메뉴 건너뛰기




Volumn 5, Issue , 2008, Pages

APOBEC3G-UBA2 fusion as a potential strategy for stable expression of APOBEC3G and inhibition of HIV-1 replication

Author keywords

[No Author keywords available]

Indexed keywords

APOLIPOPROTEIN B MESSENGER RNA EDITING ENZYME CATALYTIC POLYPEPTIDE 3G UBIQUITIN ASSOCIATED DOMAIN 2 FUSION PROTEIN; BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; HYBRID PROTEIN; POLYUBIQUITIN; PROTEASOME; UBIQUITIN; UNCLASSIFIED DRUG; VIF PROTEIN; APOBEC3G PROTEIN, HUMAN; BENZYLOXYCARBONYLLEUCYL LEUCYL LEUCINE ALDEHYDE; BENZYLOXYCARBONYLLEUCYL-LEUCYL-LEUCINE ALDEHYDE; CYSTEINE PROTEINASE INHIBITOR; CYTIDINE DEAMINASE; LEUPEPTIN; UBA2 PROTEIN, HUMAN; UBIQUITIN PROTEIN LIGASE;

EID: 52049111036     PISSN: None     EISSN: 17424690     Source Type: Journal    
DOI: 10.1186/1742-4690-5-72     Document Type: Article
Times cited : (12)

References (52)
  • 1
    • 48949118733 scopus 로고    scopus 로고
    • HIV-1 Vif, APOBEC, and intrinsic immunity
    • 2443170 18577210 10.1186/1742-4690-5-51
    • Goila-Gaur R Strebel K HIV-1 Vif, APOBEC, and intrinsic immunity Retrovirology 2008, 5:51 2443170 18577210 10.1186/1742-4690-5-51
    • (2008) Retrovirology , vol.5 , pp. 51
    • Goila-Gaur, R.1    Strebel, K.2
  • 2
    • 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(6898):646-650 10.1038/nature00939 12167863
    • (2002) Nature , vol.418 , Issue.6898 , pp. 646-650
    • Sheehy, A.M.1    Gaddis, N.C.2    Choi, J.D.3    Malim, M.H.4
  • 3
    • 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(11):1404-1407 10.1038/nm945 14528300
    • (2003) Nat Med , vol.9 , Issue.11 , pp. 1404-1407
    • Sheehy, A.M.1    Gaddis, N.C.2    Malim, M.H.3
  • 4
    • 4544232464 scopus 로고    scopus 로고
    • APOBEC3G is incorporated into virus-like particles by a direct interaction with HIV-1 Gag nucleocapsid protein
    • 10.1074/jbc.C400235200 15215254
    • Alce TM Popik W APOBEC3G is incorporated into virus-like particles by a direct interaction with HIV-1 Gag nucleocapsid protein J Biol Chem 2004, 279(33):34083-34086 10.1074/jbc.C400235200 15215254
    • (2004) J Biol Chem , vol.279 , Issue.33 , pp. 34083-34086
    • Alce, T.M.1    Popik, W.2
  • 5
    • 4043118380 scopus 로고    scopus 로고
    • The interaction between HIV-1 Gag and APOBEC3G
    • 10.1074/jbc.M402062200 15159405
    • Cen S Guo F Niu M Saadatmand J Deflassieux J Kleiman L The interaction between HIV-1 Gag and APOBEC3G J Biol Chem 2004, 279(32):33177-33184 10.1074/jbc.M402062200 15159405
    • (2004) J Biol Chem , vol.279 , Issue.32 , pp. 33177-33184
    • Cen, S.1    Guo, F.2    Niu, M.3    Saadatmand, J.4    Deflassieux, J.5    Kleiman, L.6
  • 6
    • 4344601964 scopus 로고    scopus 로고
    • HIV-1 and MLV Gag proteins are sufficient to recruit APOBEC3G into virus-like particles
    • 10.1016/j.bbrc.2004.07.005 15358144
    • Douaisi M Dussart S Courcoul M Bessou G Vigne R Decroly E HIV-1 and MLV Gag proteins are sufficient to recruit APOBEC3G into virus-like particles Biochem Biophys Res Commun 2004, 321(3):566-573 10.1016/ j.bbrc.2004.07.005 15358144
    • (2004) Biochem Biophys Res Commun , vol.321 , Issue.3 , pp. 566-573
    • Douaisi, M.1    Dussart, S.2    Courcoul, M.3    Bessou, G.4    Vigne, R.5    Decroly, E.6
  • 7
    • 6344294123 scopus 로고    scopus 로고
    • Amino-terminal region of the human immunodeficiency virus type 1 nucleocapsid is required for human APOBEC3G packaging
