메뉴 건너뛰기




Volumn 405, Issue 1, 2010, Pages 214-224

Corrigendum to Effects of retroviral envelope-protein cleavage upon trafficking, incorporation, and membrane fusion(Virology (2010) 405(1) (214–224), (S0042682210003855), (10.1016/j.virol.2010.06.004));Effects of retroviral envelope-protein cleavage upon trafficking, incorporation, and membrane fusion

Author keywords

Envelope protein; Membrane fusion; Proteolytic processing; Retrovirus; Viral incorporation

Indexed keywords

GLYCOPROTEIN; VIRUS ENVELOPE PROTEIN;

EID: 77955519056     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2021.10.006     Document Type: Erratum
Times cited : (10)

References (58)
  • 1
    • 0037225634 scopus 로고    scopus 로고
    • Cytoplasmic tail of Moloney murine leukemia virus envelope protein influences the conformation of the extracellular domain: implications for mechanism of action of the R peptide
    • Aguilar H.C., Anderson W.F., Cannon P.M. Cytoplasmic tail of Moloney murine leukemia virus envelope protein influences the conformation of the extracellular domain: implications for mechanism of action of the R peptide. J. Virol. 2003, 77(2):1281-1291.
    • (2003) J. Virol. , vol.77 , Issue.2 , pp. 1281-1291
    • Aguilar, H.C.1    Anderson, W.F.2    Cannon, P.M.3
  • 2
    • 0024370460 scopus 로고
    • A putative murine ecotropic retrovirus receptor gene encodes a multiple membrane-spanning protein and confers susceptibility to virus infection
    • Albritton L.M., Tseng L., Scadden D., Cunningham J.M. A putative murine ecotropic retrovirus receptor gene encodes a multiple membrane-spanning protein and confers susceptibility to virus infection. Cell 1989, 57(4):659-666.
    • (1989) Cell , vol.57 , Issue.4 , pp. 659-666
    • Albritton, L.M.1    Tseng, L.2    Scadden, D.3    Cunningham, J.M.4
  • 3
    • 0035253151 scopus 로고    scopus 로고
    • Implication of the proprotein convertases furin, PC5 and PC7 in the cleavage of surface glycoproteins of Hong Kong, Ebola and respiratory syncytial viruses: a comparative analysis with fluorogenic peptides
    • Basak A., Zhong M., Munzer J.S., Chretien M., Seidah N.G. Implication of the proprotein convertases furin, PC5 and PC7 in the cleavage of surface glycoproteins of Hong Kong, Ebola and respiratory syncytial viruses: a comparative analysis with fluorogenic peptides. Biochem. J. 2001, 353(3):537-545.
    • (2001) Biochem. J. , vol.353 , Issue.3 , pp. 537-545
    • Basak, A.1    Zhong, M.2    Munzer, J.S.3    Chretien, M.4    Seidah, N.G.5
  • 4
    • 0026688430 scopus 로고
    • A novel intermediate in processing of murine leukemia virus envelope glycoproteins. Proteolytic cleavage in the late Golgi region
    • Bedgood R., Stallcup M. A novel intermediate in processing of murine leukemia virus envelope glycoproteins. Proteolytic cleavage in the late Golgi region. J. Biol. Chem. 1992, 267(10):7060-7065.
    • (1992) J. Biol. Chem. , vol.267 , Issue.10 , pp. 7060-7065
    • Bedgood, R.1    Stallcup, M.2
  • 5
    • 0025319347 scopus 로고
    • Mutational analysis of the human immunodeficiency virus type 1 env gene product proteolytic cleavage site
    • Bosch V., Pawlita M. Mutational analysis of the human immunodeficiency virus type 1 env gene product proteolytic cleavage site. J. Virol. 1990, 64(5):2337-2344.
