메뉴 건너뛰기




Volumn 10, Issue 1, 2013, Pages

Interactions between HIV-1 Vif and human ElonginB-ElonginC are important for CBF-β binding to Vif

Author keywords

CBF ; Elongin BC complex; HIV 1; Protein binding; Ubiquitin protein ligases; Vif

Indexed keywords

APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3G; CORE BINDING FACTOR BETA; CULLIN; CULLIN 5; ELONGIN B; ELONGIN C; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG; VIF PROTEIN;

EID: 84883145366     PISSN: None     EISSN: 17424690     Source Type: Journal    
DOI: 10.1186/1742-4690-10-94     Document Type: Article
Times cited : (22)

References (78)
  • 1
    • 44649139364 scopus 로고    scopus 로고
    • HIV-1 accessory proteins-ensuring viral survival in a hostile environment
    • 10.1016/j.chom.2008.04.008, 18541215
    • Malim MH, Emerman M. HIV-1 accessory proteins-ensuring viral survival in a hostile environment. Cell Host Microbe 2008, 3:388-398. 10.1016/j.chom.2008.04.008, 18541215.
    • (2008) Cell Host Microbe , vol.3 , pp. 388-398
    • Malim, M.H.1    Emerman, M.2
  • 2
    • 33846973677 scopus 로고    scopus 로고
    • Three-dimensional structure of HIV-1 VIF constructed by comparative modeling and the function characterization analyzed by molecular dynamics simulation
    • 10.1039/b612050d, 17285170
    • Lv W, Liu Z, Jin H, Yu X, Zhang L. Three-dimensional structure of HIV-1 VIF constructed by comparative modeling and the function characterization analyzed by molecular dynamics simulation. Org Biomol Chem 2007, 5:617-626. 10.1039/b612050d, 17285170.
    • (2007) Org Biomol Chem , vol.5 , pp. 617-626
    • Lv, W.1    Liu, Z.2    Jin, H.3    Yu, X.4    Zhang, L.5
  • 3
    • 0242320525 scopus 로고    scopus 로고
    • The HIV-1 Vif protein: a paradigm for viral: cell interactions
    • 10.1007/s00018-003-3192-7, 14618252
    • Pomerantz RJ. The HIV-1 Vif protein: a paradigm for viral: cell interactions. Cell Mol Life Sci 2003, 60:2017-2019. 10.1007/s00018-003-3192-7, 14618252.
    • (2003) Cell Mol Life Sci , vol.60 , pp. 2017-2019
    • Pomerantz, R.J.1
  • 5
    • 70350373664 scopus 로고    scopus 로고
    • Antiviral roles of APOBEC proteins against HIV-1 and suppression by Vif
    • 10.1007/s00705-009-0481-y, 19669862
    • Romani B, Engelbrecht S, Glashoff RH. Antiviral roles of APOBEC proteins against HIV-1 and suppression by Vif. Arch Virol 2009, 154:1579-1588. 10.1007/s00705-009-0481-y, 19669862.
    • (2009) Arch Virol , vol.154 , pp. 1579-1588
    • Romani, B.1    Engelbrecht, S.2    Glashoff, R.H.3
  • 6
    • 33750344250 scopus 로고    scopus 로고
    • Identification of APOBEC3DE as another antiretroviral factor from the human APOBEC family
    • 10.1128/JVI.01123-06, 1641744, 16920826
    • Dang Y, Wang X, Esselman WJ, Zheng YH. Identification of APOBEC3DE as another antiretroviral factor from the human APOBEC family. J Virol 2006, 80:10522-10533. 10.1128/JVI.01123-06, 1641744, 16920826.
    • (2006) J Virol , vol.80 , pp. 10522-10533
    • Dang, Y.1    Wang, X.2    Esselman, W.J.3    Zheng, Y.H.4
  • 7
    • 23844483541 scopus 로고    scopus 로고
    • Human APOBEC3B is a potent inhibitor of HIV-1 infectivity and is resistant to HIV-1 Vif
    • 10.1016/j.virol.2005.06.005, 15993456
    • Doehle BP, Schafer A, Cullen BR. Human APOBEC3B is a potent inhibitor of HIV-1 infectivity and is resistant to HIV-1 Vif. Virology 2005, 339:281-288. 10.1016/j.virol.2005.06.005, 15993456.
    • (2005) Virology , vol.339 , pp. 281-288
    • Doehle, B.P.1    Schafer, A.2    Cullen, B.R.3
  • 8
    • 0037043699 scopus 로고    scopus 로고
    • Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein
    • 10.1038/nature00939, 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, 418:646-650. 10.1038/nature00939, 12167863.
    • (2002) Nature , vol.418 , pp. 646-650
    • Sheehy, A.M.1    Gaddis, N.C.2    Choi, J.D.3    Malim, M.H.4
  • 9
    • 2442692812 scopus 로고    scopus 로고
    • Human APOBEC3F is another host factor that blocks human immunodeficiency virus type 1 replication
    • 10.1128/JVI.78.11.6073-6076.2004, 415831, 15141007
    • Zheng YH, Irwin D, Kurosu T, Tokunaga K, Sata T, Peterlin BM. Human APOBEC3F is another host factor that blocks human immunodeficiency virus type 1 replication. J Virol 2004, 78:6073-6076. 10.1128/JVI.78.11.6073-6076.2004, 415831, 15141007.