    • 523292 15479826 10.1128/JVI.78.21.11841-11852.2004
    • Luo K Liu B Xiao Z Yu Y Yu X Gorelick R Yu XF Amino-terminal region of the human immunodeficiency virus type 1 nucleocapsid is required for human APOBEC3G packaging J Virol 2004, 78(21):11841-11852 523292 15479826 10.1128/JVI.78.21.11841-11852.2004
    • (2004) J Virol , vol.78 , Issue.21 , pp. 11841-11852
    • Luo, K.1    Liu, B.2    Xiao, Z.3    Yu, Y.4    Yu, X.5    Gorelick, R.6    Yu, X.F.7
  • 8
    • 5344222683 scopus 로고    scopus 로고
    • Specific packaging of APOBEC3G into HIV-1 virions is mediated by the nucleocapsid domain of the gag polyprotein precursor
    • 10.1016/j.virol.2004.08.006 15464836
    • Schafer A Bogerd HP Cullen BR Specific packaging of APOBEC3G into HIV-1 virions is mediated by the nucleocapsid domain of the gag polyprotein precursor Virology 2004, 328(2):163-168 10.1016/j.virol.2004.08.006 15464836
    • (2004) Virology , vol.328 , Issue.2 , pp. 163-168
    • Schafer, A.1    Bogerd, H.P.2    Cullen, B.R.3
  • 9
    • 35448976039 scopus 로고    scopus 로고
    • Targeting APOBEC3A to the viral nucleoprotein complex confers antiviral activity
    • 2018723 17727729 10.1186/1742-4690-4-61
    • Goila-Gaur R Khan MA Miyagi E Kao S Strebel K Targeting APOBEC3A to the viral nucleoprotein complex confers antiviral activity Retrovirology 2007, 4:61 2018723 17727729 10.1186/1742-4690-4-61
    • (2007) Retrovirology , vol.4 , pp. 61
    • Goila-Gaur, R.1    Khan, M.A.2    Miyagi, E.3    Kao, S.4    Strebel, K.5
  • 11
    • 0038681023 scopus 로고    scopus 로고
    • Broad antiretroviral defence by human APOBEC3G through lethal editing of nascent reverse transcripts
    • 10.1038/nature01709 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(6944):99-103 10.1038/ nature01709 12808466
    • (2003) Nature , vol.424 , Issue.6944 , pp. 99-103
    • Mangeat, B.1    Turelli, P.2    Caron, G.3    Friedli, M.4    Perrin, L.5    Trono, D.6
  • 13
    • 0038363470 scopus 로고    scopus 로고
    • Hypermutation of HIV-1 DNA in the absence of the Vif protein
    • 10.1126/science.1083338 12750511
    • Lecossier D Bouchonnet F Clavel F Hance AJ Hypermutation of HIV-1 DNA in the absence of the Vif protein Science 2003, 300(5622):1112 10.1126/ science.1083338 12750511
    • (2003) Science , vol.300 , Issue.5622 , pp. 1112
    • Lecossier, D.1    Bouchonnet, F.2    Clavel, F.3    Hance, A.J.4
  • 14
    • 0038004471 scopus 로고    scopus 로고
    • The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA
    • 1350966 12808465 10.1038/nature01707
    • Zhang H Yang B Pomerantz RJ Zhang C Arunachalam SC Gao L The cytidine deaminase CEM15 induces hypermutation in newly synthesized HIV-1 DNA Nature 2003, 424(6944):94-98 1350966 12808465 10.1038/nature01707
    • (2003) Nature , vol.424 , Issue.6944 , pp. 94-98
    • Zhang, H.1    Yang, B.2    Pomerantz, R.J.3    Zhang, C.4    Arunachalam, S.C.5    Gao, L.6
  • 15
    • 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(11):1398-1403 10.1038/nm946 14528301
    • (2003) Nat Med , vol.9 , Issue.11 , pp. 1398-1403
    • Marin, M.1    Rose, K.M.2    Kozak, S.L.3    Kabat, D.4
  • 16
    • 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(3):591-601 10.1016/ S1097-2765(03)00353-8 14527406
    • (2003) Mol Cell , vol.12 , Issue.3 , pp. 591-601