    • (1990) J. Virol. , vol.64 , Issue.5 , pp. 2337-2344
    • Bosch, V.1    Pawlita, M.2
  • 6
    • 77955516410 scopus 로고    scopus 로고
    • Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y, J.M. Coffin, S.H. Hughes, H.E. Varmus (Eds.)
    • Retroviruses 1997, 343-435. Cold Spring Harbor Laboratory Press, Cold Spring Harbor, N.Y. J.M. Coffin, S.H. Hughes, H.E. Varmus (Eds.).
    • (1997) Retroviruses , pp. 343-435
  • 7
    • 0026501678 scopus 로고
    • Mutations within the proteolytic cleavage site of the Rous sarcoma virus glycoprotein define a requirement for dibasic residues for intracellular cleavage
    • Dong J.Y., Dubay J.W., Perez L.G., Hunter E. Mutations within the proteolytic cleavage site of the Rous sarcoma virus glycoprotein define a requirement for dibasic residues for intracellular cleavage. J. Virol. 1992, 66(2):865-874.
    • (1992) J. Virol. , vol.66 , Issue.2 , pp. 865-874
    • Dong, J.Y.1    Dubay, J.W.2    Perez, L.G.3    Hunter, E.4
  • 8
    • 0029015314 scopus 로고
    • Analysis of the cleavage site of the human immunodeficiency virus type 1 glycoprotein: requirement of precursor cleavage for glycoprotein incorporation
    • Dubay J.W., Dubay S.R., Shin H.J., Hunter E. Analysis of the cleavage site of the human immunodeficiency virus type 1 glycoprotein: requirement of precursor cleavage for glycoprotein incorporation. J. Virol. 1995, 69(8):4675-4682.
    • (1995) J. Virol. , vol.69 , Issue.8 , pp. 4675-4682
    • Dubay, J.W.1    Dubay, S.R.2    Shin, H.J.3    Hunter, E.4
  • 9
    • 0018375906 scopus 로고
    • Cell surface expression of the env gene polyprotein of dual-tropic mink cell focus-forming murine leukemia virus
    • Famulari N.G., Jelalian K. Cell surface expression of the env gene polyprotein of dual-tropic mink cell focus-forming murine leukemia virus. J. Virol. 1979, 30(3):720-728.
    • (1979) J. Virol. , vol.30 , Issue.3 , pp. 720-728
    • Famulari, N.G.1    Jelalian, K.2
  • 11
    • 0023199650 scopus 로고
    • The role of envelope glycoprotein processing in murine leukemia virus infection
    • Freed E.O., Risser R. The role of envelope glycoprotein processing in murine leukemia virus infection. J. Virol. 1987, 61(9):2852-2856.
    • (1987) J. Virol. , vol.61 , Issue.9 , pp. 2852-2856
    • Freed, E.O.1    Risser, R.2
  • 12
    • 0024435050 scopus 로고
    • Mutational analysis of the cleavage sequence of the human immunodeficiency virus type 1 envelope glycoprotein precursor gp160
    • Freed E.O., Myers D.J., Risser R. Mutational analysis of the cleavage sequence of the human immunodeficiency virus type 1 envelope glycoprotein precursor gp160. J. Virol. 1989, 63(11):4670-4675.
    • (1989) J. Virol. , vol.63 , Issue.11 , pp. 4670-4675
    • Freed, E.O.1    Myers, D.J.2    Risser, R.3
  • 13
    • 35548998677 scopus 로고    scopus 로고
    • Ecotropic murine leukemia virus envelope protein affects interaction of cationic amino acid transporter 1 with clathrin adaptor protein complexes, leading to receptor downregulation
    • Fujisawa R., Masuda M. Ecotropic murine leukemia virus envelope protein affects interaction of cationic amino acid transporter 1 with clathrin adaptor protein complexes, leading to receptor downregulation. Virology 2007, 368(2):342-350.
