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Volumn 11, Issue 7, 2014, Pages 906-920

Characterization of RNA binding and chaperoning activities of HIV-1 Vif protein Importance of the C-terminal unstructured tail

Author keywords

HIV; Nucleocapsid; RNA chaperone; Unstructured domain; Vif

Indexed keywords

HUMAN IMMUNODEFICIENCY VIRUS 1 VIF PROTEIN; INDOLE; RNA DIRECTED DNA POLYMERASE; TRYPTOPHAN; UNCLASSIFIED DRUG; VIF PROTEIN; CHAPERONE; GAG PROTEIN; NCP7 PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1; PROTEIN BINDING; TRANSFER RNA; VIF PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 84907582154     PISSN: 15476286     EISSN: 15558584     Source Type: Journal    
DOI: 10.4161/rna.29546     Document Type: Article
Times cited : (12)

References (86)
  • 1
    • 84870335313 scopus 로고    scopus 로고
    • The restriction factors of human immunodeficiency virus
    • PMID:23043100
    • Harris RS, Hultquist JF, Evans DT. The restriction factors of human immunodeficiency virus. J Biol Chem 2012; 287:40875-83; PMID:23043100; http://dx.doi.org/10.1074/jbc.R112.416925
    • (2012) J Biol Chem , vol.287 , pp. 40875-40883
    • Harris, R.S.1    Hultquist, J.F.2    Evans, D.T.3
  • 2
    • 0037043699 scopus 로고    scopus 로고
    • Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein
    • PMID:12167863
    • Sheehy AM, Gaddis NC, Choi JD, Malim MH. Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. Nature 2002; 418:646-50; PMID:12167863; 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
  • 3
    • 0038681023 scopus 로고    scopus 로고
    • Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts
    • PMID:12808466
    • Mangeat B, Turelli P, Caron G, Friedli M, Perrin L, Trono D. Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts. Nature 2003; 424:99-103; PMID:12808466; http://dx.doi.org/10.1038/nature01709
    • (2003) Nature , vol.424 , pp. 99-103
    • Mangeat, B.1    Turelli, P.2    Caron, G.3    Friedli, M.4    Perrin, L.5    Trono, D.6
  • 5
    • 33748640960 scopus 로고    scopus 로고
    • Antiviral potency of APOBEC proteins does not correlate with cytidine deamination
    • PMID:16912295
    • Bishop KN, Holmes RK, Malim MH. Antiviral potency of APOBEC proteins does not correlate with cytidine deamination. J Virol 2006; 80:8450-8; PMID:16912295; http://dx.doi.org/10.1128/JVI.00839-06
    • (2006) J Virol , vol.80 , pp. 8450-8458
    • Bishop, K.N.1    Holmes, R.K.2    Malim, M.H.3
  • 6
    • 0344845196 scopus 로고    scopus 로고
    • HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation
    • PMID:14528301
    • Marin M, Rose KM, Kozak SL, Kabat D. HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation. Nat Med 2003; 9:1398-403; PMID:14528301; http://dx.doi.org/10.1038/nm946
    • (2003) Nat Med , vol.9 , pp. 1398-1403
    • Marin, M.1    Rose, K.M.2    Kozak, S.L.3    Kabat, D.4
  • 7
    • 10044230343 scopus 로고    scopus 로고
    • Phosphorylation of a novel SOCS-box regulates assembly of the HIV-1 Vif-Cul5 complex that promotes APOBEC3G degradation
    • PMID:15574592
    • Mehle A, Goncalves J, Santa-Marta M, McPike M, Gabuzda D. Phosphorylation of a novel SOCS-box regulates assembly of the HIV-1 Vif-Cul5 complex that promotes APOBEC3G degradation. Genes Dev 2004; 18:2861-6; PMID:15574592; http://dx.doi.org/10.1101/gad.1249904
    • (2004) Genes Dev , vol.18 , pp. 2861-2866
    • Mehle, A.1    Goncalves, J.2    Santa-Marta, M.3    McPike, M.4    Gabuzda, D.5
  • 8
    • 0242578406 scopus 로고    scopus 로고
    • Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex
    • PMID:14564014
    • Yu X, Yu Y, Liu B, Luo K, Kong W, Mao P, Yu XF. Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex. Science 2003; 302:1056-60; PMID:14564014; http://dx.doi.org/10.1126/science.1089591
    • (2003) Science , vol.302 , pp. 1056-1060
    • Yu, X.1    Yu, Y.2    Liu, B.3    Luo, K.4    Kong, W.5    Mao, P.6    Yu, X.F.7
  • 10
    • 84856014513 scopus 로고    scopus 로고
    • T-cell differentiation factor CBF-β regulates HIV-1 Vif-mediated evasion of host restriction
    • PMID:22190036
    • Zhang W, Du J, Evans SL, Yu Y, Yu XF. T-cell differentiation factor CBF-β regulates HIV-1 Vif-mediated evasion of host restriction. Nature 2012; 481:376-9; PMID:22190036
    • (2012) Nature , vol.481 , pp. 376-379
    • Zhang, W.1    Du, J.2    Evans, S.L.3    Yu, Y.4    Yu, X.F.5
  • 11
    • 84857865923 scopus 로고    scopus 로고
    • Vif proteins of human and simian immunodeficiency viruses require cellular CBFβ to degrade APOBEC3 restriction factors
    • PMID:22205746
    • Hultquist JF, Binka M, LaRue RS, Simon V, Harris RS. Vif proteins of human and simian immunodeficiency viruses require cellular CBFβ to degrade APOBEC3 restriction factors. J Virol 2012; 86:2874-7; PMID:22205746
    • (2012) J Virol , vol.86 , pp. 2874-2877
    • Hultquist, J.F.1    Binka, M.2    LaRue, R.S.3    Simon, V.4    Harris, R.S.5
  • 13
    • 0142092452 scopus 로고    scopus 로고
    • The human immunodeficiency virus type 1 Vif protein reduces intracellular expression and inhibits packaging of APOBEC3G (CEM15), a cellular inhibitor of virus infectivity
    • PMID:14557625
