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Volumn 20, Issue 11, 1999, Pages 1275-1283

Concentration-dependent differential induction of necrosis or apoptosis by HIV-1 lytic peptide 1

Author keywords

AIDS; Apoptosis; HIV 1 cytopathology; HIV 1 lytic peptide; Necrosis

Indexed keywords

HIV 1 LYTIC PEPTIDE 1; UNCLASSIFIED DRUG; VIRUS ENVELOPE PROTEIN;

EID: 0032787050     PISSN: 01969781     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0196-9781(99)00132-1     Document Type: Article
Times cited : (14)

References (97)
  • 2
    • 0029070927 scopus 로고
    • Membrane permeabilization by different regions of the human immunodeficiency virus type 1 transmembrane glycoprotein
    • Arroya J., Boceta M., Gonzalez E., Michel M., Carrasco L. Membrane permeabilization by different regions of the human immunodeficiency virus type 1 transmembrane glycoprotein. J Virol. 69:1995;4095-4102.
    • (1995) J Virol , vol.69 , pp. 4095-4102
    • Arroya, J.1    Boceta, M.2    Gonzalez, E.3    Michel, M.4    Carrasco, L.5
  • 3
    • 0029972477 scopus 로고    scopus 로고
    • Age-dependent diarrhea induced by a rotaviral nonstructural glycoprotein
    • Ball J.M., Tian P., Zeng C.Q.-Y., Morris A., Estes M.K. Age-dependent diarrhea induced by a rotaviral nonstructural glycoprotein. Science. 272:1996;101-104.
    • (1996) Science , vol.272 , pp. 101-104
    • Ball, J.M.1    Tian, P.2    Zeng, C.Q.-Y.3    Morris, A.4    Estes, M.K.5
  • 4
    • 0031908105 scopus 로고    scopus 로고
    • Interruption of T-cell signal transduction by lentivirus lytic peptides from HIV-1 transmembrane protein
    • Beary T.P., Tencza S.B., Mietzner T.A., Montelaro R.C. Interruption of T-cell signal transduction by lentivirus lytic peptides from HIV-1 transmembrane protein. J Peptide Res. 51:1998;75-79.
    • (1998) J Peptide Res , vol.51 , pp. 75-79
    • Beary, T.P.1    Tencza, S.B.2    Mietzner, T.A.3    Montelaro, R.C.4
  • 5
    • 0026768135 scopus 로고
    • Dissociation of unintegrated viral DNA accumulation from single-cell lysis induced by human immunodeficiency virus type 1
    • Bergeron L., Sodroski J. Dissociation of unintegrated viral DNA accumulation from single-cell lysis induced by human immunodeficiency virus type 1. J Virol. 66:1992;5777-5787.
    • (1992) J Virol , vol.66 , pp. 5777-5787
    • Bergeron, L.1    Sodroski, J.2
  • 6
    • 0016409169 scopus 로고
    • Blocking of bacteriophages phi W and phi 5 with lipopolysaccharides from Escherichia coli K-12 mutants
    • Boman H.G., Monner D.A. Blocking of bacteriophages phi W and phi 5 with lipopolysaccharides from Escherichia coli K-12 mutants. J Bacteriol. 121:1975;465-470.
    • (1975) J Bacteriol , vol.121 , pp. 465-470
    • Boman, H.G.1    Monner, D.A.2
  • 7
    • 0015794052 scopus 로고
    • Specific monovalent cation effects on modification of reovirus infectivity by chymotrypsin digestion in vitro
    • Borsa J., Sargent M.D., Copps T.P., Long D.G., Chapman J.D. Specific monovalent cation effects on modification of reovirus infectivity by chymotrypsin digestion in vitro. J Virol. 11:1973;1017-1019.
    • (1973) J Virol , vol.11 , pp. 1017-1019
    • Borsa, J.1    Sargent, M.D.2    Copps, T.P.3    Long, D.G.4    Chapman, J.D.5
  • 8
    • 0028857651 scopus 로고
    • HIV-gp120 activates large-conductance apamin-sensitive potassium channels in rat astrocytes
    • Bubien J.K., Benveniste E.N., Benos D.J. HIV-gp120 activates large-conductance apamin-sensitive potassium channels in rat astrocytes. Am J Physiol. 268:1995;C1440-C9.
    • (1995) Am J Physiol , vol.268
    • Bubien, J.K.1    Benveniste, E.N.2    Benos, D.J.3
  • 10
    • 0030053308 scopus 로고    scopus 로고
    • Molecular determinants of acute single-cell lysis by human immunodeficiency virus type 1
    • Cao J., Park I.-W., Cooper A., Sodroski J. Molecular determinants of acute single-cell lysis by human immunodeficiency virus type 1. J Virol. 70:1996;1340-1354.
