메뉴 건너뛰기




Volumn 86, Issue 5, 2010, Pages 1099-1108

Characterization of the effects of aryl-azido compounds and UVA irradiation on the viral proteins and infectivity of human immunodeficiency virus type 1

Author keywords

[No Author keywords available]

Indexed keywords

ANTIVIRUS AGENT; AZIDE; VIRUS PROTEIN;

EID: 77956485223     PISSN: 00318655     EISSN: 17511097     Source Type: Journal    
DOI: 10.1111/j.1751-1097.2010.00780.x     Document Type: Article
Times cited : (9)

References (36)
  • 1
    • 0024818527 scopus 로고
    • Effects of formalin inactivation on bovine herpes virus-1 glycoprotein and antibody response elicited by formalin-inactivated vaccines in rabbits
    • DOI
    • Duque, H., R. L. Marshall, B. A. Israel G. J. Letchworth (1989) Effects of formalin inactivation on bovine herpes virus-1 glycoprotein and antibody response elicited by formalin-inactivated vaccines in rabbits. Vaccine 7, 513 520. DOI
    • (1989) Vaccine , vol.7 , pp. 513-520
    • Duque, H.1    Marshall, R.L.2    Israel, B.A.3    Letchworth, G.J.4
  • 3
    • 0034125736 scopus 로고    scopus 로고
    • Enhanced binding of antibodies to neutralization epitopes following thermal and chemical inactivation of human immunodeficiency virus type 1
    • Grovit-Ferbas, K., J. F. Hsu, J. Ferbas, V. Gudeman I. S. Y. Chen (2000) Enhanced binding of antibodies to neutralization epitopes following thermal and chemical inactivation of human immunodeficiency virus type 1. J. Virol. 74 (13 5802 5809.
    • (2000) J. Virol. , vol.74 , Issue.13 , pp. 5802-5809
    • Grovit-Ferbas, K.1    Hsu, J.F.2    Ferbas, J.3    Gudeman, V.4    Chen, I.S.Y.5
  • 4
    • 34748861028 scopus 로고    scopus 로고
    • Antigenic characterization of a formalin-inactivated poliovirus vaccine derived from live-attenuated sabin strains
    • DOI
    • Tano, Y., H. Shimizu, J. Martin, Y. Nishimura, B. Simizu T. Miyamura (2007) Antigenic characterization of a formalin-inactivated poliovirus vaccine derived from live-attenuated sabin strains. Vaccine 25, 7041 7046. DOI
    • (2007) Vaccine , vol.25 , pp. 7041-7046
    • Tano, Y.1    Shimizu, H.2    Martin, J.3    Nishimura, Y.4    Simizu, B.5    Miyamura, T.6
  • 5
    • 0028789077 scopus 로고
    • Conservation of HIV-1 gp120 neutralizing epitopes after formalin inactivation
    • Sattentau, O. J. (1995) Conservation of HIV-1 gp120 neutralizing epitopes after formalin inactivation. AIDS 9, 1383 1385.
    • (1995) AIDS , vol.9 , pp. 1383-1385
    • Sattentau, O.J.1
  • 6
    • 0028279810 scopus 로고
    • Immunogenicity of a viral model vaccine after different inactivation procedures
    • DOI
    • Bachmann, M. F., C. Bast, H. Hengartner R. M. Zinkernagel (1994) Immunogenicity of a viral model vaccine after different inactivation procedures. Med. Microbiol. Immunol. 183, 95 104. DOI
    • (1994) Med. Microbiol. Immunol. , vol.183 , pp. 95-104
    • Bachmann, M.F.1    Bast, C.2    Hengartner, H.3    Zinkernagel, R.M.4
  • 7
    • 20144388317 scopus 로고    scopus 로고
    • Induction of humoral immune response following vaccination with envelope-containing, formaldehyde-treated, thermally inactivated human immunodeficiency virus type 1
    • DOI
    • Poon, B., J. T. Safrit, H. McClure, C. Kitchen, J. F. Hsu, V. Gudeman, C. Petropolous, T. Wrin, I. S. Y. Chen K. Grovit-Ferbas (2005) Induction of humoral immune response following vaccination with envelope-containing, formaldehyde-treated, thermally inactivated human immunodeficiency virus type 1. J. Virol. 79 (8 4927 4935. DOI
    • (2005) J. Virol. , vol.79 , Issue.8 , pp. 4927-4935
    • Poon, B.1    Safrit, J.T.2    McClure, H.3    Kitchen, C.4    Hsu, J.F.5    Gudeman, V.6    Petropolous, C.7    Wrin, T.8    Chen, I.S.Y.9    Grovit-Ferbas, K.10
  • 8
    • 0026541296 scopus 로고
    • Photochemical inactivation of viruses with psoralens: An overview
    • Hanson, C. V. (1992) Photochemical inactivation of viruses with psoralens: An overview. Blood Cells 18, 7 25.
