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Volumn 9, Issue 5, 2013, Pages

A Unique Spumavirus Gag N-terminal Domain with Functional Properties of Orthoretroviral Matrix and Capsid

Author keywords

[No Author keywords available]

Indexed keywords

MATRIX PROTEIN;

EID: 84878404212     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1003376     Document Type: Article
Times cited : (30)

References (104)
  • 1
    • 0343183220 scopus 로고    scopus 로고
    • Foamy viruses: between retroviruses and pararetroviruses
    • Lecellier CH, Saib A, (2000) Foamy viruses: between retroviruses and pararetroviruses. Virology 271: 1-8.
    • (2000) Virology , vol.271 , pp. 1-8
    • Lecellier, C.H.1    Saib, A.2
  • 2
    • 0028360748 scopus 로고
    • Isolation, cloning, and sequencing of simian foamy viruses from chimpanzees (SFVcpz): high homology to human foamy virus (HFV)
    • Herchenroder O, Renne R, Loncar D, Cobb EK, Murthy KK, et al. (1994) Isolation, cloning, and sequencing of simian foamy viruses from chimpanzees (SFVcpz): high homology to human foamy virus (HFV). Virology 201: 187-199.
    • (1994) Virology , vol.201 , pp. 187-199
    • Herchenroder, O.1    Renne, R.2    Loncar, D.3    Cobb, E.K.4    Murthy, K.K.5
  • 3
    • 0028952573 scopus 로고
    • A comparative study of higher primate foamy viruses, including a new virus from a gorilla
    • Bieniasz PD, Rethwilm A, Pitman R, Daniel MD, Chrystie I, et al. (1995) A comparative study of higher primate foamy viruses, including a new virus from a gorilla. Virology 207: 217-228.
    • (1995) Virology , vol.207 , pp. 217-228
    • Bieniasz, P.D.1    Rethwilm, A.2    Pitman, R.3    Daniel, M.D.4    Chrystie, I.5
  • 5
    • 0038247806 scopus 로고    scopus 로고
    • Non-primate foamy viruses
    • Saib A, (2003) Non-primate foamy viruses. Curr Top Microbiol Immunol 277: 197-211.
    • (2003) Curr Top Microbiol Immunol , vol.277 , pp. 197-211
    • Saib, A.1
  • 6
    • 0014686678 scopus 로고
    • Syncytium-forming agent isolated from domestic cats
    • Riggs JL, Oshirls, Taylor DO, Lennette EH, (1969) Syncytium-forming agent isolated from domestic cats. Nature 222: 1190-1191.
    • (1969) Nature , vol.222 , pp. 1190-1191
    • Riggs, J.L.1    Oshirls, T.D.O.2    Lennette, E.H.3
  • 7
    • 0014581998 scopus 로고
    • Feline viruses. XI. Isolation of a virus similar to a myxovirus from cats in which urolithiasis was experimentally induced
    • Fabricant CG, Rich LJ, Gillespie JH, (1969) Feline viruses. XI. Isolation of a virus similar to a myxovirus from cats in which urolithiasis was experimentally induced. The Cornell veterinarian 59: 667-672.
    • (1969) The Cornell Veterinarian , vol.59 , pp. 667-672
    • Fabricant, C.G.1    Rich, L.J.2    Gillespie, J.H.3
  • 8
    • 0014444317 scopus 로고
    • Isolation, immunodiffusion, immunofluorescence, and electron microscopy of a syncytial virus of lymphosarcomatous and apparently normal cattle
    • Malmquist WA, Van der Maaten MJ, Boothe AD, (1969) Isolation, immunodiffusion, immunofluorescence, and electron microscopy of a syncytial virus of lymphosarcomatous and apparently normal cattle. Cancer research 29: 188-200.
    • (1969) Cancer Research , vol.29 , pp. 188-200
    • Malmquist, W.A.1    van der Maaten, M.J.2    Boothe, A.D.3
  • 10
    • 0026863058 scopus 로고
    • Isolation of a spumavirus from a sheep
    • Flanagan M, (1992) Isolation of a spumavirus from a sheep. Australian veterinary journal 69: 112-113.
    • (1992) Australian Veterinary Journal , vol.69 , pp. 112-113
    • Flanagan, M.1
  • 12
    • 84863764579 scopus 로고    scopus 로고
    • An endogenous foamy virus in the aye-aye (Daubentonia madagascariensis)
    • Han GZ, Worobey M, (2012) An endogenous foamy virus in the aye-aye (Daubentonia madagascariensis). Journal of virology 86: 7696-7698.
    • (2012) Journal of Virology , vol.86 , pp. 7696-7698
    • Han, G.Z.1    Worobey, M.2
  • 13
    • 84864075474 scopus 로고    scopus 로고
    • An endogenous foamy-like viral element in the coelacanth genome
    • Han GZ, Worobey M, (2012) An endogenous foamy-like viral element in the coelacanth genome. PLoS pathogens 8: e1002790.
    • (2012) PLoS Pathogens , vol.8
    • Han, G.Z.1    Worobey, M.2
  • 14
    • 12144291413 scopus 로고    scopus 로고
    • Frequent simian foamy virus infection in persons occupationally exposed to nonhuman primates
    • Switzer WM, Bhullar V, Shanmugam V, Cong ME, Parekh B, et al. (2004) Frequent simian foamy virus infection in persons occupationally exposed to nonhuman primates. J Virol 78: 2780-2789.
    • (2004) J Virol , vol.78 , pp. 2780-2789
    • Switzer, W.M.1    Bhullar, V.2    Shanmugam, V.3    Cong, M.E.4    Parekh, B.5
  • 16
    • 0029590165 scopus 로고
    • Infectious proviral clones of chimpanzee foamy virus (SFVcpz) generated by long PCR reveal close functional relatedness to human foamy virus
    • Herchenroder O, Turek R, Neumann-Haefelin D, Rethwilm A, Schneider J, (1995) Infectious proviral clones of chimpanzee foamy virus (SFVcpz) generated by long PCR reveal close functional relatedness to human foamy virus. Virology 214: 685-689.