    • (1996) J Virol , vol.70 , pp. 1340-1354
    • Cao, J.1    Park, I.-W.2    Cooper, A.3    Sodroski, J.4
  • 11
    • 0029944880 scopus 로고    scopus 로고
    • Sequential acquisition of mitochondrial and plasma membrane alterations during early lymphocyte apoptosis
    • Castedo M., Hirsch T., Susin S.A., Zamzami N., Marchetti P., Macho A., Kroemer G. Sequential acquisition of mitochondrial and plasma membrane alterations during early lymphocyte apoptosis. J Immunol. 157:1996;512-521.
    • (1996) J Immunol , vol.157 , pp. 512-521
    • Castedo, M.1    Hirsch, T.2    Susin, S.A.3    Zamzami, N.4    Marchetti, P.5    Macho, A.6    Kroemer, G.7
  • 13
    • 0028007195 scopus 로고
    • An amphipathic peptide from the C-terminal region of the human immunodeficiency virus envelope glycoprotein causes pore formation in membranes
    • Chernomordik L., Chanturiya A., Suss-Toby E., Nora E., Zimmerburg J. An amphipathic peptide from the C-terminal region of the human immunodeficiency virus envelope glycoprotein causes pore formation in membranes. J Virol. 68:1994;7115-7123.
    • (1994) J Virol , vol.68 , pp. 7115-7123
    • Chernomordik, L.1    Chanturiya, A.2    Suss-Toby, E.3    Nora, E.4    Zimmerburg, J.5
  • 14
    • 0030008309 scopus 로고    scopus 로고
    • Envelope glycoproteins of human immunodeficiency virus type 1: Profound influences on immune functions
    • Chirmule N., Pahwa S. Envelope glycoproteins of human immunodeficiency virus type 1 profound influences on immune functions . Microbiol Rev. 60:1996;386-406.
    • (1996) Microbiol Rev , vol.60 , pp. 386-406
    • Chirmule, N.1    Pahwa, S.2
  • 15
    • 0005014748 scopus 로고    scopus 로고
    • The β-chemokine receptors CCR3 and CCR5 facilitate infection by primary HIV-1 isolates
    • Choe H., Farzan M., Sun Y., et al. The β-chemokine receptors CCR3 and CCR5 facilitate infection by primary HIV-1 isolates. Cell. 85:1996;1135-1148.
    • (1996) Cell , vol.85 , pp. 1135-1148
    • Choe, H.1    Farzan, M.2    Sun, Y.3
  • 17
    • 0030806588 scopus 로고    scopus 로고
    • A synthetic peptide corresponding to the carboxy terminus of human immunodeficiency virus type 1 transmembrane glycoprotein induces alterations in the ionic permeability of Xenopus laevis oocytes
    • Comardelle A.M., Norris C.H., Plymale D.R., Gatti P.G., Choi B., Haislip A.M., Tencza S.B., Mietzner T.A., Montelaro R.C., Garry R.F. A synthetic peptide corresponding to the carboxy terminus of human immunodeficiency virus type 1 transmembrane glycoprotein induces alterations in the ionic permeability of Xenopus laevis oocytes. AIDS Res Hum Retro. 13:1997;1525-1532.
    • (1997) AIDS Res Hum Retro , vol.13 , pp. 1525-1532
    • Comardelle, A.M.1    Norris, C.H.2    Plymale, D.R.3    Gatti, P.G.4    Choi, B.5    Haislip, A.M.6    Tencza, S.B.7    Mietzner, T.A.8    Montelaro, R.C.9    Garry, R.F.10
  • 18
    • 0000348475 scopus 로고
    • The amphipathic helix in cytotoxic peptides
    • R.M. Epand. Boca Raton, FL: CRC Press
    • Cornut I., Thiaudiere E., Dufourcq J. The amphipathic helix in cytotoxic peptides. Epand R.M. The Amphipathic Helix. 1993;174-219 CRC Press, Boca Raton, FL.
    • (1993) The Amphipathic Helix , pp. 174-219
    • Cornut, I.1    Thiaudiere, E.2    Dufourcq, J.3
  • 19
    • 0031018842 scopus 로고    scopus 로고
    • Mitochondrial alterations and a dramatic tendency to undergo apoptosis in peripheral blood lymphocytes during acute HIV syndrome
    • Cossarizza A., Mussini C., Mongiardo N., Borghi V., Sabbatini A., De Rienzo B., Franceschi C. Mitochondrial alterations and a dramatic tendency to undergo apoptosis in peripheral blood lymphocytes during acute HIV syndrome. AIDS. 11:1996;19-26.
