjack, M.R.3    Kielian, M.4
  • 15
    • 0022481884 scopus 로고
    • Sequence analysis of the E2 gene of a hyperglycosylated, host restricted mutant of Sindbis virus and estimation of mutation rate from frequency of revertants
    • R.K. Durbin, and V. Stollar Sequence analysis of the E2 gene of a hyperglycosylated, host restricted mutant of Sindbis virus and estimation of mutation rate from frequency of revertants Virology 154 1986 135 143
    • (1986) Virology , vol.154 , pp. 135-143
    • Durbin, R.K.1    Stollar, V.2
  • 16
    • 0028293943 scopus 로고
    • Membrane protein lateral interactions control Semliki Forest virus budding
    • M. Ekstrom, P. Liljestrom, and H. Garoff Membrane protein lateral interactions control Semliki Forest virus budding EMBO J. 13 1994 1058 1064
    • (1994) EMBO J. , vol.13 , pp. 1058-1064
    • Ekstrom, M.1    Liljestrom, P.2    Garoff, H.3
  • 17
    • 0029823070 scopus 로고    scopus 로고
    • Preformed cytoplasmic nucleocapsids are not necessary for alphavirus budding
    • K. Forsell, G. Griffiths, and H. Garoff Preformed cytoplasmic nucleocapsids are not necessary for alphavirus budding EMBO J. 15 1996 6495 6505
    • (1996) EMBO J. , vol.15 , pp. 6495-6505
    • Forsell, K.1    Griffiths, G.2    Garoff, H.3
  • 19
    • 0030941093 scopus 로고    scopus 로고
    • Sindbis virus replicons and Sindbis virus: Assembly of chimeras and of particles deficient in virus RNA
    • I. Frolov, E. Frolova, and S. Schlesinger Sindbis virus replicons and Sindbis virus: assembly of chimeras and of particles deficient in virus RNA J. Virol. 71 1997 2819 2829
    • (1997) J. Virol. , vol.71 , pp. 2819-2829
    • Frolov, I.1    Frolova, E.2    Schlesinger, S.3
  • 20
    • 0028171032 scopus 로고
    • Translation of Sindbis virus mRNA: Effects of sequences downstream of the initiating codon
    • I. Frolov, and S. Schlesinger Translation of Sindbis virus mRNA: effects of sequences downstream of the initiating codon J. Virol. 68 1994 8111 8117
    • (1994) J. Virol. , vol.68 , pp. 8111-8117
    • Frolov, I.1    Schlesinger, S.2
  • 21
    • 0030068269 scopus 로고    scopus 로고
    • Translation of Sindbis virus mRNA: Analysis of sequences downstream of the initiating AUG codon that enhance translation
    • I. Frolov, and S. Schlesinger Translation of Sindbis virus mRNA: analysis of sequences downstream of the initiating AUG codon that enhance translation J. Virol. 70 1996 1182 1190
    • (1996) J. Virol. , vol.70 , pp. 1182-1190
    • Frolov, I.1    Schlesinger, S.2
  • 23
    • 0024237292 scopus 로고
    • Alphavirus RNA replicase is located on the cytoplasmic surface of endosomes and lysosomes
    • S. Froshauer, J. Kartenbeck, and A. Helenius Alphavirus RNA replicase is located on the cytoplasmic surface of endosomes and lysosomes J. Cell Biol. 107 1988 2075 2086
    • (1988) J. Cell Biol. , vol.107 , pp. 2075-2086
    • Froshauer, S.1    Kartenbeck, J.2    Helenius, A.3
  • 24
    • 0029052283 scopus 로고
    • Low pH induces swiveling of the glycoprotein heterodimers in the Semliki Forest virus spike complex
    • S.D. Fuller, J.A. Berriman, S.J. Butcher, and B.E. Gowen Low pH induces swiveling of the glycoprotein heterodimers in the Semliki Forest virus spike complex Cell 81 1995 715 725
    • (1995) Cell , vol.81 , pp. 715-725
    • Fuller, S.D.1    Berriman, J.A.2    Butcher, S.J.3    Gowen, B.E.4
  • 25
    • 0025373966 scopus 로고
    • Site-directed mutations in the Sindbis virus 6 K protein reveal sites for fatty acylation and the underacylated protein affects virus release and virion structure
    • K. Gaedigk-Nitschko, M.X. Ding, M.A. Levy, and M.J. Schlesinger Site-directed mutations in the Sindbis virus 6 K protein reveal sites for fatty acylation and the underacylated protein affects virus release and virion structure Virology 175 1990 282 291
    • (1990) Virology , vol.175 , pp. 282-291
    • Gaedigk-Nitschko, K.1    Ding, M.X.2    Levy, M.A.3    Schlesinger, M.J.4
  • 26
    • 0025364097 scopus 로고
    • The Sindbis virus 6K protein can be detected in virions and is acylated with fatty acids
    • K. Gaedigk-Nitschko, and M.J. Schlesinger The Sindbis virus 6K protein can be detected in virions and is acylated with fatty acids Virology 175 1990 274 281
    • (1990) Virology , vol.175 , pp. 274-281
    • Gaedigk-Nitschko, K.1    Schlesinger, M.J.2
  • 27
    • 0035449085 scopus 로고    scopus 로고
    • The missing link between envelope formation and fusion in alphaviruses
    • H. Garoff, and R.H. Cheng The missing link between envelope formation and fusion in alphaviruses Trends Microbiol. 9 2001 408 410
    • (2001) Trends Microbiol. , vol.9 , pp. 408-410
    • Garoff, H.1    Cheng, R.H.2
  • 28
    • 0019157110 scopus 로고
    • The capsid protein of Semliki Forest virus has clusters of basic amino acids and prolines in its amino-terminal region
    • H. Garoff, A.M. Frischauf, K. Simons, H. Lehrach, and H. Delius The capsid protein of Semliki Forest virus has clusters of basic amino acids and prolines in its amino-terminal region Proc. Natl. Acad. Sci. U.S.A. 77 1980 6376 6380
