메뉴 건너뛰기




Volumn 73, Issue 5, 1999, Pages 4230-4238

The amino-terminal region of Vpr from human immunodeficiency virus type 1 forms ion channels and kills neurons

Author keywords

[No Author keywords available]

Indexed keywords

ION CHANNEL; MUTANT PROTEIN; SYNTHETIC PEPTIDE;

EID: 0032947291     PISSN: 0022538X     EISSN: None     Source Type: Journal    
DOI: 10.1128/jvi.73.5.4230-4238.1999     Document Type: Article
Times cited : (72)

References (40)
  • 1
    • 0025724956 scopus 로고
    • Interaction with phospholipid bilayers, ion channel formation, and antimicrobial activity of basic amphipathic alpha-helical model peptides of various chain lengths
    • Agawa, Y., S. Lee, S. Ono, H. Aoyagi, T. Taniguchi, K. Anzai, and Y. Kirino. 1991. Interaction with phospholipid bilayers, ion channel formation, and antimicrobial activity of basic amphipathic alpha-helical model peptides of various chain lengths. J. Biol. Chem. 266:20218-20222.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20218-20222
    • Agawa, Y.1    Lee, S.2    Ono, S.3    Aoyagi, H.4    Taniguchi, T.5    Anzai, K.6    Kirino, Y.7
  • 3
    • 0028297360 scopus 로고
    • Distinct effects in primary macrophages and lymphocytes of the human immunodeficiency virus type 1 accessory genes vpr, vpu, and nef: Mutational analysis of a primary HIV-1 isolate
    • Balliet, J. W., D. L. Kolson, G. Eiger, F. M. Kim, K. A. McGann, A. Srinivasan, and R. Collman. 1994. Distinct effects in primary macrophages and lymphocytes of the human immunodeficiency virus type 1 accessory genes vpr, vpu, and nef: mutational analysis of a primary HIV-1 isolate. Virology 200:623-631.
    • (1994) Virology , vol.200 , pp. 623-631
    • Balliet, J.W.1    Kolson, D.L.2    Eiger, G.3    Kim, F.M.4    McGann, K.A.5    Srinivasan, A.6    Collman, R.7
  • 4
    • 0029993519 scopus 로고    scopus 로고
    • 2 accumulation by a mechanism which differs from DNA damage checkpoint control
    • 2 accumulation by a mechanism which differs from DNA damage checkpoint control. J. Virol. 70:2324-2331.
    • (1996) J. Virol. , vol.70 , pp. 2324-2331
    • Bartz, S.R.1    Rogel, M.E.2    Emerman, M.3
  • 5
    • 0021099153 scopus 로고
    • Measurement of the electrochemical proton gradient in submitochondrial particles
    • Berry, E. A., and P. C. Hinkle. 1983. Measurement of the electrochemical proton gradient in submitochondrial particles. J. Biol. Chem. 258:1474-1486.
    • (1983) J. Biol. Chem. , vol.258 , pp. 1474-1486
    • Berry, E.A.1    Hinkle, P.C.2
  • 8
    • 0028824894 scopus 로고
    • Mutational analysis of cell cycle arrest, nuclear localization, and virion packaging of human immunodeficiency virus type 1 Vpr
    • Di Marzio, P., S. Choe, M. Ebright, R Knoblauch, and N. R. Landau. 1995. Mutational analysis of cell cycle arrest, nuclear localization, and virion packaging of human immunodeficiency virus type 1 Vpr. J. Virol. 69:7909-7916.
    • (1995) J. Virol. , vol.69 , pp. 7909-7916
    • Di Marzio, P.1    Choe, S.2    Ebright, M.3    Knoblauch, R.4    Landau, N.R.5
  • 9
    • 0030250588 scopus 로고    scopus 로고
    • HIV-1, Vpr and the cell cycle
    • Emerman, M. 1996, HIV-1, Vpr and the cell cycle. Curr. Biol. 6:1096-1103.
    • (1996) Curr. Biol. , vol.6 , pp. 1096-1103
    • Emerman, M.1
  • 10
    • 0029794387 scopus 로고    scopus 로고
    • The Vpu protein of human immunodeficiency virus type 1 forms cation-selective ion channels
    • Ewart, G. D., T. Sutherland, P. W. Gage, and G. B. Cox. 1996. The Vpu protein of human immunodeficiency virus type 1 forms cation-selective ion channels. J. Virol. 70:7108-7115.