    • (2007) Virology , vol.368 , Issue.2 , pp. 342-350
    • Fujisawa, R.1    Masuda, M.2
  • 14
    • 0027400392 scopus 로고
    • Trafficking of wild-type and an endoproteolytic-site mutant of the mouse mammary tumor virus glycoprotein
    • Goodman L.J., Kain S.R., Firestone G.L. Trafficking of wild-type and an endoproteolytic-site mutant of the mouse mammary tumor virus glycoprotein. J. Biol. Chem. 1993, 268(4):2329-2336.
    • (1993) J. Biol. Chem. , vol.268 , Issue.4 , pp. 2329-2336
    • Goodman, L.J.1    Kain, S.R.2    Firestone, G.L.3
  • 15
    • 0025739863 scopus 로고
    • Analysis of mutations in the envelope gene of Moloney murine leukemia virus: separation of infectivity from superinfection resistance
    • Granowitz C., Colicelli J., Goff S.P. Analysis of mutations in the envelope gene of Moloney murine leukemia virus: separation of infectivity from superinfection resistance. Virology 1991, 183(2):545-554.
    • (1991) Virology , vol.183 , Issue.2 , pp. 545-554
    • Granowitz, C.1    Colicelli, J.2    Goff, S.P.3
  • 17
    • 0021690345 scopus 로고
    • Quantitative separation of murine leukemia virus proteins by reversed-phase high-pressure liquid chromatography reveals newly described gag and env cleavage products
    • Henderson L.E., Sowder R., Copeland T.D., Smythers G., Oroszlan S. Quantitative separation of murine leukemia virus proteins by reversed-phase high-pressure liquid chromatography reveals newly described gag and env cleavage products. J. Virol. 1984, 52(2):492-500.
    • (1984) J. Virol. , vol.52 , Issue.2 , pp. 492-500
    • Henderson, L.E.1    Sowder, R.2    Copeland, T.D.3    Smythers, G.4    Oroszlan, S.5
  • 19
    • 9644281041 scopus 로고    scopus 로고
    • Proprotein convertase models based on the crystal structures of furin and kexin: explanation of their specificity
    • Henrich S., Lindberg I., Bode W., Than M.E. Proprotein convertase models based on the crystal structures of furin and kexin: explanation of their specificity. J. Mol. Biol. 2005, 345(2):211-227.
    • (2005) J. Mol. Biol. , vol.345 , Issue.2 , pp. 211-227
    • Henrich, S.1    Lindberg, I.2    Bode, W.3    Than, M.E.4
  • 20
    • 20644433322 scopus 로고    scopus 로고
    • The impact of envelope glycoprotein cleavage on the antigenicity, infectivity, and neutralization sensitivity of Env-pseudotyped human immunodeficiency virus type 1 particles
    • Herrera C., Klasse P.J., Michael E., Kake S., Barnes K., Kibler C.W., Campbell-Gardener L., Si Z., Sodroski J., Moore J.P., Beddows S. The impact of envelope glycoprotein cleavage on the antigenicity, infectivity, and neutralization sensitivity of Env-pseudotyped human immunodeficiency virus type 1 particles. Virology 2005, 338(1):154-172.
    • (2005) Virology , vol.338 , Issue.1 , pp. 154-172
    • Herrera, C.1    Klasse, P.J.2    Michael, E.3    Kake, S.4    Barnes, K.5    Kibler, C.W.6    Campbell-Gardener, L.7    Si, Z.8    Sodroski, J.9    Moore, J.P.10    Beddows, S.11
  • 21
    • 0030952367 scopus 로고    scopus 로고
    • Functional analysis of the cytoplasmic tail of Moloney murine leukemia virus envelope protein
    • Januszeski M., Cannon P., Chen D., Rozenberg Y., Anderson W. Functional analysis of the cytoplasmic tail of Moloney murine leukemia virus envelope protein. J. Virol. 1997, 71(5):3613-3619.