    • (1995) Virology , vol.214 , pp. 685-689
    • Herchenroder, O.1    Turek, R.2    Neumann-Haefelin, D.3    Rethwilm, A.4    Schneider, J.5
  • 18
    • 3242730340 scopus 로고    scopus 로고
    • Simian retroviral infections in human beings
    • author reply 139-140
    • Epstein MA, (2004) Simian retroviral infections in human beings. Lancet 364: 138-139; author reply 139-140.
    • (2004) Lancet , vol.364 , pp. 138-139
    • Epstein, M.A.1
  • 19
    • 77955552114 scopus 로고    scopus 로고
    • Molecular biology of foamy viruses
    • Rethwilm A, (2010) Molecular biology of foamy viruses. Med Microbiol Immunol 199: 197-207.
    • (2010) Med Microbiol Immunol , vol.199 , pp. 197-207
    • Rethwilm, A.1
  • 20
    • 0035134159 scopus 로고    scopus 로고
    • Historical perspective of foamy virus epidemiology and infection
    • Meiering CD, Linial ML, (2001) Historical perspective of foamy virus epidemiology and infection. Clin Microbiol Rev 14: 165-176.
    • (2001) Clin Microbiol Rev , vol.14 , pp. 165-176
    • Meiering, C.D.1    Linial, M.L.2
  • 21
    • 44949158024 scopus 로고    scopus 로고
    • Replication in a superficial epithelial cell niche explains the lack of pathogenicity of primate foamy virus infections
    • Murray SM, Picker LJ, Axthelm MK, Hudkins K, Alpers CE, et al. (2008) Replication in a superficial epithelial cell niche explains the lack of pathogenicity of primate foamy virus infections. J Virol 82: 5981-5985.
    • (2008) J Virol , vol.82 , pp. 5981-5985
    • Murray, S.M.1    Picker, L.J.2    Axthelm, M.K.3    Hudkins, K.4    Alpers, C.E.5
  • 22
    • 33745963002 scopus 로고    scopus 로고
    • Foamy virus infection in primates
    • Murray SM, Linial ML, (2006) Foamy virus infection in primates. J Med Primatol 35: 225-235.
    • (2006) J Med Primatol , vol.35 , pp. 225-235
    • Murray, S.M.1    Linial, M.L.2
  • 23
    • 79957814289 scopus 로고    scopus 로고
    • Foamy virus biology and its application for vector development
    • Lindemann D, Rethwilm A, (2011) Foamy virus biology and its application for vector development. Viruses 3: 561-585.
    • (2011) Viruses , vol.3 , pp. 561-585
    • Lindemann, D.1    Rethwilm, A.2
  • 24
    • 0029869049 scopus 로고    scopus 로고
    • Human foamy virus replication: a pathway distinct from that of retroviruses and hepadnaviruses
    • Yu SF, Baldwin DN, Gwynn SR, Yendapalli S, Linial ML, (1996) Human foamy virus replication: a pathway distinct from that of retroviruses and hepadnaviruses. Science 271: 1579-1582.
    • (1996) Science , vol.271 , pp. 1579-1582
    • Yu, S.F.1    Baldwin, D.N.2    Gwynn, S.R.3    Yendapalli, S.4    Linial, M.L.5
  • 25
    • 0030768753 scopus 로고    scopus 로고
    • Human foamy virus reverse transcription that occurs late in the viral replication cycle
    • Moebes A, Enssle J, Bieniasz PD, Heinkelein M, Lindemann D, et al. (1997) Human foamy virus reverse transcription that occurs late in the viral replication cycle. J Virol 71: 7305-7311.
    • (1997) J Virol , vol.71 , pp. 7305-7311
    • Moebes, A.1    Enssle, J.2    Bieniasz, P.D.3    Heinkelein, M.4    Lindemann, D.5
  • 26
    • 0030053661 scopus 로고    scopus 로고
    • The human foamy virus pol gene is expressed as a Pro-Pol polyprotein and not as a Gag-Pol fusion protein
    • Löchelt M, Flügel RM, (1996) The human foamy virus pol gene is expressed as a Pro-Pol polyprotein and not as a Gag-Pol fusion protein. J Virol 70: 1033-1040.
    • (1996) J Virol , vol.70 , pp. 1033-1040
    • Löchelt, M.1    Flügel, R.M.2
  • 27
    • 0029961656 scopus 로고    scopus 로고
    • Foamy virus reverse transcriptase is expressed independently from the Gag protein
    • Enssle J, Jordan I, Mauer B, Rethwilm A, (1996) Foamy virus reverse transcriptase is expressed independently from the Gag protein. Proc Natl Acad Sci U S A 93: 4137-4141.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 4137-4141
    • Enssle, J.1    Jordan, I.2    Mauer, B.3    Rethwilm, A.4
  • 28
    • 0038586451 scopus 로고    scopus 로고
    • Proteolytic processing of foamy virus Gag and Pol proteins
    • Flügel RM, Pfrepper KI, (2003) Proteolytic processing of foamy virus Gag and Pol proteins. Curr Top Microbiol Immunol 277: 63-88.
    • (2003) Curr Top Microbiol Immunol , vol.277 , pp. 63-88
    • Flügel, R.M.1    Pfrepper, K.I.2
  • 29
    • 0034864546 scopus 로고    scopus 로고
    • Specific interaction of a novel foamy virus Env leader protein with the N-terminal Gag domain
    • Wilk T, Geiselhart V, Frech M, Fuller SD, Flugel RM, et al. (2001) Specific interaction of a novel foamy virus Env leader protein with the N-terminal Gag domain. J Virol 75: 7995-8007.
