메뉴 건너뛰기




Volumn 124, Issue 1-2, 2007, Pages 103-112

Role of envelope processing and gp41 membrane spanning domain in the formation of human immunodeficiency virus type 1 (HIV-1) fusion-competent envelope glycoprotein complex

Author keywords

Envelope glycoproteins; Envelope processing; Envelope trimer; gp41; gp41 membrane spanning domain; HIV; Viral fusion

Indexed keywords

GLYCOPROTEIN GP 41; INFLUENZA VIRUS HEMAGGLUTININ; ISOLEUCINE; MEMBRANE PROTEIN;

EID: 33846861789     PISSN: 01681702     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.virusres.2006.10.009     Document Type: Article
Times cited : (15)

References (52)
  • 1
    • 0037134497 scopus 로고    scopus 로고
    • Design of a novel peptide inhibitor of HIV fusion that disrupts the internal trimeric coiled-coil of gp41
    • Bewley C.A., Louis J.M., Ghirlando R., and Clore G.M. Design of a novel peptide inhibitor of HIV fusion that disrupts the internal trimeric coiled-coil of gp41. J. Biol. Chem. 277 16 (2002) 14238-14245
    • (2002) J. Biol. Chem. , vol.277 , Issue.16 , pp. 14238-14245
    • Bewley, C.A.1    Louis, J.M.2    Ghirlando, R.3    Clore, G.M.4
  • 2
    • 0036844376 scopus 로고    scopus 로고
    • A sensitive and specific enzyme-based assay detecting HIV-1 virion fusion in primary T lymphocytes
    • Cavrois M., De Noronha C., and Greene W.C. A sensitive and specific enzyme-based assay detecting HIV-1 virion fusion in primary T lymphocytes. Nat. Biotechnol. 20 11 (2002) 1151-1154
    • (2002) Nat. Biotechnol. , vol.20 , Issue.11 , pp. 1151-1154
    • Cavrois, M.1    De Noronha, C.2    Greene, W.C.3
  • 3
    • 0032433685 scopus 로고    scopus 로고
    • Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug target
    • Chan D.C., Chutkowski C.T., and Kim P.S. Evidence that a prominent cavity in the coiled coil of HIV type 1 gp41 is an attractive drug target. Proc. Natl. Acad. Sci. U.S.A. 95 26 (1998) 15613-15617
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , Issue.26 , pp. 15613-15617
    • Chan, D.C.1    Chutkowski, C.T.2    Kim, P.S.3
  • 4
    • 0032577550 scopus 로고    scopus 로고
    • HIV entry and its inhibition
    • Chan D.C., and Kim P.S. HIV entry and its inhibition. Cell 93 5 (1998) 681-684
    • (1998) Cell , vol.93 , Issue.5 , pp. 681-684
    • Chan, D.C.1    Kim, P.S.2
  • 5
    • 0032584146 scopus 로고    scopus 로고
    • The transmembrane domain in viral fusion: essential role for a conserved glycine residue in vesicular stomatitis virus G protein
    • Cleverley D.Z., and Lenard J. The transmembrane domain in viral fusion: essential role for a conserved glycine residue in vesicular stomatitis virus G protein. Proc. Natl. Acad. Sci. U.S.A. 95 7 (1998) 3425-3430
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , Issue.7 , pp. 3425-3430
    • Cleverley, D.Z.1    Lenard, J.2
  • 7
    • 0037381269 scopus 로고    scopus 로고
    • The structural biology of type I viral membrane fusion
    • Colman P.M., and Lawrence M.C. The structural biology of type I viral membrane fusion. Nat. Rev. Mol. Cell. Biol. 4 4 (2003) 309-319
    • (2003) Nat. Rev. Mol. Cell. Biol. , vol.4 , Issue.4 , pp. 309-319
    • Colman, P.M.1    Lawrence, M.C.2
  • 8
    • 0028362008 scopus 로고
    • The convertases furin and PC1 can both cleave the human immunodeficiency virus (HIV)-1 envelope glycoprotein gp160 into gp120 (HIV-1 SU) and gp41 (HIV-I TM)