    • (1996) AIDS , vol.11 , pp. 19-26
    • Cossarizza, A.1    Mussini, C.2    Mongiardo, N.3    Borghi, V.4    Sabbatini, A.5    De Rienzo, B.6    Franceschi, C.7
  • 20
    • 0030604727 scopus 로고    scopus 로고
    • A dual-tropic primary HIV-1 isolate that uses fusin and the β-chemokine receptors CKR-5, CKR-3 and CKR-2b as fusion cofactors
    • Doranz B.J., Rucker J., Yi Y., Smyth R.J., Samson M., Peiper S.C., Parmenteir M., Collman R.G., Doms R.W. A dual-tropic primary HIV-1 isolate that uses fusin and the β-chemokine receptors CKR-5, CKR-3 and CKR-2b as fusion cofactors. Cell. 85:1996;1149-1158.
    • (1996) Cell , vol.85 , pp. 1149-1158
    • Doranz, B.J.1    Rucker, J.2    Yi, Y.3    Smyth, R.J.4    Samson, M.5    Peiper, S.C.6    Parmenteir, M.7    Collman, R.G.8    Doms, R.W.9
  • 21
    • 0031555627 scopus 로고    scopus 로고
    • Natural reverse transcription of simian immunodeficiency virus
    • Dornadula G., Zhang H., Bagasra O., Pomerantz R. Natural reverse transcription of simian immunodeficiency virus. Virology. 227:1997;260-267.
    • (1997) Virology , vol.227 , pp. 260-267
    • Dornadula, G.1    Zhang, H.2    Bagasra, O.3    Pomerantz, R.4
  • 23
    • 0029185707 scopus 로고
    • 2+ Associated with Apoptosis
    • L.M. Schwartz, & B.A. Osborne. San Diego: Academic Press
    • 2+ Associated with Apoptosis. Schwartz L.M., Osborne B.A. Methods in Cell Biology Cell Death . 1995;41-55 Academic Press, San Diego.
    • (1995) Methods in Cell Biology: Cell Death , pp. 41-55
    • Eastman, A.1
  • 24
    • 0025055304 scopus 로고
    • The most amphiphilic alpha-helices include two amino acids segments in human immunodeficiency virus
    • Eisenberg D., Wessson M. The most amphiphilic alpha-helices include two amino acids segments in human immunodeficiency virus. Biopolymers. 29:1990;171-177.
    • (1990) Biopolymers , vol.29 , pp. 171-177
    • Eisenberg, D.1    Wessson, M.2
  • 25
    • 0029794387 scopus 로고    scopus 로고
    • The Vpu protein of human immunodeficiency virus type 1 forms cation-selective ion channels
    • Ewart G.D., Sutherland T., Gage P.W., Cox G.B. The Vpu protein of human immunodeficiency virus type 1 forms cation-selective ion channels. J Virol. 70:1996;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
  • 26
    • 0029041118 scopus 로고
    • Colour thresholding in video imaging
    • Fermin C.D., Degraw S. Colour thresholding in video imaging. J Anat. 186:1995;469-481.
    • (1995) J Anat , vol.186 , pp. 469-481
    • Fermin, C.D.1    Degraw, S.2
  • 27
    • 0027064712 scopus 로고
    • Membrane alterations linked to early interactions of HIV with the cell surface
    • Fermin C.D., Garry R.F. Membrane alterations linked to early interactions of HIV with the cell surface. Virology. 191:1992;941-946.
    • (1992) Virology , vol.191 , pp. 941-946
    • Fermin, C.D.1    Garry, R.F.2
  • 28
    • 0021343516 scopus 로고
    • Dendritic growth following labyrinthectomy in the squirrel monkey
    • Fermin C.D., Igarashi M. Dendritic growth following labyrinthectomy in the squirrel monkey. Acta Otolaryngol (Stockh). 97:1984;203-212.
    • (1984) Acta Otolaryngol (Stockh) , vol.97 , pp. 203-212
    • Fermin, C.D.1    Igarashi, M.2
  • 29
    • 0028109087 scopus 로고
    • Indirect mechanisms of HIV pathogenesis: How does HIV kill T cells?
    • Finkel T.H., Banda N.K. Indirect mechanisms of HIV pathogenesis how does HIV kill T cells? Current Opinion in Immunology. 6:1994;605-615.
    • (1994) Current Opinion in Immunology , vol.6 , pp. 605-615
    • Finkel, T.H.1    Banda, N.K.2
  • 31
    • 0032238943 scopus 로고    scopus 로고
    • Inhibitors of mitochondrial energy production prevent DNA internucleosomal fragmentation in thymocytes
    • Galitovsky V.E., Gogvadze V.G. Inhibitors of mitochondrial energy production prevent DNA internucleosomal fragmentation in thymocytes. Biochemistry (Mosc). 63:1998;1374-1377.