    • (2001) J Virol , vol.75 , pp. 7995-8007
    • Wilk, T.1    Geiselhart, V.2    Frech, M.3    Fuller, S.D.4    Flugel, R.M.5
  • 30
    • 0032976195 scopus 로고    scopus 로고
    • Foamy virus capsids require the cognate envelope protein for particle export
    • Pietschmann T, Heinkelein M, Heldmann M, Zentgraf H, Rethwilm A, et al. (1999) Foamy virus capsids require the cognate envelope protein for particle export. J Virol 73: 2613-2621.
    • (1999) J Virol , vol.73 , pp. 2613-2621
    • Pietschmann, T.1    Heinkelein, M.2    Heldmann, M.3    Zentgraf, H.4    Rethwilm, A.5
  • 31
    • 0034977944 scopus 로고    scopus 로고
    • A particle-associated glycoprotein signal peptide essential for virus maturation and infectivity
    • Lindemann D, Pietschmann T, Picard-Maureau M, Berg A, Heinkelein M, et al. (2001) A particle-associated glycoprotein signal peptide essential for virus maturation and infectivity. J Virol 75: 5762-5771.
    • (2001) J Virol , vol.75 , pp. 5762-5771
    • Lindemann, D.1    Pietschmann, T.2    Picard-Maureau, M.3    Berg, A.4    Heinkelein, M.5
  • 32
    • 0141717669 scopus 로고    scopus 로고
    • The M-PMV cytoplasmic targeting-retention signal directs nascent Gag polypeptides to a pericentriolar region of the cell
    • Sfakianos JN, LaCasse RA, Hunter E, (2003) The M-PMV cytoplasmic targeting-retention signal directs nascent Gag polypeptides to a pericentriolar region of the cell. Traffic 4: 660-670.
    • (2003) Traffic , vol.4 , pp. 660-670
    • Sfakianos, J.N.1    LaCasse, R.A.2    Hunter, E.3
  • 33
    • 33745753571 scopus 로고    scopus 로고
    • Foamy virus capsid assembly occurs at a pericentriolar region through a cytoplasmic targeting/retention signal in Gag
    • Yu SF, Eastman SW, Linial ML, (2006) Foamy virus capsid assembly occurs at a pericentriolar region through a cytoplasmic targeting/retention signal in Gag. Traffic 7: 966-977.
    • (2006) Traffic , vol.7 , pp. 966-977
    • Yu, S.F.1    Eastman, S.W.2    Linial, M.L.3
  • 34
    • 0034947737 scopus 로고    scopus 로고
    • Identification of a conserved residue of foamy virus Gag required for intracellular capsid assembly
    • Eastman SW, Linial ML, (2001) Identification of a conserved residue of foamy virus Gag required for intracellular capsid assembly. J Virol 75: 6857-6864.
    • (2001) J Virol , vol.75 , pp. 6857-6864
    • Eastman, S.W.1    Linial, M.L.2
  • 35
    • 77950497956 scopus 로고    scopus 로고
    • Species-specific inhibition of foamy viruses from South American monkeys by New World Monkey TRIM5{alpha} proteins
    • Pacheco B, Finzi A, McGee-Estrada K, Sodroski J, (2010) Species-specific inhibition of foamy viruses from South American monkeys by New World Monkey TRIM5{alpha} proteins. J Virol 84: 4095-4099.
    • (2010) J Virol , vol.84 , pp. 4095-4099
    • Pacheco, B.1    Finzi, A.2    McGee-Estrada, K.3    Sodroski, J.4
  • 36
    • 43949086202 scopus 로고    scopus 로고
    • Restriction of foamy viruses by primate Trim5alpha
    • Yap MW, Lindemann D, Stanke N, Reh J, Westphal D, et al. (2008) Restriction of foamy viruses by primate Trim5alpha. J Virol 82: 5429-5439.
    • (2008) J Virol , vol.82 , pp. 5429-5439
    • Yap, M.W.1    Lindemann, D.2    Stanke, N.3    Reh, J.4    Westphal, D.5
  • 37
    • 33645794537 scopus 로고    scopus 로고
    • Specific recognition and accelerated uncoating of retroviral capsids by the TRIM5alpha restriction factor
    • Stremlau M, Perron M, Lee M, Li Y, Song B, et al. (2006) Specific recognition and accelerated uncoating of retroviral capsids by the TRIM5alpha restriction factor. Proc Natl Acad Sci U S A 103: 5514-5519.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 5514-5519
    • Stremlau, M.1    Perron, M.2    Lee, M.3    Li, Y.4    Song, B.5
  • 39
    • 4644301808 scopus 로고    scopus 로고
    • High-resolution structure of a retroviral capsid hexameric amino-terminal domain
    • Mortuza GB, Haire LF, Stevens A, Smerdon SJ, Stoye JP, et al. (2004) High-resolution structure of a retroviral capsid hexameric amino-terminal domain. Nature 431: 481-485.
    • (2004) Nature , vol.431 , pp. 481-485
    • Mortuza, G.B.1    Haire, L.F.2    Stevens, A.3    Smerdon, S.J.4    Stoye, J.P.5
  • 40
    • 39149136512 scopus 로고    scopus 로고
    • Structure of B-MLV capsid amino-terminal domain reveals key features of viral tropism, gag assembly and core formation
    • Mortuza GB, Dodding MP, Goldstone DC, Haire LF, Stoye JP, et al. (2008) Structure of B-MLV capsid amino-terminal domain reveals key features of viral tropism, gag assembly and core formation. J Mol Biol 376: 1493-1508.