    • Stopak, K.1    de Noronha, C.2    Yonemoto, W.3    Greene, W.C.4
  • 17
    • 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(5647):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
  • 18
    • 0242709301 scopus 로고    scopus 로고
    • The Vif protein of HIV triggers degradation of the human antiretroviral DNA deaminase APOBEC3G
    • 0.1016/j.cub.2003.10.034 14614829
    • Conticello SG Harris RS Neuberger MS The Vif protein of HIV triggers degradation of the human antiretroviral DNA deaminase APOBEC3G Curr Biol 2003, 13(22):2009-2013 0.1016/j.cub.2003.10.034 14614829
    • (2003) Curr Biol , vol.13 , pp. 2009-2013
    • Conticello, S.G.1    Harris, R.S.2    Neuberger, M.S.3
  • 19
    • 21444439295 scopus 로고    scopus 로고
    • Ubiquitination of APOBEC3G by an HIV-1 Vif-Cullin5-Elongin B-Elongin C complex is essential for Vif function
    • 10.1074/jbc.C500082200 15781449
    • Kobayashi M Takaori-Kondo A Miyauchi Y Iwai K Uchiyama T Ubiquitination of APOBEC3G by an HIV-1 Vif-Cullin5-Elongin B-Elongin C complex is essential for Vif function J Biol Chem 2005, 280(19):18573-18578 10.1074/ jbc.C500082200 15781449
    • (2005) J Biol Chem , vol.280 , Issue.19 , pp. 18573-18578
    • Kobayashi, M.1    Takaori-Kondo, A.2    Miyauchi, Y.3    Iwai, K.4    Uchiyama, T.5
  • 21
    • 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
    • 1182177 16076960 10.1073/pnas.0502440102
    • 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(32):11444-11449 1182177 16076960 10.1073/ pnas.0502440102
    • (2005) Proc Natl Acad Sci U S A , vol.102 , Issue.32 , 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
  • 22
    • 0036569345 scopus 로고    scopus 로고
    • From UBA to UBX: New words in the ubiquitin vocabulary
    • 10.1016/S0962-8924(02)02269-9 12062168
    • Buchberger A From UBA to UBX: New words in the ubiquitin vocabulary Trends Cell Biol 2002, 12(5):216-221 10.1016/S0962-8924(02)02269-9 12062168
    • (2002) Trends Cell Biol , vol.12 , Issue.5 , pp. 216-221
    • Buchberger, A.1
  • 23
    • 0031730342 scopus 로고    scopus 로고
    • Structure of a human DNA repair protein UBA domain that interacts with HIV-1 Vpr
    • 10.1038/4220 9846873
    • Dieckmann T Withers-Ward ES Jarosinski MA Liu CF Chen IS Feigon J Structure of a human DNA repair protein UBA domain that interacts with HIV-1 Vpr Nat Struct Biol 1998, 5(12):1042-1047 10.1038/4220 9846873
    • (1998) Nat Struct Biol , vol.5 , Issue.12 , pp. 1042-1047
    • Dieckmann, T.1    Withers-Ward, E.S.2    Jarosinski, M.A.3    Liu, C.F.4    Chen, I.S.5    Feigon, J.6
  • 24
    • 85047669941 scopus 로고    scopus 로고
    • The UBA domain: A sequence motif present in multiple enzyme classes of the ubiquitination pathway
    • 8871400
    • Hofmann K Bucher P The UBA domain: A sequence motif present in multiple enzyme classes of the ubiquitination pathway Trends Biochem Sci 1996, 21(5):172-173 8871400
    • (1996) Trends Biochem Sci , vol.21 , Issue.5 , pp. 172-173
    • Hofmann, K.1    Bucher, P.2
  • 25
    • 0037079693 scopus 로고    scopus 로고
    • Involvement of rhp23, a Schizosaccharomyces pombe homolog of the human HHR23A and Saccharomyces cerevisiae RAD23 nucleotide excision repair genes, in cell cycle control and protein ubiquitination
    • 99819 11788722 10.1093/nar/30.2.581