    • Kao S, Khan MA, Miyagi E, Plishka R, Buckler-White A, Strebel K. The human immunodeficiency virus type 1 Vif protein reduces intracellular expression and inhibits packaging of APOBEC3G (CEM15), a cellular inhibitor of virus infectivity. J Virol 2003; 77:11398-407; PMID:14557625; http://dx.doi.org/10.1128/JVI.77.21.11398-11407.2003
    • (2003) J Virol , vol.77 , pp. 11398-11407
    • Kao, S.1    Khan, M.A.2    Miyagi, E.3    Plishka, R.4    Buckler-White, A.5    Strebel, K.6
  • 14
    • 0141638436 scopus 로고    scopus 로고
    • HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability
    • PMID:14527406
    • Stopak K, de Noronha C, Yonemoto W, Greene WC. HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability. Mol Cell 2003; 12:591-601; PMID:14527406; http://dx.doi.org/10.1016/S1097-2765(03)00353-8
    • (2003) Mol Cell , vol.12 , pp. 591-601
    • Stopak, K.1    De Noronha, C.2    Yonemoto, W.3    Greene, W.C.4
  • 15
    • 34547130033 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vif inhibits packaging and antiviral activity of a degradation-resistant APOBEC3G variant
    • PMID:17522211
    • Opi S, Kao S, Goila-Gaur R, Khan MA, Miyagi E, Takeuchi H, Strebel K. Human immunodeficiency virus type 1 Vif inhibits packaging and antiviral activity of a degradation-resistant APOBEC3G variant. J Virol 2007; 81:8236-46; PMID:17522211; http://dx.doi.org/10.1128/JVI.02694-06
    • (2007) J Virol , vol.81 , pp. 8236-8246
    • Opi, S.1    Kao, S.2    Goila-Gaur, R.3    Khan, M.A.4    Miyagi, E.5    Takeuchi, H.6    Strebel, K.7
  • 16
    • 48949118733 scopus 로고    scopus 로고
    • HIV-1 Vif, APOBEC, and intrinsic immunity
    • PMID:18577210
    • Goila-Gaur R, Strebel K. HIV-1 Vif, APOBEC, and intrinsic immunity. Retrovirology 2008; 5:51; PMID:18577210; http://dx.doi.org/10.1186/1742-4690-5-51
    • (2008) Retrovirology , vol.5 , pp. 51
    • Goila-Gaur, R.1    Strebel, K.2
  • 17
    • 41249100869 scopus 로고    scopus 로고
    • Advances in the structural understanding of Vif proteins
    • PMID:18336256
    • Barraud P, Paillart JC, Marquet R, Tisné C. Advances in the structural understanding of Vif proteins. Curr HIV Res 2008; 6:91-9; PMID:18336256; http://dx.doi.org/10.2174/157016208783885056
    • (2008) Curr HIV Res , vol.6 , pp. 91-99
    • Barraud, P.1    Paillart, J.C.2    Marquet, R.3    Tisné, C.4
  • 19
    • 77956628186 scopus 로고    scopus 로고
    • Identification of a critical T(Q/D/E)x5ADx2(I/L) motif from primate lentivirus Vif proteins that regulate APOBEC3G and APOBEC3F neutralizing activity
    • PMID:20592083
    • Dang Y, Wang X, York IA, Zheng YH. Identification of a critical T(Q/D/E)x5ADx2(I/L) motif from primate lentivirus Vif proteins that regulate APOBEC3G and APOBEC3F neutralizing activity. J Virol 2010; 84:8561-70; PMID:20592083; http://dx.doi.org/10.1128/JVI.00960-10
    • (2010) J Virol , vol.84 , pp. 8561-8570
    • Dang, Y.1    Wang, X.2    York, I.A.3    Zheng, Y.H.4
  • 20
    • 34547119261 scopus 로고    scopus 로고
    • Identification of two distinct human immunodeficiency virus type 1 Vif determinants critical for interactions with human APOBEC3G and APOBEC3F
    • PMID:17522216
    • Russell RA, Pathak VK. Identification of two distinct human immunodeficiency virus type 1 Vif determinants critical for interactions with human APOBEC3G and APOBEC3F. J Virol 2007; 81:8201-10; PMID:17522216; http://dx.doi.org/10.1128/JVI.00395-07
    • (2007) J Virol , vol.81 , pp. 8201-8210
    • Russell, R.A.1    Pathak, V.K.2
  • 21
    • 33744939997 scopus 로고    scopus 로고
    • Mutational alteration of human immunodeficiency virus type 1 Vif allows for functional interaction with nonhuman primate APOBEC3G
    • PMID:16731937
    • Schröfelbauer B, Senger T, Manning G, Landau NR. Mutational alteration of human immunodeficiency virus type 1 Vif allows for functional interaction with nonhuman primate APOBEC3G. J Virol 2006; 80:5984-91; PMID:16731937; http://dx.doi.org/10.1128/JVI.00388-06
    • (2006) J Virol , vol.80 , pp. 5984-5991
    • Schröfelbauer, B.1    Senger, T.2    Manning, G.3    Landau, N.R.4
  • 22
    • 33644752777 scopus 로고    scopus 로고
    • Differential requirement for conserved tryptophans in human immunodeficiency virus type 1 Vif for the selective suppression of APOBEC3G and APOBEC3F
    • PMID:16501124
    • Tian C, Yu X, Zhang W, Wang T, Xu R, Yu XF. Differential requirement for conserved tryptophans in human immunodeficiency virus type 1 Vif for the selective suppression of APOBEC3G and APOBEC3F. J Virol 2006; 80:3112-5; PMID:16501124; http://dx.doi.org/10.1128/JVI.80.6.3112-3115.2006
    • (2006) J Virol , vol.80 , pp. 3112-3115
    • Tian, C.1    Yu, X.2    Zhang, W.3    Wang, T.4    Xu, R.5    Yu, X.F.6
  • 23
    • 58049217469 scopus 로고    scopus 로고
    • Distinct determinants in HIV-1 Vif and human APOBEC3 proteins are required for the suppression of diverse host anti-viral proteins
    • PMID:19088851
    • Zhang W, Chen G, Niewiadomska AM, Xu R, Yu XF. Distinct determinants in HIV-1 Vif and human APOBEC3 proteins are required for the suppression of diverse host anti-viral proteins. PLoS One 2008; 3:e3963; PMID:19088851; http://dx.doi.org/10.1371/journal.pone.0003963