    • (1998) Biochemistry (Mosc) , vol.63 , pp. 1374-1377
    • Galitovsky, V.E.1    Gogvadze, V.G.2
  • 33
    • 0023669119 scopus 로고
    • Detection of a fusion peptide sequence in the transmembrane protein of human immunodeficiency virus
    • Gallaher W.R. Detection of a fusion peptide sequence in the transmembrane protein of human immunodeficiency virus. Cell. 50:1987;327-328.
    • (1987) Cell , vol.50 , pp. 327-328
    • Gallaher, W.R.1
  • 35
    • 0024807136 scopus 로고
    • Potential mechanisms for the cytopathic properties of human immunodeficiency virus
    • Garry R.F. Potential mechanisms for the cytopathic properties of human immunodeficiency virus. AIDS. 3:1989;683-684.
    • (1989) AIDS , vol.3 , pp. 683-684
    • Garry, R.F.1
  • 36
    • 0344622129 scopus 로고
    • Viral burden in AIDS
    • Garry R.F., Fermin C.D. Viral burden in AIDS. Nature. 365:1993;301-302.
    • (1993) Nature , vol.365 , pp. 301-302
    • Garry, R.F.1    Fermin, C.D.2
  • 37
    • 0027090041 scopus 로고
    • Tat contains a sequence related to snake neurotoxins
    • Garry R.F., Koch G. Tat contains a sequence related to snake neurotoxins. AIDS. 6:1992;1541-1542.
    • (1992) AIDS , vol.6 , pp. 1541-1542
    • Garry, R.F.1    Koch, G.2
  • 38
    • 0025939590 scopus 로고
    • Similarities of viral proteins to toxins that interact with monovalent cation channels
    • Garry R.F., Kort J.J., Koch-Nolte F., Koch G. Similarities of viral proteins to toxins that interact with monovalent cation channels. AIDS. 5:1991;1381-1384.
    • (1991) AIDS , vol.5 , pp. 1381-1384
    • Garry, R.F.1    Kort, J.J.2    Koch-Nolte, F.3    Koch, G.4
  • 39
    • 0027523631 scopus 로고
    • Interaction of peptide fragment 828-848 of the envelope glycoprotein of human immunodeficiency virus type I with lipid bilayers
    • Gawrisch K., Han K.-H., Yang J.-S., Bergelson L.D., Ferretti J.A. Interaction of peptide fragment 828-848 of the envelope glycoprotein of human immunodeficiency virus type I with lipid bilayers. Biochemistry. 32:1993;3112-3118.
    • (1993) Biochemistry , vol.32 , pp. 3112-3118
    • Gawrisch, K.1    Han, K.-H.2    Yang, J.-S.3    Bergelson, L.D.4    Ferretti, J.A.5
  • 44
    • 0031037897 scopus 로고    scopus 로고
    • The release of cytochrome c from mitochondria: A primary site for Bcl-2 regulation of apoptosis
    • Kluck R.M., Bossy-Wetzel E., Green D.R., Newmeyer D.D. The release of cytochrome c from mitochondria a primary site for Bcl-2 regulation of apoptosis . Science. 275:1997;1132-1136.
    • (1997) Science , vol.275 , pp. 1132-1136
    • Kluck, R.M.1    Bossy-Wetzel, E.2    Green, D.R.3    Newmeyer, D.D.4
  • 45
    • 0032541120 scopus 로고    scopus 로고
    • The nef protein of the human immunodeficiency virus type 1 (HIV-1) inhibits a large-conductance potassium channel in human glial cells
    • Kort J.J., Jalonen T.O. The nef protein of the human immunodeficiency virus type 1 (HIV-1) inhibits a large-conductance potassium channel in human glial cells. Neurosci Lett. 251:1998;1-4.
    • (1998) Neurosci Lett , vol.251 , pp. 1-4
    • Kort, J.J.1    Jalonen, T.O.2
  • 46
    • 0031550769 scopus 로고    scopus 로고
    • Do Vpu and Vpr of human immunodeficiency virus type 1 and NB of influenza B virus have ion channel activities in the viral life cycles?
    • Lamb R.A., Pinto L.H. Do Vpu and Vpr of human immunodeficiency virus type 1 and NB of influenza B virus have ion channel activities in the viral life cycles? Virology. 229:1997;1-11.