    • (2004) J Virol , vol.78 , pp. 6073-6076
    • Zheng, Y.H.1    Irwin, D.2    Kurosu, T.3    Tokunaga, K.4    Sata, T.5    Peterlin, B.M.6
  • 10
    • 3242712200 scopus 로고    scopus 로고
    • A second human antiretroviral factor, APOBEC3F, is suppressed by the HIV-1 and HIV-2 Vif proteins
    • 10.1038/sj.emboj.7600246, 423288, 15152192
    • Wiegand HL, Doehle BP, Bogerd HP, Cullen BR. A second human antiretroviral factor, APOBEC3F, is suppressed by the HIV-1 and HIV-2 Vif proteins. EMBO J 2004, 23:2451-2458. 10.1038/sj.emboj.7600246, 423288, 15152192.
    • (2004) EMBO J , vol.23 , pp. 2451-2458
    • Wiegand, H.L.1    Doehle, B.P.2    Bogerd, H.P.3    Cullen, B.R.4
  • 11
    • 33847636341 scopus 로고    scopus 로고
    • APOBEC-mediated viral restriction: not simply editing?
    • 10.1016/j.tibs.2007.01.004, 17303427
    • Holmes RK, Malim MH, Bishop KN. APOBEC-mediated viral restriction: not simply editing?. Trends Biochem Sci 2007, 32:118-128. 10.1016/j.tibs.2007.01.004, 17303427.
    • (2007) Trends Biochem Sci , vol.32 , pp. 118-128
    • Holmes, R.K.1    Malim, M.H.2    Bishop, K.N.3
  • 13
    • 0242578406 scopus 로고    scopus 로고
    • Induction of APOBEC3G ubiquitination and degradation by an HIV-1 Vif-Cul5-SCF complex
    • 10.1126/science.1089591, 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, 302:1056-1060. 10.1126/science.1089591, 14564014.
    • (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
  • 15
    • 22544465590 scopus 로고    scopus 로고
    • Regulation of Apobec3F and human immunodeficiency virus type 1 Vif by Vif-Cul5-ElonB/C E3 ubiquitin ligase
    • 10.1128/JVI.79.15.9579-9587.2005, 1181563, 16014920
    • Liu B, Sarkis PT, Luo K, Yu Y, Yu XF. Regulation of Apobec3F and human immunodeficiency virus type 1 Vif by Vif-Cul5-ElonB/C E3 ubiquitin ligase. J Virol 2005, 79:9579-9587. 10.1128/JVI.79.15.9579-9587.2005, 1181563, 16014920.
    • (2005) J Virol , vol.79 , pp. 9579-9587
    • Liu, B.1    Sarkis, P.T.2    Luo, K.3    Yu, Y.4    Yu, X.F.5
  • 16
    • 0344413641 scopus 로고    scopus 로고
    • The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif
    • 10.1038/nm945, 14528300
    • Sheehy AM, Gaddis NC, Malim MH. The antiretroviral enzyme APOBEC3G is degraded by the proteasome in response to HIV-1 Vif. Nat Med 2003, 9:1404-1407. 10.1038/nm945, 14528300.
    • (2003) Nat Med , vol.9 , pp. 1404-1407
    • Sheehy, A.M.1    Gaddis, N.C.2    Malim, M.H.3
  • 17
    • 0344845196 scopus 로고    scopus 로고
    • HIV-1 Vif protein binds the editing enzyme APOBEC3G and induces its degradation
    • 10.1038/nm946, 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, 9:1398-1403. 10.1038/nm946, 14528301.
    • (2003) Nat Med , vol.9 , pp. 1398-1403
    • Marin, M.1    Rose, K.M.2    Kozak, S.L.3    Kabat, D.4
  • 18
    • 77953757638 scopus 로고    scopus 로고
    • Dissection of the HIV Vif interaction with human E3 ubiquitin ligase
    • 10.1128/JVI.00031-10, 2898223, 20463065
    • Wolfe LS, Stanley BJ, Liu C, Eliason WK, Xiong Y. Dissection of the HIV Vif interaction with human E3 ubiquitin ligase. J Virol 2010, 84:7135-7139. 10.1128/JVI.00031-10, 2898223, 20463065.
    • (2010) J Virol , vol.84 , pp. 7135-7139
    • Wolfe, L.S.1    Stanley, B.J.2    Liu, C.3    Eliason, W.K.4    Xiong, Y.5
  • 19
    • 41249100869 scopus 로고    scopus 로고
    • Advances in the structural understanding of Vif proteins
    • 10.2174/157016208783885056, 2704546, 18336256
    • Barraud P, Paillart JC, Marquet R, Tisne C. Advances in the structural understanding of Vif proteins. Curr HIV Res 2008, 6:91-99. 10.2174/157016208783885056, 2704546, 18336256.
    • (2008) Curr HIV Res , vol.6 , pp. 91-99
    • Barraud, P.1    Paillart, J.C.2    Marquet, R.3    Tisne, C.4
  • 20
    • 84873043568 scopus 로고    scopus 로고
    • Differential Requirements for HIV-1 Vif-mediated APOBEC3G degradation and RUNX1-mediated transcription by core binding factor beta
    • 3554157, 23175372
    • Du J, Zhao K, Rui Y, Li P, Zhou X, Zhang W, Yu XF. Differential Requirements for HIV-1 Vif-mediated APOBEC3G degradation and RUNX1-mediated transcription by core binding factor beta. J Virol 2012, 87:1906-1911. 3554157, 23175372.