    • Decroly E., Vandenbranden M., Ruysschaert J.M., Cogniaux J., Jacob G.S., Howard S.C., Marshall G., Kompelli A., Basak A., Jean F., et al. The convertases furin and PC1 can both cleave the human immunodeficiency virus (HIV)-1 envelope glycoprotein gp160 into gp120 (HIV-1 SU) and gp41 (HIV-I TM). J. Biol. Chem. 269 16 (1994) 12240-12247
    • (1994) J. Biol. Chem. , vol.269 , Issue.16 , pp. 12240-12247
    • Decroly, E.1    Vandenbranden, M.2    Ruysschaert, J.M.3    Cogniaux, J.4    Jacob, G.S.5    Howard, S.C.6    Marshall, G.7    Kompelli, A.8    Basak, A.9    Jean, F.10
  • 9
    • 0027157736 scopus 로고
    • Folding and assembly of viral membrane proteins
    • Doms R.W., Lamb R.A., Rose J.K., and Helenius A. Folding and assembly of viral membrane proteins. Virology 193 2 (1993) 545-562
    • (1993) Virology , vol.193 , Issue.2 , pp. 545-562
    • Doms, R.W.1    Lamb, R.A.2    Rose, J.K.3    Helenius, A.4
  • 10
    • 0027979135 scopus 로고
    • Role of the matrix protein in the virion association of the human immunodeficiency virus type 1 envelope glycoprotein
    • Dorfman T., Mammano F., Haseltine W.A., and Gottlinger H.G. Role of the matrix protein in the virion association of the human immunodeficiency virus type 1 envelope glycoprotein. J. Virol. 68 3 (1994) 1689-1696
    • (1994) J. Virol. , vol.68 , Issue.3 , pp. 1689-1696
    • Dorfman, T.1    Mammano, F.2    Haseltine, W.A.3    Gottlinger, H.G.4
  • 11
    • 0029015314 scopus 로고
    • Analysis of the cleavage site of the human immunodeficiency virus type 1 glycoprotein: requirement of precursor cleavage for glycoprotein incorporation
    • Dubay J.W., Dubay S.R., Shin H.J., and Hunter E. Analysis of the cleavage site of the human immunodeficiency virus type 1 glycoprotein: requirement of precursor cleavage for glycoprotein incorporation. J. Virol. 69 8 (1995) 4675-4682
    • (1995) J. Virol. , vol.69 , Issue.8 , pp. 4675-4682
    • Dubay, J.W.1    Dubay, S.R.2    Shin, H.J.3    Hunter, E.4
  • 12
    • 0026029621 scopus 로고
    • Folding, interaction with GRP78-BiP, assembly, and transport of the human immunodeficiency virus type 1 envelope protein
    • Earl P.L., Moss B., and Doms R.W. Folding, interaction with GRP78-BiP, assembly, and transport of the human immunodeficiency virus type 1 envelope protein. J. Virol. 65 4 (1991) 2047-2055
    • (1991) J. Virol. , vol.65 , Issue.4 , pp. 2047-2055
    • Earl, P.L.1    Moss, B.2    Doms, R.W.3
  • 13
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • Eckert D.M., and Kim P.S. Mechanisms of viral membrane fusion and its inhibition. Annu. Rev. Biochem. 70 (2001) 777-810
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 14
    • 0024237306 scopus 로고
    • Brefeldin A causes disassembly of the Golgi complex and accumulation of secretory proteins in the endoplasmic reticulum
    • Fujiwara T., Oda K., Yokota S., Takatsuki A., and Ikehara Y. Brefeldin A causes disassembly of the Golgi complex and accumulation of secretory proteins in the endoplasmic reticulum. J. Biol. Chem. 263 34 (1988) 18545-18552
    • (1988) J. Biol. Chem. , vol.263 , Issue.34 , pp. 18545-18552
    • Fujiwara, T.1    Oda, K.2    Yokota, S.3    Takatsuki, A.4    Ikehara, Y.5
  • 15
    • 0031959601 scopus 로고    scopus 로고
    • Capture of an early fusion-active conformation of HIV-1 gp41
    • Furuta R.A., Wild C.T., Weng Y., and Weiss C.D. Capture of an early fusion-active conformation of HIV-1 gp41. Nat. Struct. Biol. 5 4 (1998) 276-279
    • (1998) Nat. Struct. Biol. , vol.5 , Issue.4 , pp. 276-279