    • (1997) Virology , vol.229 , pp. 1-11
    • Lamb, R.A.1    Pinto, L.H.2
  • 51
    • 0023870511 scopus 로고
    • Human immunodeficiency virus-induced pathology favored by cellular transmission and activation
    • Lewis D.E., Yoffe B., Bosworth C.G., Hollinger F.B., Rich R.R. Human immunodeficiency virus-induced pathology favored by cellular transmission and activation. FASEB J. 2:1988;251-255.
    • (1988) FASEB J , vol.2 , pp. 251-255
    • Lewis, D.E.1    Yoffe, B.2    Bosworth, C.G.3    Hollinger, F.B.4    Rich, R.R.5
  • 52
    • 0032910196 scopus 로고    scopus 로고
    • Uncouplers of oxidative phosphorylation can enhance a fas death signal
    • Linsinger G., Wilhelm S., Wagner H., Hacker G. Uncouplers of oxidative phosphorylation can enhance a fas death signal. Mol Cell Biol. 19:1999;3299-3331.
    • (1999) Mol Cell Biol , vol.19 , pp. 3299-3331
    • Linsinger, G.1    Wilhelm, S.2    Wagner, H.3    Hacker, G.4
  • 53
    • 0027296972 scopus 로고
    • Reovirus M2 gene is associated with chromium release from mouse L cells
    • Lucia-Jandris P., Hooper J., Fields B. Reovirus M2 gene is associated with chromium release from mouse L cells. J Virol. 67:1993;5339-5345.
    • (1993) J Virol , vol.67 , pp. 5339-5345
    • Lucia-Jandris, P.1    Hooper, J.2    Fields, B.3
  • 55
    • 0022259814 scopus 로고
    • Effects of calmodulin and related proteins on the hemolytic activity of mellitin
    • Malencik D.A., Anderson S.R. Effects of calmodulin and related proteins on the hemolytic activity of mellitin. Biochem Biophys Res Comm. 130:1985;22-29.
    • (1985) Biochem Biophys Res Comm , vol.130 , pp. 22-29
    • Malencik, D.A.1    Anderson, S.R.2
  • 58
    • 0025895768 scopus 로고
    • A structural correlation between lentivirus transmembrane proteins and natural cytolytic peptides
    • Miller M.A., Garry R.F., Jaynes J.M., Montelaro R.C. A structural correlation between lentivirus transmembrane proteins and natural cytolytic peptides. AIDS Res Hum Retro. 7:1991;511-519.
    • (1991) AIDS Res Hum Retro , vol.7 , pp. 511-519
    • Miller, M.A.1    Garry, R.F.2    Jaynes, J.M.3    Montelaro, R.C.4
  • 59
    • 0027421380 scopus 로고
    • Identification of a calmodulin-binding and inhibitory peptide domain in the HIV-1 transmembrane glycoprotein
    • Miller M.A., Mietzner T.A., Cloyd M.W., Robey W.G., Montelaro R.C. Identification of a calmodulin-binding and inhibitory peptide domain in the HIV-1 transmembrane glycoprotein. AIDS Res Hum Retro. 9:1993;1057-1066.
    • (1993) AIDS Res Hum Retro , vol.9 , pp. 1057-1066
    • Miller, M.A.1    Mietzner, T.A.2    Cloyd, M.W.3    Robey, W.G.4    Montelaro, R.C.5
  • 61
    • 9544230790 scopus 로고    scopus 로고
    • Effects of human immunodeficiency virus type 1 infection on programmed cell death in the presence or absence of Bcl-2
    • Park I.W., Kondo E., Bergeron L., Park J., Sodroski J. Effects of human immunodeficiency virus type 1 infection on programmed cell death in the presence or absence of Bcl-2. J Acquired Immune Defic Syndr Hum Retrovirol. 12:1996;321-328.
    • (1996) J Acquired Immune Defic Syndr Hum Retrovirol , vol.12 , pp. 321-328
    • Park, I.W.1    Kondo, E.2    Bergeron, L.3    Park, J.4    Sodroski, J.5
  • 63
    • 9044243753 scopus 로고    scopus 로고
    • Vpr protein of human immunodeficiency virus type 1 forms cation-selective channels in planar lipid bilayers
    • Piller S.C., Ewart G.D., Premkumar A., Cox G.B., Gage P.W. Vpr protein of human immunodeficiency virus type 1 forms cation-selective channels in planar lipid bilayers. Proc Natl Acad Sci USA. 93:1996;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
  • 64
    • 0032947291 scopus 로고    scopus 로고
    • The amino-terminal region of Vpr from human immunodeficiency virus type 1 forms ion channels and kills neurons
    • Piller S.C., Ewart G.D., Jans D.A., Gage P.W., Cox G.B. The amino-terminal region of Vpr from human immunodeficiency virus type 1 forms ion channels and kills neurons. J Virol. 73:1999;4230-4238.