    • (1997) J. Virol. , vol.71 , Issue.5 , pp. 3613-3619
    • Januszeski, M.1    Cannon, P.2    Chen, D.3    Rozenberg, Y.4    Anderson, W.5
  • 22
    • 0026075572 scopus 로고
    • Oligomerization and transport of the envelope protein of Moloney murine leukemia virus-TB and of ts1, a neurovirulent temperature-sensitive mutant of MoMuLV-TB
    • Kamps C.A., Lin Y.C., Wong P.K. Oligomerization and transport of the envelope protein of Moloney murine leukemia virus-TB and of ts1, a neurovirulent temperature-sensitive mutant of MoMuLV-TB. Virology 1991, 184(2):687-694.
    • (1991) Virology , vol.184 , Issue.2 , pp. 687-694
    • Kamps, C.A.1    Lin, Y.C.2    Wong, P.K.3
  • 23
    • 0025944961 scopus 로고
    • Mutational analysis of N-linked glycosylation sites of friend murine leukemia virus envelope protein
    • Kayman S.C., Kopelman R., Projan S., Kinney D.M., Pinter A. Mutational analysis of N-linked glycosylation sites of friend murine leukemia virus envelope protein. J. Virol. 1991, 65(10):5323-5332.
    • (1991) J. Virol. , vol.65 , Issue.10 , pp. 5323-5332
    • Kayman, S.C.1    Kopelman, R.2    Projan, S.3    Kinney, D.M.4    Pinter, A.5
  • 24
  • 26
    • 0042167361 scopus 로고    scopus 로고
    • Mutational analysis of the R peptide cleavage site of Moloney murine leukaemia virus envelope protein
    • Kubo Y., Amanuma H. Mutational analysis of the R peptide cleavage site of Moloney murine leukaemia virus envelope protein. J. Gen. Virol. 2003, 84(8):2253-2257.
    • (2003) J. Gen. Virol. , vol.84 , Issue.8 , pp. 2253-2257
    • Kubo, Y.1    Amanuma, H.2
  • 27
    • 36749036754 scopus 로고    scopus 로고
    • Characterization of R peptide of murine leukemia virus envelope glycoproteins in syncytia formation and entry
    • Kubo Y., Tominaga C., Yoshii H., Kamiyama H., Mitani C., Amanuma H., Yamamoto N. Characterization of R peptide of murine leukemia virus envelope glycoproteins in syncytia formation and entry. Arch. Virol. 2007, 152(12):2169-2182.
    • (2007) Arch. Virol. , vol.152 , Issue.12 , pp. 2169-2182
    • Kubo, Y.1    Tominaga, C.2    Yoshii, H.3    Kamiyama, H.4    Mitani, C.5    Amanuma, H.6    Yamamoto, N.7
  • 28
    • 1842294027 scopus 로고    scopus 로고
    • The critical N-linked glycan of murine leukemia virus envelope protein promotes both folding of the C-terminal domains of the precursor polyprotein and stability of the postcleavage envelope complex
    • Li Z., Pinter A., Kayman S. The critical N-linked glycan of murine leukemia virus envelope protein promotes both folding of the C-terminal domains of the precursor polyprotein and stability of the postcleavage envelope complex. J. Virol. 1997, 71(9):7012-7019.
    • (1997) J. Virol. , vol.71 , Issue.9 , pp. 7012-7019
    • Li, Z.1    Pinter, A.2    Kayman, S.3
  • 29
    • 0020353193 scopus 로고
    • Role of partial proteolysis in processing murine leukemia virus membrane envelope glycoproteins to the cell surface. A viral mutant with uncleaved glycoprotein
    • Machida C.A., Kabat D. Role of partial proteolysis in processing murine leukemia virus membrane envelope glycoproteins to the cell surface. A viral mutant with uncleaved glycoprotein. J. Biol. Chem. 1982, 257(23):14018-14022.