    • Elder RT Song XQ Chen M Hopkins KM Lieberman HB Zhao Y Involvement of rhp23, a Schizosaccharomyces pombe homolog of the human HHR23A and Saccharomyces cerevisiae RAD23 nucleotide excision repair genes, in cell cycle control and protein ubiquitination Nucleic Acids Res 2002, 30(2):581-591 99819 11788722 10.1093/nar/30.2.581
    • (2002) Nucleic Acids Res , vol.30 , Issue.2 , pp. 581-591
    • Elder, R.T.1    Song, X.Q.2    Chen, M.3    Hopkins, K.M.4    Lieberman, H.B.5    Zhao, Y.6
  • 26
  • 27
    • 0032879814 scopus 로고    scopus 로고
    • Pleiotropic defects caused by loss of the proteasome-interacting factors Rad23 and Rpn10 of Saccharomyces cerevisiae
    • 1460738 10471701
    • Lambertson D Chen L Madura K Pleiotropic defects caused by loss of the proteasome-interacting factors Rad23 and Rpn10 of Saccharomyces cerevisiae Genetics 1999, 153(1):69-79 1460738 10471701
    • (1999) Genetics , vol.153 , Issue.1 , pp. 69-79
    • Lambertson, D.1    Chen, L.2    Madura, K.3
  • 28
    • 0033600798 scopus 로고    scopus 로고
    • Interaction of hHR23 with S5a. The ubiquitin-like domain of hHR23 mediates interaction with S5a subunit of 26 S proteasome
    • 10.1074/jbc.274.39.28019 10488153
    • Hiyama H Yokoi M Masutani C Sugasawa K Maekawa T Tanaka K Hoeijmakers JH Hanaoka F Interaction of hHR23 with S5a. The ubiquitin-like domain of hHR23 mediates interaction with S5a subunit of 26 S proteasome J Biol Chem 1999, 274(39):28019-28025 10.1074/jbc.274.39.28019 10488153
    • (1999) J Biol Chem , vol.274 , Issue.39 , pp. 28019-28025
    • Hiyama, H.1    Yokoi, M.2    Masutani, C.3    Sugasawa, K.4    Maekawa, T.5    Tanaka, K.6    Hoeijmakers, J.H.7    Hanaoka, F.8
  • 30
    • 0034762028 scopus 로고    scopus 로고
    • Ubiquitin-associated (UBA) domains in Rad23 bind ubiquitin and promote inhibition of multi-ubiquitin chain assembly
    • 1084081 11571271 10.1093/embo-reports/kve203
    • Chen L Shinde U Ortolan TG Madura K Ubiquitin-associated (UBA) domains in Rad23 bind ubiquitin and promote inhibition of multi-ubiquitin chain assembly EMBO Rep 2001, 2(10):933-938 1084081 11571271 10.1093/ embo-reports/kve203
    • (2001) EMBO Rep , vol.2 , Issue.10 , pp. 933-938
    • Chen, L.1    Shinde, U.2    Ortolan, T.G.3    Madura, K.4
  • 32
    • 3042677641 scopus 로고    scopus 로고
    • Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome
    • 10.1074/jbc.M404020200 15117949
    • Elsasser S Chandler-Militello D Muller B Hanna J Finley D Rad23 and Rpn10 serve as alternative ubiquitin receptors for the proteasome J Biol Chem 2004, 279(26):26817-26822 10.1074/jbc.M404020200 15117949
    • (2004) J Biol Chem , vol.279 , Issue.26 , pp. 26817-26822
    • Elsasser, S.1    Chandler-Militello, D.2    Muller, B.3    Hanna, J.4    Finley, D.5
  • 33
    • 0036295955 scopus 로고    scopus 로고
    • Ubiquitin-like proteins and Rpn10 play cooperative roles in ubiquitin-dependent proteolysis
    • 10.1016/S0006-291X(02)00340-6 12051757
    • Saeki Y Saitoh A Toh-e A Yokosawa H Ubiquitin-like proteins and Rpn10 play cooperative roles in ubiquitin-dependent proteolysis Biochem Biophys Res Commun 2002, 293(3):986-992 10.1016/S0006-291X(02)00340-6 12051757
    • (2002) Biochem Biophys Res Commun , vol.293 , Issue.3 , pp. 986-992
    • Saeki, Y.1    Saitoh, A.2    Toh-e, A.3    Yokosawa, H.4
  • 34
    • 3142566639 scopus 로고    scopus 로고
    • Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system
