메뉴 건너뛰기




Volumn 21, Issue 10, 2005, Pages 886-893

Differences in the length of Gag proteins among different HIV type 1 subtypes

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; GAG PROTEIN; PROTEIN P10;

EID: 31444445342     PISSN: 08892229     EISSN: None     Source Type: Journal    
DOI: 10.1089/aid.2005.21.886     Document Type: Article
Times cited : (10)

References (44)
  • 1
    • 0030406701 scopus 로고    scopus 로고
    • Dynamic interactions of the Gag polyprotein
    • Craven R and Parent L: Dynamic interactions of the Gag polyprotein. Curr Top Microbiol Immunol 1996;214:65-94.
    • (1996) Curr Top Microbiol Immunol , vol.214 , pp. 65-94
    • Craven, R.1    Parent, L.2
  • 2
    • 10744233294 scopus 로고    scopus 로고
    • The protein network of HIV budding
    • von Schwedler U, Stuchell M, Muller B, et al.: The protein network of HIV budding. Cell 2003;114:701-713.
    • (2003) Cell , vol.114 , pp. 701-713
    • Schwedler, U.1    Stuchell, M.2    Muller, B.3
  • 3
    • 0027932364 scopus 로고
    • The activity of the protease of HIV-1 is initiated at the membrane of infected cells before the release of viral proteins and is required for release to occur with maximum efficiency
    • Kaplan A, Manchester M, and Swanstrom R: The activity of the protease of HIV-1 is initiated at the membrane of infected cells before the release of viral proteins and is required for release to occur with maximum efficiency. J Virol 1994;68:6782-6786.
    • (1994) J Virol , vol.68 , pp. 6782-6786
    • Kaplan, A.1    Manchester, M.2    Swanstrom, R.3
  • 4
    • 0001118596 scopus 로고    scopus 로고
    • Retroviral gene expression. II. Synthesis, processing, and assembly of viral proteins
    • (Coffin JM, Hughes SH, and Varmus HE, eds). Cold Spring Harbor Laboratory, Cold Spring Harbor, NY
    • Swanstrom R and Wills J: Retroviral gene expression. II. Synthesis, processing, and assembly of viral proteins. In: Retroviruses (Coffin JM, Hughes SH, and Varmus HE, eds). Cold Spring Harbor Laboratory, Cold Spring Harbor, NY, 1997, pp. 263-334.
    • (1997) Retroviruses , pp. 263-334
    • Swanstrom, R.1    Wills, J.2
  • 5
    • 0023870815 scopus 로고    scopus 로고
    • Characterization of ribosomal frameshifting in HIV-1 gag-pol expression
    • Jacks T, Power M, Masiarz F, Luciw P, Barr P, and Varmus H: Characterization of ribosomal frameshifting in HIV-1 gag-pol expression. Nature 1998;331:280-283.
    • (1998) Nature , vol.331 , pp. 280-283
    • Jacks, T.1    Power, M.2    Masiarz, F.3    Luciw, P.4    Barr, P.5    Varmus, H.6
  • 6
    • 0029013602 scopus 로고
    • Domains upstream of the protease in HIV-1 gag-pol influence PI autoprocessing
    • Zybarth G and Carter C: Domains upstream of the protease in HIV-1 gag-pol influence PI autoprocessing. J Virol 1995;69:3878-3884.
    • (1995) J Virol , vol.69 , pp. 3878-3884
    • Zybarth, G.1    Carter, C.2
  • 7
    • 2642680072 scopus 로고    scopus 로고
    • Cleavage of HIV-1 proteinase from the N-terminally adjacent P6* protein is essential for efficient gag polyprotein processing and viral infectivity
    • Tessmer U and Karausslich H: Cleavage of HIV-1 proteinase from the N-terminally adjacent P6* protein is essential for efficient gag polyprotein processing and viral infectivity. J Virol 1998;72:3459-3463.
    • (1998) J Virol , vol.72 , pp. 3459-3463
    • Tessmer, U.1    Karausslich, H.2
  • 9
    • 0345599160 scopus 로고    scopus 로고
    • Effects of a single amino acid substitution within the p2 region of HIV-1 on packaging of spliced viral RNA
    • Russell R, Roldan A, Detorio M, Hu J, Wainberg M, and Liang C: Effects of a single amino acid substitution within the p2 region of HIV-1 on packaging of spliced viral RNA. J Virol 2003;77: 12986-12995.