    • (1982) J. Biol. Chem. , vol.257 , Issue.23 , pp. 14018-14022
    • Machida, C.A.1    Kabat, D.2
  • 30
    • 0023921610 scopus 로고
    • Endoproteolytic cleavage of gp160 is required for the activation of human immunodeficiency virus
    • McCune J.M., Rabin L.B., Feinberg M.B., Lieberman M., Kosek J.C., Reyes G.R., Weissman I.L. Endoproteolytic cleavage of gp160 is required for the activation of human immunodeficiency virus. Cell 1988, 53(1):55-67.
    • (1988) Cell , vol.53 , Issue.1 , pp. 55-67
    • McCune, J.M.1    Rabin, L.B.2    Feinberg, M.B.3    Lieberman, M.4    Kosek, J.C.5    Reyes, G.R.6    Weissman, I.L.7
  • 31
    • 0031927203 scopus 로고    scopus 로고
    • Moloney murine leukemia virus envelope protein subunits, gp70 and Pr15E, form a stable disulfide-linked complex
    • Opstelten D.J., Wallin M., Garoff H. Moloney murine leukemia virus envelope protein subunits, gp70 and Pr15E, form a stable disulfide-linked complex. J. Virol. 1998, 72(8):6537-6545.
    • (1998) J. Virol. , vol.72 , Issue.8 , pp. 6537-6545
    • Opstelten, D.J.1    Wallin, M.2    Garoff, H.3
  • 32
    • 0029862497 scopus 로고    scopus 로고
    • A stable human-derived packaging cell line for production of high titer retrovirus/vesicular stomatitis virus G pseudotypes
    • Ory D.S., Neugeboren B.A., Mulligan R.C. A stable human-derived packaging cell line for production of high titer retrovirus/vesicular stomatitis virus G pseudotypes. Proc. Natl. Acad. Sci. U. S. A. 1996, 93(21):11400-11406.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , Issue.21 , pp. 11400-11406
    • Ory, D.S.1    Neugeboren, B.A.2    Mulligan, R.C.3
  • 33
    • 0023213323 scopus 로고
    • Mutations within the proteolytic cleavage site of the Rous sarcoma virus glycoprotein that block processing to gp85 and gp37
    • Perez L.G., Hunter E. Mutations within the proteolytic cleavage site of the Rous sarcoma virus glycoprotein that block processing to gp85 and gp37. J. Virol. 1987, 61(5):1609-1614.
    • (1987) J. Virol. , vol.61 , Issue.5 , pp. 1609-1614
    • Perez, L.G.1    Hunter, E.2
  • 34
    • 0017719251 scopus 로고
    • The presence of disulfide-linked gp70-p15(E) complexes in AKR murine leukemia virus
    • Pinter A., Fleissner E. The presence of disulfide-linked gp70-p15(E) complexes in AKR murine leukemia virus. Virology 1977, 83(2):417-422.
    • (1977) Virology , vol.83 , Issue.2 , pp. 417-422
    • Pinter, A.1    Fleissner, E.2
  • 35
    • 0030842622 scopus 로고    scopus 로고
    • Localization of the labile disulfide bond between SU and TM of the murine leukemia virus envelope protein complex to a highly conserved CWLC motif in SU that resembles the active-site sequence of thiol- disulfide exchange enzymes
    • Pinter A., Kopelman R., Li Z., Kayman S., Sanders D. Localization of the labile disulfide bond between SU and TM of the murine leukemia virus envelope protein complex to a highly conserved CWLC motif in SU that resembles the active-site sequence of thiol- disulfide exchange enzymes. J. Virol. 1997, 71(10):8073-8077.
    • (1997) J. Virol. , vol.71 , Issue.10 , pp. 8073-8077
    • Pinter, A.1    Kopelman, R.2    Li, Z.3    Kayman, S.4    Sanders, D.5
  • 36
    • 0028271720 scopus 로고
    • PH-independent murine leukemia virus ecotropic envelope-mediated cell fusion: implications for the role of the R peptide and p12E TM in viral entry
    • Ragheb J.A., Anderson W.F. pH-independent murine leukemia virus ecotropic envelope-mediated cell fusion: implications for the role of the R peptide and p12E TM in viral entry. J. Virol. 1994, 68(5):3220-3231.
