메뉴 건너뛰기




Volumn 88, Issue 12, 2014, Pages 6556-6575

Nuclear magnetic resonance structure revealed that the human polyomavirus JC virus agnoprotein contains an α-helix encompassing the Leu/Ile/Phe-rich domain

Author keywords

[No Author keywords available]

Indexed keywords

AGNOPROTEIN; ISOLEUCINE; LEUCINE; PHENYLALANINE;

EID: 84901341422     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.00146-14     Document Type: Article
Times cited : (22)

References (79)
  • 1
    • 84879782413 scopus 로고    scopus 로고
    • Essential roles of Leu/Ile/Phe-rich domain of JC virus agnoprotein in dimer/oligomer formation, protein stability and splicing of viral transcripts
    • Sami Saribas A, Abou-Gharbia M, Childers W, Sariyer IK, White MK, Safak M. 2013. Essential roles of Leu/Ile/Phe-rich domain of JC virus agnoprotein in dimer/oligomer formation, protein stability and splicing of viral transcripts. Virology 443:161-176. http://dx.doi.org/10.1016/j.virol.2013.05.003.
    • (2013) Virology , vol.443 , pp. 161-176
    • Sami Saribas, A.1    Abou-gharbia, M.2    Childers, W.3    Sariyer, I.K.4    White, M.K.5    Safak, M.6
  • 2
    • 84893010348 scopus 로고    scopus 로고
    • Agnogene deletion in a novel pathogenic JC virus isolate impairs VP1 expression and virion production
    • Ellis LC, Norton E, Dang X, Koralnik IJ. 2013. Agnogene deletion in a novel pathogenic JC virus isolate impairs VP1 expression and virion production. PLoS One 8:e80840. http://dx.doi.org/10.1371/journal.pone.0080840.
    • (2013) PLoS One , vol.8
    • Ellis, L.C.1    Norton, E.2    Dang, X.3    Koralnik, I.J.4
  • 3
    • 84877932972 scopus 로고    scopus 로고
    • Human polyomavirus reactivation: disease pathogenesis and treatment approaches
    • De Gascun CF, Carr MJ. 2013. Human polyomavirus reactivation: disease pathogenesis and treatment approaches. Clin. Dev. Immunol. 2013: 373579. http://dx.doi.org/10.1155/2013/373579.
    • (2013) Clin. Dev. Immunol. , vol.2013 , pp. 373579
    • De Gascun, C.F.1    Carr, M.J.2
  • 4
    • 84866179864 scopus 로고    scopus 로고
    • JC virus agnoprotein enhances large T antigen binding to the origin of viralDNAreplication: evidence for its involvement in viral DNA replication
    • Saribas AS, White MK, Safak M. 2012. JC virus agnoprotein enhances large T antigen binding to the origin of viralDNAreplication: evidence for its involvement in viral DNA replication. Virology 433:12-26. http://dx.doi.org/10.1016/j.virol.2012.06.017.
    • (2012) Virology , vol.433 , pp. 12-26
    • Saribas, A.S.1    White, M.K.2    Safak, M.3
  • 5
  • 6
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER: a unified platform for automated protein structure and function prediction
    • Roy A, Kucukural A, Zhang Y. 2010. I-TASSER: a unified platform for automated protein structure and function prediction. Nat. Protoc. 5:725-738. http://dx.doi.org/10.1038/nprot.2010.5.
    • (2010) Nat. Protoc. , vol.5 , pp. 725-738
    • Roy, A.1    Kucukural, A.2    Zhang, Y.3
  • 7
    • 80053386766 scopus 로고    scopus 로고
    • Human polyomavirus JC small regulatory agnoprotein forms highly stable dimers and oligomers: implications for their roles in agnoprotein function
    • Saribas AS, Arachea BT, White MK, Viola RE, Safak M. 2011. Human polyomavirus JC small regulatory agnoprotein forms highly stable dimers and oligomers: implications for their roles in agnoprotein function. Virology 420:51-65. http://dx.doi.org/10.1016/j.virol.2011.08.015.