    • (2008) J Mol Biol , vol.376 , pp. 1493-1508
    • Mortuza, G.B.1    Dodding, M.P.2    Goldstone, D.C.3    Haire, L.F.4    Stoye, J.P.5
  • 41
    • 0035793720 scopus 로고    scopus 로고
    • Structural analysis of the N-terminal domain of the human T-cell leukemia virus capsid protein
    • Cornilescu CC, Bouamr F, Yao X, Carter C, Tjandra N, (2001) Structural analysis of the N-terminal domain of the human T-cell leukemia virus capsid protein. J Mol Biol 306: 783-797.
    • (2001) J Mol Biol , vol.306 , pp. 783-797
    • Cornilescu, C.C.1    Bouamr, F.2    Yao, X.3    Carter, C.4    Tjandra, N.5
  • 42
    • 0030448994 scopus 로고    scopus 로고
    • Crystal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid
    • Gamble TR, Vajdos FF, Yoo S, Worthylake DK, Houseweart M, et al. (1996) Crystal structure of human cyclophilin A bound to the amino-terminal domain of HIV-1 capsid. Cell 87: 1285-1294.
    • (1996) Cell , vol.87 , pp. 1285-1294
    • Gamble, T.R.1    Vajdos, F.F.2    Yoo, S.3    Worthylake, D.K.4    Houseweart, M.5
  • 43
    • 0033548068 scopus 로고    scopus 로고
    • Model for lentivirus capsid core assembly based on crystal dimers of EIAV p26
    • Jin Z, Jin L, Peterson DL, Lawson CL, (1999) Model for lentivirus capsid core assembly based on crystal dimers of EIAV p26. J Mol Biol 286: 83-93.
    • (1999) J Mol Biol , vol.286 , pp. 83-93
    • Jin, Z.1    Jin, L.2    Peterson, D.L.3    Lawson, C.L.4
  • 44
    • 0030693391 scopus 로고    scopus 로고
    • Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein
    • Gamble TR, Yoo S, Vajdos FF, von Schwedler UK, Worthylake DK, et al. (1997) Structure of the carboxyl-terminal dimerization domain of the HIV-1 capsid protein. Science 278: 849-853.
    • (1997) Science , vol.278 , pp. 849-853
    • Gamble, T.R.1    Yoo, S.2    Vajdos, F.F.3    von Schwedler, U.K.4    Worthylake, D.K.5
  • 45
    • 0032781006 scopus 로고    scopus 로고
    • Solution structure of the capsid protein from the human T-cell leukemia virus type-I
    • Khorasanizadeh S, Campos-Olivas R, Summers MF, (1999) Solution structure of the capsid protein from the human T-cell leukemia virus type-I. J Mol Biol 291: 491-505.
    • (1999) J Mol Biol , vol.291 , pp. 491-505
    • Khorasanizadeh, S.1    Campos-Olivas, R.2    Summers, M.F.3
  • 46
    • 0034681298 scopus 로고    scopus 로고
    • Solution structure and dynamics of the Rous sarcoma virus capsid protein and comparison with capsid proteins of other retroviruses
    • Campos-Olivas R, Newman JL, Summers MF, (2000) Solution structure and dynamics of the Rous sarcoma virus capsid protein and comparison with capsid proteins of other retroviruses. J Mol Biol 296: 633-649.
    • (2000) J Mol Biol , vol.296 , pp. 633-649
    • Campos-Olivas, R.1    Newman, J.L.2    Summers, M.F.3
  • 47
    • 0029794123 scopus 로고    scopus 로고
    • Structure of the amino-terminal core domain of the HIV-1 capsid protein
    • Gitti RK, Lee BM, Walker J, Summers MF, Yoo S, et al. (1996) Structure of the amino-terminal core domain of the HIV-1 capsid protein. Science 273: 231-235.
    • (1996) Science , vol.273 , pp. 231-235
    • Gitti, R.K.1    Lee, B.M.2    Walker, J.3    Summers, M.F.4    Yoo, S.5
  • 48
    • 0028871926 scopus 로고
    • Dali: a network tool for protein structure comparison
    • Holm L, Sander C, (1995) Dali: a network tool for protein structure comparison. Trends Biochem Sci 20: 478-480.
    • (1995) Trends Biochem Sci , vol.20 , pp. 478-480
    • Holm, L.1    Sander, C.2
  • 49
    • 13444307044 scopus 로고    scopus 로고
    • Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions
    • Krissinel E, Henrick K, (2004) Secondary-structure matching (SSM), a new tool for fast protein structure alignment in three dimensions. Acta Crystallogr D Biol Crystallogr 60: 2256-2268.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2256-2268
    • Krissinel, E.1    Henrick, K.2
  • 51
    • 67549109069 scopus 로고    scopus 로고
    • X-ray structures of the hexameric building block of the HIV capsid
    • Pornillos O, Ganser-Pornillos BK, Kelly BN, Hua Y, Whitby FG, et al. (2009) X-ray structures of the hexameric building block of the HIV capsid. Cell 137: 1282-1292.
    • (2009) Cell , vol.137 , pp. 1282-1292
    • Pornillos, O.1    Ganser-Pornillos, B.K.2    Kelly, B.N.3    Hua, Y.4    Whitby, F.G.5
  • 53
    • 25144495591 scopus 로고    scopus 로고
    • N-terminal Gag domain required for foamy virus particle assembly and export
    • Cartellieri M, Herchenroder O, Rudolph W, Heinkelein M, Lindemann D, et al. (2005) N-terminal Gag domain required for foamy virus particle assembly and export. J Virol 79: 12464-12476.
    • (2005) J Virol , vol.79 , pp. 12464-12476
    • Cartellieri, M.1    Herchenroder, O.2    Rudolph, W.3    Heinkelein, M.4    Lindemann, D.5
  • 54
    • 45749100479 scopus 로고    scopus 로고
    • Mutations in the amino terminus of foamy virus Gag disrupt morphology and infectivity but do not target assembly
    • Life RB, Lee EG, Eastman SW, Linial ML, (2008) Mutations in the amino terminus of foamy virus Gag disrupt morphology and infectivity but do not target assembly. J Virol 82: 6109-6119.