    • (1994) J. Virol. , vol.68 , Issue.5 , pp. 3220-3231
    • Ragheb, J.A.1    Anderson, W.F.2
  • 37
    • 0028047579 scopus 로고
    • Function of the cytoplasmic domain of a retroviral transmembrane protein: p15E-p2E cleavage activates the membrane fusion capability of the murine leukemia virus Env protein
    • Rein A., Mirro J., Haynes J.G., Ernst S.M., Nagashima K. Function of the cytoplasmic domain of a retroviral transmembrane protein: p15E-p2E cleavage activates the membrane fusion capability of the murine leukemia virus Env protein. J. Virol. 1994, 68(3):1773-1781.
    • (1994) J. Virol. , vol.68 , Issue.3 , pp. 1773-1781
    • Rein, A.1    Mirro, J.2    Haynes, J.G.3    Ernst, S.M.4    Nagashima, K.5
  • 39
    • 0032502065 scopus 로고    scopus 로고
    • Interplay between S1 and S4 Subsites in Kex2 protease: Kex2 exhibits dual specificity for the P4 side chain
    • Rockwell N.C., Fuller R.S. Interplay between S1 and S4 Subsites in Kex2 protease: Kex2 exhibits dual specificity for the P4 side chain. Biochemistry 1998, 37(10):3386-3391.
    • (1998) Biochemistry , vol.37 , Issue.10 , pp. 3386-3391
    • Rockwell, N.C.1    Fuller, R.S.2
  • 40
    • 0037124085 scopus 로고    scopus 로고
    • Specific modulation of Kex2/furin family proteases by potassium
    • Rockwell N.C., Fuller R.S. Specific modulation of Kex2/furin family proteases by potassium. J. Biol. Chem. 2002, 277(20):17531-17537.
    • (2002) J. Biol. Chem. , vol.277 , Issue.20 , pp. 17531-17537
    • Rockwell, N.C.1    Fuller, R.S.2
  • 41
    • 0442292293 scopus 로고    scopus 로고
    • The kindest cuts of all: crystal structures of Kex2 and furin reveal secrets of precursor processing
    • Rockwell N.C., Thorner J.W. The kindest cuts of all: crystal structures of Kex2 and furin reveal secrets of precursor processing. Trends Biochem. Sci. 2004, 29(2):80-87.
    • (2004) Trends Biochem. Sci. , vol.29 , Issue.2 , pp. 80-87
    • Rockwell, N.C.1    Thorner, J.W.2
  • 43
    • 0033658703 scopus 로고    scopus 로고
    • Sulfhydryl involvement in fusion mechanisms
    • Kluwe Academic/Plenum Publishers, New York, H. Hilderson, S. Fuller (Eds.)
    • Sanders D.A. Sulfhydryl involvement in fusion mechanisms. Fusion of Biological Membranes and Related Problems 2000, 483-514. Kluwe Academic/Plenum Publishers, New York. H. Hilderson, S. Fuller (Eds.).
    • (2000) Fusion of Biological Membranes and Related Problems , pp. 483-514
    • Sanders, D.A.1
  • 44
    • 33644862821 scopus 로고    scopus 로고
    • Intracellular versus cell surface assembly of retroviral pseudotypes is determined by the cellular localization of the viral glycoprotein, its capacity to interact with Gag, and the expression of the Nef protein
    • Sandrin V., Cosset F.L. Intracellular versus cell surface assembly of retroviral pseudotypes is determined by the cellular localization of the viral glycoprotein, its capacity to interact with Gag, and the expression of the Nef protein. J. Biol. Chem. 2006, 281(1):528-542.