    • 10.1016/j.cell.2004.06.014 15242647
    • Verma R Oania R Graumann J Deshaies RJ Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system Cell 2004, 118(1):99-110 10.1016/j.cell.2004.06.014 15242647
    • (2004) Cell , vol.118 , Issue.1 , pp. 99-110
    • Verma, R.1    Oania, R.2    Graumann, J.3    Deshaies, R.J.4
  • 35
    • 17044368771 scopus 로고    scopus 로고
    • The UBA2 domain functions as an intrinsic stabilization signal that protects Rad23 from proteasomal degradation
    • 10.1016/j.molcel.2005.03.015 15837425
    • Heessen S Masucci MG Dantuma NP The UBA2 domain functions as an intrinsic stabilization signal that protects Rad23 from proteasomal degradation Mol Cell 2005, 18(2):225-235 10.1016/j.molcel.2005.03.015 15837425
    • (2005) Mol Cell , vol.18 , Issue.2 , pp. 225-235
    • Heessen, S.1    Masucci, M.G.2    Dantuma, N.P.3
  • 36
    • 0027367944 scopus 로고
    • The Saccharomyces cerevisiae DNA repair gene RAD23 encodes a nuclear protein containing a ubiquitin-like domain required for biological function
    • 364847 8246991
    • Watkins JF Sung P Prakash L Prakash S The Saccharomyces cerevisiae DNA repair gene RAD23 encodes a nuclear protein containing a ubiquitin-like domain required for biological function Mol Cell Biol 1993, 13(12):7757-7765 364847 8246991
    • (1993) Mol Cell Biol , vol.13 , Issue.12 , pp. 7757-7765
    • Watkins, J.F.1    Sung, P.2    Prakash, L.3    Prakash, S.4
  • 37
    • 0037010150 scopus 로고    scopus 로고
    • Stabilization signals: A novel regulatory mechanism in the ubiquitin/ proteasome system
    • 10.1016/S0014-5793(02)03252-0 12354607
    • Dantuma NP Masucci MG Stabilization signals: A novel regulatory mechanism in the ubiquitin/proteasome system FEBS Lett 2002, 529(1):22-26 10.1016/S0014-5793(02)03252-0 12354607
    • (2002) FEBS Lett , vol.529 , Issue.1 , pp. 22-26
    • Dantuma, N.P.1    Masucci, M.G.2
  • 38
    • 0031716649 scopus 로고    scopus 로고
    • The proteasome: A protein-destroying machine
    • 10.1046/j.1365-2443.1998.00207.x 9797452
    • Tanaka K Chiba T The proteasome: A protein-destroying machine Genes Cells 1998, 3(8):499-510 10.1046/j.1365-2443.1998.00207.x 9797452
    • (1998) Genes Cells , vol.3 , Issue.8 , pp. 499-510
    • Tanaka, K.1    Chiba, T.2
  • 39
    • 0034282219 scopus 로고    scopus 로고
    • The DNA repair protein rad23 is a negative regulator of multi-ubiquitin chain assembly
    • 10.1038/35023547 10980700
    • Ortolan TG Tongaonkar P Lambertson D Chen L Schauber C Madura K The DNA repair protein rad23 is a negative regulator of multi-ubiquitin chain assembly Nat Cell Biol 2000, 2(9):601-608 10.1038/35023547 10980700
    • (2000) Nat Cell Biol , vol.2 , Issue.9 , pp. 601-608
    • Ortolan, T.G.1    Tongaonkar, P.2    Lambertson, D.3    Chen, L.4    Schauber, C.5    Madura, K.6
  • 40
    • 0037195907 scopus 로고    scopus 로고
    • Ubiquitylation of BAG-1 suggests a novel regulatory mechanism during the sorting of chaperone substrates to the proteasome
    • 10.1074/jbc.M204196200 12297498
    • Alberti S Demand J Esser C Emmerich N Schild H Hohfeld J Ubiquitylation of BAG-1 suggests a novel regulatory mechanism during the sorting of chaperone substrates to the proteasome J Biol Chem 2002, 277(48):45920-45927 10.1074/jbc.M204196200 12297498
    • (2002) J Biol Chem , vol.277 , Issue.48 , pp. 45920-45927