    • (2012) J Virol , vol.87 , pp. 1906-1911
    • Du, J.1    Zhao, K.2    Rui, Y.3    Li, P.4    Zhou, X.5    Zhang, W.6    Yu, X.F.7
  • 21
    • 84870002103 scopus 로고    scopus 로고
    • HIV type 1 viral infectivity factor and the RUNX transcription factors interact with core binding factor beta on genetically distinct surfaces
    • 10.1089/aid.2012.0142, 22725134
    • Hultquist JF, McDougle RM, Anderson BD, Harris RS. HIV type 1 viral infectivity factor and the RUNX transcription factors interact with core binding factor beta on genetically distinct surfaces. AIDS Res Hum Retroviruses 2012, 28:1543-1551. 10.1089/aid.2012.0142, 22725134.
    • (2012) AIDS Res Hum Retroviruses , vol.28 , pp. 1543-1551
    • Hultquist, J.F.1    McDougle, R.M.2    Anderson, B.D.3    Harris, R.S.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
    • 10.1128/JVI.80.6.3112-3115.2006, 1395459, 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, 80:3112-3115. 10.1128/JVI.80.6.3112-3115.2006, 1395459, 16501124.
    • (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
    • 36348946397 scopus 로고    scopus 로고
    • Identification of an APOBEC3G binding site in human immunodeficiency virus type 1 Vif and inhibitors of Vif-APOBEC3G binding
    • 10.1128/JVI.00204-07, 2169136, 17898068
    • Mehle A, Wilson H, Zhang C, Brazier AJ, McPike M, Pery E, Gabuzda D. Identification of an APOBEC3G binding site in human immunodeficiency virus type 1 Vif and inhibitors of Vif-APOBEC3G binding. J Virol 2007, 81:13235-13241. 10.1128/JVI.00204-07, 2169136, 17898068.
    • (2007) J Virol , vol.81 , pp. 13235-13241
    • Mehle, A.1    Wilson, H.2    Zhang, C.3    Brazier, A.J.4    McPike, M.5    Pery, E.6    Gabuzda, D.7
  • 24
    • 34547119261 scopus 로고    scopus 로고
    • Identification of two distinct human immunodeficiency virus type 1 Vif determinants critical for interactions with human APOBEC3G and APOBEC3F
    • 10.1128/JVI.00395-07, 1951317, 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, 81:8201-8210. 10.1128/JVI.00395-07, 1951317, 17522216.
    • (2007) J Virol , vol.81 , pp. 8201-8210
    • Russell, R.A.1    Pathak, V.K.2
  • 25
    • 84857865923 scopus 로고    scopus 로고
    • Vif proteins of human and simian immunodeficiency viruses require cellular CBFbeta to degrade APOBEC3 restriction factors
    • 3302251, 22205746
    • Hultquist JF, Binka M, LaRue RS, Simon V, Harris RS. Vif proteins of human and simian immunodeficiency viruses require cellular CBFbeta to degrade APOBEC3 restriction factors. J Virol 2011, 86:2874-2877. 3302251, 22205746.
    • (2011) 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
  • 26
    • 77954684927 scopus 로고    scopus 로고
    • The SOCS-box of HIV-1 Vif interacts with ElonginBC by induced-folding to recruit its Cul5-containing ubiquitin ligase complex
    • 10.1371/journal.ppat.1000925, 2880568, 20532212
    • Bergeron JR, Huthoff H, Veselkov DA, Beavil RL, Simpson PJ, Matthews SJ, Malim MH, Sanderson MR. The SOCS-box of HIV-1 Vif interacts with ElonginBC by induced-folding to recruit its Cul5-containing ubiquitin ligase complex. PLoS Pathog 2010, 6:e1000925. 10.1371/journal.ppat.1000925, 2880568, 20532212.
    • (2010) PLoS Pathog , vol.6
    • Bergeron, J.R.1    Huthoff, H.2    Veselkov, D.A.3    Beavil, R.L.4    Simpson, P.J.5    Matthews, S.J.6    Malim, M.H.7    Sanderson, M.R.8
  • 27
    • 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
    • 10.1101/gad.1250204, 534647, 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, 18:2867-2872. 10.1101/gad.1250204, 534647, 15574593.
    • (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
  • 28
    • 50149097544 scopus 로고    scopus 로고
    • Structural insight into the human immunodeficiency virus Vif SOCS box and its role in human E3 ubiquitin ligase assembly
    • 10.1128/JVI.00767-08, 2519636, 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, 82:8656-8663. 10.1128/JVI.00767-08, 2519636, 18562529.
    • (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
  • 29
    • 33745225450 scopus 로고    scopus 로고
    • A zinc-binding region in Vif binds Cul5 and determines cullin selection
    • 10.1074/jbc.M602413200, 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, 281:17259-17265. 10.1074/jbc.M602413200, 16636053.