    • (2003) J Virol , vol.77 , pp. 12986-12995
    • Russell, R.1    Roldan, A.2    Detorio, M.3    Hu, J.4    Wainberg, M.5    Liang, C.6
  • 10
    • 0027176378 scopus 로고
    • Maturation of dimeric RNA of Moloney murine leukemia virus
    • Fu W and Rein A: Maturation of dimeric RNA of Moloney murine leukemia virus. J Virol 1993;67:5443-5449.
    • (1993) J Virol , vol.67 , pp. 5443-5449
    • Fu, W.1    Rein, A.2
  • 11
    • 0032928073 scopus 로고    scopus 로고
    • The HIV-1 Gag polyprotein has chaperone activity: Possible role in dimerization of genomic RNA and placement of tRNA on the primer binding site
    • Feng Y, Campbell S, Harvin D, Ehresmann B, Ehresmann C, and Rein A: The HIV-1 Gag polyprotein has chaperone activity: Possible role in dimerization of genomic RNA and placement of tRNA on the primer binding site. J Virol 1999;73:4251-4256.
    • (1999) J Virol , vol.73 , pp. 4251-4256
    • Feng, Y.1    Campbell, S.2    Harvin, D.3    Ehresmann, B.4    Ehresmann, C.5    Rein, A.6
  • 12
    • 0029798209 scopus 로고    scopus 로고
    • HIV-1 nucleocapsid protein induces maturation of dimeric retroviral RNA in vitro
    • Feng Y, Copeland T, Henderson L, et al.: HIV-1 nucleocapsid protein induces maturation of dimeric retroviral RNA in vitro. Proc Natl Acad Sci USA 1996;93:7577-7581.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 7577-7581
    • Feng, Y.1    Copeland, T.2    Henderson, L.3
  • 13
    • 0030480326 scopus 로고    scopus 로고
    • NCp7 activates HIVLai RNA dimerization by converting a transient loop-loop complex into a stable dimer
    • Muriaux D, De Rocquigny H, Roques B, and Paoletti J: NCp7 activates HIVLai RNA dimerization by converting a transient loop-loop complex into a stable dimer. J Biol Chem 1996;271:33686-33692.
    • (1996) J Biol Chem , vol.271 , pp. 33686-33692
    • Muriaux, D.1    De Rocquigny, H.2    Roques, B.3    Paoletti, J.4
  • 14
    • 0034856077 scopus 로고    scopus 로고
    • Proteolytic processing of the P2/nucleocapsid cleavage site is critical for HIV-1 RNA dimer maturation
    • Shehu-Xhilaga M, Kraeusslich H, Pettit S, et al: Proteolytic processing of the P2/nucleocapsid cleavage site is critical for HIV-1 RNA dimer maturation. J Virol 2001;75:9156-9164.
    • (2001) J Virol , vol.75 , pp. 9156-9164
    • Shehu-Xhilaga, M.1    Kraeusslich, H.2    Pettit, S.3
  • 15
    • 0036784575 scopus 로고    scopus 로고
    • Replacement of the pi amino acid of HIV-1 gag processing sites can inhibit or enhance the rate of cleavage by the viral protease
    • Petit S, Henderson G, Schiffer C, and Swanstrom R: Replacement of the pi amino acid of HIV-1 gag processing sites can inhibit or enhance the rate of cleavage by the viral protease. J Virol 2002; 76:10226-10233.
    • (2002) J Virol , vol.76 , pp. 10226-10233
    • Petit, S.1    Henderson, G.2    Schiffer, C.3    Swanstrom, R.4
  • 16
    • 5444255004 scopus 로고    scopus 로고
    • Selected amino acid substitutions in the C-terminal region of HIV-1 capsid protein affect virus assembly and release
    • Addurahman S, Hoglund S, Goobar-Larsson L, and VahIne A: Selected amino acid substitutions in the C-terminal region of HIV-1 capsid protein affect virus assembly and release. J Gen Virol 2004; 85:2903-2913.
    • (2004) J Gen Virol , vol.85 , pp. 2903-2913
    • Addurahman, S.1    Hoglund, S.2    Goobar-Larsson, L.3    Vahine, A.4
  • 17
    • 0036056291 scopus 로고    scopus 로고
    • Naturally occurring amino acid polymorphisms in HIV-1 gag p7 (NC) and the C-cleavage site impact gag-pol processing by HIV-1 protease
    • Goodenow M, Bloom G, Rose S, et al.: Naturally occurring amino acid polymorphisms in HIV-1 gag p7 (NC) and the C-cleavage site impact gag-pol processing by HIV-1 protease. Virology 2002;292: 137-149.