    • Alberti, S.1    Demand, J.2    Esser, C.3    Emmerich, N.4    Schild, H.5    Hohfeld, J.6
  • 41
    • 0037155884 scopus 로고    scopus 로고
    • The tight junction-specific protein occludin is a functional target of the E3 ubiquitin-protein ligase itch
    • 10.1074/jbc.M111384200 11782481
    • Traweger A Fang D Liu YC Stelzhammer W Krizbai IA Fresser F Bauer HC Bauer H The tight junction-specific protein occludin is a functional target of the E3 ubiquitin-protein ligase itch J Biol Chem 2002, 277(12):10201-10208 10.1074/jbc.M111384200 11782481
    • (2002) J Biol Chem , vol.277 , Issue.12 , pp. 10201-10208
    • Traweger, A.1    Fang, D.2    Liu, Y.C.3    Stelzhammer, W.4    Krizbai, I.A.5    Fresser, F.6    Bauer, H.C.7    Bauer, H.8
  • 42
    • 0022495870 scopus 로고
    • Production of acquired immunodeficiency syndrome-associated retrovirus in human and nonhuman cells transfected with an infectious molecular clone
    • 253077 3016298
    • Adachi A Gendelman HE Koenig S Folks T Willey R Rabson A Martin MA Production of acquired immunodeficiency syndrome-associated retrovirus in human and nonhuman cells transfected with an infectious molecular clone J Virol 1986, 59(2):284-291 253077 3016298
    • (1986) J Virol , vol.59 , Issue.2 , pp. 284-291
    • Adachi, A.1    Gendelman, H.E.2    Koenig, S.3    Folks, T.4    Willey, R.5    Rabson, A.6    Martin, M.A.7
  • 43
    • 0030899871 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 coreceptors participate in postentry stages in the virus replication cycle and function in simian immunodeficiency virus infection
    • 191545 9094670
    • Chackerian B Long EM Luciw PA Overbaugh J Human immunodeficiency virus type 1 coreceptors participate in postentry stages in the virus replication cycle and function in simian immunodeficiency virus infection J Virol 1997, 71(5):3932-3939 191545 9094670
    • (1997) J Virol , vol.71 , Issue.5 , pp. 3932-3939
    • Chackerian, B.1    Long, E.M.2    Luciw, P.A.3    Overbaugh, J.4
  • 44
    • 4744374755 scopus 로고    scopus 로고
    • Transcriptional regulation of APOBEC3G, a cytidine deaminase that hypermutates human immunodeficiency virus
    • 10.1074/jbc.M406760200 15297452
    • Rose KM Marin M Kozak SL Kabat D Transcriptional regulation of APOBEC3G, a cytidine deaminase that hypermutates human immunodeficiency virus J Biol Chem 2004, 279(40):41744-41749 10.1074/jbc.M406760200 15297452
    • (2004) J Biol Chem , vol.279 , Issue.40 , pp. 41744-41749
    • Rose, K.M.1    Marin, M.2    Kozak, S.L.3    Kabat, D.4
  • 45
    • 34547130033 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vif inhibits packaging and antiviral activity of a degradation-resistant APOBEC3G variant
    • 1951302 17522211 10.1128/JVI.02694-06
    • 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(15):8236-8246 1951302 17522211 10.1128/JVI.02694-06
    • (2007) J Virol , vol.81 , Issue.15 , 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
  • 46
    • 2442511993 scopus 로고    scopus 로고
    • A single amino acid determinant governs the species-specific sensitivity of APOBEC3G to Vif action
    • 10.1074/jbc.C400060200 14966139
    • Mangeat B Turelli P Liao S Trono D A single amino acid determinant governs the species-specific sensitivity of APOBEC3G to Vif action J Biol Chem 2004, 279(15):14481-14483 10.1074/jbc.C400060200 14966139