    • (1996) J. Virol. , vol.70 , pp. 7108-7115
    • Ewart, G.D.1    Sutherland, T.2    Gage, P.W.3    Cox, G.B.4
  • 11
    • 0030065395 scopus 로고    scopus 로고
    • Role of the karyopherin pathway in human immunodeficiency virus type 1 nuclear import
    • Gallay, P., V. Stitt, C. Mundy, M. Oettinger, and D. Trono. 1996. Role of the karyopherin pathway in human immunodeficiency virus type 1 nuclear import. J. Virol. 70:1027-1032.
    • (1996) J. Virol. , vol.70 , pp. 1027-1032
    • Gallay, P.1    Stitt, V.2    Mundy, C.3    Oettinger, M.4    Trono, D.5
  • 14
    • 0028181687 scopus 로고
    • Influenza a virus M2 ion channel protein: A structure-function analysis
    • Holsinger, L. J., D. Nichani, L. H. Pinto, and R A. Lamb. 1994. Influenza A virus M2 ion channel protein: a structure-function analysis. J. Virol. 68:1551-1563.
    • (1994) J. Virol. , vol.68 , pp. 1551-1563
    • Holsinger, L.J.1    Nichani, D.2    Pinto, L.H.3    Lamb, R.A.4
  • 15
    • 0029844220 scopus 로고    scopus 로고
    • Nuclear transport of granzyme B (fragmentin-2)-dependence on perform in vivo and cytosolic factors in vitro
    • Jans, D. A., P. Jans, L. J. Briggs, V. Sutton, and J. A. Trapani. 1996. Nuclear transport of granzyme B (fragmentin-2)-dependence on perform in vivo and cytosolic factors in vitro. J. Biol. Chem. 271:30781-30789.
    • (1996) J. Biol. Chem. , vol.271 , pp. 30781-30789
    • Jans, D.A.1    Jans, P.2    Briggs, L.J.3    Sutton, V.4    Trapani, J.A.5
  • 17
    • 0028116938 scopus 로고
    • Serum Vpr regulates productive infection and latency of human immunodeficiency virus type 1
    • Levy, D. N., Y. Refaeli, R. R. MacGregor, and D. B. Weiner. 1994. Serum Vpr regulates productive infection and latency of human immunodeficiency virus type 1. Proc. Natl. Acad. Sci. USA 91:10873-10877.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10873-10877
    • Levy, D.N.1    Refaeli, Y.2    MacGregor, R.R.3    Weiner, D.B.4
  • 19
    • 0027376064 scopus 로고
    • Human immunodeficiency virus type 1 viral protein R localization in infected cells and virions
    • Lu, Y. L., P. Spearman, and L. Ratner. 1993. Human immunodeficiency virus type 1 viral protein R localization in infected cells and virions. J. Virol. 67:6542-6550.
    • (1993) J. Virol. , vol.67 , pp. 6542-6550
    • Lu, Y.L.1    Spearman, P.2    Ratner, L.3
  • 20
  • 21
    • 0029880071 scopus 로고    scopus 로고
    • Extracellular addition of a domain of HIV-1 Vpr containing the amino acid sequence motif H(S/F)RIG causes cell membrane permeabilization and death
    • Macreadie, I. G., C. K. Arunagiri, D. R. Hewish, J. F. White, and A. A. Azad. 1996. Extracellular addition of a domain of HIV-1 Vpr containing the amino acid sequence motif H(S/F)RIG causes cell membrane permeabilization and death. Mol. Microbiol. 19:1185-1192.
    • (1996) Mol. Microbiol. , vol.19 , pp. 1185-1192
    • Macreadie, I.G.1    Arunagiri, C.K.2    Hewish, D.R.3    White, J.F.4    Azad, A.A.5
  • 22
    • 0030795827 scopus 로고    scopus 로고
    • HIV-1 protein Vpr causes gross mitochondrial dysfunction in the yeast Saccharomyces cerevisiae
    • Macreadie, I. G., D. R. Thorburn, D. M. Kirby, L. A. Castelli, N. L. Rozario, and A. A. Azad. 1997. HIV-1 protein Vpr causes gross mitochondrial dysfunction in the yeast Saccharomyces cerevisiae. FEBS Lett. 410:145-149.
    • (1997) FEBS Lett. , vol.410 , pp. 145-149
    • Macreadie, I.G.1    Thorburn, D.R.2    Kirby, D.M.3    Castelli, L.A.4    Rozario, N.L.5    Azad, A.A.6