    • (2011) Virology , vol.420 , pp. 51-65
    • Saribas, A.S.1    Arachea, B.T.2    White, M.K.3    Viola, R.E.4    Safak, M.5
  • 8
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson HJ, Wright PE. 2005. Intrinsically unstructured proteins and their functions. Nat. Rev. Mol. Cell Biol. 6:197-208. http://dx.doi.org/10.1038/nrm1589.
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 9
    • 13844255387 scopus 로고    scopus 로고
    • Natively unfolded proteins
    • Fink AL. 2005. Natively unfolded proteins. Curr. Opin. Struct. Biol. 15: 35-41. http://dx.doi.org/10.1016/j.sbi.2005.01.002.
    • (2005) Curr. Opin. Struct. Biol. , vol.15 , pp. 35-41
    • Fink, A.L.1
  • 11
    • 0036194516 scopus 로고    scopus 로고
    • Functional interaction between JC virus late regulatory agnoprotein and cellular Y-box binding transcription factor, YB-1
    • Safak M, Sadowska B, Barrucco R, Khalili K. 2002. Functional interaction between JC virus late regulatory agnoprotein and cellular Y-box binding transcription factor, YB-1. J. Virol. 76:3828-3838. http://dx.doi.org/10.1128/JVI.76.8.3828-3838.2002.
    • (2002) J. Virol. , vol.76 , pp. 3828-3838
    • Safak, M.1    Sadowska, B.2    Barrucco, R.3    Khalili, K.4
  • 12
    • 0037103974 scopus 로고    scopus 로고
    • Evidence for dysregulation of cell cycle by human polyomavirus, JCV, late auxiliary protein
    • Darbinyan A, Darbinian N, Safak M, Radhakrishnan S, Giordano A, Khalili K. 2002. Evidence for dysregulation of cell cycle by human polyomavirus, JCV, late auxiliary protein. Oncogene 21:5574-5581. http://dx.doi.org/10.1038/sj.onc.1205744.
    • (2002) Oncogene , vol.21 , pp. 5574-5581
    • Darbinyan, A.1    Darbinian, N.2    Safak, M.3    Radhakrishnan, S.4    Giordano, A.5    Khalili, K.6
  • 13
    • 20144370936 scopus 로고    scopus 로고
    • Dissociation of heterochromatin protein 1 from lamin B receptor induced by human polyomavirus agnoprotein: role in nuclear egress of viral particles
    • Okada Y, Suzuki T, Sunden Y, Orba Y, Kose S, Imamoto N, Takahashi H, Tanaka S, Hall WW, Nagashima K, Sawa H. 2005. Dissociation of heterochromatin protein 1 from lamin B receptor induced by human polyomavirus agnoprotein: role in nuclear egress of viral particles. EMBO Rep. 6:452-457. http://dx.doi.org/10.1038/sj.embor.7400406.
    • (2005) EMBO Rep. , vol.6 , pp. 452-457
    • Okada, Y.1    Suzuki, T.2    Sunden, Y.3    Orba, Y.4    Kose, S.5    Imamoto, N.6    Takahashi, H.7    Tanaka, S.8    Hall, W.W.9    Nagashima, K.10    Sawa, H.11
  • 14
    • 84887433014 scopus 로고    scopus 로고
    • Viroporin activity of the JC polyomavirus is regulated by interactions with the adaptor protein complex 3
    • Suzuki T, Orba Y, Makino Y, Okada Y, Sunden Y, Hasegawa H, Hall WW, Sawa H. 2013. Viroporin activity of the JC polyomavirus is regulated by interactions with the adaptor protein complex 3. Proc. Natl. Acad. Sci. U. S. A. 110:18668-18673. http://dx.doi.org/10.1073/pnas.1311457110.
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 18668-18673
    • Suzuki, T.1    Orba, Y.2    Makino, Y.3    Okada, Y.4    Sunden, Y.5    Hasegawa, H.6    Hall, W.W.7    Sawa, H.8
  • 15
    • 43249107658 scopus 로고    scopus 로고
    • Dephosphorylation of JC virus agnoprotein by protein phosphatase 2A: inhibition by small t antigen
    • Sariyer IK, Khalili K, Safak M. 2008. Dephosphorylation of JC virus agnoprotein by protein phosphatase 2A: inhibition by small t antigen. Virology 375:464-479. http://dx.doi.org/10.1016/j.virol.2008.02.020.