    • (2006) J. Biol. Chem. , vol.281 , Issue.1 , pp. 528-542
    • Sandrin, V.1    Cosset, F.L.2
  • 45
    • 0036893450 scopus 로고    scopus 로고
    • The furin inhibitor hexa-d-arginine blocks the activation of pseudomonas aeruginosa exotoxin a in vivo
    • Sarac M.S., Cameron A., Lindberg I. The furin inhibitor hexa-d-arginine blocks the activation of pseudomonas aeruginosa exotoxin a in vivo. Infect. Immun. 2002, 70(12):7136-7139.
    • (2002) Infect. Immun. , vol.70 , Issue.12 , pp. 7136-7139
    • Sarac, M.S.1    Cameron, A.2    Lindberg, I.3
  • 46
    • 0014405092 scopus 로고
    • On the active site of proteases. 3. Mapping the active site of papain; specific peptide inhibitors of papain
    • Schechter I., Berger A. On the active site of proteases. 3. Mapping the active site of papain; specific peptide inhibitors of papain. Biochem. Biophys. Res. Commun. 1968, 32:898-902.
    • (1968) Biochem. Biophys. Res. Commun. , vol.32 , pp. 898-902
    • Schechter, I.1    Berger, A.2
  • 47
    • 0021806159 scopus 로고
    • Maturation of murine leukemia virus env proteins in the absence of other viral proteins
    • Schultz A., Rein A. Maturation of murine leukemia virus env proteins in the absence of other viral proteins. Virology 1985, 145(2):335-339.
    • (1985) Virology , vol.145 , Issue.2 , pp. 335-339
    • Schultz, A.1    Rein, A.2
  • 48
    • 0035123812 scopus 로고    scopus 로고
    • Ross River virus glycoprotein-pseudotyped retroviruses and stable cell lines for their production
    • Sharkey C.M., North C.L., Kuhn R.J., Sanders D.A. Ross River virus glycoprotein-pseudotyped retroviruses and stable cell lines for their production. J. Virol. 2001, 75(6):2653-2659.
    • (2001) J. Virol. , vol.75 , Issue.6 , pp. 2653-2659
    • Sharkey, C.M.1    North, C.L.2    Kuhn, R.J.3    Sanders, D.A.4
  • 49
    • 0019856424 scopus 로고
    • Nucleotide sequence of Moloney murine leukaemia virus
    • Shinnick T.M., Lerner R.A., Sutcliffe J.G. Nucleotide sequence of Moloney murine leukaemia virus. Nature 1981, 293(5833):543-548.
    • (1981) Nature , vol.293 , Issue.5833 , pp. 543-548
    • Shinnick, T.M.1    Lerner, R.A.2    Sutcliffe, J.G.3
  • 50
    • 0013939318 scopus 로고
    • The mechanism of interference between an avian leukosis virus and Rous sarcoma virus. I. Establishment of interference. The mechanism of interference between an avian leukosis virus and Rous sarcoma virus. II. Early steps of infection by RSV of cells under conditions of interference
    • Steck F.T., Rubin H. The mechanism of interference between an avian leukosis virus and Rous sarcoma virus. I. Establishment of interference. The mechanism of interference between an avian leukosis virus and Rous sarcoma virus. II. Early steps of infection by RSV of cells under conditions of interference. Virology 1966, 29(4):628-641.
    • (1966) Virology , vol.29 , Issue.4 , pp. 628-641
    • Steck, F.T.1    Rubin, H.2
  • 51
    • 0030827587 scopus 로고    scopus 로고
    • Variable regions A and B in the envelope glycoproteins of feline leukemia virus subgroup B and amphotropic murine leukemia virus interact with discrete receptor domains
    • Tailor C., Kabat D. Variable regions A and B in the envelope glycoproteins of feline leukemia virus subgroup B and amphotropic murine leukemia virus interact with discrete receptor domains. J. Virol. 1997, 71(12):9383-9391.