    • (1980) Proc. Natl. Acad. Sci. U.S.A. , vol.77 , pp. 6376-6380
    • Garoff, H.1    Frischauf, A.M.2    Simons, K.3    Lehrach, H.4    Delius, H.5
  • 29
    • 0019300295 scopus 로고
    • Nucleotide sequence of cDNA coding for Semliki Forest virus membrane glycoproteins
    • H. Garoff, A.M. Frischauf, K. Simons, H. Lehrach, and H. Delius Nucleotide sequence of cDNA coding for Semliki Forest virus membrane glycoproteins Nature 288 1980 236 241
    • (1980) Nature , vol.288 , pp. 236-241
    • Garoff, H.1    Frischauf, A.M.2    Simons, K.3    Lehrach, H.4    Delius, H.5
  • 31
    • 2542497232 scopus 로고
    • Location of the spike glycoproteins in the Semliki Forest virus membrane
    • H. Garoff, and K. Simons Location of the spike glycoproteins in the Semliki Forest virus membrane Proc. Natl. Acad. Sci. U.S.A. 71 1974 3988 3992
    • (1974) Proc. Natl. Acad. Sci. U.S.A. , vol.71 , pp. 3988-3992
    • Garoff, H.1    Simons, K.2
  • 32
    • 0018177156 scopus 로고
    • Assembly of the Semliki Forest virus membrane glycoproteins in the membrane of the endoplasmic reticulum in vitro
    • H. Garoff, K. Simons, and B. Dobberstein Assembly of the Semliki Forest virus membrane glycoproteins in the membrane of the endoplasmic reticulum in vitro J. Mol. Biol. 124 1978 587 600
    • (1978) J. Mol. Biol. , vol.124 , pp. 587-600
    • Garoff, H.1    Simons, K.2    Dobberstein, B.3
  • 33
    • 0018175019 scopus 로고
    • The amphiphilic membrane glycoproteins of Semliki Forest virus are attached to the lipid bilayer by their COOH-terminal ends
    • H. Garoff, and H. Soderlund The amphiphilic membrane glycoproteins of Semliki Forest virus are attached to the lipid bilayer by their COOH-terminal ends J. Mol. Biol. 124 1978 535 549
    • (1978) J. Mol. Biol. , vol.124 , pp. 535-549
    • Garoff, H.1    Soderlund, H.2
  • 35
    • 0027510702 scopus 로고
    • Deletion analysis of the capsid protein of Sindbis virus: Identification of the RNA binding region
    • U. Geigenmuller-Gnirke, H. Nitschko, and S. Schlesinger Deletion analysis of the capsid protein of Sindbis virus: identification of the RNA binding region J. Virol. 67 1993 1620 1626
    • (1993) J. Virol. , vol.67 , pp. 1620-1626
    • Geigenmuller-Gnirke, U.1    Nitschko, H.2    Schlesinger, S.3
  • 37
  • 39
    • 0037009367 scopus 로고    scopus 로고
    • Acid-induced movements in the glycoprotein shell of an alphavirus turn the spikes into membrane fusion mode
    • L. Haag, H. Garoff, L. Xing, L. Hammar, S.T. Kan, and R.H. Cheng Acid-induced movements in the glycoprotein shell of an alphavirus turn the spikes into membrane fusion mode EMBO J. 21 2002 4402 4410
    • (2002) EMBO J. , vol.21 , pp. 4402-4410
    • Haag, L.1    Garoff, H.2    Xing, L.3    Hammar, L.4    Kan, S.T.5    Cheng, R.H.6
  • 40
    • 0024413396 scopus 로고
    • Sindbis virus ts103 has a mutation in glycoprotein E2 that leads to defective assembly of virions
    • C.S. Hahn, C.M. Rice, E.G. Strauss, E.M. Lenches, and J.H. Strauss Sindbis virus ts103 has a mutation in glycoprotein E2 that leads to defective assembly of virions J. Virol. 63 1989 3459 3465
    • (1989) J. Virol. , vol.63 , pp. 3459-3465
    • Hahn, C.S.1    Rice, C.M.2    Strauss, E.G.3    Lenches, E.M.4    Strauss, J.H.5
  • 41
    • 0025352036 scopus 로고
    • Site-directed mutagenesis of the proposed catalytic amino acids of the Sindbis virus capsid protein autoprotease
    • C.S. Hahn, and J.H. Strauss Site-directed mutagenesis of the proposed catalytic amino acids of the Sindbis virus capsid protein autoprotease J. Virol. 64 1990 3069 3073
    • (1990) J. Virol. , vol.64 , pp. 3069-3073
    • Hahn, C.S.1    Strauss, J.H.2
  • 42
    • 0019433134 scopus 로고
    • Evidence for a separate signal sequence for the carboxy-terminal envelope glycoprotein E1 of Semliki forest virus
    • K. Hashimoto, S. Erdei, S. Keranen, J. Saraste, and L. Kaariainen Evidence for a separate signal sequence for the carboxy-terminal envelope glycoprotein E1 of Semliki forest virus J. Virol. 38 1981 34 40
    • (1981) J. Virol. , vol.38 , pp. 34-40
    • Hashimoto, K.1    Erdei, S.2    Keranen, S.3    Saraste, J.4    Kaariainen, L.5
  • 43
    • 0028985015 scopus 로고    scopus 로고
    • A pseudo-revertant of a Sindbis virus 6 K protein mutant, which corrects for aberrant particle formation, contains two new mutations that map to the ectodomain of the E2 glycoprotein
    • L. Ivanova, S. Lustig, and M.J. Schlesinger A pseudo-revertant of a Sindbis virus 6 K protein mutant, which corrects for aberrant particle formation, contains two new mutations that map to the ectodomain of the E2 glycoprotein Virology 206 1999 1027 1034
    • (1999) Virology , vol.206 , pp. 1027-1034
    • Ivanova, L.1    Lustig, S.2    Schlesinger, M.J.3
  • 44
    • 0027419559 scopus 로고