    • (2002) Virology , vol.292 , pp. 137-149
    • Goodenow, M.1    Bloom, G.2    Rose, S.3
  • 18
    • 7044222138 scopus 로고    scopus 로고
    • Effects of mutations in an HIV-1 gag gene containing a 107-codon tandem repeat in the matrix region on assembly and processing of the protein product
    • Liao W, Chiu H, and Wang C: Effects of mutations in an HIV-1 gag gene containing a 107-codon tandem repeat in the matrix region on assembly and processing of the protein product. J Med Virol 2004;74:528-535.
    • (2004) J Med Virol , vol.74 , pp. 528-535
    • Liao, W.1    Chiu, H.2    Wang, C.3
  • 19
    • 2642680072 scopus 로고    scopus 로고
    • Cleavage of HIV-1 proteinase from the N-terminally adjacent P6* protein is essential for efficient gag polyprotein processing and viral infectivity
    • Tessmer U and Karausslich H: Cleavage of HIV-1 proteinase from the N-terminally adjacent P6* protein is essential for efficient gag polyprotein processing and viral infectivity. J Virol 1998;72: 3459-3463.
    • (1998) J Virol , vol.72 , pp. 3459-3463
    • Tessmer, U.1    Karausslich, H.2
  • 20
    • 0041888278 scopus 로고    scopus 로고
    • Variability at HIV-1 subtype C protease cleavage sites and indication of viral fitness?
    • De Oliveira T, Engelbrecht S, van Rensburg E, et al.: Variability at HIV-1 subtype C protease cleavage sites and indication of viral fitness? J Virol 2003;77:9422-9430.
    • (2003) J Virol , vol.77 , pp. 9422-9430
    • De Oliveira, T.1    Engelbrecht, S.2    Van Rensburg, E.3
  • 21
    • 0942290560 scopus 로고    scopus 로고
    • Gag non-cleavage site mutations contribute to full recovery of viral fitness in protease inhibitor-resistant HIV-1
    • Myint L, Matsuda M, Matsuda Z, et al.: Gag non-cleavage site mutations contribute to full recovery of viral fitness in protease inhibitor-resistant HIV-1. Antimicrob Agents Chemother 2004;48: 444-452.
    • (2004) Antimicrob Agents Chemother , vol.48 , pp. 444-452
    • Myint, L.1    Matsuda, M.2    Matsuda, Z.3
  • 23
    • 0034284897 scopus 로고    scopus 로고
    • Polymorphisms of HIV-1 gag p7/p1 and p1/p6 cleavage sites: Clinical significance and implications for resistance to protease inhibitors
    • Bally F, MartÌnez R, Peters S, Sudre P, and Telenti A: Polymorphisms of HIV-1 gag p7/p1 and p1/p6 cleavage sites: clinical significance and implications for resistance to protease inhibitors. AIDS Res Human Retroviruses 2000;16:1209-1213.
    • (2000) AIDS Res Human Retroviruses , vol.16 , pp. 1209-1213
    • Bally, F.1    Martìnez, R.2    Peters, S.3    Sudre, P.4    Telenti, A.5
  • 24
    • 0030007802 scopus 로고    scopus 로고
    • Natural variation in HIV-1 protease, gag p7 and p6, and protease cleavage sites within Gag/Pol polyproteins: Amino acid substitutions in the absence of protease inhibitors in mothers and children infected by HIV-1
    • Barrie K, Pérez E, Lamers S, et al.: Natural variation in HIV-1 protease, gag p7 and p6, and protease cleavage sites within Gag/Pol polyproteins: Amino acid substitutions in the absence of protease inhibitors in mothers and children infected by HIV-1. Virology 1996;219:407-416.
    • (1996) Virology , vol.219 , pp. 407-416
    • Barrie, K.1    Pérez, E.2    Lamers, S.3
  • 25
    • 0036310578 scopus 로고    scopus 로고
    • Changes in HIV-1 gag at positions L449 and P453 are linked to 150V protease mutants in vivo and cause reduction of sensitivity to amprenavir and improved viral fitness in vitro
    • Manguire M, Guinea R, Griffin P, et al.: Changes in HIV-1 gag at positions L449 and P453 are linked to 150V protease mutants in vivo and cause reduction of sensitivity to amprenavir and improved viral fitness in vitro. J Virol 2002;76:7398-7406.
    • (2002) J Virol , vol.76 , pp. 7398-7406
    • Manguire, M.1    Guinea, R.2    Griffin, P.3
  • 26
    • 0034812843 scopus 로고    scopus 로고
    • Resistance to analog reverse transcriptase inhibitors mediated by HIV-1 P6 protein
    • Peters S, Muñoz M, Yerly S, et al.: Resistance to analog reverse transcriptase inhibitors mediated by HIV-1 P6 protein. J Virol 2001;75:9644-9653.