    • (2008) Virology , vol.375 , pp. 464-479
    • Sariyer, I.K.1    Khalili, K.2    Safak, M.3
  • 16
    • 0034827329 scopus 로고    scopus 로고
    • Physical and functional interaction between viral and cellular proteins modulate JCV gene transcription
    • Safak M, Khalili K. 2001. Physical and functional interaction between viral and cellular proteins modulate JCV gene transcription. J. Neurovirol. 7:288-292. http://dx.doi.org/10.1080/13550280152537111.
    • (2001) J. Neurovirol. , vol.7 , pp. 288-292
    • Safak, M.1    Khalili, K.2
  • 17
    • 0035152379 scopus 로고    scopus 로고
    • Interaction of JC virus agno protein with T antigen modulates transcription and replication of the viral genome in glial cells
    • Safak M, Barrucco R, Darbinyan A, Okada Y, Nagashima K, Khalili K. 2001. Interaction of JC virus agno protein with T antigen modulates transcription and replication of the viral genome in glial cells. J. Virol. 75: 1476-1486. http://dx.doi.org/10.1128/JVI.75.3.1476-1486.2001.
    • (2001) J. Virol. , vol.75 , pp. 1476-1486
    • Safak, M.1    Barrucco, R.2    Darbinyan, A.3    Okada, Y.4    Nagashima, K.5    Khalili, K.6
  • 19
    • 33645777611 scopus 로고    scopus 로고
    • Phosphorylation mutants of JC virus agnoprotein are unable to sustain the viral infection cycle
    • Sariyer IK, Akan I, Palermo V, Gordon J, Khalili K, Safak M. 2006. Phosphorylation mutants of JC virus agnoprotein are unable to sustain the viral infection cycle. J. Virol. 80:3893-3903. http://dx.doi.org/10.1128/JVI.80.8.3893-3903.2006.
    • (2006) J. Virol. , vol.80 , pp. 3893-3903
    • Sariyer, I.K.1    Akan, I.2    Palermo, V.3    Gordon, J.4    Khalili, K.5    Safak, M.6
  • 20
    • 80052612580 scopus 로고    scopus 로고
    • BKV agnoprotein interacts with alpha-soluble N-ethylmaleimidesensitive fusion attachment protein, and negatively influences transport of VSVG-EGFP
    • Johannessen M, Walquist M, Gerits N, Dragset M, Spang A, Moens U. 2011. BKV agnoprotein interacts with alpha-soluble N-ethylmaleimidesensitive fusion attachment protein, and negatively influences transport of VSVG-EGFP. PLoS One 6:e24489. http://dx.doi.org/10.1371/journal.pone.0024489.
    • (2011) PLoS One , vol.6
    • Johannessen, M.1    Walquist, M.2    Gerits, N.3    Dragset, M.4    Spang, A.5    Moens, U.6
  • 21
    • 84860484358 scopus 로고    scopus 로고
    • JCV agnoprotein-induced reduction in CXCL5/LIX secretion by oligodendrocytes is associated with activation of apoptotic signaling in neurons
    • Merabova N, Kaminski R, Krynska B, Amini S, Khalili K, Darbinyan A. 2012. JCV agnoprotein-induced reduction in CXCL5/LIX secretion by oligodendrocytes is associated with activation of apoptotic signaling in neurons. J. Cell. Physiol. 227:3119-3127. http://dx.doi.org/10.1002/jcp.23065.
    • (2012) J. Cell. Physiol. , vol.227 , pp. 3119-3127
    • Merabova, N.1    Kaminski, R.2    Krynska, B.3    Amini, S.4    Khalili, K.5    Darbinyan, A.6
  • 22
  • 23
    • 75849144771 scopus 로고    scopus 로고
    • Clinical polyomavirus BK variants with agnogene deletion are nonfunctional but rescued by trans-complementation
    • Myhre MR, Olsen GH, Gosert R, Hirsch HH, Rinaldo CH. 2010. Clinical polyomavirus BK variants with agnogene deletion are nonfunctional but rescued by trans-complementation. Virology 398:12-20. http://dx.doi.org/10.1016/j.virol.2009.11.029.