    • (1999) J Virol , vol.73 , pp. 4230-4238
    • Piller, S.C.1    Ewart, G.D.2    Jans, D.A.3    Gage, P.W.4    Cox, G.B.5
  • 65
    • 0026612385 scopus 로고
    • Influenza virus M2 protein has ion channel activity
    • Pinto L.H., Holsinger L.J., Lamb R.A. Influenza virus M2 protein has ion channel activity. Cell. 69:1992;517-528.
    • (1992) Cell , vol.69 , pp. 517-528
    • Pinto, L.H.1    Holsinger, L.J.2    Lamb, R.A.3
  • 67
  • 68
    • 0020209553 scopus 로고
    • Poliovirus-induced alterations in HeLa cell membrane functions
    • Schaefer A., Kuhne J., Zibirre R., Koch G. Poliovirus-induced alterations in HeLa cell membrane functions. J Virol. 44:1982;445-449.
    • (1982) J Virol , vol.44 , pp. 445-449
    • Schaefer, A.1    Kuhne, J.2    Zibirre, R.3    Koch, G.4
  • 69
    • 0026341766 scopus 로고
    • Semliki Forest Virus envelope proteins function as proton channels
    • Schegel A., Omar A., Jentsch P., Morell A., Kempf C. Semliki Forest Virus envelope proteins function as proton channels. Biosci Rep. 11:1991;243-255.
    • (1991) Biosci Rep , vol.11 , pp. 243-255
    • Schegel, A.1    Omar, A.2    Jentsch, P.3    Morell, A.4    Kempf, C.5
  • 74
    • 0029984098 scopus 로고    scopus 로고
    • Bcl-2 expression prevents activation of the ICE protease cascade
    • Shimizu S., Eguchi Y., Kamiike W., Matsuda H., Tsujimoto Y. Bcl-2 expression prevents activation of the ICE protease cascade. Oncogene. 12:1996;2251-2257.
    • (1996) Oncogene , vol.12 , pp. 2251-2257
    • Shimizu, S.1    Eguchi, Y.2    Kamiike, W.3    Matsuda, H.4    Tsujimoto, Y.5
  • 75
    • 0023182637 scopus 로고
    • A major mechanism of HIV-induced cell killing does not involve cell fusion
    • Somasundaran M., Robinson H. A major mechanism of HIV-induced cell killing does not involve cell fusion. J Virol. 61:1988;3114-3119.
    • (1988) J Virol , vol.61 , pp. 3114-3119
    • Somasundaran, M.1    Robinson, H.2
  • 76
    • 0027971451 scopus 로고
    • Calmodulin antagonists inhibit human immunodeficiency virus-induced cell fusion but not virus replication
    • Srinivas R.V., Bernstein H., Oliver C., Compans R.W. Calmodulin antagonists inhibit human immunodeficiency virus-induced cell fusion but not virus replication. AIDS Res Hum Retro. 10:1994;1489-1496.
    • (1994) AIDS Res Hum Retro , vol.10 , pp. 1489-1496
    • Srinivas, R.V.1    Bernstein, H.2    Oliver, C.3    Compans, R.W.4
  • 77
    • 0027505042 scopus 로고
    • Cytosolic domain of the HIV envelope glycoprotein binds to calmodulin and inhibits calmodulin-regulated proteins
    • Srinivas S., Srinivas R., Anantharamaiah G., Segrest J., Compans R., Segrest J. Cytosolic domain of the HIV envelope glycoprotein binds to calmodulin and inhibits calmodulin-regulated proteins. J Biol Chem. 268:1993;22895-22899.
    • (1993) J Biol Chem , vol.268 , pp. 22895-22899
    • Srinivas, S.1    Srinivas, R.2    Anantharamaiah, G.3    Segrest, J.4    Compans, R.5    Segrest, J.6
  • 78
    • 0023933994 scopus 로고
    • Envelope glycoprotein of HIV induces interference and cytolysis resistence in CD4+ cells: Mechanism for persistence in AIDS
    • Stevenson M., Meier C., Mann A.M., Chapman N., Wasiak A. Envelope glycoprotein of HIV induces interference and cytolysis resistence in CD4+ cells Mechanism for persistence in AIDS . Cell. 53:1988;483-496.
    • (1988) Cell , vol.53 , pp. 483-496
    • Stevenson, M.1    Meier, C.2    Mann, A.M.3    Chapman, N.4    Wasiak, A.5
  • 79
    • 0031569469 scopus 로고    scopus 로고
    • HIV-induced T cell syncytia are self-perpetuating and the primary cause of T cell death in culture
    • Sylwester A., Murphy S., Shutt D., Soll D.R. HIV-induced T cell syncytia are self-perpetuating and the primary cause of T cell death in culture. J Immunol. 158:1997;3996-4007.