    • (2006) J Biol Chem , vol.281 , pp. 17259-17265
    • Mehle, A.1    Thomas, E.R.2    Rajendran, K.S.3    Gabuzda, D.4
  • 30
    • 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
    • 10.1073/pnas.0604150103, 1693687, 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, 103:18475-18480. 10.1073/pnas.0604150103, 1693687, 17132731.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 18475-18480
    • Paul, I.1    Cui, J.2    Maynard, E.L.3
  • 31
    • 33646866382 scopus 로고    scopus 로고
    • Assembly of HIV-1 Vif-Cul5 E3 ubiquitin ligase through a novel zinc-binding domain-stabilized hydrophobic interface in Vif
    • 10.1016/j.virol.2006.02.002, 16530799
    • Xiao Z, Ehrlich E, Yu Y, Luo K, Wang T, Tian C, Yu XF. Assembly of HIV-1 Vif-Cul5 E3 ubiquitin ligase through a novel zinc-binding domain-stabilized hydrophobic interface in Vif. Virology 2006, 349:290-299. 10.1016/j.virol.2006.02.002, 16530799.
    • (2006) Virology , vol.349 , pp. 290-299
    • Xiao, Z.1    Ehrlich, E.2    Yu, Y.3    Luo, K.4    Wang, T.5    Tian, C.6    Yu, X.F.7
  • 32
    • 23844473725 scopus 로고    scopus 로고
    • Primate lentiviral virion infectivity factors are substrate receptors that assemble with cullin 5-E3 ligase through a HCCH motif to suppress APOBEC3G
    • 10.1073/pnas.0502440102, 1182177, 16076960
    • Luo K, Xiao Z, Ehrlich E, Yu Y, Liu B, Zheng S, Yu XF. Primate lentiviral virion infectivity factors are substrate receptors that assemble with cullin 5-E3 ligase through a HCCH motif to suppress APOBEC3G. Proc Natl Acad Sci U S A 2005, 102:11444-11449. 10.1073/pnas.0502440102, 1182177, 16076960.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 11444-11449
    • Luo, K.1    Xiao, Z.2    Ehrlich, E.3    Yu, Y.4    Liu, B.5    Zheng, S.6    Yu, X.F.7
  • 33
    • 84856014513 scopus 로고    scopus 로고
    • T-cell differentiation factor CBF-beta regulates HIV-1 Vif-mediated evasion of host restriction
    • Zhang W, Du J, Evans SL, Yu Y, Yu XF. T-cell differentiation factor CBF-beta regulates HIV-1 Vif-mediated evasion of host restriction. Nature 2011, 481:376-379.
    • (2011) Nature , vol.481 , pp. 376-379
    • Zhang, W.1    Du, J.2    Evans, S.L.3    Yu, Y.4    Yu, X.F.5
  • 34
    • 84874283933 scopus 로고    scopus 로고
    • CBFbeta Stabilizes HIV Vif to counteract APOBEC3 at the expense of RUNX1 target gene expression
    • 10.1016/j.molcel.2012.12.012, 23333304
    • Kim DY, Kwon E, Hartley PD, Crosby DC, Mann S, Krogan NJ, Gross JD. CBFbeta Stabilizes HIV Vif to counteract APOBEC3 at the expense of RUNX1 target gene expression. Mol Cell 2013, 49:632-644. 10.1016/j.molcel.2012.12.012, 23333304.
    • (2013) Mol Cell , vol.49 , pp. 632-644
    • Kim, D.Y.1    Kwon, E.2    Hartley, P.D.3    Crosby, D.C.4    Mann, S.5    Krogan, N.J.6    Gross, J.D.7
  • 37
    • 0027378324 scopus 로고
    • RNA polymerase II transcription factor SIII. I: identification, purification, and properties
    • Bradsher JN, Jackson KW, Conaway RC, Conaway JW. RNA polymerase II transcription factor SIII. I: identification, purification, and properties. J Biol Chem 1993, 268:25587-25593.
    • (1993) J Biol Chem , vol.268 , pp. 25587-25593
    • Bradsher, J.N.1    Jackson, K.W.2    Conaway, R.C.3    Conaway, J.W.4
  • 38
    • 0029084914 scopus 로고
    • Elongin (SIII): a multisubunit regulator of elongation by RNA polymerase II
    • 10.1126/science.7660129, 7660129
    • Aso T, Lane WS, Conaway JW, Conaway RC. Elongin (SIII): a multisubunit regulator of elongation by RNA polymerase II. Science 1995, 269:1439-1443. 10.1126/science.7660129, 7660129.
    • (1995) Science , vol.269 , pp. 1439-1443
    • Aso, T.1    Lane, W.S.2    Conaway, J.W.3    Conaway, R.C.4
  • 39
    • 0035577765 scopus 로고    scopus 로고
    • Degradation of p53 by adenovirus E4orf6 and E1B55K proteins occurs via a novel mechanism involving a Cullin-containing complex
    • 10.1101/gad.926401, 312842, 11731475
    • Querido E, Blanchette P, Yan Q, Kamura T, Morrison M, Boivin D, Kaelin WG, Conaway RC, Conaway JW, Branton PE. Degradation of p53 by adenovirus E4orf6 and E1B55K proteins occurs via a novel mechanism involving a Cullin-containing complex. Genes Dev 2001, 15:3104-3117. 10.1101/gad.926401, 312842, 11731475.
    • (2001) Genes Dev , vol.15 , pp. 3104-3117
    • Querido, E.1    Blanchette, P.2    Yan, Q.3    Kamura, T.4    Morrison, M.5    Boivin, D.6    Kaelin, W.G.7    Conaway, R.C.8    Conaway, J.W.9    Branton, P.E.10
  • 40
    • 0033776536 scopus 로고    scopus 로고
    • Ubiquitination of hypoxia-inducible factor requires direct binding to the beta-domain of the von Hippel-Lindau protein
    • 10.1038/35017054, 10878807
    • Ohh M, Park CW, Ivan M, Hoffman MA, Kim TY, Huang LE, Pavletich N, Chau V, Kaelin WG. Ubiquitination of hypoxia-inducible factor requires direct binding to the beta-domain of the von Hippel-Lindau protein. Nat Cell Biol 2000, 2:423-427. 10.1038/35017054, 10878807.