    • (1992) Blood Cells , vol.18 , pp. 7-25
    • Hanson, C.V.1
  • 9
    • 0020437546 scopus 로고
    • Repair of psoralen-induced crosslinks in cells multiply infected with SV40
    • DOI
    • Hall, J. D. (1982) Repair of psoralen-induced crosslinks in cells multiply infected with SV40. Mol. Gen. Genet. 188, 135 138. DOI
    • (1982) Mol. Gen. Genet. , vol.188 , pp. 135-138
    • Hall, J.D.1
  • 10
    • 0027203297 scopus 로고
    • New photolabeling and crosslinking methods
    • DOI
    • Brunner, J. (1993) New photolabeling and crosslinking methods. Annu. Rev. Biochem. 62, 483 514. DOI
    • (1993) Annu. Rev. Biochem. , vol.62 , pp. 483-514
    • Brunner, J.1
  • 11
    • 0019198278 scopus 로고
    • Photogenerated reagents for membranes: Selective labeling of intrinsic membrane proteins in the human erythrocyte membrane
    • DOI
    • Bayley, H. J. R. Knowles (1980) Photogenerated reagents for membranes: Selective labeling of intrinsic membrane proteins in the human erythrocyte membrane. Biochemistry 19 (17 3883 3892. DOI
    • (1980) Biochemistry , vol.19 , Issue.17 , pp. 3883-3892
    • Bayley, H.1    Knowles, J.R.2
  • 12
    • 0017904529 scopus 로고
    • 5-[125I]Iodonaphthyl azide, a reagent to determine the penetration of proteins into the lipid bilayer of biological membranes
    • DOI
    • Bercovici, T. C. Gitler (1978) 5-[125I]Iodonaphthyl azide, a reagent to determine the penetration of proteins into the lipid bilayer of biological membranes. Biochemistry 17 (8 1484 1489. DOI
    • (1978) Biochemistry , vol.17 , Issue.8 , pp. 1484-1489
    • Bercovici, T.1    Gitler, C.2
  • 13
    • 0028285947 scopus 로고
    • Detection of influenza hemagglutinin interaction with biological membranes by photosensitized activation of [125I]iodonaphthylazide
    • Pak, C. C., M. Krumbiegel, R. Blumenthal Y. Raviv (1994) Detection of influenza hemagglutinin interaction with biological membranes by photosensitized activation of [125I]iodonaphthylazide. J. Biol. Chem. 269, 14614 14619.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14614-14619
    • Pak, C.C.1    Krumbiegel, M.2    Blumenthal, R.3    Raviv, Y.4
  • 14
    • 0036057903 scopus 로고    scopus 로고
    • Quantitative measurement of fusion of HIV-1 and SIV with cultured cells using photosensitized labeling
    • DOI
    • Raviv, Y., M. Viard, J. W. Bess Jr. R. Blumenthal (2002) Quantitative measurement of fusion of HIV-1 and SIV with cultured cells using photosensitized labeling. Virology 293 (2 243 251. DOI
    • (2002) Virology , vol.293 , Issue.2 , pp. 243-251
    • Raviv, Y.1    Viard, M.2    Bess Jr., J.W.3    Blumenthal, R.4
  • 15
    • 39649094102 scopus 로고    scopus 로고
    • Photoinduced reactivity of the HIV-1 envelope glycoprotein with a membrane-embedded probe reveals insertion of portions of the HIV-1 gp41 cytoplasmic tail into the viral membrane
    • DOI
    • Viard, M., S. D. Ablan, M. Zhou, T. Veenstra, E. O. Freed, Y. Raviv R. Blumenthal (2008) Photoinduced reactivity of the HIV-1 envelope glycoprotein with a membrane-embedded probe reveals insertion of portions of the HIV-1 gp41 cytoplasmic tail into the viral membrane. Biochemistry 47 (7 1977 1983. DOI