  • 23
    • 0028892209 scopus 로고
    • Functional analysis of HIV-1 Vpr: Identification of determinants essential for subcellular localization
    • Mahalingam, S., R. G. Collman, M. Patel, C. E. Monken, and A. Srinivasan. 1995. Functional analysis of HIV-1 Vpr: identification of determinants essential for subcellular localization. Virology 212:331-339.
    • (1995) Virology , vol.212 , pp. 331-339
    • Mahalingam, S.1    Collman, R.G.2    Patel, M.3    Monken, C.E.4    Srinivasan, A.5
  • 24
    • 0028963445 scopus 로고
    • Identification of residues in the N-terminal acidic domain of HIV-1 Vpr essential for virion incorporation
    • Mahalingam, S., S. A. Khan, M. A. Jabbar, C. E. Monken, R. G. Collman, and A. Srinivasan. 1995. Identification of residues in the N-terminal acidic domain of HIV-1 Vpr essential for virion incorporation. Virology 207:297-302.
    • (1995) Virology , vol.207 , pp. 297-302
    • Mahalingam, S.1    Khan, S.A.2    Jabbar, M.A.3    Monken, C.E.4    Collman, R.G.5    Srinivasan, A.6
  • 25
    • 0028988970 scopus 로고
    • Mutagenesis of the putative alpha-helical domain of the Vpr protein of human immunodeficiency virus type 1: Effect on stability and virion incorporation
    • Mahalingam, S., S. A. Khan, R. Murali, M. A. Jabbar, C. E. Monken, R. G. Collman, and A. Srinivasan. 1995. Mutagenesis of the putative alpha-helical domain of the Vpr protein of human immunodeficiency virus type 1: effect on stability and virion incorporation. Proc. Natl. Acad. Sci. USA 92:3794-3798.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3794-3798
    • Mahalingam, S.1    Khan, S.A.2    Murali, R.3    Jabbar, M.A.4    Monken, C.E.5    Collman, R.G.6    Srinivasan, A.7
  • 27
    • 9044243753 scopus 로고    scopus 로고
    • Vpr protein of human immunodeficiency virus type 1 forms cation-selective channels in planar lipid bilayers
    • Piller, S. C., G. D. Ewart, A. Premkumar, G. B. Cox, and P. W. Gage. 1996. Vpr protein of human immunodeficiency virus type 1 forms cation-selective channels in planar lipid bilayers. Proc. Natl. Acad. Sci. USA 93:111-115.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 111-115
    • Piller, S.C.1    Ewart, G.D.2    Premkumar, A.3    Cox, G.B.4    Gage, P.W.5
  • 28
    • 0032515995 scopus 로고    scopus 로고
    • Extracellular HIV-1 virus protein R causes a large inward current and cell death in cultured hippocampal neurons: Implications for AIDS pathology
    • Piller, S. C., P. Jans, P. W. Gage, and D. A. Jans. 1998. Extracellular HIV-1 virus protein R causes a large inward current and cell death in cultured hippocampal neurons: implications for AIDS pathology. Proc. Natl. Acad. Sci. USA 95:4595-4600.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 4595-4600
    • Piller, S.C.1    Jans, P.2    Gage, P.W.3    Jans, D.A.4
  • 30
    • 0029869861 scopus 로고    scopus 로고
    • Vpr-induced cell cycle arrest is conserved among primate lentiviruses
    • Planelles, V., J. B. Jowett, Q. X. Li, Y. Xie, B. Hahn, and I. S. Chen. 1996. Vpr-induced cell cycle arrest is conserved among primate lentiviruses. J. Virol. 70:2516-2524.
    • (1996) J. Virol. , vol.70 , pp. 2516-2524
    • Planelles, V.1    Jowett, J.B.2    Li, Q.X.3    Xie, Y.4    Hahn, B.5    Chen, I.S.6
  • 31
    • 0025165855 scopus 로고
    • Coupled potassium channels induced by arachidonic acid in cultured neurons
    • Premkumar, L. S., P. W. Gage, and S. H. Chung. 1990. Coupled potassium channels induced by arachidonic acid in cultured neurons. Proc. R. Soc. Lond. B Biol. Sci. 242:17-22.