    • (2010) Virology , vol.398 , pp. 12-20
    • Myhre, M.R.1    Olsen, G.H.2    Gosert, R.3    Hirsch, H.H.4    Rinaldo, C.H.5
  • 24
    • 79956273896 scopus 로고    scopus 로고
    • Infection by agnoprotein- negative mutants of polyomavirus JC and SV40 results in the release of virions that are mostly deficient in DNA content
    • Sariyer IK, Saribas AS, White MK, Safak M. 2011. Infection by agnoprotein- negative mutants of polyomavirus JC and SV40 results in the release of virions that are mostly deficient in DNA content. Virol. J. 8:255. http://dx.doi.org/10.1186/1743-422X-8-255.
    • (2011) Virol. J. , vol.8 , pp. 255
    • Sariyer, I.K.1    Saribas, A.S.2    White, M.K.3    Safak, M.4
  • 25
    • 77949375380 scopus 로고    scopus 로고
    • Progressive multifocal leukoencephalopathy in patients on immunomodulatory therapies
    • Major EO. 2010. Progressive multifocal leukoencephalopathy in patients on immunomodulatory therapies. Annu. Rev. Med. 61:35-47. http://dx.doi.org/10.1146/annurev.med.080708.082655.
    • (2010) Annu. Rev. Med. , vol.61 , pp. 35-47
    • Major, E.O.1
  • 26
    • 0029258002 scopus 로고
    • Progressive multifocal leukoencephalopathy: the evolution of a disease once considered rare
    • Berger JR, Concha M. 1995. Progressive multifocal leukoencephalopathy: the evolution of a disease once considered rare. J. Neurovirol. 1:5-18. http://dx.doi.org/10.3109/13550289509111006.
    • (1995) J. Neurovirol. , vol.1 , pp. 5-18
    • Berger, J.R.1    Concha, M.2
  • 27
    • 79955623973 scopus 로고    scopus 로고
    • The basis for modeling progressive multifocal leukoencephalopathy pathogenesis
    • Berger JR. 2011. The basis for modeling progressive multifocal leukoencephalopathy pathogenesis. Curr. Opin. Neurol. 24:262-267. http://dx.doi.org/10.1097/WCO.0b013e328346d2a3.
    • (2011) Curr. Opin. Neurol. , vol.24 , pp. 262-267
    • Berger, J.R.1
  • 28
    • 0026500952 scopus 로고
    • Pathogenesis and molecular biology of progressive multifocal leukoencephalopathy, the JC virus-induced demyelinating disease of the human brain
    • Major EO, Amemiya K, Tornatore CS, HouffSA, Berger JR. 1992. Pathogenesis and molecular biology of progressive multifocal leukoencephalopathy, the JC virus-induced demyelinating disease of the human brain. Clin. Microbiol. Rev. 5:49-73.
    • (1992) Clin. Microbiol. Rev. , vol.5 , pp. 49-73
    • Major, E.O.1    Amemiya, K.2    Tornatore, C.S.3    Houff, S.A.4    Berger, J.R.5
  • 30
    • 77958084582 scopus 로고    scopus 로고
    • Structure-function analysis of the human JC polyomavirus establishes the LSTc pentasaccharide as a functional receptor motif
    • Neu U, Maginnis MS, Palma AS, Stroh LJ, Nelson CD, Feizi T, Atwood WJ, Stehle T. 2010. Structure-function analysis of the human JC polyomavirus establishes the LSTc pentasaccharide as a functional receptor motif. Cell Host Microbe 8:309-319. http://dx.doi.org/10.1016/j.chom.2010.09.004.
    • (2010) Cell Host Microbe , vol.8 , pp. 309-319
    • Neu, U.1    Maginnis, M.S.2    Palma, A.S.3    Stroh, L.J.4    Nelson, C.D.5    Feizi, T.6    Atwood, W.J.7    Stehle, T.8
  • 31
    • 22844445230 scopus 로고    scopus 로고
    • Progressive multifocal leukoencephalopathy in a patient treated with natalizumab
    • Langer-Gould A, Atlas SW, Green AJ, Bollen AW, Pelletier D. 2005. Progressive multifocal leukoencephalopathy in a patient treated with natalizumab. N. Engl. J. Med. 353:375-381. http://dx.doi.org/10.1056/NEJMoa051847.