    • (1997) J Immunol , vol.158 , pp. 3996-4007
    • Sylwester, A.1    Murphy, S.2    Shutt, D.3    Soll, D.R.4
  • 80
    • 0029921168 scopus 로고    scopus 로고
    • T lymphocyte recruitment by interleukin-8 (IL-8). IL-8-induced degranulation of neutrophils releases potent chemoattractants for human T lymphocytes both in vitro and in vivo
    • Taub D.D., Anver M., Oppenheim J.J., Longo D.L., Murphy W.J. T lymphocyte recruitment by interleukin-8 (IL-8). IL-8-induced degranulation of neutrophils releases potent chemoattractants for human T lymphocytes both in vitro and in vivo. J Clin Invest. 97:1996;1931-1941.
    • (1996) J Clin Invest , vol.97 , pp. 1931-1941
    • Taub, D.D.1    Anver, M.2    Oppenheim, J.J.3    Longo, D.L.4    Murphy, W.J.5
  • 81
    • 0029037538 scopus 로고
    • Effect of amino acid substitutions on calcodulin binding and cytolytic properties of the LLP-1 peptide segment of HIV-1 transmembrane protein
    • Tencza S., Miller M., Islam K., Mietzner T., Montelaro R. Effect of amino acid substitutions on calcodulin binding and cytolytic properties of the LLP-1 peptide segment of HIV-1 transmembrane protein. J Virol. 69:1995;5199-5202.
    • (1995) J Virol , vol.69 , pp. 5199-5202
    • Tencza, S.1    Miller, M.2    Islam, K.3    Mietzner, T.4    Montelaro, R.5
  • 82
    • 0030722714 scopus 로고    scopus 로고
    • Novel antimicrobial peptides derived from human immunodefiency virus type 1 and other lentivirus transmembrane proteins
    • Tencza S.B., Douglas J.P., Creighton D.J. Jr, Montelaro R.C., Mietzner T.A. Novel antimicrobial peptides derived from human immunodefiency virus type 1 and other lentivirus transmembrane proteins. Antimicro Agents Chemother. 41:1997;2394-2398.
    • (1997) Antimicro Agents Chemother , vol.41 , pp. 2394-2398
    • Tencza, S.B.1    Douglas, J.P.2    Creighton D.J., Jr.3    Montelaro, R.C.4    Mietzner, T.A.5
  • 83
    • 0031039143 scopus 로고    scopus 로고
    • Calmodulin-binding function of LLP segments from the HIV type 1 transmembrane protein is conserved among natural sequence variants
    • Tencza S.B., Mietzner T.A., Montelaro R.C. Calmodulin-binding function of LLP segments from the HIV type 1 transmembrane protein is conserved among natural sequence variants. AIDS Res Hum Retro. 13:1997;263-269.
    • (1997) AIDS Res Hum Retro , vol.13 , pp. 263-269
    • Tencza, S.B.1    Mietzner, T.A.2    Montelaro, R.C.3
  • 84
    • 0025830099 scopus 로고
    • Apoptosis as a mechanism of cell death in cultured T lymphoblasts acutely infected with HIV-1
    • Terai C., Kornbluth R.S., Pauza C.D., Richman D.D., Carson D.A. Apoptosis as a mechanism of cell death in cultured T lymphoblasts acutely infected with HIV-1. J Clin Invest. 87:1991;1710-1715.
    • (1991) J Clin Invest , vol.87 , pp. 1710-1715
    • Terai, C.1    Kornbluth, R.S.2    Pauza, C.D.3    Richman, D.D.4    Carson, D.A.5
  • 85
    • 0029085955 scopus 로고
    • The rotavirus nonstructural glycoprotein NSP4 mobilizes Ca2+ from the endoplasmic reticulum
    • Tian P., Estes M.K., Hu Y., Ball J.M., Zeng C.Q., Schilling W.P. The rotavirus nonstructural glycoprotein NSP4 mobilizes Ca2+ from the endoplasmic reticulum. J Virol. 69:1995;5763-5772.
    • (1995) J Virol , vol.69 , pp. 5763-5772
    • Tian, P.1    Estes, M.K.2    Hu, Y.3    Ball, J.M.4    Zeng, C.Q.5    Schilling, W.P.6
  • 86
    • 0031060329 scopus 로고    scopus 로고
    • Characterization of ion channels formed by poliovirus in planar lipid membranes
    • Tosteson M.T., Chow M. Characterization of ion channels formed by poliovirus in planar lipid membranes. J Virol. 71:1997;507-511.