    • (2001) J Virol , vol.75 , pp. 9644-9653
    • Peters, S.1    Muñoz, M.2    Yerly, S.3
  • 27
    • 0004040205 scopus 로고    scopus 로고
    • (Kuiken C, Foley B, Hahn B, et al., eds). Theoretical Biology and Biophysics Group, Los Alamos National Laboratory, Los Alamos, NM
    • Kuiken C, Foley B, Hahn B, et al.: In: HIV Sequence Compendium (Kuiken C, Foley B, Hahn B, et al., eds). Theoretical Biology and Biophysics Group, Los Alamos National Laboratory, Los Alamos, NM, 2000.
    • (2000) HIV Sequence Compendium
    • Kuiken, C.1    Foley, B.2    Hahn, B.3
  • 28
    • 0001792727 scopus 로고    scopus 로고
    • Recombinant HIV sequences: Their role in the global epidemic
    • (Kuiken C, Foley B, Hahn B et al., eds.). Theoretical Biology and Biophysics Group, Los Alamos National Laboratory, Los Alamos, NM
    • Peeters M: Recombinant HIV sequences: Their role in the global epidemic. In: HIV Sequence Compendium (Kuiken C, Foley B, Hahn B et al., eds.). Theoretical Biology and Biophysics Group, Los Alamos National Laboratory, Los Alamos, NM, 2000, pp. 54-72.
    • (2000) HIV Sequence Compendium , pp. 54-72
    • Peeters, M.1
  • 29
    • 1642465048 scopus 로고    scopus 로고
    • Genetic diversity of HIV in Africa: Impact on diagnosis, treatment, vaccine development and trials
    • Peeters M, Toure-Kane C, and Nkengasong J: Genetic diversity of HIV in Africa: Impact on diagnosis, treatment, vaccine development and trials. AIDS 2003;17:2547-2560.
    • (2003) AIDS , vol.17 , pp. 2547-2560
    • Peeters, M.1    Toure-Kane, C.2    Nkengasong, J.3
  • 30
    • 12944274913 scopus 로고    scopus 로고
    • Heterogeneous nature of HIV-1 recombinants spreading in Southern Europe
    • Holguín A, Alvarez A, and Soriano V: Heterogeneous nature of HIV-1 recombinants spreading in Southern Europe. J Med Virol 2005;75:374-380.
    • (2005) J Med Virol , vol.75 , pp. 374-380
    • Holguín, A.1    Alvarez, A.2    Soriano, V.3
  • 31
    • 25144444139 scopus 로고    scopus 로고
    • HIV-1 subtypes in Spain, 1995-2003: A retrospective analysis
    • Lospitao E, Álvarez A, Soriano V, and Holguín A: HIV-1 subtypes in Spain, 1995-2003: A retrospective analysis. HIV Med 2005;6: 313-320.
    • (2005) HIV Med , vol.6 , pp. 313-320
    • Lospitao, E.1    Álvarez, A.2    Soriano, V.3    Holguín, A.4
  • 32
    • 0037662635 scopus 로고    scopus 로고
    • High prevalence of non-B subtypes among HIV-positive immigrants in the Canary Islands, Spain. Implications for public health in Europe
    • Holguín A, Alvarez A, Pena MJ, Artiles, Molina L, and Soriano V: High prevalence of non-B subtypes among HIV-positive immigrants in the Canary Islands, Spain. Implications for public health in Europe. HIV Clin Trials 2003;4:184-192.
    • (2003) HIV Clin Trials , vol.4 , pp. 184-192
    • Holguín, A.1    Alvarez, A.2    Pena, M.J.3    Artiles4    Molina, L.5    Soriano, V.6
  • 33
    • 0037165905 scopus 로고    scopus 로고
    • High prevalence of subtype among HIV-infected immigrants attended in Madrid
    • Holguín A, Álvarez A, and Soriano V: High prevalence of subtype among HIV-infected immigrants attended in Madrid. AIDS 2002;16:1163-1170.
    • (2002) AIDS , vol.16 , pp. 1163-1170
    • Holguín, A.1    Álvarez, A.2    Soriano, V.3
  • 34
    • 0031846317 scopus 로고    scopus 로고
    • Resistance-associated loss of viral fitness in HIV-1: Phenotypic analysis of protease and gag co-evolution in protease inhibitor-treated patients
    • Mammano F, Petit C, and Clavel F: Resistance-associated loss of viral fitness in HIV-1: Phenotypic analysis of protease and gag co-evolution in protease inhibitor-treated patients. J Virol 1998;72: 7632-7637.