    • (2005) N. Engl. J. Med. , vol.353 , pp. 375-381
    • Langer-gould, A.1    Atlas, S.W.2    Green, A.J.3    Bollen, A.W.4    Pelletier, D.5
  • 32
    • 22844439662 scopus 로고    scopus 로고
    • Progressive multifocal leukoencephalopathy complicating treatment with natalizumab and interferon beta-1a for multiple sclerosis
    • Kleinschmidt-DeMasters BK, Tyler KL. 2005. Progressive multifocal leukoencephalopathy complicating treatment with natalizumab and interferon beta-1a for multiple sclerosis. N. Engl. J. Med. 353:369-374. http://dx.doi.org/10.1056/NEJMoa051782.
    • (2005) N. Engl. J. Med. , vol.353 , pp. 369-374
    • Kleinschmidt-demasters, B.K.1    Tyler, K.L.2
  • 34
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • McGuffin LJ, Bryson K, Jones DT. 2000. The PSIPRED protein structure prediction server. Bioinformatics 16:404-405. http://dx.doi.org/10.1093/bioinformatics/16.4.404.
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 35
    • 0032704310 scopus 로고    scopus 로고
    • Efficient solid-phase synthesis of Vpr from HIV-1 using low quantities of uniformly 13C-, 15N-labeled amino acids for NMR structural studies
    • Cornille F, Wecker K, Loffet A, Genet Roques RB. 1999. Efficient solid-phase synthesis of Vpr from HIV-1 using low quantities of uniformly 13C-, 15N-labeled amino acids for NMR structural studies. J. Pept. Res. 54:427-435. http://dx.doi.org/10.1034/j.1399-3011.1999.00129.x.
    • (1999) J. Pept. Res. , vol.54 , pp. 427-435
    • Cornille, F.1    Wecker, K.2    Loffet, A.3    Genet Roques, R.B.4
  • 36
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • Piotto M, Saudek V, Sklenar V. 1992. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J. Biomol. NMR 2:661-665. http://dx.doi.org/10.1007/BF02192855.
    • (1992) J. Biomol. NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenar, V.3
  • 38
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional NMR spectroscopy
    • Jeener J, Meier BH, Bachmann P, Ernst RR. 1979. Investigation of exchange processes by two-dimensional NMR spectroscopy. J. Chem. Phys. 71:5246-5253. http://dx.doi.org/10.1063/1.438333.
    • (1979) J. Chem. Phys. , vol.71 , pp. 5246-5253
    • Jeener, J.1    Meier, B.H.2    Bachmann, P.3    Ernst, R.R.4
  • 44
    • 17644366469 scopus 로고    scopus 로고
    • The C-terminal domain of the HIV-1 regulatory protein Vpr adopts an antiparallel dimeric structure in solution via its leucine-zipperlike domain
    • Bourbigot S, Beltz H, Denis J, Morellet N, Roques BP, Mely Y, Bouaziz S. 2005. The C-terminal domain of the HIV-1 regulatory protein Vpr adopts an antiparallel dimeric structure in solution via its leucine-zipperlike domain. Biochem. J. 387:333-341. http://dx.doi.org/10.1042/BJ20041759.
    • (2005) Biochem. J. , vol.387 , pp. 333-341
    • Bourbigot, S.1    Beltz, H.2    Denis, J.3    Morellet, N.4    Roques, B.P.5    Mely, Y.6    Bouaziz, S.7
  • 45
    • 0032472846 scopus 로고    scopus 로고
    • Helicity, membrane incorporation, orientation and thermal stability of the large conductance mechanosensitive ion channel from E
    • Arkin IT, Sukharev SI, Blount P, Kung C, Brunger AT. 1998. Helicity, membrane incorporation, orientation and thermal stability of the large conductance mechanosensitive ion channel from E. coli. Biochim. Biophys. Acta 1369:131-140. http://dx.doi.org/10.1016/S0005-2736(97)00219-8.