    • Site-directed mutations in the Sindbis virus E2 glycoprotein identify palmitoylation sites and affect virus budding
    • L. Ivanova, and M.J. Schlesinger Site-directed mutations in the Sindbis virus E2 glycoprotein identify palmitoylation sites and affect virus budding J. Virol. 67 1993 2546 2551
    • (1993) J. Virol. , vol.67 , pp. 2546-2551
    • Ivanova, L.1    Schlesinger, M.J.2
  • 45
    • 0019475927 scopus 로고
    • Fluorescence photobleaching recovery measurements reveal differences in envelopment of Sindbis and vesicular stomatitis viruses
    • D.C. Johnson, M.J. Schlesinger, and E.L. Elson Fluorescence photobleaching recovery measurements reveal differences in envelopment of Sindbis and vesicular stomatitis viruses Cell 23 1981 423 431
    • (1981) Cell , vol.23 , pp. 423-431
    • Johnson, D.C.1    Schlesinger, M.J.2    Elson, E.L.3
  • 46
    • 0033649526 scopus 로고    scopus 로고
    • Specific roles for lipids in virus fusion and exit. Examples from the alphaviruses
    • M. Kielian, P.K. Chatterjee, D.L. Gibbons, and Y.E. Lu Specific roles for lipids in virus fusion and exit. Examples from the alphaviruses Subcell Biochem. 34 2000 409 455
    • (2000) Subcell Biochem. , vol.34 , pp. 409-455
    • Kielian, M.1    Chatterjee, P.K.2    Gibbons, D.L.3    Lu, Y.E.4
  • 47
    • 0022273625 scopus 로고
    • PH-induced alterations in the fusogenic spike protein of Semliki Forest virus
    • M. Kielian, and A. Helenius pH-induced alterations in the fusogenic spike protein of Semliki Forest virus J. Cell Biol. 101 1985 2284 2291
    • (1985) J. Cell Biol. , vol.101 , pp. 2284-2291
    • Kielian, M.1    Helenius, A.2
  • 49
    • 0020504586 scopus 로고
    • Expression of Semliki Forest virus proteins from cloned complementary DNA. I. The fusion activity of the spike glycoprotein
    • C. Kondor-Koch, B. Burke, and H. Garoff Expression of Semliki Forest virus proteins from cloned complementary DNA. I. The fusion activity of the spike glycoprotein J. Cell Biol. 97 1983 644 651
    • (1983) J. Cell Biol. , vol.97 , pp. 644-651
    • Kondor-Koch, C.1    Burke, B.2    Garoff, H.3
  • 51
    • 0027989589 scopus 로고
    • Mutations in an exposed domain of Sindbis virus capsid protein result in the production of noninfectious virions and morphological variants
    • H. Lee, and D.T. Brown Mutations in an exposed domain of Sindbis virus capsid protein result in the production of noninfectious virions and morphological variants Virology 202 1994 390 400
    • (1994) Virology , vol.202 , pp. 390-400
    • Lee, H.1    Brown, D.T.2
  • 52
    • 0031666973 scopus 로고    scopus 로고
    • Probing the potential glycoprotein binding site of Sindbis virus capsid protein with dioxane and model building
    • S. Lee, R.J. Kuhn, and M.G. Rossmann Probing the potential glycoprotein binding site of Sindbis virus capsid protein with dioxane and model building Proteins 33 1998 311 317
    • (1998) Proteins , vol.33 , pp. 311-317
    • Lee, S.1    Kuhn, R.J.2    Rossmann, M.G.3
  • 53
    • 0030585119 scopus 로고    scopus 로고
    • Identification of a protein binding site on the surface of the alphavirus nucleocapsid and its implication in virus assembly
    • S. Lee, K.E. Owen, H.K. Choi, H. Lee, G. Lu, G. Wengler, D.T. Brown, M.G. Rossmann, and R.J. Kuhn Identification of a protein binding site on the surface of the alphavirus nucleocapsid and its implication in virus assembly Structure 4 1996 531 541
    • (1996) Structure , vol.4 , pp. 531-541
    • Lee, S.1    Owen, K.E.2    Choi, H.K.3    Lee, H.4    Lu, G.5    Wengler, G.6    Brown, D.T.7    Rossmann, M.G.8    Kuhn, R.J.9
  • 54
    • 0035815282 scopus 로고    scopus 로고
    • The fusion glycoprotein shell of Semliki Forest virus: An icosahedral assembly primed for fusogenic activation at endosomal pH
    • J. Lescar, A. Roussel, M.W. Wien, J. Navaza, S.D. Fuller, G. Wengler, and F.A. Rey The fusion glycoprotein shell of Semliki Forest virus: an icosahedral assembly primed for fusogenic activation at endosomal pH Cell 105 2001 137 148
    • (2001) Cell , vol.105 , pp. 137-148
    • Lescar, J.1    Roussel, A.2    Wien, M.W.3    Navaza, J.4    Fuller, S.D.5    Wengler, G.6    Rey, F.A.7
  • 55
    • 0025812961 scopus 로고
    • Mutagenesis of the putative fusion domain of the Semliki Forest virus spike protein
    • P. Levy-Mintz, and M. Kielian Mutagenesis of the putative fusion domain of the Semliki Forest virus spike protein J. Virol. 65 1991 4292 4300
    • (1991) J. Virol. , vol.65 , pp. 4292-4300
    • Levy-Mintz, P.1    Kielian, M.2
  • 56
    • 0025957563 scopus 로고
    • Internally located cleavable signal sequences direct the formation of Semliki Forest virus membrane proteins from a polyprotein precursor
    • P. Liljestrom, and H. Garoff Internally located cleavable signal sequences direct the formation of Semliki Forest virus membrane proteins from a polyprotein precursor J. Virol. 65 1991 147 154
    • (1991) J. Virol. , vol.65 , pp. 147-154
    • Liljestrom, P.1    Garoff, H.2
  • 57
    • 0025912001 scopus 로고