    • (2008) PLoS One , vol.3 , pp. e3963
    • Zhang, W.1    Chen, G.2    Niewiadomska, A.M.3    Xu, R.4    Yu, X.F.5
  • 24
    • 60049098639 scopus 로고    scopus 로고
    • Regulation of APOBEC3 proteins by a novel YXXL motif in human immunodeficiency virus type 1 Vif and simian immunodeficiency virus SIVagm Vif
    • PMID:19109396
    • Pery E, Rajendran KS, Brazier AJ, Gabuzda D. Regulation of APOBEC3 proteins by a novel YXXL motif in human immunodeficiency virus type 1 Vif and simian immunodeficiency virus SIVagm Vif. J Virol 2009; 83:2374-81; PMID:19109396; http://dx.doi.org/10.1128/JVI.01898-08
    • (2009) J Virol , vol.83 , pp. 2374-2381
    • Pery, E.1    Rajendran, K.S.2    Brazier, A.J.3    Gabuzda, D.4
  • 25
    • 84855982190 scopus 로고    scopus 로고
    • The activity spectrum of Vif from multiple HIV-1 subtypes against APOBEC3G, APOBEC3F, and APOBEC3H
    • PMID:22013041
    • Binka M, Ooms M, Steward M, Simon V. The activity spectrum of Vif from multiple HIV-1 subtypes against APOBEC3G, APOBEC3F, and APOBEC3H. J Virol 2012; 86:49-59; PMID:22013041; http://dx.doi.org/10.1128/JVI.06082-11
    • (2012) J Virol , vol.86 , pp. 49-59
    • Binka, M.1    Ooms, M.2    Steward, M.3    Simon, V.4
  • 26
    • 0033863969 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vif protein is an integral component of an mRNP complex of viral RNA and could be involved in the viral RNA folding and packaging process
    • PMID:10954522
    • Zhang H, Pomerantz RJ, Dornadula G, Sun Y. Human immunodeficiency virus type 1 Vif protein is an integral component of an mRNP complex of viral RNA and could be involved in the viral RNA folding and packaging process. J Virol 2000; 74:8252-61; PMID:10954522; http://dx.doi.org/10.1128/JVI.74.18.8252-8261.2000
    • (2000) J Virol , vol.74 , pp. 8252-8261
    • Zhang, H.1    Pomerantz, R.J.2    Dornadula, G.3    Sun, Y.4
  • 27
    • 0034899286 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vif protein is packaged into the nucleoprotein complex through an interaction with viral genomic RNA
    • PMID:11461998
    • Khan MA, Aberham C, Kao S, Akari H, Gorelick R, Bour S, Strebel K. Human immunodeficiency virus type 1 Vif protein is packaged into the nucleoprotein complex through an interaction with viral genomic RNA. J Virol 2001; 75:7252-65; PMID:11461998; http://dx.doi.org/10.1128/JVI.75.16.7252-7265.2001
    • (2001) J Virol , vol.75 , pp. 7252-7265
    • Khan, M.A.1    Aberham, C.2    Kao, S.3    Akari, H.4    Gorelick, R.5    Bour, S.6    Strebel, K.7
  • 28
    • 84857865923 scopus 로고    scopus 로고
    • Vif proteins of human and simian immunodeficiency viruses require cellular CBFβ to degrade APOBEC3 restriction factors
    • PMID:22205746
    • Hultquist JF, Binka M, LaRue RS, Simon V, Harris RS. Vif proteins of human and simian immunodeficiency viruses require cellular CBFβ to degrade APOBEC3 restriction factors. J Virol 2012; 86:2874-7; PMID:22205746; http://dx.doi.org/10.1128/JVI.06950-11
    • (2012) J Virol , vol.86 , pp. 2874-2877
    • Hultquist, J.F.1    Binka, M.2    LaRue, R.S.3    Simon, V.4    Harris, R.S.5
  • 29
    • 33745225450 scopus 로고    scopus 로고
    • A zinc-binding region in Vif binds Cul5 and determines cullin selection
    • PMID:16636053
    • Mehle A, Thomas ER, Rajendran KS, Gabuzda D. A zinc-binding region in Vif binds Cul5 and determines cullin selection. J Biol Chem 2006; 281:17259-65; PMID:16636053; http://dx.doi.org/10.1074/jbc.M602413200
    • (2006) J Biol Chem , vol.281 , pp. 17259-17265
    • Mehle, A.1    Thomas, E.R.2    Rajendran, K.S.3    Gabuzda, D.4
  • 30
    • 33845996549 scopus 로고    scopus 로고
    • Zinc chelation inhibits HIV Vif activity and liberates antiviral function of the cytidine deaminase APOBEC3G
    • PMID:17135358
    • Xiao Z, Ehrlich E, Luo K, Xiong Y, Yu XF. Zinc chelation inhibits HIV Vif activity and liberates antiviral function of the cytidine deaminase APOBEC3G. FASEB J 2007; 21:217-22; PMID:17135358; http://dx.doi.org/10.1096/fj.06-6773com
    • (2007) FASEB J , vol.21 , pp. 217-222
    • Xiao, Z.1    Ehrlich, E.2    Luo, K.3    Xiong, Y.4    Yu, X.F.5
  • 31
    • 10044228286 scopus 로고    scopus 로고
    • Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines
    • PMID:15574593
    • Yu Y, Xiao Z, Ehrlich ES, Yu X, Yu XF. Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines. Genes Dev 2004; 18:2867-72; PMID:15574593; http://dx.doi.org/10.1101/gad.1250204
    • (2004) Genes Dev , vol.18 , pp. 2867-2872
    • Yu, Y.1    Xiao, Z.2    Ehrlich, E.S.3    Yu, X.4    Yu, X.F.5
  • 32
    • 50149097544 scopus 로고    scopus 로고
    • Structural insight into the human immunodeficiency virus Vif SOCS box and its role in human E3 ubiquitin ligase assembly
    • PMID:18562529
    • Stanley BJ, Ehrlich ES, Short L, Yu Y, Xiao Z, Yu XF, Xiong Y. Structural insight into the human immunodeficiency virus Vif SOCS box and its role in human E3 ubiquitin ligase assembly. J Virol 2008; 82:8656-63; PMID:18562529; http://dx.doi.org/10.1128/JVI.00767-08
    • (2008) J Virol , vol.82 , pp. 8656-8663
    • Stanley, B.J.1    Ehrlich, E.S.2    Short, L.3    Yu, Y.4    Xiao, Z.5    Yu, X.F.6    Xiong, Y.7
  • 33
    • 0035895896 scopus 로고    scopus 로고