    • (1998) coli. Biochim. Biophys. Acta , vol.1369 , pp. 131-140
    • Arkin, I.T.1    Sukharev, S.I.2    Blount, P.3    Kung, C.4    Brunger, A.T.5
  • 47
    • 0037436404 scopus 로고    scopus 로고
    • NMR structure of the HIV-1 regulatory protein VPR
    • Morellet N, Bouaziz S, Petitjean P, Roques BP. 2003. NMR structure of the HIV-1 regulatory protein VPR. J. Mol. Biol. 327:215-227. http://dx.doi.org/10.1016/S0022-2836(03)00060-3.
    • (2003) J. Mol. Biol. , vol.327 , pp. 215-227
    • Morellet, N.1    Bouaziz, S.2    Petitjean, P.3    Roques, B.P.4
  • 53
    • 73149101885 scopus 로고    scopus 로고
    • MPEx: a tool for exploring membrane proteins
    • Snider C, Jayasinghe S, Hristova K, White SH. 2009. MPEx: a tool for exploring membrane proteins. Protein Sci. 18:2624-2628. http://dx.doi.org/10.1002/pro.256.
    • (2009) Protein Sci. , vol.18 , pp. 2624-2628
    • Snider, C.1    Jayasinghe, S.2    Hristova, K.3    White, S.H.4
  • 54
    • 0036360507 scopus 로고    scopus 로고
    • 2O/trifluoroethanol. Comparison with the Vpr N-terminal (1-51) and C-terminal (52-96) domains
    • 2O/trifluoroethanol. Comparison with the Vpr N-terminal (1-51) and C-terminal (52-96) domains. Eur. J. Biochem. 269:3779-3788. http://dx.doi.org/10.1046/j.1432-1033.2002.03067.x.
    • (2002) Eur. J. Biochem , vol.269 , pp. 3779-3788
    • Wecker, K.1    Morellet, N.2    Bouaziz, S.3    Roques, B.P.4
  • 56
    • 0021114895 scopus 로고
    • Application of phase sensitive twodimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins
    • Marion D, Wuthrich K. 1983. Application of phase sensitive twodimensional correlated spectroscopy (COSY) for measurements of 1H-1H spin-spin coupling constants in proteins. Biochem. Biophys. Res. Commun. 113:967-974. http://dx.doi.org/10.1016/0006-291X(83)91093-8.
    • (1983) Biochem. Biophys. Res. Commun. , vol.113 , pp. 967-974
    • Marion, D.1    Wuthrich, K.2
  • 57
    • 0024282849 scopus 로고
    • Clear TOCSY for 1H spin system identification in macromolecules
    • Griesinger C, Otting G, Wuthrich K, Ernst RR. 1988. Clear TOCSY for 1H spin system identification in macromolecules. J. Am. Chem. Soc. 110: 7870-7872. http://dx.doi.org/10.1021/ja00231a044.
    • (1988) J. Am. Chem. Soc. , vol.110 , pp. 7870-7872
    • Griesinger, C.1    Otting, G.2    Wuthrich, K.3    Ernst, R.R.4
  • 58
    • 0019327003 scopus 로고
    • A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules
    • Kumar A, Ernst RR, Wuthrich K. 1980. A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. Biochem. Biophys. Res. Commun. 95:1-6. http://dx.doi.org/10.1016/0006-291X(80)90695-6.
    • (1980) Biochem. Biophys. Res. Commun. , vol.95 , pp. 1-6
    • Kumar, A.1    Ernst, R.R.2    Wuthrich, K.3
  • 61
    • 0014202537 scopus 로고
    • Selective extraction of polyoma DNA from infected mouse cell cultures
    • Hirt B. 1967. Selective extraction of polyoma DNA from infected mouse cell cultures. J. Mol. Biol. 26:365-369. http://dx.doi.org/10.1016/0022-2836(67)90307-5.
    • (1967) J. Mol. Biol. , vol.26 , pp. 365-369
    • Hirt, B.1
  • 63
    • 25144472591 scopus 로고    scopus 로고
    • Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling
    • Uversky VN, Oldfield CJ, Dunker AK. 2005. Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling. J. Mol. Recognit. 18:343-384. http://dx.doi.org/10.1002/jmr.747.