    • In vitro mutagenesis of a full-length cDNA clone of Semliki Forest virus: The small 6,000-molecular-weight membrane protein modulates virus release
    • P. Liljestrom, S. Lusa, D. Huylebroeck, and H. Garoff In vitro mutagenesis of a full-length cDNA clone of Semliki Forest virus: the small 6,000-molecular-weight membrane protein modulates virus release J. Virol. 65 1991 4107 4113
    • (1991) J. Virol. , vol.65 , pp. 4107-4113
    • Liljestrom, P.1    Lusa, S.2    Huylebroeck, D.3    Garoff, H.4
  • 58
    • 0022613059 scopus 로고
    • Sindbis virus mutant ts20 of complementation group e contains a lesion in glycoprotein E2
    • B.H. Lindqvist, J. DiSalvo, C.M. Rice, J.H. Strauss, and E.G. Strauss Sindbis virus mutant ts20 of complementation group E contains a lesion in glycoprotein E2 Virology 151 1986 10 20
    • (1986) Virology , vol.151 , pp. 10-20
    • Lindqvist, B.H.1    Disalvo, J.2    Rice, C.M.3    Strauss, J.H.4    Strauss, E.G.5
  • 59
    • 0030219994 scopus 로고    scopus 로고
    • Mutations in the endo domain of Sindbis virus glycoprotein E2 block phosphorylation, reorientation of the endo domain, and nucleocapsid binding
    • L.N. Liu, H. Lee, R. Hernandez, and D.T. Brown Mutations in the endo domain of Sindbis virus glycoprotein E2 block phosphorylation, reorientation of the endo domain, and nucleocapsid binding Virology 222 1996 236 246
    • (1996) Virology , vol.222 , pp. 236-246
    • Liu, L.N.1    Lee, H.2    Hernandez, R.3    Brown, D.T.4
  • 60
    • 0027365321 scopus 로고
    • Phosphorylation and dephosphorylation events play critical roles in Sindbis virus maturation
    • N. Liu, and D.T. Brown Phosphorylation and dephosphorylation events play critical roles in Sindbis virus maturation Virology 196 1993 703 711
    • (1993) Virology , vol.196 , pp. 703-711
    • Liu, N.1    Brown, D.T.2
  • 61
    • 0027452740 scopus 로고
    • Transient translocation of the cytoplasmic (endo) domain of a type I membrane glycoprotein into cellular membranes
    • N. Liu, and D.T. Brown Transient translocation of the cytoplasmic (endo) domain of a type I membrane glycoprotein into cellular membranes J. Cell Biol. 120 1993 877 883
    • (1993) J. Cell Biol. , vol.120 , pp. 877-883
    • Liu, N.1    Brown, D.T.2
  • 62
    • 0028936836 scopus 로고
    • The 6-kilodalton membrane protein of Semliki Forest virus is involved in the budding process
    • A. Loewy, J. Smyth, C.H. von Bonsdorff, P. Liljestrom, and M.J. Schlesinger The 6-kilodalton membrane protein of Semliki Forest virus is involved in the budding process J. Virol. 69 1995 469 475
    • (1995) J. Virol. , vol.69 , pp. 469-475
    • Loewy, A.1    Smyth, J.2    Von Bonsdorff, C.H.3    Liljestrom, P.4    Schlesinger, M.J.5
  • 63
    • 0027976652 scopus 로고
    • Nucleocapsid-glycoprotein interactions required for assembly of alphaviruses
    • S. Lopez, J.S. Yao, R.J. Kuhn, E.G. Strauss, and J.H. Strauss Nucleocapsid-glycoprotein interactions required for assembly of alphaviruses J. Virol. 68 1994 1316 1323
    • (1994) J. Virol. , vol.68 , pp. 1316-1323
    • Lopez, S.1    Yao, J.S.2    Kuhn, R.J.3    Strauss, E.G.4    Strauss, J.H.5
  • 64
    • 0033871174 scopus 로고    scopus 로고
    • Semliki forest virus budding: Assay, mechanisms, and cholesterol requirement
    • Y.E. Lu, and M. Kielian Semliki forest virus budding: assay, mechanisms, and cholesterol requirement J. Virol. 74 2000 7708 7719
    • (2000) J. Virol. , vol.74 , pp. 7708-7719
    • Lu, Y.E.1    Kielian, M.2
  • 65
    • 0026323917 scopus 로고
    • Fate of the 6 K membrane protein of Semliki Forest virus during virus assembly
    • S. Lusa, H. Garoff, and P. Liljestrom Fate of the 6 K membrane protein of Semliki Forest virus during virus assembly Virology 185 1991 843 846
    • (1991) Virology , vol.185 , pp. 843-846
    • Lusa, S.1    Garoff, H.2    Liljestrom, P.3
  • 66
    • 0033854594 scopus 로고    scopus 로고
    • Cryo-electron microscopy reveals the functional organization of an enveloped virus. Semliki Forest virus
    • E.J. Mancini, M. Clarke, B.E. Gowen, T. Rutten, and S.D. Fuller Cryo-electron microscopy reveals the functional organization of an enveloped virus. Semliki Forest virus Mol. Cell. 5 2000 255 266
    • (2000) Mol. Cell. , vol.5 , pp. 255-266
    • Mancini, E.J.1    Clarke, M.2    Gowen, B.E.3    Rutten, T.4    Fuller, S.D.5
  • 67
    • 0020724144 scopus 로고
    • Penetration of Semliki Forest virus from acidic prelysosomal vacuoles
    • M. Marsh, E. Bolzau, and A. Helenius Penetration of Semliki Forest virus from acidic prelysosomal vacuoles Cell 32 1983 931 940
    • (1983) Cell , vol.32 , pp. 931-940
    • Marsh, M.1    Bolzau, E.2    Helenius, A.3
  • 68
    • 0022748203 scopus 로고
    • Reinitiation of translocation in the Semliki Forest virus structural polyprotein: Identification of the signal for the E1 glycoprotein
    • P. Melancon, and H. Garoff Reinitiation of translocation in the Semliki Forest virus structural polyprotein: identification of the signal for the E1 glycoprotein EMBO J. 5 1986 1551 1560