    • (2008) Biochemistry , vol.47 , Issue.7 , pp. 1977-1983
    • Viard, M.1    Ablan, S.D.2    Zhou, M.3    Veenstra, T.4    Freed, E.O.5    Raviv, Y.6    Blumenthal, R.7
  • 18
    • 25144500093 scopus 로고    scopus 로고
    • Inactivation of retroviruses with preservation of structural integrity by targeting the hydrophobic domain of the viral envelope
    • DOI
    • Raviv, Y., M. Viard, J. W. Bess Jr., E. Chertova R. Blumenthal (2005) Inactivation of retroviruses with preservation of structural integrity by targeting the hydrophobic domain of the viral envelope. J. Virol. 79 (19 12394 12400. DOI
    • (2005) J. Virol. , vol.79 , Issue.19 , pp. 12394-12400
    • Raviv, Y.1    Viard, M.2    Bess Jr., J.W.3    Chertova, E.4    Blumenthal, R.5
  • 19
    • 42449113988 scopus 로고    scopus 로고
    • Hydrophobic inactivation of influenza viruses confers preservation of viral structure with enhanced immunogenicity
    • DOI
    • Raviv, Y., R. Blumenthal, S. M. Tompkins, J. Humberd, R. J. Hogan M. Viard (2008) Hydrophobic inactivation of influenza viruses confers preservation of viral structure with enhanced immunogenicity. J. Virol. 82 (9 4612 4619. DOI
    • (2008) J. Virol. , vol.82 , Issue.9 , pp. 4612-4619
    • Raviv, Y.1    Blumenthal, R.2    Tompkins, S.M.3    Humberd, J.4    Hogan, R.J.5    Viard, M.6
  • 20
    • 0036091692 scopus 로고    scopus 로고
    • Envelope glycoprotein incorporation, not shedding of surface envelope glycoprotein (gp120/SU), is the primary determinant of SU content of purified human immunodeficiency virus type i and simian immunodeficiency virus
    • DOI
    • Chertova, E., J. W. Bess Jr., B. J. Crise, R. C. Sowder II., T. M. Schaden, J. M. Hilburn, J. A. Hoxie, R. E. Benveniste, J. D. Lifson, L. E. Henderson L. O. Arthur (2002) Envelope glycoprotein incorporation, not shedding of surface envelope glycoprotein (gp120/SU), is the primary determinant of SU content of purified human immunodeficiency virus type I and simian immunodeficiency virus. J. Virol. 76 (11 5315 5325. DOI
    • (2002) J. Virol. , vol.76 , Issue.11 , pp. 5315-5325
    • Chertova, E.1    Bess Jr., J.W.2    Crise, B.J.3    Sowder II, R.C.4    Schaden, T.M.5    Hilburn, J.M.6    Hoxie, J.A.7    Benveniste, R.E.8    Lifson, J.D.9    Henderson, L.E.10    Arthur, L.O.11
  • 21
    • 0000564433 scopus 로고
    • Models for intramolecular exchange in organic pi-conjugated open-shell systems. A comparison of 1,1-ethenediyl and carbonyl linked bis(arylnitrenes)
    • DOI
    • Ling, C., M. Minato, P. M. Lahti H. Van Willigen (1992) Models for intramolecular exchange in organic pi-conjugated open-shell systems. A comparison of 1,1-ethenediyl and carbonyl linked bis(arylnitrenes). J. Am. Chem. Soc. 114 (25 9959 9969. DOI
    • (1992) J. Am. Chem. Soc. , vol.114 , Issue.25 , pp. 9959-9969
    • Ling, C.1    Minato, M.2    Lahti, P.M.3    Van Willigen, H.4
  • 22
    • 0038070880 scopus 로고
    • The reaction of aryl azides with hydrogen halides
    • Smith, P. A. S. B. B. Brown (1951) The reaction of aryl azides with hydrogen halides. J. Am. Chem. Soc. 73 (6 2438 2441.