    • (1997) J. Virol. , vol.71 , Issue.12 , pp. 9383-9391
    • Tailor, C.1    Kabat, D.2
  • 52
    • 0032865298 scopus 로고    scopus 로고
    • The role of the membrane-spanning domain sequence in glycoprotein-mediated membrane fusion
    • Taylor G.M., Sanders D.A. The role of the membrane-spanning domain sequence in glycoprotein-mediated membrane fusion. Mol. Biol. Cell 1999, 10(9):2803-2815.
    • (1999) Mol. Biol. Cell , vol.10 , Issue.9 , pp. 2803-2815
    • Taylor, G.M.1    Sanders, D.A.2
  • 53
    • 0043064053 scopus 로고    scopus 로고
    • Structural criteria for regulation of membrane fusion and virion incorporation by the murine leukemia virus TM cytoplasmic domain
    • Taylor G.M., Sanders D.A. Structural criteria for regulation of membrane fusion and virion incorporation by the murine leukemia virus TM cytoplasmic domain. Virology 2003, 312(2):295-305.
    • (2003) Virology , vol.312 , Issue.2 , pp. 295-305
    • Taylor, G.M.1    Sanders, D.A.2
  • 54
    • 0025734320 scopus 로고
    • Cell-surface receptor for ecotropic murine retroviruses is a basic amino-acid transporter
    • Wang H., Kavanaugh M.P., North R.A., Kabat D. Cell-surface receptor for ecotropic murine retroviruses is a basic amino-acid transporter. Nature 1991, 352(6337):729-731.
    • (1991) Nature , vol.352 , Issue.6337 , pp. 729-731
    • Wang, H.1    Kavanaugh, M.P.2    North, R.A.3    Kabat, D.4
  • 55
    • 0028960688 scopus 로고
    • Engineered serine protease inhibitor prevents furin-catalyzed activation of the fusion glycoprotein and production of infectious measles virus
    • Watanabe M., Hirano A., Stenglein S., Nelson J., Thomas G., Wong T.C. Engineered serine protease inhibitor prevents furin-catalyzed activation of the fusion glycoprotein and production of infectious measles virus. J. Virol. 1995, 69(5):3206-3210.
    • (1995) J. Virol. , vol.69 , Issue.5 , pp. 3206-3210
    • Watanabe, M.1    Hirano, A.2    Stenglein, S.3    Nelson, J.4    Thomas, G.5    Wong, T.C.6
  • 56
    • 0018390929 scopus 로고
    • Structure of the murine leukemia virus envelope glycoprotein precursor
    • Witte O.N., Wirth D.F. Structure of the murine leukemia virus envelope glycoprotein precursor. J. Virol. 1979, 29(2):735-743.
    • (1979) J. Virol. , vol.29 , Issue.2 , pp. 735-743
    • Witte, O.N.1    Wirth, D.F.2
  • 57
    • 0017359935 scopus 로고
    • Cellular maturation of oncornavirus glycoproteins: topological arrangement of precursor and product forms in cellular membranes
    • Witte O.N., Tsukamoto-Adey A., Weissman I.L. Cellular maturation of oncornavirus glycoproteins: topological arrangement of precursor and product forms in cellular membranes. Virology 1977, 76(2):539-553.
    • (1977) Virology , vol.76 , Issue.2 , pp. 539-553
    • Witte, O.N.1    Tsukamoto-Adey, A.2    Weissman, I.L.3
  • 58
    • 0032989259 scopus 로고    scopus 로고
    • Failure to cleave murine leukemia virus envelope protein does not preclude its incorporation in virions and productive virus-receptor interaction
    • Zavorotinskaya T., Albritton L.M. Failure to cleave murine leukemia virus envelope protein does not preclude its incorporation in virions and productive virus-receptor interaction. J. Virol. 1999, 73(7):5621-5629.
    • (1999) J. Virol. , vol.73 , Issue.7 , pp. 5621-5629
    • Zavorotinskaya, T.1    Albritton, L.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.