    • (1986) EMBO J. , vol.5 , pp. 1551-1560
    • Melancon, P.1    Garoff, H.2
  • 69
    • 0023275581 scopus 로고
    • Processing of the Semliki Forest virus structural polyprotein: Role of the capsid protease
    • P. Melancon, and H. Garoff Processing of the Semliki Forest virus structural polyprotein: role of the capsid protease J. Virol. 61 1987 1301 1309
    • (1987) J. Virol. , vol.61 , pp. 1301-1309
    • Melancon, P.1    Garoff, H.2
  • 71
    • 0029876709 scopus 로고    scopus 로고
    • Identification of a region in the Sindbis virus nucleocapsid protein that is involved in specificity of RNA encapsidation
    • K.E. Owen, and R.J. Kuhn Identification of a region in the Sindbis virus nucleocapsid protein that is involved in specificity of RNA encapsidation J. Virol. 70 1996 2757 2763
    • (1996) J. Virol. , vol.70 , pp. 2757-2763
    • Owen, K.E.1    Kuhn, R.J.2
  • 72
    • 0030916277 scopus 로고    scopus 로고
    • Alphavirus budding is dependent on the interaction between the nucleocapsid and hydrophobic amino acids on the cytoplasmic domain of the E2 envelope glycoprotein
    • K.E. Owen, and R.J. Kuhn Alphavirus budding is dependent on the interaction between the nucleocapsid and hydrophobic amino acids on the cytoplasmic domain of the E2 envelope glycoprotein Virology 230 1997 187 196
    • (1997) Virology , vol.230 , pp. 187-196
    • Owen, K.E.1    Kuhn, R.J.2
  • 73
    • 0037213901 scopus 로고    scopus 로고
    • Structure of isolated nucleocapsids from Venezuelan equine encephalitis virus and implications for assembly and disassembly of enveloped virus
    • A. Paredes, K. Alwell-Warda, S.C. Weaver, W. Chiu, and S.J. Watowich Structure of isolated nucleocapsids from Venezuelan equine encephalitis virus and implications for assembly and disassembly of enveloped virus J. Virol. 77 2003 659 664
    • (2003) J. Virol. , vol.77 , pp. 659-664
    • Paredes, A.1    Alwell-Warda, K.2    Weaver, S.C.3    Chiu, W.4    Watowich, S.J.5
  • 76
    • 0041488655 scopus 로고    scopus 로고
    • Infectious HIV-1 assembles in late endosomes in primary macrophages
    • A. Pelchen-Matthews, B. Kramer, and M. Marsh Infectious HIV-1 assembles in late endosomes in primary macrophages J. Cell Biol. 162 2003 443 455
    • (2003) J. Cell Biol. , vol.162 , pp. 443-455
    • Pelchen-Matthews, A.1    Kramer, B.2    Marsh, M.3
  • 77
    • 0038447231 scopus 로고    scopus 로고
    • A heterologous coiled coil can substitute for helix I of the Sindbis virus capsid protein
    • R. Perera, C. Navaratnarajah, and R.J. Kuhn A heterologous coiled coil can substitute for helix I of the Sindbis virus capsid protein J. Virol. 77 2003 8345 8353
    • (2003) J. Virol. , vol.77 , pp. 8345-8353
    • Perera, R.1    Navaratnarajah, C.2    Kuhn, R.J.3
  • 78
    • 0034751125 scopus 로고    scopus 로고
    • Alphavirus nucleocapsid protein contains a putative coiled coil alpha-helix important for core assembly
    • R. Perera, K.E. Owen, T.L. Tellinghuisen, A.E. Gorbalenya, and R.J. Kuhn Alphavirus nucleocapsid protein contains a putative coiled coil alpha-helix important for core assembly J. Virol. 75 2001 1 10
    • (2001) J. Virol. , vol.75 , pp. 1-10
    • Perera, R.1    Owen, K.E.2    Tellinghuisen, T.L.3    Gorbalenya, A.E.4    Kuhn, R.J.5
  • 81
    • 0020033052 scopus 로고
    • Isolation and characterization of the hydrophobic COOH-terminal domains of the Sindbis virion glycoproteins
    • C.M. Rice, J.R. Bell, M.W. Hunkapiller, E.G. Strauss, and J.H. Strauss Isolation and characterization of the hydrophobic COOH-terminal domains of the Sindbis virion glycoproteins J. Mol. Biol. 154 1982 355 378
    • (1982) J. Mol. Biol. , vol.154 , pp. 355-378
    • Rice, C.M.1    Bell, J.R.2    Hunkapiller, M.W.3    Strauss, E.G.4    Strauss, J.H.5
  • 82
    • 0020085011 scopus 로고
    • Association of Sindbis virion glycoproteins and their precursors
    • C.M. Rice, and J.H. Strauss Association of Sindbis virion glycoproteins and their precursors J. Mol. Biol. 154 1982 325 348
    • (1982) J. Mol. Biol. , vol.154 , pp. 325-348
    • Rice, C.M.1    Strauss, J.H.2
  • 83
    • 0029011658 scopus 로고
    • Communication of post-Golgi elements with early endocytic pathway: Regulation of endoproteolytic cleavage of Semliki Forest virus p62 precursor
    • M. Sariola, J. Saraste, and E. Kuismanen Communication of post-Golgi elements with early endocytic pathway: regulation of endoproteolytic cleavage of Semliki Forest virus p62 precursor J. Cell Sci. 108 1995 2465 2475
    • (1995) J. Cell Sci. , vol.108 , pp. 2465-2475
    • Sariola, M.1    Saraste, J.2    Kuismanen, E.3
  • 84
    • 0014498741 scopus 로고
    • Kinetics of incorporation of structural proteins into Sindbis virions
    • C.M. Scheele, and E.R. Pfefferkorn Kinetics of incorporation of structural proteins into Sindbis virions J. Virol. 3 1969 369 375
    • (1969) J. Virol. , vol.3 , pp. 369-375