    • The multimerization of human immunodeficiency virus type I Vif protein: A requirement for Vif function in the viral life cycle
    • PMID:11071884
    • Yang S, Sun Y, Zhang H. The multimerization of human immunodeficiency virus type I Vif protein: a requirement for Vif function in the viral life cycle. J Biol Chem 2001; 276:4889-93; PMID:11071884; http://dx.doi.org/10.1074/jbc.M004895200
    • (2001) J Biol Chem , vol.276 , pp. 4889-4893
    • Yang, S.1    Sun, Y.2    Zhang, H.3
  • 35
    • 14844337426 scopus 로고    scopus 로고
    • The tyrosine kinases Fyn and Hck favor the recruitment of tyrosine-phosphorylated APOBEC3G into vif-defective HIV-1 particles
    • PMID:15752743
    • Douaisi M, Dussart S, Courcoul M, Bessou G, Lerner EC, Decroly E, Vigne R. The tyrosine kinases Fyn and Hck favor the recruitment of tyrosine-phosphorylated APOBEC3G into vif-defective HIV-1 particles. Biochem Biophys Res Commun 2005; 329:917-24; PMID:15752743; http://dx.doi.org/10.1016/j.bbrc.2005.02.057
    • (2005) Biochem Biophys Res Commun , vol.329 , pp. 917-924
    • Douaisi, M.1    Dussart, S.2    Courcoul, M.3    Bessou, G.4    Lerner, E.C.5    Decroly, E.6    Vigne, R.7
  • 37
    • 0033052695 scopus 로고    scopus 로고
    • Vif and the p55(Gag) polyprotein of human immunodeficiency virus type 1 are present in colocalizing membrane-free cytoplasmic complexes
    • PMID:10074112
    • Simon JH, Carpenter EA, Fouchier RA, Malim MH. Vif and the p55(Gag) polyprotein of human immunodeficiency virus type 1 are present in colocalizing membrane-free cytoplasmic complexes. J Virol 1999; 73:2667-74; PMID:10074112
    • (1999) J Virol , vol.73 , pp. 2667-2674
    • Simon, J.H.1    Carpenter, E.A.2    Fouchier, R.A.3    Malim, M.H.4
  • 38
    • 0028871720 scopus 로고
    • Biological activity of human immunodeficiency virus type 1 Vif requires membrane targeting by C-terminal basic domains
    • PMID:7474141
    • Goncalves J, Shi B, Yang X, Gabuzda D. Biological activity of human immunodeficiency virus type 1 Vif requires membrane targeting by C-terminal basic domains. J Virol 1995; 69:7196-204; PMID:7474141
    • (1995) J Virol , vol.69 , pp. 7196-7204
    • Goncalves, J.1    Shi, B.2    Yang, X.3    Gabuzda, D.4
  • 39
    • 67649888378 scopus 로고    scopus 로고
    • Mutational analysis of the HIV-1 auxiliary protein Vif identifies independent domains important for the physical and functional interaction with HIV-1 reverse transcriptase
    • PMID:19369217
    • Kataropoulou A, Bovolenta C, Belfiore A, Trabatti S, Garbelli A, Porcellini S, Lupo R, Maga G. Mutational analysis of the HIV-1 auxiliary protein Vif identifies independent domains important for the physical and functional interaction with HIV-1 reverse transcriptase. Nucleic Acids Res 2009; 37:3660-9; PMID:19369217; http://dx.doi.org/10.1093/nar/gkp226
    • (2009) Nucleic Acids Res , vol.37 , pp. 3660-3669
    • Kataropoulou, A.1    Bovolenta, C.2    Belfiore, A.3    Trabatti, S.4    Garbelli, A.5    Porcellini, S.6    Lupo, R.7    Maga, G.8
  • 40
    • 84892188402 scopus 로고    scopus 로고
    • Structural basis for hijacking CBF-β and CUL5 E3 ligase complex by HIV-1 Vif
    • PMID:24402281
    • Guo Y, Dong L, Qiu X, Wang Y, Zhang B, Liu H, Yu Y, Zang Y, Yang M, Huang Z. Structural basis for hijacking CBF-β and CUL5 E3 ligase complex by HIV-1 Vif. Nature 2014; 505:229-33; PMID:24402281; http://dx.doi.org/10.1038/nature12884
    • (2014) Nature , vol.505 , pp. 229-233
    • Guo, Y.1    Dong, L.2    Qiu, X.3    Wang, Y.4    Zhang, B.5    Liu, H.6    Yu, Y.7    Zang, Y.8    Yang, M.9    Huang, Z.10
  • 41
    • 34548713478 scopus 로고    scopus 로고
    • Mass spectrometry analysis of HIV-1 Vif reveals an increase in ordered structure upon oligomerization in regions necessary for viral infectivity
    • PMID:17598142
    • Auclair JR, Green KM, Shandilya S, Evans JE, Somasundaran M, Schiffer CA. Mass spectrometry analysis of HIV-1 Vif reveals an increase in ordered structure upon oligomerization in regions necessary for viral infectivity. Proteins 2007; 69:270-84; PMID:17598142; http://dx.doi.org/10.1002/prot.21471
    • (2007) Proteins , vol.69 , pp. 270-284
    • Auclair, J.R.1    Green, K.M.2    Shandilya, S.3    Evans, J.E.4    Somasundaran, M.5    Schiffer, C.A.6
  • 42
    • 79960371732 scopus 로고    scopus 로고
    • On the solution conformation and dynamics of the HIV-1 viral infectivity factor
    • PMID:21763503
    • Marcsisin SR, Narute PS, Emert-Sedlak LA, Kloczewiak M, Smithgall TE, Engen JR. On the solution conformation and dynamics of the HIV-1 viral infectivity factor. J Mol Biol 2011; 410:1008-22; PMID:21763503; http://dx.doi.org/10.1016/j.jmb.2011.04.053
    • (2011) J Mol Biol , vol.410 , pp. 1008-1022
    • Marcsisin, S.R.1    Narute, P.S.2    Emert-Sedlak, L.A.3    Kloczewiak, M.4    Smithgall, T.E.5    Engen, J.R.6
  • 43
    • 65349148040 scopus 로고    scopus 로고
    • The C-terminal domain of the HIV-1 Vif protein is natively unfolded in its unbound state
    • PMID:19218568
    • Reingewertz TH, Benyamini H, Lebendiker M, Shalev DE, Friedler A. The C-terminal domain of the HIV-1 Vif protein is natively unfolded in its unbound state. Protein Eng Des Sel 2009; 22:281-7; PMID:19218568; http://dx.doi.org/10.1093/protein/gzp004