    • (2004) J Biol Chem , vol.279 , Issue.15 , pp. 14481-14483
    • Mangeat, B.1    Turelli, P.2    Liao, S.3    Trono, D.4
  • 47
    • 1642380210 scopus 로고    scopus 로고
    • A single amino acid of APOBEC3G controls its species-specific interaction with virion infectivity factor (Vif)
    • 374346 14978281 10.1073/pnas.0307132101
    • Schrofelbauer B Chen D Landau NR A single amino acid of APOBEC3G controls its species-specific interaction with virion infectivity factor (Vif) Proc Natl Acad Sci U S A 2004, 101(11):3927-3932 374346 14978281 10.1073/pnas.0307132101
    • (2004) Proc Natl Acad Sci U S A , vol.101 , Issue.11 , pp. 3927-3932
    • Schrofelbauer, B.1    Chen, D.2    Landau, N.R.3
  • 48
    • 0345686439 scopus 로고    scopus 로고
    • Ubiquitin recognition by the DNA repair protein hHR23a
    • 10.1021/bi035391j 14621999
    • Wang Q Goh AM Howley PM Walters KJ Ubiquitin recognition by the DNA repair protein hHR23a Biochemistry 2003, 42(46):13529-13535 10.1021/ bi035391j 14621999
    • (2003) Biochemistry , vol.42 , Issue.46 , pp. 13529-13535
    • Wang, Q.1    Goh, A.M.2    Howley, P.M.3    Walters, K.J.4
  • 49
    • 0141480905 scopus 로고    scopus 로고
    • Binding surface mapping of intra- and interdomain interactions among hHR23B, ubiquitin, and polyubiquitin binding site 2 of S5a
    • 10.1074/jbc.M304628200 12832454
    • Ryu KS Lee KJ Bae SH Kim BK Kim KA Choi BS Binding surface mapping of intra- and interdomain interactions among hHR23B, ubiquitin, and polyubiquitin binding site 2 of S5a J Biol Chem 2003, 278(38):36621-36627 10.1074/jbc.M304628200 12832454
    • (2003) J Biol Chem , vol.278 , Issue.38 , pp. 36621-36627
    • Ryu, K.S.1    Lee, K.J.2    Bae, S.H.3    Kim, B.K.4    Kim, K.A.5    Choi, B.S.6
  • 50
    • 4344559454 scopus 로고    scopus 로고
    • An unstructured initiation site is required for efficient proteasome-mediated degradation
    • 10.1038/nsmb814 15311270
    • Prakash S Tian L Ratliff KS Lehotzky RE Matouschek A An unstructured initiation site is required for efficient proteasome-mediated degradation Nat Struct Mol Biol 2004, 11(9):830-837 10.1038/nsmb814 15311270
    • (2004) Nat Struct Mol Biol , vol.11 , Issue.9 , pp. 830-837
    • Prakash, S.1    Tian, L.2    Ratliff, K.S.3    Lehotzky, R.E.4    Matouschek, A.5
  • 51
    • 0035694696 scopus 로고    scopus 로고
    • Proteins are unfolded on the surface of the ATPase ring before transport into the proteasome
    • 10.1016/S1097-2765(01)00407-5 11779508
    • Navon A Goldberg AL Proteins are unfolded on the surface of the ATPase ring before transport into the proteasome Mol Cell 2001, 8(6):1339-1349 10.1016/S1097-2765(01)00407-5 11779508
    • (2001) Mol Cell , vol.8 , Issue.6 , pp. 1339-1349
    • Navon, A.1    Goldberg, A.L.2
  • 52
    • 0037646406 scopus 로고    scopus 로고
    • Rad23 ubiquitin-associated domains (UBA) inhibit 26 S proteasome-catalyzed proteolysis by sequestering lysine 48-linked polyubiquitin chains
    • 10.1074/jbc.M212841200 12643283
    • Raasi S Pickart CM Rad23 ubiquitin-associated domains (UBA) inhibit 26 S proteasome-catalyzed proteolysis by sequestering lysine 48-linked polyubiquitin chains J Biol Chem 2003, 278(11):8951-8959 10.1074/ jbc.M212841200 12643283
    • (2003) J Biol Chem , vol.278 , Issue.11 , pp. 8951-8959
    • Raasi, S.1    Pickart, C.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.