    • Scheele, C.M.1    Pfefferkorn, E.R.2
  • 85
    • 0015427088 scopus 로고
    • Formation of Sindbis virus proteins: Identification of a precursor for one of the envelope proteins
    • S. Schlesinger, and M.J. Schlesinger Formation of Sindbis virus proteins: identification of a precursor for one of the envelope proteins J. Virol. 10 1972 925 932
    • (1972) J. Virol. , vol.10 , pp. 925-932
    • Schlesinger, S.1    Schlesinger, M.J.2
  • 86
    • 0019332459 scopus 로고
    • Relation of fatty acid attachment to the translation and maturation of vesicular stomatitis and Sindbis virus membrane glycoproteins
    • M.F. Schmidt, and M.J. Schlesinger Relation of fatty acid attachment to the translation and maturation of vesicular stomatitis and Sindbis virus membrane glycoproteins J. Biol. Chem. 255 1980 3334 3339
    • (1980) J. Biol. Chem. , vol.255 , pp. 3334-3339
    • Schmidt, M.F.1    Schlesinger, M.J.2
  • 87
    • 0026490846 scopus 로고
    • Role of ribosomes in Semliki Forest virus nucleocapsid uncoating
    • I. Singh, and A. Helenius Role of ribosomes in Semliki Forest virus nucleocapsid uncoating J. Virol. 66 1992 7049 7058
    • (1992) J. Virol. , vol.66 , pp. 7049-7058
    • Singh, I.1    Helenius, A.2
  • 88
    • 0030977374 scopus 로고    scopus 로고
    • Multiple mechanisms for the inhibition of entry and uncoating of superinfecting Semliki Forest virus
    • I.R. Singh, M. Suomalainen, S. Varadarajan, H. Garoff, and A. Helenius Multiple mechanisms for the inhibition of entry and uncoating of superinfecting Semliki Forest virus Virology 231 1997 59 71
    • (1997) Virology , vol.231 , pp. 59-71
    • Singh, I.R.1    Suomalainen, M.2    Varadarajan, S.3    Garoff, H.4    Helenius, A.5
  • 89
    • 8944255627 scopus 로고    scopus 로고
    • The translation-enhancing region of the Semliki Forest virus subgenome is only functional in the virus-infected cell
    • E.M. Sjoberg, and H. Garoff The translation-enhancing region of the Semliki Forest virus subgenome is only functional in the virus-infected cell J. Gen. Virol. 77 1996 1323 1327
    • (1996) J. Gen. Virol. , vol.77 , pp. 1323-1327
    • Sjoberg, E.M.1    Garoff, H.2
  • 90
    • 0028152741 scopus 로고
    • A significantly improved Semliki Forest virus expression system based on translation enhancer segments from the viral capsid gene
    • E.M. Sjoberg, M. Suomalainen, and H. Garoff A significantly improved Semliki Forest virus expression system based on translation enhancer segments from the viral capsid gene Biotechnology (NY) 12 1994 1127 1131
    • (1994) Biotechnology (NY) , vol.12 , pp. 1127-1131
    • Sjoberg, E.M.1    Suomalainen, M.2    Garoff, H.3
  • 91
    • 0037334555 scopus 로고    scopus 로고
    • Interactions between the transmembrane segments of the alphavirus E1 and E2 proteins play a role in virus budding and fusion
    • M. Sjoberg, and H. Garoff Interactions between the transmembrane segments of the alphavirus E1 and E2 proteins play a role in virus budding and fusion J. Virol. 77 2003 3441 3450
    • (2003) J. Virol. , vol.77 , pp. 3441-3450
    • Sjoberg, M.1    Garoff, H.2
  • 92
    • 0030585135 scopus 로고    scopus 로고
    • Aromatic interactions define the binding of the alphavirus spike to its nucleocapsid
    • U. Skoging, M. Vihinen, L. Nilsson, and P. Liljestrom Aromatic interactions define the binding of the alphavirus spike to its nucleocapsid Structure 4 1996 519 529
    • (1996) Structure , vol.4 , pp. 519-529
    • Skoging, U.1    Vihinen, M.2    Nilsson, L.3    Liljestrom, P.4
  • 93
    • 0033923591 scopus 로고    scopus 로고
    • A conserved leucine in the cytoplasmic domain of the Semliki Forest virus spike protein is important for budding
    • U. Skoging-Nyberg, and P. Liljestrom A conserved leucine in the cytoplasmic domain of the Semliki Forest virus spike protein is important for budding Arch. Virol. 145 2000 1225 1230
    • (2000) Arch. Virol. , vol.145 , pp. 1225-1230
    • Skoging-Nyberg, U.1    Liljestrom, P.2
  • 94
    • 0035033753 scopus 로고    scopus 로고
    • M-X-I motif of Semliki Forest virus capsid protein affects nucleocapsid assembly
    • U. Skoging-Nyberg, and P. Liljestrom M-X-I motif of Semliki Forest virus capsid protein affects nucleocapsid assembly J. Virol. 75 2001 4625 4632
    • (2001) J. Virol. , vol.75 , pp. 4625-4632
    • Skoging-Nyberg, U.1    Liljestrom, P.2
  • 95
    • 0031060529 scopus 로고    scopus 로고
    • Efficient multiplication of a Semliki Forest virus chimera containing Sindbis virus spikes
    • J. Smyth, M. Suomalainen, and H. Garoff Efficient multiplication of a Semliki Forest virus chimera containing Sindbis virus spikes J. Virol. 71 1997 818 823
    • (1997) J. Virol. , vol.71 , pp. 818-823
    • Smyth, J.1    Suomalainen, M.2    Garoff, H.3
  • 96
    • 0028088152 scopus 로고
    • The alphaviruses: Gene expression, replication, and evolution
    • J.H. Strauss, and E.G. Strauss The alphaviruses: gene expression, replication, and evolution Microbiol. Rev. 58 1994 491 562