    • (2008) J Virol , vol.82 , pp. 6109-6119
    • Life, R.B.1    Lee, E.G.2    Eastman, S.W.3    Linial, M.L.4
  • 55
    • 79953278693 scopus 로고    scopus 로고
    • Novel escape mutants suggest an extensive TRIM5alpha binding site spanning the entire outer surface of the murine leukemia virus capsid protein
    • Ohkura S, Goldstone DC, Yap MW, Holden-Dye K, Taylor IA, et al. (2011) Novel escape mutants suggest an extensive TRIM5alpha binding site spanning the entire outer surface of the murine leukemia virus capsid protein. PLoS Pathog 7: e1002011.
    • (2011) PLoS Pathog , vol.7
    • Ohkura, S.1    Goldstone, D.C.2    Yap, M.W.3    Holden-Dye, K.4    Taylor, I.A.5
  • 56
    • 0025176624 scopus 로고
    • Myristoylation-dependent replication and assembly of human immunodeficiency virus 1
    • Bryant M, Ratner L, (1990) Myristoylation-dependent replication and assembly of human immunodeficiency virus 1. Proc Natl Acad Sci U S A 87: 523-527.
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 523-527
    • Bryant, M.1    Ratner, L.2
  • 57
    • 0022794486 scopus 로고
    • Myristylation site in Pr65gag is essential for virus particle formation by Moloney murine leukemia virus
    • Rein A, McClure MR, Rice NR, Luftig RB, Schultz AM, (1986) Myristylation site in Pr65gag is essential for virus particle formation by Moloney murine leukemia virus. Proc Natl Acad Sci U S A 83: 7246-7250.
    • (1986) Proc Natl Acad Sci U S A , vol.83 , pp. 7246-7250
    • Rein, A.1    McClure, M.R.2    Rice, N.R.3    Luftig, R.B.4    Schultz, A.M.5
  • 58
    • 26444444082 scopus 로고    scopus 로고
    • Retroviral matrix domains share electrostatic homology: models for membrane binding function throughout the viral life cycle
    • Murray PS, Li Z, Wang J, Tang CL, Honig B, et al. (2005) Retroviral matrix domains share electrostatic homology: models for membrane binding function throughout the viral life cycle. Structure 13: 1521-1531.
    • (2005) Structure , vol.13 , pp. 1521-1531
    • Murray, P.S.1    Li, Z.2    Wang, J.3    Tang, C.L.4    Honig, B.5
  • 59
    • 0030869124 scopus 로고    scopus 로고
    • The three-dimensional solution structure of the matrix protein from the type D retrovirus, the Mason-Pfizer monkey virus, and implications for the morphology of retroviral assembly
    • Conte MR, Klikova M, Hunter E, Ruml T, Matthews S, (1997) The three-dimensional solution structure of the matrix protein from the type D retrovirus, the Mason-Pfizer monkey virus, and implications for the morphology of retroviral assembly. Embo J 16: 5819-5826.
    • (1997) Embo J , vol.16 , pp. 5819-5826
    • Conte, M.R.1    Klikova, M.2    Hunter, E.3    Ruml, T.4    Matthews, S.5
  • 60
    • 0036149965 scopus 로고    scopus 로고
    • Structure of equine infectious anemia virus matrix protein
    • Hatanaka H, Iourin O, Rao Z, Fry E, Kingsman A, et al. (2002) Structure of equine infectious anemia virus matrix protein. J Virol 76: 1876-1883.
    • (2002) J Virol , vol.76 , pp. 1876-1883
    • Hatanaka, H.1    Iourin, O.2    Rao, Z.3    Fry, E.4    Kingsman, A.5
  • 61
    • 0029565831 scopus 로고
    • Crystal structure of SIV matrix antigen and implications for virus assembly
    • Rao Z, Belyaev AS, Fry E, Roy P, Jones IM, et al. (1995) Crystal structure of SIV matrix antigen and implications for virus assembly. Nature 378: 743-747.
    • (1995) Nature , vol.378 , pp. 743-747
    • Rao, Z.1    Belyaev, A.S.2    Fry, E.3    Roy, P.4    Jones, I.M.5
  • 62
    • 1842859044 scopus 로고    scopus 로고
    • Atomic resolution structure of Moloney murine leukemia virus matrix protein and its relationship to other retroviral matrix proteins
    • Riffel N, Harlos K, Iourin O, Rao Z, Kingsman A, et al. (2002) Atomic resolution structure of Moloney murine leukemia virus matrix protein and its relationship to other retroviral matrix proteins. Structure 10: 1627-1636.
    • (2002) Structure , vol.10 , pp. 1627-1636
    • Riffel, N.1    Harlos, K.2    Iourin, O.3    Rao, Z.4    Kingsman, A.5
  • 63
    • 0029966361 scopus 로고    scopus 로고
    • Crystal structures of the trimeric human immunodeficiency virus type 1 matrix protein: implications for membrane association and assembly
    • Hill CP, Worthylake D, Bancroft DP, Christensen AM, Sundquist WI, (1996) Crystal structures of the trimeric human immunodeficiency virus type 1 matrix protein: implications for membrane association and assembly. Proc Natl Acad Sci U S A 93: 3099-3104.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 3099-3104
    • Hill, C.P.1    Worthylake, D.2    Bancroft, D.P.3    Christensen, A.M.4    Sundquist, W.I.5
  • 64
    • 33746625935 scopus 로고    scopus 로고
    • Structural basis for targeting HIV-1 Gag proteins to the plasma membrane for virus assembly
    • Saad JS, Miller J, Tai J, Kim A, Ghanam RH, et al. (2006) Structural basis for targeting HIV-1 Gag proteins to the plasma membrane for virus assembly. Proc Natl Acad Sci U S A 103: 11364-11369.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 11364-11369
    • Saad, J.S.1    Miller, J.2    Tai, J.3    Kim, A.4    Ghanam, R.H.5
  • 65
    • 84867071581 scopus 로고    scopus 로고
    • The structure of myristoylated mason-pfizer monkey virus matrix protein and the role of phosphatidylinositol-(4,5)-bisphosphate in its membrane binding
    • Prchal J, Srb P, Hunter E, Ruml T, Hrabal R, (2012) The structure of myristoylated mason-pfizer monkey virus matrix protein and the role of phosphatidylinositol-(4,5)-bisphosphate in its membrane binding. Journal of molecular biology 423: 427-438.