    • (2000) Nat Cell Biol , vol.2 , pp. 423-427
    • Ohh, M.1    Park, C.W.2    Ivan, M.3    Hoffman, M.A.4    Kim, T.Y.5    Huang, L.E.6    Pavletich, N.7    Chau, V.8    Kaelin, W.G.9
  • 41
    • 0035036625 scopus 로고    scopus 로고
    • Socs-1 inhibits TEL-JAK2-mediated transformation of hematopoietic cells through inhibition of JAK2 kinase activity and induction of proteasome-mediated degradation
    • 10.1128/MCB.21.10.3547-3557.2001, 100276, 11313480
    • Frantsve J, Schwaller J, Sternberg DW, Kutok J, Gilliland DG. Socs-1 inhibits TEL-JAK2-mediated transformation of hematopoietic cells through inhibition of JAK2 kinase activity and induction of proteasome-mediated degradation. Mol Cell Biol 2001, 21:3547-3557. 10.1128/MCB.21.10.3547-3557.2001, 100276, 11313480.
    • (2001) Mol Cell Biol , vol.21 , pp. 3547-3557
    • Frantsve, J.1    Schwaller, J.2    Sternberg, D.W.3    Kutok, J.4    Gilliland, D.G.5
  • 42
    • 13044263097 scopus 로고    scopus 로고
    • The conserved SOCS box motif in suppressors of cytokine signaling binds to elongins B and C and may couple bound proteins to proteasomal degradation
    • 10.1073/pnas.96.5.2071, 26738, 10051596
    • Zhang JG, Farley A, Nicholson SE, Willson TA, Zugaro LM, Simpson RJ, Moritz RL, Cary D, Richardson R, Hausmann G, et al. The conserved SOCS box motif in suppressors of cytokine signaling binds to elongins B and C and may couple bound proteins to proteasomal degradation. Proc Natl Acad Sci U S A 1999, 96:2071-2076. 10.1073/pnas.96.5.2071, 26738, 10051596.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 2071-2076
    • Zhang, J.G.1    Farley, A.2    Nicholson, S.E.3    Willson, T.A.4    Zugaro, L.M.5    Simpson, R.J.6    Moritz, R.L.7    Cary, D.8    Richardson, R.9    Hausmann, G.10
  • 43
    • 67649964217 scopus 로고    scopus 로고
    • RING domain E3 ubiquitin ligases
    • 10.1146/annurev.biochem.78.101807.093809, 19489725
    • Deshaies RJ, Joazeiro CA. RING domain E3 ubiquitin ligases. Annu Rev Biochem 2009, 78:399-434. 10.1146/annurev.biochem.78.101807.093809, 19489725.
    • (2009) Annu Rev Biochem , vol.78 , pp. 399-434
    • Deshaies, R.J.1    Joazeiro, C.A.2
  • 44
    • 0032535364 scopus 로고    scopus 로고
    • The Elongin BC complex interacts with the conserved SOCS-box motif present in members of the SOCS, ras, WD-40 repeat, and ankyrin repeat families
    • 10.1101/gad.12.24.3872, 317264, 9869640
    • Kamura T, Sato S, Haque D, Liu L, Kaelin WG, Conaway RC, Conaway JW. The Elongin BC complex interacts with the conserved SOCS-box motif present in members of the SOCS, ras, WD-40 repeat, and ankyrin repeat families. Genes Dev 1998, 12:3872-3881. 10.1101/gad.12.24.3872, 317264, 9869640.
    • (1998) Genes Dev , vol.12 , pp. 3872-3881
    • Kamura, T.1    Sato, S.2    Haque, D.3    Liu, L.4    Kaelin, W.G.5    Conaway, R.C.6    Conaway, J.W.7
  • 45
    • 0033776182 scopus 로고    scopus 로고
    • VHL takes HIF's breath away
    • 10.1038/35017129, 10878820
    • Krek W. VHL takes HIF's breath away. Nat Cell Biol 2000, 2:E121-E123. 10.1038/35017129, 10878820.
    • (2000) Nat Cell Biol , vol.2
    • Krek, W.1
  • 47
  • 49
    • 35748984946 scopus 로고    scopus 로고
    • Structure of the SOCS4-ElonginB/C complex reveals a distinct SOCS box interface and the molecular basis for SOCS-dependent EGFR degradation
    • 10.1016/j.str.2007.09.016, 2225448, 17997974
    • Bullock AN, Rodriguez MC, Debreczeni JE, Songyang Z, Knapp S. Structure of the SOCS4-ElonginB/C complex reveals a distinct SOCS box interface and the molecular basis for SOCS-dependent EGFR degradation. Structure 2007, 15:1493-1504. 10.1016/j.str.2007.09.016, 2225448, 17997974.