    • (1994) Microbiol. Rev. , vol.58 , pp. 491-562
    • Strauss, J.H.1    Strauss, E.G.2
  • 97
    • 0026691322 scopus 로고
    • Spike protein-nucleocapsid interactions drive the budding of alphaviruses
    • M. Suomalainen, P. Liljestrom, and H. Garoff Spike protein-nucleocapsid interactions drive the budding of alphaviruses J. Virol. 66 1992 4737 4747
    • (1992) J. Virol. , vol.66 , pp. 4737-4747
    • Suomalainen, M.1    Liljestrom, P.2    Garoff, H.3
  • 98
    • 0015752210 scopus 로고
    • Kinetics of the formation of the Semliki Forest virus nucleocapsid
    • H. Söderlund Kinetics of the formation of the Semliki Forest virus nucleocapsid Intervirology 1 1973 110 118
    • (1973) Intervirology , vol.1 , pp. 110-118
    • Söderlund, H.1
  • 99
    • 0033028591 scopus 로고    scopus 로고
    • In vitro assembly of alphavirus cores by using nucleocapsid protein expressed in Escherichia coli
    • T.L. Tellinghuisen, A.E. Hamburger, B.R. Fisher, R. Ostendorp, and R.J. Kuhn In vitro assembly of alphavirus cores by using nucleocapsid protein expressed in Escherichia coli J. Virol. 73 1999 5309 5319
    • (1999) J. Virol. , vol.73 , pp. 5309-5319
    • Tellinghuisen, T.L.1    Hamburger, A.E.2    Fisher, B.R.3    Ostendorp, R.4    Kuhn, R.J.5
  • 100
    • 0017110423 scopus 로고
    • Semliki Forest virus capsid protein associates with the 60S ribosomal subunit in infected cells
    • I. Ulmanen, H. Soderlund, and L. Kaariainen Semliki Forest virus capsid protein associates with the 60S ribosomal subunit in infected cells J. Virol. 20 1976 203 210
    • (1976) J. Virol. , vol.20 , pp. 203-210
    • Ulmanen, I.1    Soderlund, H.2    Kaariainen, L.3
  • 101
    • 0024455501 scopus 로고
    • The heterodimeric association between the membrane proteins of Semliki Forest virus changes its sensitivity to low pH during virus maturation
    • J.M. Wahlberg, W.A. Boere, and H. Garoff The heterodimeric association between the membrane proteins of Semliki Forest virus changes its sensitivity to low pH during virus maturation J. Virol. 63 1989 4991 4997
    • (1989) J. Virol. , vol.63 , pp. 4991-4997
    • Wahlberg, J.M.1    Boere, W.A.2    Garoff, H.3
  • 102
    • 0026584727 scopus 로고
    • Membrane fusion process of Semliki Forest virus. I: Low pH-induced rearrangement in spike protein quaternary structure precedes virus penetration into cells
    • J.M. Wahlberg, and H. Garoff Membrane fusion process of Semliki Forest virus. I: low pH-induced rearrangement in spike protein quaternary structure precedes virus penetration into cells J. Cell Biol. 116 1992 339 348
    • (1992) J. Cell Biol. , vol.116 , pp. 339-348
    • Wahlberg, J.M.1    Garoff, H.2
  • 103
    • 0028359402 scopus 로고
    • Interactions between Sindbis virus RNAs and a 68 amino acid derivative of the viral capsid protein further defines the capsid binding site
    • B. Weiss, U. Geigenmuller-Gnirke, and S. Schlesinger Interactions between Sindbis virus RNAs and a 68 amino acid derivative of the viral capsid protein further defines the capsid binding site Nucleic Acids Res. 22 1994 780 786
    • (1994) Nucleic Acids Res. , vol.22 , pp. 780-786
    • Weiss, B.1    Geigenmuller-Gnirke, U.2    Schlesinger, S.3
  • 104
    • 0024428285 scopus 로고
    • Evidence for specificity in the encapsidation of Sindbis virus RNAs
    • B. Weiss, H. Nitschko, I. Ghattas, R. Wright, and S. Schlesinger Evidence for specificity in the encapsidation of Sindbis virus RNAs J. Virol. 63 1989 5310 5318
    • (1989) J. Virol. , vol.63 , pp. 5310-5318
    • Weiss, B.1    Nitschko, H.2    Ghattas, I.3    Wright, R.4    Schlesinger, S.5
  • 105
    • 0021262413 scopus 로고
    • Identification of a transfer of viral core protein to cellular ribosomes during the early stages of alphavirus infection
    • G. Wengler Identification of a transfer of viral core protein to cellular ribosomes during the early stages of alphavirus infection Virology 134 1984 435 442
    • (1984) Virology , vol.134 , pp. 435-442
    • Wengler, G.1
  • 106
    • 0020053676 scopus 로고
    • The core protein of the alphavirus Sindbis virus assembles into core-like nucleoproteins with the viral genome RNA and with other single-stranded nucleic acids in vitro
    • G. Wengler, U. Boege, H. Bischoff, and K. Wahn The core protein of the alphavirus Sindbis virus assembles into core-like nucleoproteins with the viral genome RNA and with other single-stranded nucleic acids in vitro Virology 118 1982 401 410
    • (1982) Virology , vol.118 , pp. 401-410
    • Wengler, G.1    Boege, U.2    Bischoff, H.3    Wahn, K.4
  • 107
    • 0021357579 scopus 로고
    • Establishment and analysis of a system which allows assembly and disassembly of alphavirus core-like particles under physiological conditions in vitro
    • G. Wengler, U. Boege, and K. Wahn Establishment and analysis of a system which allows assembly and disassembly of alphavirus core-like particles under physiological conditions in vitro Virology 132 1984 401 412