    • (2012) Journal of Molecular Biology , vol.423 , pp. 427-438
    • Prchal, J.1    Srb, P.2    Hunter, E.3    Ruml, T.4    Hrabal, R.5
  • 66
    • 67649886954 scopus 로고    scopus 로고
    • Nonmyristoylated matrix protein from the Mason-Pfizer monkey virus forms oligomers
    • Vlach J, Srb P, Prchal J, Grocky M, Lang J, et al. (2009) Nonmyristoylated matrix protein from the Mason-Pfizer monkey virus forms oligomers. Journal of molecular biology 390: 967-980.
    • (2009) Journal of Molecular Biology , vol.390 , pp. 967-980
    • Vlach, J.1    Srb, P.2    Prchal, J.3    Grocky, M.4    Lang, J.5
  • 67
    • 5144222004 scopus 로고    scopus 로고
    • In vivo homodimerisation of HTLV-1 Gag and MA gives clues to the retroviral capsid and TM envelope protein arrangement
    • Rayne F, Kajava AV, Lalanne J, Mamoun RZ, (2004) In vivo homodimerisation of HTLV-1 Gag and MA gives clues to the retroviral capsid and TM envelope protein arrangement. Journal of molecular biology 343: 903-916.
    • (2004) Journal of Molecular Biology , vol.343 , pp. 903-916
    • Rayne, F.1    Kajava, A.V.2    Lalanne, J.3    Mamoun, R.Z.4
  • 68
    • 0033152857 scopus 로고    scopus 로고
    • The crystal structure of the human hepatitis B virus capsid
    • Wynne SA, Crowther RA, Leslie AG, (1999) The crystal structure of the human hepatitis B virus capsid. Mol Cell 3: 771-780.
    • (1999) Mol Cell , vol.3 , pp. 771-780
    • Wynne, S.A.1    Crowther, R.A.2    Leslie, A.G.3
  • 69
    • 0032991707 scopus 로고    scopus 로고
    • Identification of a cytoplasmic targeting/retention signal in a retroviral Gag polyprotein
    • Choi G, Park S, Choi B, Hong S, Lee J, et al. (1999) Identification of a cytoplasmic targeting/retention signal in a retroviral Gag polyprotein. J Virol 73: 5431-5437.
    • (1999) J Virol , vol.73 , pp. 5431-5437
    • Choi, G.1    Park, S.2    Choi, B.3    Hong, S.4    Lee, J.5
  • 70
    • 0025027813 scopus 로고
    • A single amino acid substitution within the matrix protein of a type D retrovirus converts its morphogenesis to that of a type C retrovirus
    • Rhee SS, Hunter E, (1990) A single amino acid substitution within the matrix protein of a type D retrovirus converts its morphogenesis to that of a type C retrovirus. Cell 63: 77-86.
    • (1990) Cell , vol.63 , pp. 77-86
    • Rhee, S.S.1    Hunter, E.2
  • 71
    • 84872596511 scopus 로고    scopus 로고
    • Characterization and manipulation of foamy virus membrane interactions
    • Swiersy A, Wiek C, Zentgraf H, Lindemann D, (2012) Characterization and manipulation of foamy virus membrane interactions. Cell Microbiol 15: 227-36.
    • (2012) Cell Microbiol , vol.15 , pp. 227-236
    • Swiersy, A.1    Wiek, C.2    Zentgraf, H.3    Lindemann, D.4
  • 72
    • 0037462921 scopus 로고    scopus 로고
    • Identification of novel interactions in HIV-1 capsid protein assembly by high-resolution mass spectrometry
    • Lanman J, Lam TT, Barnes S, Sakalian M, Emmett MR, et al. (2003) Identification of novel interactions in HIV-1 capsid protein assembly by high-resolution mass spectrometry. J Mol Biol 325: 759-772.
    • (2003) J Mol Biol , vol.325 , pp. 759-772
    • Lanman, J.1    Lam, T.T.2    Barnes, S.3    Sakalian, M.4    Emmett, M.R.5
  • 73
    • 70350771279 scopus 로고    scopus 로고
    • Structural convergence between Cryo-EM and NMR reveals intersubunit interactions critical for HIV-1 capsid function
    • Byeon IJ, Meng X, Jung J, Zhao G, Yang R, et al. (2009) Structural convergence between Cryo-EM and NMR reveals intersubunit interactions critical for HIV-1 capsid function. Cell 139: 780-790.
    • (2009) Cell , vol.139 , pp. 780-790
    • Byeon, I.J.1    Meng, X.2    Jung, J.3    Zhao, G.4    Yang, R.5
  • 74
    • 0035050188 scopus 로고    scopus 로고
    • Human foamy virus capsid formation requires an interaction domain in the N terminus of Gag
    • Tobaly-Tapiero J, Bittoun P, Giron ML, Neves M, Koken M, et al. (2001) Human foamy virus capsid formation requires an interaction domain in the N terminus of Gag. J Virol 75: 4367-4375.