    • (1998) J Virol , vol.72 , pp. 7632-7637
    • Mammano, F.1    Petit, C.2    Clavel, F.3
  • 35
    • 0037338574 scopus 로고    scopus 로고
    • Changes in HIV-1 p7/p1/p6 gag gene in drug naive and pretreated patients
    • Gallego O, de Mendoza C, Corral A, and Soriano V: Changes in HIV-1 p7/p1/p6 gag gene in drug naive and pretreated patients. J Clin Microbiol 2003;41:1245-1247.
    • (2003) J Clin Microbiol , vol.41 , pp. 1245-1247
    • Gallego, O.1    De Mendoza, C.2    Corral, A.3    Soriano, V.4
  • 38
    • 0035008028 scopus 로고    scopus 로고
    • A complex HIV type 1 A/G/J recombinant virus isolated from a seronegative patient with AIDS from Benin, West Africa
    • Baldrich-Rubio E, Anagonou S, Stirrups K, et al.: A complex HIV type 1 A/G/J recombinant virus isolated from a seronegative patient with AIDS from Benin, West Africa. J Gen Virol 2001;82:1095-1106.
    • (2001) J Gen Virol , vol.82 , pp. 1095-1106
    • Baldrich-Rubio, E.1    Anagonou, S.2    Stirrups, K.3
  • 39
    • 0032730134 scopus 로고    scopus 로고
    • Comparison of three commercial methods for quantification of plasma viraemia in clinical specimens belonging to non-B HIV-1 subtypes
    • Holguín A, de Mendoza C, and Soriano V: Comparison of three commercial methods for quantification of plasma viraemia in clinical specimens belonging to non-B HIV-1 subtypes. Eur J Clin Microb Infect Dis 1999;18:256-259.
    • (1999) Eur J Clin Microb Infect Dis , vol.18 , pp. 256-259
    • Holguín, A.1    De Mendoza, C.2    Soriano, V.3
  • 40
    • 0032543744 scopus 로고    scopus 로고
    • Naturally occurring decreased susceptibility of HIV-1 subtype G to protease inhibitors
    • Descamps D, Apetrei C, Collin G, et al.: Naturally occurring decreased susceptibility of HIV-1 subtype G to protease inhibitors. AIDS 1998;12:1109-1111.
    • (1998) AIDS , vol.12 , pp. 1109-1111
    • Descamps, D.1    Apetrei, C.2    Collin, G.3
  • 41
    • 0036750078 scopus 로고    scopus 로고
    • Resistance to antiretroviral agents in individuals with HIV-1 non-B subtypes
    • Holguin A and Soriano V: Resistance to antiretroviral agents in individuals with HIV-1 non-B subtypes. HIV Clin Trials 2002;3: 403-411.
    • (2002) HIV Clin Trials , vol.3 , pp. 403-411
    • Holguin, A.1    Soriano, V.2
  • 42
    • 0038727277 scopus 로고    scopus 로고
    • The impact of HIV-1 subtype on the clinical response on HAART
    • Prater J: The impact of HIV-1 subtype on the clinical response on HAART. J. HIV Ther 2002;7:92-96.
    • (2002) J HIV Ther , vol.7 , pp. 92-96
    • Prater, J.1
  • 43
    • 4344689447 scopus 로고    scopus 로고
    • Non-B HIV-1 subtypes: Replicative capacity and responses to antiretroviral therapy
    • Nicastri E, Sarmati L, dÉttorre G, et al.: Non-B HIV-1 subtypes: Replicative capacity and responses to antiretroviral therapy. AIDS Res Hum Retroviruses 2004;20:816-818.
    • (2004) AIDS Res Hum Retroviruses , vol.20 , pp. 816-818
    • Nicastri, E.1    Sarmati, L.2    Déttorre, G.3
  • 44
    • 0001792727 scopus 로고    scopus 로고
    • Recombinant HIV sequences: Their role in the global epidemic
    • (Kuiken C, Foley B, Hahn B, et al., eds). Theoretical Biology and Biophysics Group, Los Alamos National Laboratory, Los Alamos, NM
    • Peeters M: Recombinant HIV sequences: Their role in the global epidemic. In: HIV Sequence Compendium (Kuiken C, Foley B, Hahn B, et al., eds). Theoretical Biology and Biophysics Group, Los Alamos National Laboratory, Los Alamos, NM, 2000, pp. 54-72.
    • (2000) HIV Sequence Compendium , pp. 54-72
    • Peeters, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.