    • (2009) Protein Eng des Sel , vol.22 , pp. 281-287
    • Reingewertz, T.H.1    Benyamini, H.2    Lebendiker, M.3    Shalev, D.E.4    Friedler, A.5
  • 44
    • 77957244332 scopus 로고    scopus 로고
    • Structural disorder in the HIV-1 Vif protein and interactiondependent gain of structure
    • PMID:20450485
    • Reingewertz TH, Shalev DE, Friedler A. Structural disorder in the HIV-1 Vif protein and interactiondependent gain of structure. Protein Pept Lett 2010; 17:988-98; PMID:20450485; http://dx.doi.org/10.2174/092986610791498876
    • (2010) Protein Pept Lett , vol.17 , pp. 988-998
    • Reingewertz, T.H.1    Shalev, D.E.2    Friedler, A.3
  • 45
    • 77957235518 scopus 로고    scopus 로고
    • Molecular insight into the conformational dynamics of the Elongin BC complex and its interaction with HIV-1 Vif
    • PMID:20728451
    • Marcsisin SR, Engen JR. Molecular insight into the conformational dynamics of the Elongin BC complex and its interaction with HIV-1 Vif. J Mol Biol 2010; 402:892-904; PMID:20728451; http://dx.doi.org/10.1016/j.jmb.2010.08.026
    • (2010) J Mol Biol , vol.402 , pp. 892-904
    • Marcsisin, S.R.1    Engen, J.R.2
  • 46
    • 34548833825 scopus 로고    scopus 로고
    • RNA and DNA binding properties of HIV-1 Vif protein: A fluorescence study
    • PMID:17609216
    • Bernacchi S, Henriet S, Dumas P, Paillart JC, Marquet R. RNA and DNA binding properties of HIV-1 Vif protein: a fluorescence study. J Biol Chem 2007; 282:26361-8; PMID:17609216; http://dx.doi.org/10.1074/jbc.M703122200
    • (2007) J Biol Chem , vol.282 , pp. 26361-26368
    • Bernacchi, S.1    Henriet, S.2    Dumas, P.3    Paillart, J.C.4    Marquet, R.5
  • 47
    • 79953686217 scopus 로고    scopus 로고
    • Importance of the proline-rich multimerization domain on the oligomerization and nucleic acid binding properties of HIV-1 Vif
    • PMID:21076154
    • Bernacchi S, Mercenne G, Tournaire C, Marquet R, Paillart JC. Importance of the proline-rich multimerization domain on the oligomerization and nucleic acid binding properties of HIV-1 Vif. Nucleic Acids Res 2011; 39:2404-15; PMID:21076154; 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
  • 49
    • 84865294380 scopus 로고    scopus 로고
    • Sequence and structure requirements for specific recognition of HIV-1 TAR and DIS RNA by the HIV-1 Vif protein
    • PMID:22767258
    • Freisz S, Mezher J, Hafirassou L, Wolff P, Nominé Y, Romier C, Dumas P, Ennifar E. Sequence and structure requirements for specific recognition of HIV-1 TAR and DIS RNA by the HIV-1 Vif protein. RNA Biol 2012; 9:966-77; PMID:22767258; http://dx.doi.org/10.4161/rna.20483
    • (2012) RNA Biol , vol.9 , pp. 966-977
    • Freisz, S.1    Mezher, J.2    Hafirassou, L.3    Wolff, P.4    Nominé, Y.5    Romier, C.6    Dumas, P.7    Ennifar, E.8
  • 51
    • 0033798414 scopus 로고    scopus 로고
    • Association of human immunodeficiency virus type 1 Vif with RNA and its role in reverse transcription
    • PMID:10982337
    • Dettenhofer M, Cen S, Carlson BA, Kleiman L, Yu XF. Association of human immunodeficiency virus type 1 Vif with RNA and its role in reverse transcription. J Virol 2000; 74:8938-45; PMID:10982337; http://dx.doi.org/10.1128/JVI.74.19.8938-8945.2000
    • (2000) J Virol , vol.74 , pp. 8938-8945
    • Dettenhofer, M.1    Cen, S.2    Carlson, B.A.3    Kleiman, L.4    Yu, X.F.5
  • 52
    • 34548585250 scopus 로고    scopus 로고
    • Vif is a RNA chaperone that could temporally regulate RNA dimerization and the early steps of HIV-1 reverse transcription
    • PMID:17660191
    • Henriet S, Sinck L, Bec G, Gorelick RJ, Marquet R, Paillart JC. Vif is a RNA chaperone that could temporally regulate RNA dimerization and the early steps of HIV-1 reverse transcription. Nucleic Acids Res 2007; 35:5141-53; PMID:17660191; http://dx.doi.org/10.1093/nar/gkm542
    • (2007) Nucleic Acids Res , vol.35 , pp. 5141-5153
    • Henriet, S.1    Sinck, L.2    Bec, G.3    Gorelick, R.J.4    Marquet, R.5    Paillart, J.C.6
  • 53
    • 18144378465 scopus 로고    scopus 로고
    • Structural bases of the annealing of primer tRNA(3Lys) to the HIV-1 viral RNA
    • PMID:15853720
    • Tisné C. Structural bases of the annealing of primer tRNA(3Lys) to the HIV-1 viral RNA. Curr HIV Res 2005; 3:147-56; PMID:15853720; http://dx.doi.org/10.2174/1570162053506919
    • (2005) Curr HIV Res , vol.3 , pp. 147-156
    • Tisné, C.1
  • 54
    • 2342564387 scopus 로고    scopus 로고
    • The fragile X mental retardation protein has nucleic acid chaperone properties
    • PMID:15096575
    • Gabus C, Mazroui R, Tremblay S, Khandjian EW, Darlix JL. The fragile X mental retardation protein has nucleic acid chaperone properties. Nucleic Acids Res 2004; 32:2129-37; PMID:15096575; http://dx.doi.org/10.1093/nar/gkh535
    • (2004) Nucleic Acids Res , vol.32 , pp. 2129-2137
    • Gabus, C.1    Mazroui, R.2    Tremblay, S.3    Khandjian, E.W.4    Darlix, J.L.5
  • 56
    • 0036720794 scopus 로고    scopus 로고
    • Intravirion processing of the human immunodeficiency virus type 1 Vif protein by the viral protease may be correlated with Vif function