    • Furuta, R.A.1    Wild, C.T.2    Weng, Y.3    Weiss, C.D.4
  • 16
    • 0026755725 scopus 로고
    • Effects of deletions in the cytoplasmic domain on biological functions of human immunodeficiency virus type 1 envelope glycoproteins
    • Gabuzda D.H., Lever A., Terwilliger E., and Sodroski J. Effects of deletions in the cytoplasmic domain on biological functions of human immunodeficiency virus type 1 envelope glycoproteins. J. Virol. 66 6 (1992) 3306-3315
    • (1992) J. Virol. , vol.66 , Issue.6 , pp. 3306-3315
    • Gabuzda, D.H.1    Lever, A.2    Terwilliger, E.3    Sodroski, J.4
  • 17
    • 3042615492 scopus 로고    scopus 로고
    • Temperature-dependent intermediates in HIV-1 envelope glycoprotein-mediated fusion revealed by inhibitors that target N- and C-terminal helical regions of HIV-1 gp41
    • Gallo S.A., Clore G.M., Louis J.M., Bewley C.A., and Blumenthal R. Temperature-dependent intermediates in HIV-1 envelope glycoprotein-mediated fusion revealed by inhibitors that target N- and C-terminal helical regions of HIV-1 gp41. Biochemistry 43 25 (2004) 8230-8233
    • (2004) Biochemistry , vol.43 , Issue.25 , pp. 8230-8233
    • Gallo, S.A.1    Clore, G.M.2    Louis, J.M.3    Bewley, C.A.4    Blumenthal, R.5
  • 18
    • 33745833942 scopus 로고    scopus 로고
    • Dominant-negative effect of hetero-oligomerization on the function of the human immunodeficiency virus type 1 envelope glycoprotein complex
    • Herrera C., Klasse P.J., Kibler C.W., Michael E., Moore J.P., and Beddows S. Dominant-negative effect of hetero-oligomerization on the function of the human immunodeficiency virus type 1 envelope glycoprotein complex. Virology 351 1 (2006) 121-132
    • (2006) Virology , vol.351 , Issue.1 , pp. 121-132
    • Herrera, C.1    Klasse, P.J.2    Kibler, C.W.3    Michael, E.4    Moore, J.P.5    Beddows, S.6
  • 19
    • 20644433322 scopus 로고    scopus 로고
    • The impact of envelope glycoprotein cleavage on the antigenicity, infectivity, and neutralization sensitivity of Env-pseudotyped human immunodeficiency virus type 1 particles
    • Herrera C., Klasse P.J., Michael E., Kake S., Barnes K., Kibler C.W., Campbell-Gardener L., Si Z., Sodroski J., Moore J.P., and Beddows S. The impact of envelope glycoprotein cleavage on the antigenicity, infectivity, and neutralization sensitivity of Env-pseudotyped human immunodeficiency virus type 1 particles. Virology 338 1 (2005) 154-172
    • (2005) Virology , vol.338 , Issue.1 , pp. 154-172
    • Herrera, C.1    Klasse, P.J.2    Michael, E.3    Kake, S.4    Barnes, K.5    Kibler, C.W.6    Campbell-Gardener, L.7    Si, Z.8    Sodroski, J.9    Moore, J.P.10    Beddows, S.11
  • 20
    • 0035919637 scopus 로고    scopus 로고
    • Analysis of dominant-negative effects of mutant Env proteins of human immunodeficiency virus type 1
    • Iwatani Y., Kawano K., Ueno T., Tanaka M., Ishimoto A., Ito M., and Sakai H. Analysis of dominant-negative effects of mutant Env proteins of human immunodeficiency virus type 1. Virology 286 1 (2001) 45-53
    • (2001) Virology , vol.286 , Issue.1 , pp. 45-53
    • Iwatani, Y.1    Kawano, K.2    Ueno, T.3    Tanaka, M.4    Ishimoto, A.5    Ito, M.6    Sakai, H.7
  • 21
    • 22844441184 scopus 로고    scopus 로고
    • Alanine scanning mutants of the HIV gp41 loop
    • Jacobs A., Sen J., Rong L., and Caffrey M. Alanine scanning mutants of the HIV gp41 loop. J. Biol. Chem. 280 29 (2005) 27284-27288
    • (2005) J. Biol. Chem. , vol.280 , Issue.29 , pp. 27284-27288