    • (1997) J Virol , vol.71 , pp. 507-511
    • Tosteson, M.T.1    Chow, M.2
  • 87
    • 0030796183 scopus 로고    scopus 로고
    • Bcl-2 and Bcl-xL block apoptosis as well as necrosis: Possible involvement of common mediators in apoptotic and necrotic signal transduction pathways
    • Tsujimoto Y., Shimizu S., Eguchi Y., Kamiike W., Matsuda H. Bcl-2 and Bcl-xL block apoptosis as well as necrosis possible involvement of common mediators in apoptotic and necrotic signal transduction pathways . Leukemia. 11:(Suppl 3):1997;380-382.
    • (1997) Leukemia , vol.11 , Issue.SUPPL. 3 , pp. 380-382
    • Tsujimoto, Y.1    Shimizu, S.2    Eguchi, Y.3    Kamiike, W.4    Matsuda, H.5
  • 88
    • 0024442637 scopus 로고
    • The role of monovalent cation transport in Sindbis virus maturation and release
    • Ulug E., Garry R., Bose J.H.R. The role of monovalent cation transport in Sindbis virus maturation and release. Virology. 172:1989;42-50.
    • (1989) Virology , vol.172 , pp. 42-50
    • Ulug, E.1    Garry, R.2    Bose, J.H.R.3
  • 89
    • 0024515174 scopus 로고
    • Theoretically determined three-dimensional structures for amphipathic segments of the HIV-1 gp41 envelope protein
    • Venable R.M., Pastor R.W., Brookes B.R., Carson F.W. Theoretically determined three-dimensional structures for amphipathic segments of the HIV-1 gp41 envelope protein. AIDS Res Hum Retro. 5:1989;7-22.
    • (1989) AIDS Res Hum Retro , vol.5 , pp. 7-22
    • Venable, R.M.1    Pastor, R.W.2    Brookes, B.R.3    Carson, F.W.4
  • 90
    • 0014724971 scopus 로고
    • Inhibition of Sindbis virus production by media of low ionic strength: Intracellular events and requirements for reversal
    • Waite M.R., Pfefferkorn E.R. Inhibition of Sindbis virus production by media of low ionic strength intracellular events and requirements for reversal . J Virol. 5:1970;60-71.
    • (1970) J Virol , vol.5 , pp. 60-71
    • Waite, M.R.1    Pfefferkorn, E.R.2
  • 92
    • 0025990816 scopus 로고
    • HIV-1 Nef protein exhibits structural and functional similarity to scorpion peptides interacting with potassium channels
    • Werner T., Ferrroni S., Saermark T., Brack-Werner R., Banati R., Mager R., Steinaa L., Kreutzberg G., Erfle V. HIV-1 Nef protein exhibits structural and functional similarity to scorpion peptides interacting with potassium channels. AIDS. 5:1991;1301-1308.
    • (1991) AIDS , vol.5 , pp. 1301-1308
    • Werner, T.1    Ferrroni, S.2    Saermark, T.3    Brack-Werner, R.4    Banati, R.5    Mager, R.6    Steinaa, L.7    Kreutzberg, G.8    Erfle, V.9
  • 94
    • 0023854883 scopus 로고
    • Antimicrobial activity of synthetic magainin peptides and several analogues
    • Zasloff M., Martin B., Chen H.-C. Antimicrobial activity of synthetic magainin peptides and several analogues. Proc Natl Acad Sci USA. 85:1988;910-913.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 910-913
    • Zasloff, M.1    Martin, B.2    Chen, H.-C.3
  • 96
    • 0029970774 scopus 로고    scopus 로고
    • Amphipathic domains in the C terminus of the transmembrane protein (gp41) permeabilize HIV-1 virions: A molecular mechanism underlying natural endogenous reverse transcriptase
    • Zhang H., Dornadula G., Laughlin M., Pomerantz R. Amphipathic domains in the C terminus of the transmembrane protein (gp41) permeabilize HIV-1 virions a molecular mechanism underlying natural endogenous reverse transcriptase . Proc Natl Acad Sci USA. 93:1996;12519-12524.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 12519-12524
    • Zhang, H.1    Dornadula, G.2    Laughlin, M.3    Pomerantz, R.4
  • 97
    • 0032530375 scopus 로고    scopus 로고
    • HIV-1 Tat inhibits human natural killer cell function by blocking L-type calcium channels
    • Zocchi M.R., Rubartelli A., Morgavi P., Poggi A. HIV-1 Tat inhibits human natural killer cell function by blocking L-type calcium channels. J Immunol. 161:1998;2938-2943.
    • (1998) J Immunol , vol.161 , pp. 2938-2943
    • Zocchi, M.R.1    Rubartelli, A.2    Morgavi, P.3    Poggi, A.4


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