    • (1951) J. Am. Chem. Soc. , vol.73 , Issue.6 , pp. 2438-2441
    • Smith, P.A.S.1    Brown, B.B.2
  • 23
    • 0036827702 scopus 로고    scopus 로고
    • Carbon networks based on 1,5-naphthalene units. Synthesis of 1,5-naphthalene nanostructures with extended pi-conjugation
    • DOI
    • Rodriguez, J. G. J. L. Tejedor (2002) Carbon networks based on 1,5-naphthalene units. Synthesis of 1,5-naphthalene nanostructures with extended pi-conjugation. J. Org. Chem. 67, 7631 7640. DOI
    • (2002) J. Org. Chem. , vol.67 , pp. 7631-7640
    • Rodriguez, J.G.1    Tejedor, J.L.2
  • 24
    • 0034255169 scopus 로고    scopus 로고
    • LuSIV cells: A reporter cell line for the detection and quantitation of a single cycle of HIV and SIV replication
    • DOI
    • Roos, J. W., M. F. Maughan, Z. Liao, J. E. K. Hildreth J. E. Clements (2000) LuSIV cells: A reporter cell line for the detection and quantitation of a single cycle of HIV and SIV replication. Virology 273, 307 315. DOI
    • (2000) Virology , vol.273 , pp. 307-315
    • Roos, J.W.1    Maughan, M.F.2    Liao, Z.3    Hildreth, J.E.K.4    Clements, J.E.5
  • 25
    • 0032581364 scopus 로고    scopus 로고
    • The HIV-inactivating protein, Cyanovirin-N, does not block gp120-mediated virus-to-cell binding
    • DOI
    • Mariner, J. M., J. B. McMahon, B. R. O'Keefe, K. Nagashima M. R. Boyd (1998) The HIV-inactivating protein, Cyanovirin-N, does not block gp120-mediated virus-to-cell binding. Biochem. Biophys. Res. Commun. 248, 841 845. DOI
    • (1998) Biochem. Biophys. Res. Commun. , vol.248 , pp. 841-845
    • Mariner, J.M.1    McMahon, J.B.2    O'Keefe, B.R.3    Nagashima, K.4    Boyd, M.R.5
  • 26
    • 0035400403 scopus 로고    scopus 로고
    • A virus binding assay for studying the antigenic landscape on intact, native, primary human immunodeficiency virus-type 1
    • DOI
    • Nyambi, P. N., S. Burda, L. Bastiani C. Williams (2001) A virus binding assay for studying the antigenic landscape on intact, native, primary human immunodeficiency virus-type 1. J. Immunol. Methods 253, 253 262. DOI
    • (2001) J. Immunol. Methods , vol.253 , pp. 253-262
    • Nyambi, P.N.1    Burda, S.2    Bastiani, L.3    Williams, C.4
  • 27
    • 0030889782 scopus 로고    scopus 로고
    • 5-Iodonaphthyl-1-azide labeling of plasma membrane proteins adjacent to specific sites via energy transfer
    • DOI
    • Meiklejohn, B. I., N. A. Rahman, D. A. Roess B. G. Barisas (1997) 5-Iodonaphthyl-1-azide labeling of plasma membrane proteins adjacent to specific sites via energy transfer. Biochim. Biophys. Acta 1324, 320 332. DOI
    • (1997) Biochim. Biophys. Acta , vol.1324 , pp. 320-332
    • Meiklejohn, B.I.1    Rahman, N.A.2    Roess, D.A.3    Barisas, B.G.4
  • 28
    • 0031592573 scopus 로고    scopus 로고
    • Microvesicles are a source of contaminating cellular proteins found in purified HIV-1 preparations
    • DOI
    • Bess, J. W. Jr., R. J. Gorelick, W. J. Bosche, L. E. Henderson L. O. Arthur (1997) Microvesicles are a source of contaminating cellular proteins found in purified HIV-1 preparations. Virology 230 (1 134 144. DOI
    • (1997) Virology , vol.230 , Issue.1 , pp. 134-144
    • Bess Jr., J.W.1    Gorelick, R.J.2    Bosche, W.J.3    Henderson, L.E.4    Arthur, L.O.5
  • 29
    • 70350319089 scopus 로고    scopus 로고
    • Truncation of the membrane-spanning domain of human immunodeficiency virus type 1 envelope glycoprotein defines elements required for fusion, incorporation, and infectivity