    • (2007) Structure , vol.15 , pp. 1493-1504
    • Bullock, A.N.1    Rodriguez, M.C.2    Debreczeni, J.E.3    Songyang, Z.4    Knapp, S.5
  • 50
    • 33646733227 scopus 로고    scopus 로고
    • Crystal structure of the SOCS2-elongin C-elongin B complex defines a prototypical SOCS box ubiquitin ligase
    • 10.1073/pnas.0601638103, 1472497, 16675548
    • Bullock AN, Debreczeni JE, Edwards AM, Sundstrom M, Knapp S. Crystal structure of the SOCS2-elongin C-elongin B complex defines a prototypical SOCS box ubiquitin ligase. Proc Natl Acad Sci U S A 2006, 103:7637-7642. 10.1073/pnas.0601638103, 1472497, 16675548.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 7637-7642
    • Bullock, A.N.1    Debreczeni, J.E.2    Edwards, A.M.3    Sundstrom, M.4    Knapp, S.5
  • 51
    • 84859119983 scopus 로고    scopus 로고
    • Characterization of the interaction of full-length HIV-1 Vif protein with its key regulator CBFbeta and CRL5 E3 ubiquitin ligase components
    • 10.1371/journal.pone.0033495, 3316577, 22479405
    • Zhou X, Evans SL, Han X, Liu Y, Yu XF. Characterization of the interaction of full-length HIV-1 Vif protein with its key regulator CBFbeta and CRL5 E3 ubiquitin ligase components. PLoS One 2012, 7:e33495. 10.1371/journal.pone.0033495, 3316577, 22479405.
    • (2012) PLoS One , vol.7
    • Zhou, X.1    Evans, S.L.2    Han, X.3    Liu, Y.4    Yu, X.F.5
  • 52
    • 65349148040 scopus 로고    scopus 로고
    • The C-terminal domain of the HIV-1 Vif protein is natively unfolded in its unbound state
    • 10.1093/protein/gzp004, 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, 22:281-287. 10.1093/protein/gzp004, 19218568.
    • (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
  • 53
    • 79956119050 scopus 로고    scopus 로고
    • Elongin B-mediated epigenetic alteration of viral chromatin correlates with efficient human cytomegalovirus gene expression and replication
    • 3063379, 21447700
    • Hwang J, Saffert RT, Kalejta RF. Elongin B-mediated epigenetic alteration of viral chromatin correlates with efficient human cytomegalovirus gene expression and replication. MBio 2011, 2:e00023-00011. 3063379, 21447700.
    • (2011) MBio , vol.2
    • Hwang, J.1    Saffert, R.T.2    Kalejta, R.F.3
  • 54
    • 0141638436 scopus 로고    scopus 로고
    • HIV-1 Vif blocks the antiviral activity of APOBEC3G by impairing both its translation and intracellular stability
    • 10.1016/S1097-2765(03)00353-8, 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. 10.1016/S1097-2765(03)00353-8, 14527406.
    • (2003) Mol Cell , vol.12 , pp. 591-601
    • Stopak, K.1    De Noronha, C.2    Yonemoto, W.3    Greene, W.C.4
  • 55
    • 46549089412 scopus 로고    scopus 로고
    • The HIV-1 Vif PPLP motif is necessary for human APOBEC3G binding and degradation
    • 10.1016/j.virol.2008.04.017, 2474554, 18499212
    • Donahue JP, Vetter ML, Mukhtar NA, D'Aquila RT. The HIV-1 Vif PPLP motif is necessary for human APOBEC3G binding and degradation. Virology 2008, 377:49-53. 10.1016/j.virol.2008.04.017, 2474554, 18499212.
    • (2008) Virology , vol.377 , pp. 49-53
    • Donahue, J.P.1    Vetter, M.L.2    Mukhtar, N.A.3    D'Aquila, R.T.4
  • 56
    • 1842425615 scopus 로고    scopus 로고
    • High level expression of human immunodeficiency virus type-1 Vif inhibits viral infectivity by modulating proteolytic processing of the Gag precursor at the p2/nucleocapsid processing site
    • Akari H, Fujita M, Kao S, Khan MA, Shehu-Xhilaga M, Adachi A, Strebel K. High level expression of human immunodeficiency virus type-1 Vif inhibits viral infectivity by modulating proteolytic processing of the Gag precursor at the p2/nucleocapsid processing site. J Biol Chem 2004, 279:12355-12362.
    • (2004) J Biol Chem , vol.279 , pp. 12355-12362
    • Akari, H.1    Fujita, M.2    Kao, S.3    Khan, M.A.4    Shehu-Xhilaga, M.5    Adachi, A.6    Strebel, K.7
  • 58
    • 0034682465 scopus 로고    scopus 로고
    • Elongin BC complex prevents degradation of von Hippel-Lindau tumor suppressor gene products
    • 10.1073/pnas.97.15.8507, 26978, 10900011
    • Schoenfeld AR, Davidowitz EJ, Burk RD. Elongin BC complex prevents degradation of von Hippel-Lindau tumor suppressor gene products. Proc Natl Acad Sci U S A 2000, 97:8507-8512. 10.1073/pnas.97.15.8507, 26978, 10900011.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 8507-8512
    • Schoenfeld, A.R.1    Davidowitz, E.J.2    Burk, R.D.3
  • 59
    • 45149106103 scopus 로고    scopus 로고
    • APOBEC3G is degraded by the proteasomal pathway in a Vif-dependent manner without being polyubiquitylated
    • 10.1074/jbc.M708728200, 2430655,2430655, 18326044
    • Dang Y, Siew LM, Zheng YH. APOBEC3G is degraded by the proteasomal pathway in a Vif-dependent manner without being polyubiquitylated. J Biol Chem 2008, 283:13124-13131. 10.1074/jbc.M708728200, 2430655,2430655, 18326044.