    • PMID:12186895
    • Khan MA, Akari H, Kao S, Aberham C, Davis D, Buckler-White A, Strebel K. Intravirion processing of the human immunodeficiency virus type 1 Vif protein by the viral protease may be correlated with Vif function. J Virol 2002; 76:9112-23; PMID:12186895; http://dx.doi.org/10.1128/JVI.76.18.9112-9123.2002
    • (2002) J Virol , vol.76 , pp. 9112-9123
    • Khan, M.A.1    Akari, H.2    Kao, S.3    Aberham, C.4    Davis, D.5    Buckler-White, A.6    Strebel, K.7
  • 57
    • 0029874943 scopus 로고    scopus 로고
    • Phosphorylation of Vif and its role in HIV-1 replication
    • PMID:8626571
    • Yang X, Goncalves J, Gabuzda D. Phosphorylation of Vif and its role in HIV-1 replication. J Biol Chem 1996; 271:10121-9; PMID:8626571; http://dx.doi.org/10.1074/jbc.271.17.10121
    • (1996) J Biol Chem , vol.271 , pp. 10121-10129
    • Yang, X.1    Goncalves, J.2    Gabuzda, D.3
  • 58
    • 79954438224 scopus 로고    scopus 로고
    • Biophysical characterization of recombinant HIV-1 subtype C virus infectivity factor
    • PMID:20809132
    • Gallerano D, Devanaboyina SC, Swoboda I, Linhart B, Mittermann I, Keller W, Valenta R. Biophysical characterization of recombinant HIV-1 subtype C virus infectivity factor. Amino Acids 2011; 40:981-9; PMID:20809132; http://dx.doi.org/10.1007/s00726-010-0725-x
    • (2011) Amino Acids , vol.40 , pp. 981-989
    • Gallerano, D.1    Devanaboyina, S.C.2    Swoboda, I.3    Linhart, B.4    Mittermann, I.5    Keller, W.6    Valenta, R.7
  • 59
    • 84858216657 scopus 로고    scopus 로고
    • Hydrodynamic and functional analysis of HIV-1 Vif oligomerization
    • PMID:22369580
    • Techtmann SM, Ghirlando R, Kao S, Strebel K, Maynard EL. Hydrodynamic and functional analysis of HIV-1 Vif oligomerization. Biochemistry 2012; 51:2078-86; PMID:22369580; http://dx.doi.org/10.1021/bi201738a
    • (2012) Biochemistry , vol.51 , pp. 2078-2086
    • Techtmann, S.M.1    Ghirlando, R.2    Kao, S.3    Strebel, K.4    Maynard, E.L.5
  • 60
    • 28444482398 scopus 로고    scopus 로고
    • Bioinformatics analyses of circular dichroism protein reference databases
    • PMID:16188926
    • Janes RW. Bioinformatics analyses of circular dichroism protein reference databases. Bioinformatics 2005; 21:4230-8; PMID:16188926; http://dx.doi.org/10.1093/bioinformatics/bti690
    • (2005) Bioinformatics , vol.21 , pp. 4230-4238
    • Janes, R.W.1
  • 61
    • 0942298105 scopus 로고    scopus 로고
    • The annealing mechanism of HIV-1 reverse transcription primer onto the viral genome
    • PMID:14602716
    • Tisné C, Roques BP, Dardel F. The annealing mechanism of HIV-1 reverse transcription primer onto the viral genome. J Biol Chem 2004; 279:3588-95; PMID:14602716; http://dx.doi.org/10.1074/jbc.M310368200
    • (2004) J Biol Chem , vol.279 , pp. 3588-3595
    • Tisné, C.1    Roques, B.P.2    Dardel, F.3
  • 62
    • 0033735041 scopus 로고    scopus 로고
    • NMR and biochemical characterization of recombinant human tRNA(Lys)3 expressed in Escherichia coli: Identification of posttranscriptional nucleotide modifications required for efficient initiation of HIV-1 reverse transcription
    • PMID:11073216
    • Tisné C, Rigourd M, Marquet R, Ehresmann C, Dardel F. NMR and biochemical characterization of recombinant human tRNA(Lys)3 expressed in Escherichia coli: identification of posttranscriptional nucleotide modifications required for efficient initiation of HIV-1 reverse transcription. RNA 2000; 6:1403-12; PMID:11073216; http://dx.doi.org/10.1017/S1355838200000947
    • (2000) RNA , vol.6 , pp. 1403-1412
    • Tisné, C.1    Rigourd, M.2    Marquet, R.3    Ehresmann, C.4    Dardel, F.5
  • 63
    • 0028955753 scopus 로고
    • Binding of the HIV-1 nucleocapsid protein to the primer tRNA(3Lys), in vitro, is essentially not specific
    • PMID:7829498
    • Mély Y, de Rocquigny H, Sorinas-Jimeno M, Keith G, Roques BP, Marquet R, Gérard D. Binding of the HIV-1 nucleocapsid protein to the primer tRNA(3Lys), in vitro, is essentially not specific. J Biol Chem 1995; 270:1650-6; PMID:7829498; http://dx.doi.org/10.1074/jbc.270.4.1650
    • (1995) J Biol Chem , vol.270 , pp. 1650-1656
    • Mély, Y.1    De Rocquigny, H.2    Sorinas-Jimeno, M.3    Keith, G.4    Roques, B.P.5    Marquet, R.6    Gérard, D.7
  • 64
    • 0035936695 scopus 로고    scopus 로고
    • Heteronuclear NMR studies of the interaction of tRNA(Lys)3 with HIV-1 nucleocapsid protein
    • PMID:11178904
    • Tisné C, Roques BP, Dardel F. Heteronuclear NMR studies of the interaction of tRNA(Lys)3 with HIV-1 nucleocapsid protein. J Mol Biol 2001; 306:443-54; PMID:11178904; http://dx.doi.org/10.1006/jmbi.2000.4391
    • (2001) J Mol Biol , vol.306 , pp. 443-454
    • Tisné, C.1    Roques, B.P.2    Dardel, F.3
  • 65
    • 9144247039 scopus 로고    scopus 로고
    • First snapshots of the HIV-1 RNA structure in infected cells and in virions
    • PMID:15355993
    • Paillart JC, Dettenhofer M, Yu XF, Ehresmann C, Ehresmann B, Marquet R. First snapshots of the HIV-1 RNA structure in infected cells and in virions. J Biol Chem 2004; 279:48397-403; PMID:15355993; http://dx.doi.org/10.1074/jbc.M408294200
    • (2004) J Biol Chem , vol.279 , pp. 48397-48403