    • (1984) Virology , vol.132 , pp. 401-412
    • Wengler, G.1    Boege, U.2    Wahn, K.3
  • 108
    • 0030219428 scopus 로고    scopus 로고
    • Analyses of the role of structural changes in the regulation of uncoating and assembly of alphavirus cores
    • G. Wengler, and C. Gros Analyses of the role of structural changes in the regulation of uncoating and assembly of alphavirus cores Virology 222 1996 123 132
    • (1996) Virology , vol.222 , pp. 123-132
    • Wengler, G.1    Gros, C.2
  • 109
    • 0027054277 scopus 로고
    • Identification of a sequence element in the alphavirus core protein which mediates interaction of cores with ribosomes and the disassembly of cores
    • G. Wengler, and D. Wurkner Identification of a sequence element in the alphavirus core protein which mediates interaction of cores with ribosomes and the disassembly of cores Virology 191 1992 880 888
    • (1992) Virology , vol.191 , pp. 880-888
    • Wengler, G.1    Wurkner, D.2
  • 110
    • 0001696895 scopus 로고
    • PH-dependent fusion between the Semliki Forest virus membrane and liposomes
    • J. White, and A. Helenius pH-dependent fusion between the Semliki Forest virus membrane and liposomes Proc. Natl. Acad. Sci. U.S.A. 77 1980 3273 3277
    • (1980) Proc. Natl. Acad. Sci. U.S.A. , vol.77 , pp. 3273-3277
    • White, J.1    Helenius, A.2
  • 111
    • 0019069749 scopus 로고
    • Fusion of Semliki forest virus with the plasma membrane can be induced by low pH
    • J. White, J. Kartenbeck, and A. Helenius Fusion of Semliki forest virus with the plasma membrane can be induced by low pH J. Cell Biol. 87 1980 264 272
    • (1980) J. Cell Biol. , vol.87 , pp. 264-272
    • White, J.1    Kartenbeck, J.2    Helenius, A.3
  • 112
    • 0025728301 scopus 로고
    • Form, function, and use of retroviral gag proteins
    • J.W. Wills, and R.C. Craven Form, function, and use of retroviral gag proteins AIDS 5 1991 639 654
    • (1991) AIDS , vol.5 , pp. 639-654
    • Wills, J.W.1    Craven, R.C.2
  • 113
    • 0017348936 scopus 로고
    • How a single Sindbis virus mRNA directs the synthesis of one soluble protein and two integral membrane glycoproteins
    • D.F. Wirth, F. Katz, B. Small, and H.F. Lodish How a single Sindbis virus mRNA directs the synthesis of one soluble protein and two integral membrane glycoproteins Cell 10 1977 253 263
    • (1977) Cell , vol.10 , pp. 253-263
    • Wirth, D.F.1    Katz, F.2    Small, B.3    Lodish, H.F.4
  • 114
    • 0031931226 scopus 로고    scopus 로고
    • Molecular genetic study of the interaction of Sindbis virus E2 with Ross River virus E1 for virus budding
    • J. Yao, E.G. Strauss, and J.H. Strauss Molecular genetic study of the interaction of Sindbis virus E2 with Ross River virus E1 for virus budding J. Virol. 72 1998 1418 1423
    • (1998) J. Virol. , vol.72 , pp. 1418-1423
    • Yao, J.1    Strauss, E.G.2    Strauss, J.H.3
  • 115
    • 0013007874 scopus 로고    scopus 로고
    • Interactions between PE2, E1, and 6K required for assembly of alphaviruses studied with chimeric viruses
    • J.S. Yao, E.G. Strauss, and J.H. Strauss Interactions between PE2, E1, and 6K required for assembly of alphaviruses studied with chimeric viruses J. Virol. 70 1996 7910 7920
    • (1996) J. Virol. , vol.70 , pp. 7910-7920
    • Yao, J.S.1    Strauss, E.G.2    Strauss, J.H.3
  • 117
    • 0026490847 scopus 로고
    • Role of cell surface spikes in alphavirus budding
    • H. Zhao, and H. Garoff Role of cell surface spikes in alphavirus budding J. Virol. 66 1992 7089 7095
    • (1992) J. Virol. , vol.66 , pp. 7089-7095
    • Zhao, H.1    Garoff, H.2
  • 118
    • 0027965259 scopus 로고
    • A tyrosine-based motif in the cytoplasmic domain of the alphavirus envelope protein is essential for budding
    • H. Zhao, B. Lindqvist, H. Garoff, C.H. von Bonsdorff, and P. Liljestrom A tyrosine-based motif in the cytoplasmic domain of the alphavirus envelope protein is essential for budding EMBO J. 13 1994 4204 4211
    • (1994) EMBO J. , vol.13 , pp. 4204-4211
    • Zhao, H.1    Lindqvist, B.2    Garoff, H.3    Von Bonsdorff, C.H.4    Liljestrom, P.5
  • 119
    • 0019216782 scopus 로고
    • Formation of the Semliki Forest virus membrane glycoprotein complexes in the infected cell
    • A. Ziemiecki, H. Garoff, and K. Simons Formation of the Semliki Forest virus membrane glycoprotein complexes in the infected cell J. Gen. Virol. 50 1980 111 123
    • (1980) J. Gen. Virol. , vol.50 , pp. 111-123
    • Ziemiecki, A.1    Garoff, H.2    Simons, K.3
  • 120
    • 0017803335 scopus 로고
    • Subunit composition of the membrane glycoprotein complex of Semliki Forest virus
    • A. Ziemiecki, and H. Garofff Subunit composition of the membrane glycoprotein complex of Semliki Forest virus J. Mol. Biol. 122 1978 259 269
    • (1978) J. Mol. Biol. , vol.122 , pp. 259-269
    • Ziemiecki, A.1    Garofff, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.