    • (2005) J. Mol. Recognit. , vol.18 , pp. 343-384
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 64
    • 0037043699 scopus 로고    scopus 로고
    • Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein
    • Sheehy AM, Gaddis NC, Choi JD, Malim MH. 2002. Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. Nature 418:646-650. http://dx.doi.org/10.1038/nature00939.
    • (2002) Nature , vol.418 , pp. 646-650
    • Sheehy, A.M.1    Gaddis, N.C.2    Choi, J.D.3    Malim, M.H.4
  • 65
    • 77649175920 scopus 로고    scopus 로고
    • Hepatitis C virus nonstructural protein 4B: a journey into unexplored territory
    • Gouttenoire J, Penin F, Moradpour D. 2010. Hepatitis C virus nonstructural protein 4B: a journey into unexplored territory. Rev. Med. Virol. 20:117-129. http://dx.doi.org/10.1002/rmv.640.
    • (2010) Rev. Med. Virol. , vol.20 , pp. 117-129
    • Gouttenoire, J.1    Penin, F.2    Moradpour, D.3
  • 66
    • 77953742423 scopus 로고    scopus 로고
    • Oligomerization of Ebola virus VP40 is essential for particle morphogenesis and regulation of viral transcription
    • Hoenen T, Biedenkopf N, Zielecki F, Jung S, Groseth A, Feldmann H, Becker S. 2010. Oligomerization of Ebola virus VP40 is essential for particle morphogenesis and regulation of viral transcription. J. Virol. 84: 7053-7063. http://dx.doi.org/10.1128/JVI.00737-10.
    • (2010) J. Virol. , vol.84 , pp. 7053-7063
    • Hoenen, T.1    Biedenkopf, N.2    Zielecki, F.3    Jung, S.4    Groseth, A.5    Feldmann, H.6    Becker, S.7
  • 67
    • 77950519240 scopus 로고    scopus 로고
    • Conformational rearrangements of SV40 large T antigen during early replication events
    • Cuesta I, Nunez-Ramirez R, Scheres SH, Gai D, Chen XS, Fanning E, Carazo JM. 2010. Conformational rearrangements of SV40 large T antigen during early replication events. J. Mol. Biol. 397:1276-1286. http://dx.doi.org/10.1016/j.jmb.2010.02.042.
    • (2010) J. Mol. Biol. , vol.397 , pp. 1276-1286
    • Cuesta, I.1    Nunez-ramirez, R.2    Scheres, S.H.3    Gai, D.4    Chen, X.S.5    Fanning, E.6    Carazo, J.M.7
  • 68
    • 77949369974 scopus 로고    scopus 로고
    • The SV40 large T-antigen origin binding domain directly participates in DNA unwinding
    • Foster EC, Simmons DT. 2010. The SV40 large T-antigen origin binding domain directly participates in DNA unwinding. Biochemistry 49:2087-2096. http://dx.doi.org/10.1021/bi901827k.
    • (2010) Biochemistry , vol.49 , pp. 2087-2096
    • Foster, E.C.1    Simmons, D.T.2
  • 69
    • 79953686217 scopus 로고    scopus 로고
    • Importance of the proline-rich multimerization domain on the oligomerization and nucleic acid binding properties of HIV-1 Vif
    • Bernacchi S, Mercenne G, Tournaire C, Marquet R, Paillart JC. 2011. Importance of the proline-rich multimerization domain on the oligomerization and nucleic acid binding properties of HIV-1 Vif. Nucleic Acids Res. 39:2404-2415. http://dx.doi.org/10.1093/nar/gkq979.
    • (2011) Nucleic Acids Res. , vol.39 , pp. 2404-2415
    • Bernacchi, S.1    Mercenne, G.2    Tournaire, C.3    Marquet, R.4    Paillart, J.C.5
  • 70
    • 77957299044 scopus 로고    scopus 로고
    • Oligomerization state and supramolecular structure of the HIV-1 Vpu protein transmembrane segment in phospholipid bilayers
    • Lu JX, Sharpe S, Ghirlando R, Yau WM, Tycko R. 2010. Oligomerization state and supramolecular structure of the HIV-1 Vpu protein transmembrane segment in phospholipid bilayers. Protein Sci. 19:1877-1896. http://dx.doi.org/10.1002/pro.474.