    • (2001) J Virol , vol.75 , pp. 4367-4375
    • Tobaly-Tapiero, J.1    Bittoun, P.2    Giron, M.L.3    Neves, M.4    Koken, M.5
  • 75
    • 33947415278 scopus 로고    scopus 로고
    • Correct capsid assembly mediated by a conserved YXXLGL motif in prototype foamy virus Gag is essential for infectivity and reverse transcription of the viral genome
    • Mannigel I, Stange A, Zentgraf H, Lindemann D, (2007) Correct capsid assembly mediated by a conserved YXXLGL motif in prototype foamy virus Gag is essential for infectivity and reverse transcription of the viral genome. J Virol 81: 3317-3326.
    • (2007) J Virol , vol.81 , pp. 3317-3326
    • Mannigel, I.1    Stange, A.2    Zentgraf, H.3    Lindemann, D.4
  • 76
    • 79955377543 scopus 로고    scopus 로고
    • TRIM5 is an innate immune sensor for the retrovirus capsid lattice
    • Pertel T, Hausmann S, Morger D, Zuger S, Guerra J, et al. (2011) TRIM5 is an innate immune sensor for the retrovirus capsid lattice. Nature 472: 361-365.
    • (2011) Nature , vol.472 , pp. 361-365
    • Pertel, T.1    Hausmann, S.2    Morger, D.3    Zuger, S.4    Guerra, J.5
  • 78
  • 79
    • 0023084783 scopus 로고
    • Analysis of mutation in human cells by using an Epstein-Barr virus shuttle system
    • DuBridge RB, Tang P, Hsia HC, Leong PM, Miller JH, et al. (1987) Analysis of mutation in human cells by using an Epstein-Barr virus shuttle system. Mol Cell Biol 7: 379-387.
    • (1987) Mol Cell Biol , vol.7 , pp. 379-387
    • DuBridge, R.B.1    Tang, P.2    Hsia, H.C.3    Leong, P.M.4    Miller, J.H.5
  • 80
    • 0036199768 scopus 로고    scopus 로고
    • Improved primate foamy virus vectors and packaging constructs
    • Heinkelein M, Dressler M, Jarmy G, Rammling M, Imrich H, et al. (2002) Improved primate foamy virus vectors and packaging constructs. J Virol 76: 3774-3783.
    • (2002) J Virol , vol.76 , pp. 3774-3783
    • Heinkelein, M.1    Dressler, M.2    Jarmy, G.3    Rammling, M.4    Imrich, H.5
  • 81
    • 77952222409 scopus 로고    scopus 로고
    • Analysis of prototype foamy virus particle-host cell interaction with autofluorescent retroviral particles
    • Stirnnagel K, Luftenegger D, Stange A, Swiersy A, Mullers E, et al. (2010) Analysis of prototype foamy virus particle-host cell interaction with autofluorescent retroviral particles. Retrovirology 7: 45.
    • (2010) Retrovirology , vol.7 , pp. 45
    • Stirnnagel, K.1    Luftenegger, D.2    Stange, A.3    Swiersy, A.4    Mullers, E.5
  • 82
    • 33748662658 scopus 로고    scopus 로고
    • All three variable regions of the TRIM5alpha B30.2 domain can contribute to the specificity of retrovirus restriction
    • Ohkura S, Yap MW, Sheldon T, Stoye JP, (2006) All three variable regions of the TRIM5alpha B30.2 domain can contribute to the specificity of retrovirus restriction. J Virol 80: 8554-8565.
    • (2006) J Virol , vol.80 , pp. 8554-8565
    • Ohkura, S.1    Yap, M.W.2    Sheldon, T.3    Stoye, J.P.4
  • 83
    • 0033854253 scopus 로고    scopus 로고
    • Use of a transient assay for studying the genetic determinants of Fv1 restriction
    • Bock M, Bishop KN, Towers G, Stoye JP, (2000) Use of a transient assay for studying the genetic determinants of Fv1 restriction. J Virol 74: 7422-7430.
    • (2000) J Virol , vol.74 , pp. 7422-7430
    • Bock, M.1    Bishop, K.N.2    Towers, G.3    Stoye, J.P.4
  • 84
    • 78951483245 scopus 로고    scopus 로고
    • Novel functions of prototype foamy virus Gag glycine- arginine-rich boxes in reverse transcription and particle morphogenesis
    • Müllers E, Uhlig T, Stirnnagel K, Fiebig U, Zentgraf H, et al. (2011) Novel functions of prototype foamy virus Gag glycine- arginine-rich boxes in reverse transcription and particle morphogenesis. J Virol 85: 1452-1463.
    • (2011) J Virol , vol.85 , pp. 1452-1463
    • Müllers, E.1    Uhlig, T.2    Stirnnagel, K.3    Fiebig, U.4    Zentgraf, H.5
  • 86
  • 87
    • 20244370593 scopus 로고    scopus 로고
    • Characterization of prototype foamy virus gag late assembly domain motifs and their role in particle egress and infectivity
    • Stange A, Mannigel I, Peters K, Heinkelein M, Stanke N, et al. (2005) Characterization of prototype foamy virus gag late assembly domain motifs and their role in particle egress and infectivity. J Virol 79: 5466-5476.
    • (2005) J Virol , vol.79 , pp. 5466-5476
    • Stange, A.1    Mannigel, I.2    Peters, K.3    Heinkelein, M.4    Stanke, N.5
  • 88
    • 0031045585 scopus 로고    scopus 로고
    • Preparation of selenomethionyl proteins for phase determination
    • Doublie S, (1997) Preparation of selenomethionyl proteins for phase determination. Methods in enzymology 276: 523-530.