    • (1990) Proc. R. Soc. Lond. B Biol. Sci. , vol.242 , pp. 17-22
    • Premkumar, L.S.1    Gage, P.W.2    Chung, S.H.3
  • 33
    • 0030602182 scopus 로고    scopus 로고
    • Identification of an ion channel activity of the Vpu transmembrane domain and its involvement in the regulation of virus release from HIV-1-infected cells
    • Schubert, U., A. V. Ferrer Montiel, M. Oblatt Montal, P. Henklein, K. Strebel, and M. Montal. 1996. Identification of an ion channel activity of the Vpu transmembrane domain and its involvement in the regulation of virus release from HIV-1-infected cells. FEBS Lett. 398:12-18.
    • (1996) FEBS Lett. , vol.398 , pp. 12-18
    • Schubert, U.1    Ferrer Montiel, A.V.2    Oblatt Montal, M.3    Henklein, P.4    Strebel, K.5    Montal, M.6
  • 34
    • 0030920243 scopus 로고    scopus 로고
    • Human immunodeficiency virus type 1 Vpr induces apoptosis following cell cycle arrest
    • Stewart, S. A., B. Poon, J. B. Jowett, and I. S. Chen. 1997. Human immunodeficiency virus type 1 Vpr induces apoptosis following cell cycle arrest. J. Virol. 71:5579-5592.
    • (1997) J. Virol. , vol.71 , pp. 5579-5592
    • Stewart, S.A.1    Poon, B.2    Jowett, J.B.3    Chen, I.S.4
  • 36
    • 0026739866 scopus 로고
    • Evolution of the primate lentiviruses: Evidence from vpx and vpr
    • Tristem, M., C. Marshall, A. Karpas, and F. Hill. 1992. Evolution of the primate lentiviruses: evidence from vpx and vpr. EMBO J. 11:3405-3412.
    • (1992) EMBO J. , vol.11 , pp. 3405-3412
    • Tristem, M.1    Marshall, C.2    Karpas, A.3    Hill, F.4
  • 37
    • 0019394881 scopus 로고
    • Membrane potentials in yeast cells measured by direct and indirect methods
    • Vacata, V., A. Kotyk, and K. Sigler. 1981. Membrane potentials in yeast cells measured by direct and indirect methods. Biochim. Biophys. Acta 643:265-268.
    • (1981) Biochim. Biophys. Acta , vol.643 , pp. 265-268
    • Vacata, V.1    Kotyk, A.2    Sigler, K.3
  • 38
    • 0028840657 scopus 로고
    • Mutagenic analysis of human immunodeficiency virus type 1 Vpr: Role of a predicted N-terminal alpha-helical structure in Vpr nuclear localization and virion incorporation
    • Yao, X. J., R. A. Subbramanian, N. Rougeau, F. Boisvert, D. Bergeron, and E. A. Cohen. 1995. Mutagenic analysis of human immunodeficiency virus type 1 Vpr: role of a predicted N-terminal alpha-helical structure in Vpr nuclear localization and virion incorporation. J. Virol. 69:7032-7044.
    • (1995) J. Virol. , vol.69 , pp. 7032-7044
    • Yao, X.J.1    Subbramanian, R.A.2    Rougeau, N.3    Boisvert, F.4    Bergeron, D.5    Cohen, E.A.6
  • 39
    • 0028600072 scopus 로고
    • Biochemical mechanism of HIV-1 Vpr function. Oligomerization mediated by the N-terminal domain
    • Zhao, L. J., L. Wang, S. Mukherjee, and O. Narayan. 1994. Biochemical mechanism of HIV-1 Vpr function. Oligomerization mediated by the N-terminal domain. J. Biol. Chem. 269:32131-32137.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32131-32137
    • Zhao, L.J.1    Wang, L.2    Mukherjee, S.3    Narayan, O.4
  • 40
    • 0032520546 scopus 로고    scopus 로고
    • Arginine residues in the C-terminus of HIV-1 Vpr are important for nuclear localization and cell cycle arrest
    • Zhou, Y., Y. Lu, and L. Ratner. 1998. Arginine residues in the C-terminus of HIV-1 Vpr are important for nuclear localization and cell cycle arrest. Virology 242:414-424.
    • (1998) Virology , vol.242 , pp. 414-424
    • Zhou, Y.1    Lu, Y.2    Ratner, L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.