    • (2010) Protein Sci. , vol.19 , pp. 1877-1896
    • Lu, J.X.1    Sharpe, S.2    Ghirlando, R.3    Yau, W.M.4    Tycko, R.5
  • 71
    • 77955446835 scopus 로고    scopus 로고
    • HIV Rev response element (RRE) directs assembly of the Rev homooligomer into discrete asymmetric complexes
    • Daugherty MD, Booth DS, Jayaraman B, Cheng Y, Frankel AD. 2010. HIV Rev response element (RRE) directs assembly of the Rev homooligomer into discrete asymmetric complexes. Proc. Natl. Acad. Sci. U. S. A. 107:12481-12486. http://dx.doi.org/10.1073/pnas.1007022107.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , pp. 12481-12486
    • Daugherty, M.D.1    Booth, D.S.2    Jayaraman, B.3    Cheng, Y.4    Frankel, A.D.5
  • 72
    • 78549248443 scopus 로고    scopus 로고
    • Structural basis for cooperative RNA binding and export complex assembly by HIV Rev
    • Daugherty MD, Liu B, Frankel AD. 2010. Structural basis for cooperative RNA binding and export complex assembly by HIV Rev. Nat. Struct. Mol. Biol. 17:1337-1342. http://dx.doi.org/10.1038/nsmb.1902.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 1337-1342
    • Daugherty, M.D.1    Liu, B.2    Frankel, A.D.3
  • 73
    • 0042658190 scopus 로고    scopus 로고
    • Nuclear mRNA export: insights from virology
    • Cullen BR. 2003. Nuclear mRNA export: insights from virology. Trends Biochem. Sci. 28:419-424. http://dx.doi.org/10.1016/S0968-0004(03)00142-7.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 419-424
    • Cullen, B.R.1
  • 74
    • 0037443026 scopus 로고    scopus 로고
    • Nuclear RNA export
    • Cullen BR. 2003. Nuclear RNA export. J. Cell Sci. 116:587-597. http://dx.doi.org/10.1242/jcs.00268.
    • (2003) J. Cell Sci. , vol.116 , pp. 587-597
    • Cullen, B.R.1
  • 75
    • 84887535735 scopus 로고    scopus 로고
    • Human polyoma JC virus minor capsid proteins, VP2 and VP3, enhance large T antigen binding to the origin of viral DNA replication: evidence for their involvement in regulation of the viral DNA replication
    • Saribas SA, Mun S, Johnson J, El-Hajmoussa M, White MK, Safak S. 2014. Human polyoma JC virus minor capsid proteins, VP2 and VP3, enhance large T antigen binding to the origin of viral DNA replication: evidence for their involvement in regulation of the viral DNA replication. Virology 449:1-16. http://dx.doi.org/10.1016/j.virol.2013.10.031.
    • (2014) Virology , vol.449 , pp. 1-16
    • Saribas, S.A.1    Mun, S.2    Johnson, J.3    El-hajmoussa, M.4    White, M.K.5    Safak, S.6
  • 76
    • 78951492762 scopus 로고    scopus 로고
    • Export of adenoviral late mRNA from the nucleus requires the Nxf1/Tap export receptor
    • Yatherajam G, Huang W, Flint SJ. 2011. Export of adenoviral late mRNA from the nucleus requires the Nxf1/Tap export receptor. J. Virol. 85: 1429-1438. http://dx.doi.org/10.1128/JVI.02108-10.
    • (2011) J. Virol. , vol.85 , pp. 1429-1438
    • Yatherajam, G.1    Huang, W.2    Flint, S.J.3
  • 77
    • 0024297354 scopus 로고
    • Multiple sequence alignment with hierarchical clustering
    • Corpet F. 1988. Multiple sequence alignment with hierarchical clustering. Nucleic Acids Res. 16:10881-10890. http://dx.doi.org/10.1093/nar/16.22.10881.
    • (1988) Nucleic Acids Res. , vol.16 , pp. 10881-10890
    • Corpet, F.1
  • 78
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson JD, Higgins DG, Gibson TJ. 1994. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680. http://dx.doi.org/10.1093/nar/22.22.4673.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.