    • (1997) Methods in Enzymology , vol.276 , pp. 523-530
    • Doublie, S.1
  • 89
    • 0002498995 scopus 로고
    • Computer-aided interpretation of analytical sedimentation data for proteins
    • In: Harding SE, Rowe AJ, Horton JC, editors, Cambridge, United Kingdom: The Royal Society of Chemistry
    • Laue TM, Shah BD, Ridgeway TM, Pelletier SL (1992) Computer-aided interpretation of analytical sedimentation data for proteins. In: Harding SE, Rowe AJ, Horton JC, editors. Analytical Ultracentrifugation in Biochemistry and Polymer Science. Cambridge, United Kingdom: The Royal Society of Chemistry. pp. 90-125.
    • (1992) Analytical Ultracentrifugation in Biochemistry and Polymer Science , pp. 90-125
    • Laue, T.M.1    Shah, B.D.2    Ridgeway, T.M.3    Pelletier, S.L.4
  • 90
    • 0036154258 scopus 로고    scopus 로고
    • Size-distribution analysis of proteins by analytical ultracentrifugation: strategies and application to model systems
    • Schuck P, Perugini MA, Gonzales NR, Howlett GJ, Schubert D, (2002) Size-distribution analysis of proteins by analytical ultracentrifugation: strategies and application to model systems. Biophys J 82: 1096-1111.
    • (2002) Biophys J , vol.82 , pp. 1096-1111
    • Schuck, P.1    Perugini, M.A.2    Gonzales, N.R.3    Howlett, G.J.4    Schubert, D.5
  • 91
    • 0034009520 scopus 로고    scopus 로고
    • Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling
    • Schuck P, (2000) Size-distribution analysis of macromolecules by sedimentation velocity ultracentrifugation and lamm equation modeling. Biophys J 78: 1606-1619.
    • (2000) Biophys J , vol.78 , pp. 1606-1619
    • Schuck, P.1
  • 92
    • 33744809773 scopus 로고    scopus 로고
    • Macromolecular size-and-shape distributions by sedimentation velocity analytical ultracentrifugation
    • Brown PH, Schuck P, (2006) Macromolecular size-and-shape distributions by sedimentation velocity analytical ultracentrifugation. Biophys J 90: 4651-4661.
    • (2006) Biophys J , vol.90 , pp. 4651-4661
    • Brown, P.H.1    Schuck, P.2
  • 93
    • 1442274756 scopus 로고    scopus 로고
    • Sedimentation equilibrium analysis of protein interactions with global implicit mass conservation constraints and systematic noise decomposition
    • Vistica J, Dam J, Balbo A, Yikilmaz E, Mariuzza RA, et al. (2004) Sedimentation equilibrium analysis of protein interactions with global implicit mass conservation constraints and systematic noise decomposition. Anal Biochem 326: 234-256.
    • (2004) Anal Biochem , vol.326 , pp. 234-256
    • Vistica, J.1    Dam, J.2    Balbo, A.3    Yikilmaz, E.4    Mariuzza, R.A.5
  • 94
    • 0042855798 scopus 로고    scopus 로고
    • On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation
    • Schuck P, (2003) On the analysis of protein self-association by sedimentation velocity analytical ultracentrifugation. Anal Biochem 320: 104-124.
    • (2003) Anal Biochem , vol.320 , pp. 104-124
    • Schuck, P.1
  • 95
    • 0017077538 scopus 로고
    • DNA "melting" proteins. IV. Fluorescence measurements of binding parameters for bacteriophage T4 gene 32-protein to mono-, oligo-, and polynucleotides
    • Kelly RC, Jensen DE, von Hippel PH, (1976) DNA "melting" proteins. IV. Fluorescence measurements of binding parameters for bacteriophage T4 gene 32-protein to mono-, oligo-, and polynucleotides. J Biol Chem 251: 7240-7250.
    • (1976) J Biol Chem , vol.251 , pp. 7240-7250
    • Kelly, R.C.1    Jensen, D.E.2    von Hippel, P.H.3
  • 96
    • 0034636161 scopus 로고    scopus 로고
    • Characterization of the DNA-binding domains from the yeast cell-cycle transcription factors Mbp1 and Swi4
    • Taylor IA, McIntosh PB, Pala P, Treiber MK, Howell S, et al. (2000) Characterization of the DNA-binding domains from the yeast cell-cycle transcription factors Mbp1 and Swi4. Biochemistry 39: 3943-3954.
    • (2000) Biochemistry , vol.39 , pp. 3943-3954
    • Taylor, I.A.1    McIntosh, P.B.2    Pala, P.3    Treiber, M.K.4    Howell, S.5
  • 97
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Otwinowski Z, Minor W, (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276: 307-326.
    • (1997) Methods Enzymol , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 99
    • 0347383760 scopus 로고    scopus 로고
    • ARP/wARP and automatic interpretation of protein electron density maps
    • Morris RJ, Perrakis A, Lamzin VS, (2003) ARP/wARP and automatic interpretation of protein electron density maps. Methods Enzymol 374: 229-244.
    • (2003) Methods Enzymol , vol.374 , pp. 229-244
    • Morris, R.J.1    Perrakis, A.2    Lamzin, V.S.3
  • 100
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P, Cowtan K, (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60: 2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 101
    • 33646260450 scopus 로고    scopus 로고
    • Optimal description of a protein structure in terms of multiple groups undergoing TLS motion
    • Painter J, Merritt EA, (2006) Optimal description of a protein structure in terms of multiple groups undergoing TLS motion. Acta Crystallogr D Biol Crystallogr 62: 439-450.
    • (2006) Acta Crystallogr D Biol Crystallogr , vol.62 , pp. 439-450
    • Painter, J.1    Merritt, E.A.2
  • 104
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of Macromolecular Structures by the Maximum-Likelihood Method
    • Murshudov GN, Vagin AA, Dodson EJ, (1997) Refinement of Macromolecular Structures by the Maximum-Likelihood Method. Acta Crystallogr D Biol Crystallogr 53 (Pt 3): 240-255.
    • (1997) Acta Crystallogr D Biol Crystallogr , vol.53 , Issue.Pt 3 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3


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