    • Paillart, J.C.1    Dettenhofer, M.2    Yu, X.F.3    Ehresmann, C.4    Ehresmann, B.5    Marquet, R.6
  • 66
    • 0025736770 scopus 로고
    • Dimerization of human immunodeficiency virus (type 1) RNA: Stimulation by cations and possible mechanism
    • PMID:1645868
    • Marquet R, Baudin F, Gabus C, Darlix JL, Mougel M, Ehresmann C, Ehresmann B. Dimerization of human immunodeficiency virus (type 1) RNA: stimulation by cations and possible mechanism. Nucleic Acids Res 1991; 19:2349-57; PMID:1645868; http://dx.doi.org/10.1093/nar/19.9.2349
    • (1991) Nucleic Acids Res , vol.19 , pp. 2349-2357
    • Marquet, R.1    Baudin, F.2    Gabus, C.3    Darlix, J.L.4    Mougel, M.5    Ehresmann, C.6    Ehresmann, B.7
  • 67
    • 0027996464 scopus 로고
    • Mutational analysis of the bipartite dimer linkage structure of human immunodeficiency virus type 1 genomic RNA
    • PMID:7961663
    • Paillart JC, Marquet R, Skripkin E, Ehresmann B, Ehresmann C. Mutational analysis of the bipartite dimer linkage structure of human immunodeficiency virus type 1 genomic RNA. J Biol Chem 1994; 269:27486-93; PMID:7961663
    • (1994) J Biol Chem , vol.269 , pp. 27486-27493
    • Paillart, J.C.1    Marquet, R.2    Skripkin, E.3    Ehresmann, B.4    Ehresmann, C.5
  • 68
    • 33750016312 scopus 로고    scopus 로고
    • Rapid kinetics of protein-nucleic acid interaction is a major component of HIV-1 nucleocapsid protein's nucleic acid chaperone function
    • PMID:16997322
    • Cruceanu M, Gorelick RJ, Musier-Forsyth K, Rouzina I, Williams MC. Rapid kinetics of protein-nucleic acid interaction is a major component of HIV-1 nucleocapsid protein's nucleic acid chaperone function. J Mol Biol 2006; 363:867-77; PMID:16997322; http://dx.doi.org/10.1016/j.jmb.2006.08.070
    • (2006) J Mol Biol , vol.363 , pp. 867-877
    • Cruceanu, M.1    Gorelick, R.J.2    Musier-Forsyth, K.3    Rouzina, I.4    Williams, M.C.5
  • 69
    • 33744957724 scopus 로고    scopus 로고
    • Nucleotide excision repair and template-independent addition by HIV-1 reverse transcriptase in the presence of nucleocapsid protein
    • PMID:16500895
    • Bampi C, Bibillo A, Wendeler M, Divita G, Gorelick RJ, Le Grice SF, Darlix JL. Nucleotide excision repair and template-independent addition by HIV-1 reverse transcriptase in the presence of nucleocapsid protein. J Biol Chem 2006; 281:11736-43; PMID:16500895; http://dx.doi.org/10.1074/jbc.M600290200
    • (2006) J Biol Chem , vol.281 , pp. 11736-11743
    • Bampi, C.1    Bibillo, A.2    Wendeler, M.3    Divita, G.4    Gorelick, R.J.5    Le Grice, S.F.6    Darlix, J.L.7
  • 70
    • 0029059339 scopus 로고
    • Complementation of vif-defective human immunodeficiency virus type 1 by primate, but not nonprimate, lentivirus vif genes
    • PMID:7769676
    • Simon JH, Southerling TE, Peterson JC, Meyer BE, Malim MH. Complementation of vif-defective human immunodeficiency virus type 1 by primate, but not nonprimate, lentivirus vif genes. J Virol 1995; 69:4166-72; PMID:7769676
    • (1995) J Virol , vol.69 , pp. 4166-4172
    • Simon, J.H.1    Southerling, T.E.2    Peterson, J.C.3    Meyer, B.E.4    Malim, M.H.5
  • 71
    • 84880428052 scopus 로고    scopus 로고
    • Gene loss and adaptation to hominids underlie the ancient origin of HIV-1
    • PMID:23870316
    • Etienne L, Hahn BH, Sharp PM, Matsen FA, Emerman M. Gene loss and adaptation to hominids underlie the ancient origin of HIV-1. Cell Host Microbe 2013; 14:85-92; PMID:23870316; http://dx.doi.org/10.1016/j.chom.2013.06.002
    • (2013) Cell Host Microbe , vol.14 , pp. 85-92
    • Etienne, L.1    Hahn, B.H.2    Sharp, P.M.3    Matsen, F.A.4    Emerman, M.5
  • 72
    • 84870057622 scopus 로고    scopus 로고
    • Intrinsically disordered proteins: A 10-year recap
    • PMID:22989858
    • Tompa P. Intrinsically disordered proteins: a 10-year recap. Trends Biochem Sci 2012; 37:509-16; PMID:22989858; http://dx.doi.org/10.1016/j.tibs.2012.08.004
    • (2012) Trends Biochem Sci , vol.37 , pp. 509-516
    • Tompa, P.1
  • 73
    • 84866644698 scopus 로고    scopus 로고
    • Diverse functional manifestations of intrinsic structural disorder in molecular chaperones
    • PMID:22988848
    • Kovacs D, Tompa P. Diverse functional manifestations of intrinsic structural disorder in molecular chaperones. Biochem Soc Trans 2012; 40:963-8; PMID:22988848; http://dx.doi.org/10.1042/BST20120108
    • (2012) Biochem Soc Trans , vol.40 , pp. 963-968
    • Kovacs, D.1    Tompa, P.2
  • 74
    • 84860843718 scopus 로고    scopus 로고
    • Protein intrinsic disorder as a flexible armor and a weapon of HIV-1
    • PMID:22033837
    • Xue B, Mizianty MJ, Kurgan L, Uversky VN. Protein intrinsic disorder as a flexible armor and a weapon of HIV-1. Cell Mol Life Sci 2012; 69:1211-59; PMID:22033837; http://dx.doi.org/10.1007/s00018-011-0859-3
    • (2012) Cell Mol Life Sci , vol.69 , pp. 1211-1259
    • Xue, B.1    Mizianty, M.J.2    Kurgan, L.3    Uversky, V.N.4
  • 75
    • 2242469712 scopus 로고    scopus 로고
    • Structure of the HIV-1 nucleocapsid protein bound to the SL3 psi-RNA recognition element
    • PMID:9430589