    • (2008) J Biol Chem , vol.283 , pp. 13124-13131
    • Dang, Y.1    Siew, L.M.2    Zheng, Y.H.3
  • 60
    • 3242702452 scopus 로고    scopus 로고
    • Expression of HIV-1 accessory protein Vif is controlled uniquely to be low and optimal by proteasome degradation
    • 10.1016/j.micinf.2004.04.011, 15374000
    • Fujita M, Akari H, Sakurai A, Yoshida A, Chiba T, Tanaka K, Strebel K, Adachi A. Expression of HIV-1 accessory protein Vif is controlled uniquely to be low and optimal by proteasome degradation. Microbes Infect 2004, 6:791-798. 10.1016/j.micinf.2004.04.011, 15374000.
    • (2004) Microbes Infect , vol.6 , pp. 791-798
    • Fujita, M.1    Akari, H.2    Sakurai, A.3    Yoshida, A.4    Chiba, T.5    Tanaka, K.6    Strebel, K.7    Adachi, A.8
  • 61
    • 1542379821 scopus 로고    scopus 로고
    • Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway
    • Mehle A, Strack B, Ancuta P, Zhang C, McPike M, Gabuzda D. Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway. J Biol Chem 2004, 279:7792-7798.
    • (2004) J Biol Chem , vol.279 , pp. 7792-7798
    • Mehle, A.1    Strack, B.2    Ancuta, P.3    Zhang, C.4    McPike, M.5    Gabuzda, D.6
  • 62
    • 0035895435 scopus 로고    scopus 로고
    • Dissecting the interaction network of multiprotein complexes by pairwise coexpression of subunits in E. coli
    • 10.1006/jmbi.2000.4376, 11237605
    • Fribourg S, Romier C, Werten S, Gangloff YG, Poterszman A, Moras D. Dissecting the interaction network of multiprotein complexes by pairwise coexpression of subunits in E. coli. J Mol Biol 2001, 306:363-373. 10.1006/jmbi.2000.4376, 11237605.
    • (2001) J Mol Biol , vol.306 , pp. 363-373
    • Fribourg, S.1    Romier, C.2    Werten, S.3    Gangloff, Y.G.4    Poterszman, A.5    Moras, D.6
  • 63
    • 0034963119 scopus 로고    scopus 로고
    • A modular polycistronic expression system for overexpressing protein complexes in Escherichia coli
    • 10.1006/prep.2000.1363, 11162410
    • Tan S. A modular polycistronic expression system for overexpressing protein complexes in Escherichia coli. Protein Expr Purif 2001, 21:224-234. 10.1006/prep.2000.1363, 11162410.
    • (2001) Protein Expr Purif , vol.21 , pp. 224-234
    • Tan, S.1
  • 64
    • 0032822103 scopus 로고    scopus 로고
    • Principles of protein folding in the cellular environment
    • 10.1016/S0959-440X(99)80013-X, 10047582
    • Ellis RJ, Hartl FU. Principles of protein folding in the cellular environment. Curr Opin Struct Biol 1999, 9:102-110. 10.1016/S0959-440X(99)80013-X, 10047582.
    • (1999) Curr Opin Struct Biol , vol.9 , pp. 102-110
    • Ellis, R.J.1    Hartl, F.U.2
  • 65
    • 0031923551 scopus 로고    scopus 로고
    • Protein self-organization in vitro and in vivo: partitioning between physical biochemistry and cell biology
    • Jaenicke R. Protein self-organization in vitro and in vivo: partitioning between physical biochemistry and cell biology. Biol Chem 1998, 379:237-243.
    • (1998) Biol Chem , vol.379 , pp. 237-243
    • Jaenicke, R.1
  • 66
    • 0029923751 scopus 로고    scopus 로고
    • Structure of the C-terminal end of the nascent peptide influences translation termination
    • 450081, 8612594
    • Bjornsson A, Mottagui-Tabar S, Isaksson LA. Structure of the C-terminal end of the nascent peptide influences translation termination. EMBO J 1996, 15:1696-1704. 450081, 8612594.
    • (1996) EMBO J , vol.15 , pp. 1696-1704
    • Bjornsson, A.1    Mottagui-Tabar, S.2    Isaksson, L.A.3
  • 68
    • 33751419975 scopus 로고    scopus 로고
    • Strategies to maximize heterologous protein expression in Escherichia coli with minimal cost
    • 10.1016/j.pep.2006.06.024, 16904906
    • Peti W, Page R. Strategies to maximize heterologous protein expression in Escherichia coli with minimal cost. Protein Expr Purif 2007, 51:1-10. 10.1016/j.pep.2006.06.024, 16904906.
    • (2007) Protein Expr Purif , vol.51 , pp. 1-10
    • Peti, W.1    Page, R.2
  • 70
    • 0033404668 scopus 로고    scopus 로고
    • Synthetic peptides define critical contacts between elongin C, elongin B, and the von Hippel-Lindau protein
    • 10.1172/JCI8161, 481054, 10587522
    • Ohh M, Takagi Y, Aso T, Stebbins CE, Pavletich NP, Zbar B, Conaway RC, Conaway JW, Kaelin WG. Synthetic peptides define critical contacts between elongin C, elongin B, and the von Hippel-Lindau protein. J Clin Invest 1999, 104:1583-1591. 10.1172/JCI8161, 481054, 10587522.