    • DOI
    • Yue, L., L. Shang E. Hunter (2009) Truncation of the membrane-spanning domain of human immunodeficiency virus type 1 envelope glycoprotein defines elements required for fusion, incorporation, and infectivity. J. Virol. 83 (22 11588 11598. DOI
    • (2009) J. Virol. , vol.83 , Issue.22 , pp. 11588-11598
    • Yue, L.1    Shang, L.2    Hunter, E.3
  • 30
    • 0028179011 scopus 로고
    • Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion
    • DOI
    • Kemble, G. W., T. Danieli J. M. White (1994) Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion. Cell 76 (2 383 391. DOI
    • (1994) Cell , vol.76 , Issue.2 , pp. 383-391
    • Kemble, G.W.1    Danieli, T.2    White, J.M.3
  • 31
    • 0345828873 scopus 로고    scopus 로고
    • The rearrangements of naphthylnitrenes: UV/Vis and IR spectra of azirines, cyclic ketenimines, and cyclic nitrile ylides
    • DOI
    • Maltsev, A., T. Bally, M.-L. Tsao, M. S. Platz, A. Kuhn, M. Vosswinkel C. Wentrup (2004) The rearrangements of naphthylnitrenes: UV/Vis and IR spectra of azirines, cyclic ketenimines, and cyclic nitrile ylides. J. Am. Chem. Soc. 126, 237 249. DOI
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 237-249
    • Maltsev, A.1    Bally, T.2    Tsao, M.-L.3    Platz, M.S.4    Kuhn, A.5    Vosswinkel, M.6    Wentrup, C.7
  • 32
    • 35448961737 scopus 로고    scopus 로고
    • Kinetics and spectroscopy of substituted phenylnitrenes
    • DOI
    • Gritsan, N. P. M. S. Platz (2001) Kinetics and spectroscopy of substituted phenylnitrenes. Adv. Phys. Org. Chem. 36, 255 304. DOI
    • (2001) Adv. Phys. Org. Chem. , vol.36 , pp. 255-304
    • Gritsan, N.P.1    Platz, M.S.2
  • 33
    • 0017089931 scopus 로고
    • Photoactivated cross-linking of proteins within the erythrocyte membrane core
    • Mikkelson, R. B. D. F. H. Wallach (1976) Photoactivated cross-linking of proteins within the erythrocyte membrane core. J. Biol. Chem. 251 (23 7413 7416.
    • (1976) J. Biol. Chem. , vol.251 , Issue.23 , pp. 7413-7416
    • Mikkelson, R.B.1    Wallach, D.F.H.2
  • 34
    • 59849087132 scopus 로고    scopus 로고
    • Variation in the cross-linking pattern of porcine myofibrillar protein exposed to three oxidative environments
    • DOI
    • Xiong, Y. L., D. Park T. Ooizumi (2009) Variation in the cross-linking pattern of porcine myofibrillar protein exposed to three oxidative environments. J. Agric. Food. Chem. 57, 153 159. DOI
    • (2009) J. Agric. Food. Chem. , vol.57 , pp. 153-159
    • Xiong, Y.L.1    Park, D.2    Ooizumi, T.3
  • 35
    • 0025096219 scopus 로고
    • Conference Reports: Workshop on HIV inactivated vaccines
    • Schultz, A. M., C. W. Koff D. N. Lawrence (1990) Conference Reports: Workshop on HIV inactivated vaccines. Vaccine 8, 516 517.
    • (1990) Vaccine , vol.8 , pp. 516-517
    • Schultz, A.M.1    Koff, C.W.2    Lawrence, D.N.3
  • 36
    • 33744783359 scopus 로고    scopus 로고
    • In vivo experimentation with Simian Herpesviruses: Assessment of biosafety and molecular contamination
    • Ritchey, J. W., D. H. Black, K. M. Rogers R. Eberle (2006) In vivo experimentation with Simian Herpesviruses: Assessment of biosafety and molecular contamination. J. Am. Assoc. Lab. Anim. Sci. 45 (2 7 12.
    • (2006) J. Am. Assoc. Lab. Anim. Sci. , vol.45 , Issue.2 , pp. 7-12
    • Ritchey, J.W.1    Black, D.H.2    Rogers, K.M.3    Eberle, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.