    • De Guzman RN, Wu ZR, Stalling CC, Pappalardo L, Borer PN, Summers MF. Structure of the HIV-1 nucleocapsid protein bound to the SL3 psi-RNA recognition element. Science 1998; 279:384-8; PMID:9430589; http://dx.doi.org/10.1126/science.279.5349.384
    • (1998) Science , vol.279 , pp. 384-388
    • De Guzman, R.N.1    Wu, Z.R.2    Stalling, C.C.3    Pappalardo, L.4    Borer, P.N.5    Summers, M.F.6
  • 76
    • 33845505955 scopus 로고    scopus 로고
    • Zinc binding to the HCCH motif of HIV-1 virion infectivity factor induces a conformational change that mediates protein-protein interactions
    • PMID:17132731
    • Paul I, Cui J, Maynard EL. Zinc binding to the HCCH motif of HIV-1 virion infectivity factor induces a conformational change that mediates protein-protein interactions. Proc Natl Acad Sci U S A 2006; 103:18475-80; PMID:17132731; http://dx.doi.org/10.1073/pnas.0604150103
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 18475-18480
    • Paul, I.1    Cui, J.2    Maynard, E.L.3
  • 78
    • 52649129852 scopus 로고    scopus 로고
    • Mutations in human immunodeficiency virus type 1 nucleocapsid protein zinc fingers cause premature reverse transcription
    • PMID:18667500
    • Thomas JA, Bosche WJ, Shatzer TL, Johnson DG, Gorelick RJ. Mutations in human immunodeficiency virus type 1 nucleocapsid protein zinc fingers cause premature reverse transcription. J Virol 2008; 82:9318-28; PMID:18667500; http://dx.doi.org/10.1128/JVI.00583-08
    • (2008) J Virol , vol.82 , pp. 9318-9328
    • Thomas, J.A.1    Bosche, W.J.2    Shatzer, T.L.3    Johnson, D.G.4    Gorelick, R.J.5
  • 79
    • 0029821868 scopus 로고    scopus 로고
    • Characterization of human immunodeficiency virus type 1 Vif particle incorporation
    • PMID:8709234
    • Camaur D, Trono D. Characterization of human immunodeficiency virus type 1 Vif particle incorporation. J Virol 1996; 70:6106-11; PMID:8709234
    • (1996) J Virol , vol.70 , pp. 6106-6111
    • Camaur, D.1    Trono, D.2
  • 80
    • 0029961360 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vif does not influence expression or virion incorporation of gag-, pol-, and env-encoded proteins
    • PMID:8970945
    • Fouchier RA, Simon JH, Jaffe AB, Malim MH. Human immunodeficiency virus type 1 Vif does not influence expression or virion incorporation of gag-, pol-, and env-encoded proteins. J Virol 1996; 70:8263-9; PMID:8970945
    • (1996) J Virol , vol.70 , pp. 8263-8269
    • Fouchier, R.A.1    Simon, J.H.2    Jaffe, A.B.3    Malim, M.H.4
  • 81
    • 0037155223 scopus 로고    scopus 로고
    • In vitro evidence for a long range pseudoknot in the 5′-untranslated and matrix coding regions of HIV-1 genomic RNA
    • PMID:11744696
    • Paillart JC, Skripkin E, Ehresmann B, Ehresmann C, Marquet R. In vitro evidence for a long range pseudoknot in the 5′-untranslated and matrix coding regions of HIV-1 genomic RNA. J Biol Chem 2002; 277:5995-6004; PMID:11744696; http://dx.doi.org/10.1074/jbc.M108972200
    • (2002) J Biol Chem , vol.277 , pp. 5995-6004
    • Paillart, J.C.1    Skripkin, E.2    Ehresmann, B.3    Ehresmann, C.4    Marquet, R.5
  • 82
    • 0028242962 scopus 로고
    • MC-Fit: Using Monte-Carlo methods to get accurate confidence limits on enzyme parameters
    • PMID:7922682
    • Dardel F. MC-Fit: using Monte-Carlo methods to get accurate confidence limits on enzyme parameters. Comput Appl Biosci 1994; 10:273-5; PMID:7922682
    • (1994) Comput Appl Biosci , vol.10 , pp. 273-275
    • Dardel, F.1
  • 83
    • 0026951903 scopus 로고
    • Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions
    • PMID:1490109
    • Piotto M, Saudek V, Sklenár V. Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions. J Biomol NMR 1992; 2:661-5; PMID:1490109; http://dx.doi.org/10.1007/BF02192855
    • (1992) J Biomol NMR , vol.2 , pp. 661-665
    • Piotto, M.1    Saudek, V.2    Sklenár, V.3
  • 84
    • 0032556228 scopus 로고    scopus 로고
    • Single scan, sensitivity- and gradient-enhanced TROSY for multidimensional NMR experiments
    • Weigelt J. Single scan, sensitivity- and gradient-enhanced TROSY for multidimensional NMR experiments. J Am Chem Soc 1998; 120:10778-9; http://dx.doi.org/10.1021/ja982649y
    • (1998) J Am Chem Soc , vol.120 , pp. 10778-10779
    • Weigelt, J.1
  • 85
    • 39449097872 scopus 로고    scopus 로고
    • RNA chaperoning and intrinsic disorder in the core proteins of Flaviviridae
    • PMID:18033802
    • Ivanyi-Nagy R, Lavergne JP, Gabus C, Ficheux D, Darlix JL. RNA chaperoning and intrinsic disorder in the core proteins of Flaviviridae. Nucleic Acids Res 2008; 36:712-25; PMID:18033802; http://dx.doi.org/10.1093/nar/gkm1051
    • (2008) Nucleic Acids Res , vol.36 , pp. 712-725
    • Ivanyi-Nagy, R.1    Lavergne, J.P.2    Gabus, C.3    Ficheux, D.4    Darlix, J.L.5
  • 86
    • 0027190754 scopus 로고
    • Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network
    • PMID:8332596
    • Andrade MA, Chacón P, Merelo JJ, Morán F. Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network. Protein Eng 1993; 6:383-90; PMID:8332596; http://dx.doi.org/10.1093/protein/6.4.383
    • (1993) Protein Eng , vol.6 , pp. 383-390
    • Andrade, M.A.1    Chacón, P.2    Merelo, J.J.3    Morán, F.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.