    • (1999) J Clin Invest , vol.104 , pp. 1583-1591
    • Ohh, M.1    Takagi, Y.2    Aso, T.3    Stebbins, C.E.4    Pavletich, N.P.5    Zbar, B.6    Conaway, R.C.7    Conaway, J.W.8    Kaelin, W.G.9
  • 71
    • 0033574737 scopus 로고    scopus 로고
    • Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function
    • 10.1126/science.284.5413.455, 10205047
    • Stebbins CE, Kaelin WG, Pavletich NP. Structure of the VHL-ElonginC-ElonginB complex: implications for VHL tumor suppressor function. Science 1999, 284:455-461. 10.1126/science.284.5413.455, 10205047.
    • (1999) Science , vol.284 , pp. 455-461
    • Stebbins, C.E.1    Kaelin, W.G.2    Pavletich, N.P.3
  • 72
    • 0023644679 scopus 로고
    • Structure of ubiquitin refined at 1.8 A resolution
    • 10.1016/0022-2836(87)90679-6, 3041007
    • Vijay-Kumar S, Bugg CE, Cook WJ. Structure of ubiquitin refined at 1.8 A resolution. J Mol Biol 1987, 194:531-544. 10.1016/0022-2836(87)90679-6, 3041007.
    • (1987) J Mol Biol , vol.194 , pp. 531-544
    • Vijay-Kumar, S.1    Bugg, C.E.2    Cook, W.J.3
  • 73
    • 34249784818 scopus 로고    scopus 로고
    • Adenovirus E4orf6 assembles with Cullin5-ElonginB-ElonginC E3 ubiquitin ligase through an HIV/SIV Vif-like BC-box to regulate p53
    • 10.1096/fj.06-7241com, 17351129
    • Luo K, Ehrlich E, Xiao Z, Zhang W, Ketner G, Yu XF. Adenovirus E4orf6 assembles with Cullin5-ElonginB-ElonginC E3 ubiquitin ligase through an HIV/SIV Vif-like BC-box to regulate p53. FASEB J 2007, 21:1742-1750. 10.1096/fj.06-7241com, 17351129.
    • (2007) FASEB J , vol.21 , pp. 1742-1750
    • Luo, K.1    Ehrlich, E.2    Xiao, Z.3    Zhang, W.4    Ketner, G.5    Yu, X.F.6
  • 74
    • 35448967068 scopus 로고    scopus 로고
    • Ternary complex formation of pVHL, elongin B and elongin C visualized in living cells by a fluorescence resonance energy transfer-fluorescence lifetime imaging microscopy technique
    • 10.1111/j.1742-4658.2007.06075.x, 17922844
    • Kinoshita K, Goryo K, Takada M, Tomokuni Y, Aso T, Okuda H, Shuin T, Fukumura H, Sogawa K. Ternary complex formation of pVHL, elongin B and elongin C visualized in living cells by a fluorescence resonance energy transfer-fluorescence lifetime imaging microscopy technique. FEBS J 2007, 274:5567-5575. 10.1111/j.1742-4658.2007.06075.x, 17922844.
    • (2007) FEBS J , vol.274 , pp. 5567-5575
    • Kinoshita, K.1    Goryo, K.2    Takada, M.3    Tomokuni, Y.4    Aso, T.5    Okuda, H.6    Shuin, T.7    Fukumura, H.8    Sogawa, K.9
  • 75
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • 10.1038/381571a0, 8637592
    • Hartl FU. Molecular chaperones in cellular protein folding. Nature 1996, 381:571-579. 10.1038/381571a0, 8637592.
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 76
    • 24644437419 scopus 로고    scopus 로고
    • Protein degradation and aging
    • 10.1016/j.exger.2005.07.005, 16125351
    • Martinez-Vicente M, Sovak G, Cuervo AM. Protein degradation and aging. Exp Gerontol 2005, 40:622-633. 10.1016/j.exger.2005.07.005, 16125351.
    • (2005) Exp Gerontol , vol.40 , pp. 622-633
    • Martinez-Vicente, M.1    Sovak, G.2    Cuervo, A.M.3
  • 77
    • 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
    • 10.1371/journal.pone.0003963, 2597746, 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. 10.1371/journal.pone.0003963, 2597746, 19088851.
    • (2008) PLoS One , vol.3
    • Zhang, W.1    Chen, G.2    Niewiadomska, A.M.3    Xu, R.4    Yu, X.F.5
  • 78
    • 84861313225 scopus 로고    scopus 로고
    • Small-molecule inhibition of human immunodeficiency virus type 1 replication by targeting the interaction between Vif and ElonginC
    • 10.1128/JVI.06957-11, 3347289, 22379088
    • Zuo T, Liu D, Lv W, Wang X, Wang J, Lv M, Huang W, Wu J, Zhang H, Jin H, et al. Small-molecule inhibition of human immunodeficiency virus type 1 replication by targeting the interaction between Vif and ElonginC. J Virol 2012, 86:5497-5507. 10.1128/JVI.06957-11, 3347289, 22379088.
    • (2012) J Virol , vol.86 , pp. 5497-5507
    • Zuo, T.1    Liu, D.2    Lv, W.3    Wang, X.4    Wang, J.5    Lv, M.6    Huang, W.7    Wu, J.8    Zhang, H.9    Jin, H.10


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.