    • Jacobs, A.1    Sen, J.2    Rong, L.3    Caffrey, M.4
  • 22
    • 0028179011 scopus 로고
    • Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion
    • Kemble G.W., Danieli T., and White J.M. Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion. Cell 76 2 (1994) 383-391
    • (1994) Cell , vol.76 , Issue.2 , pp. 383-391
    • Kemble, G.W.1    Danieli, T.2    White, J.M.3
  • 23
    • 0026562720 scopus 로고
    • Detection of replication-competent and pseudotyped human immunodeficiency virus with a sensitive cell line on the basis of activation of an integrated beta-galactosidase gene
    • Kimpton J., and Emerman M. Detection of replication-competent and pseudotyped human immunodeficiency virus with a sensitive cell line on the basis of activation of an integrated beta-galactosidase gene. J. Virol. 66 4 (1992) 2232-2239
    • (1992) J. Virol. , vol.66 , Issue.4 , pp. 2232-2239
    • Kimpton, J.1    Emerman, M.2
  • 24
    • 18144375202 scopus 로고    scopus 로고
    • Amino acid 36 in the human immunodeficiency virus type 1 gp41 ectodomain controls fusogenic activity: implications for the molecular mechanism of viral escape from a fusion inhibitor
    • Kinomoto M., Yokoyama M., Sato H., Kojima A., Kurata T., Ikuta K., Sata T., and Tokunaga K. Amino acid 36 in the human immunodeficiency virus type 1 gp41 ectodomain controls fusogenic activity: implications for the molecular mechanism of viral escape from a fusion inhibitor. J. Virol. 79 10 (2005) 5996-6004
    • (2005) J. Virol. , vol.79 , Issue.10 , pp. 5996-6004
    • Kinomoto, M.1    Yokoyama, M.2    Sato, H.3    Kojima, A.4    Kurata, T.5    Ikuta, K.6    Sata, T.7    Tokunaga, K.8
  • 25
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte J., and Doolittle R.F. A simple method for displaying the hydropathic character of a protein. J. Mol. Biol. 157 1 (1982) 105-132
    • (1982) J. Mol. Biol. , vol.157 , Issue.1 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 26
    • 0042346262 scopus 로고    scopus 로고
    • Vpu exerts a positive effect on HIV-1 infectivity by down-modulating CD4 receptor molecules at the surface of HIV-1-producing cells
    • Levesque K., Zhao Y.S., and Cohen E.A. Vpu exerts a positive effect on HIV-1 infectivity by down-modulating CD4 receptor molecules at the surface of HIV-1-producing cells. J. Biol. Chem. 278 30 (2003) 28346-28353
    • (2003) J. Biol. Chem. , vol.278 , Issue.30 , pp. 28346-28353
    • Levesque, K.1    Zhao, Y.S.2    Cohen, E.A.3
  • 27
    • 0032514155 scopus 로고    scopus 로고
    • Mutations in the middle of the transmembrane domain reverse the polarity of transport of the influenza virus hemagglutinin in MDCK epithelial cells
    • Lin S., Naim H.Y., Rodriguez A.C., and Roth M.G. Mutations in the middle of the transmembrane domain reverse the polarity of transport of the influenza virus hemagglutinin in MDCK epithelial cells. J. Cell. Biol. 142 1 (1998) 51-57
    • (1998) J. Cell. Biol. , vol.142 , Issue.1 , pp. 51-57
    • Lin, S.1    Naim, H.Y.2    Rodriguez, A.C.3    Roth, M.G.4
  • 28
    • 0035814911 scopus 로고    scopus 로고
    • Structural and functional analysis of the HIV gp41 core containing an Ile573 to Thr substitution: implications for membrane fusion
    • Liu J., Shu W., Fagan M.B., Nunberg J.H., and Lu M. Structural and functional analysis of the HIV gp41 core containing an Ile573 to Thr substitution: implications for membrane fusion. Biochemistry 40 9 (2001) 2797-2807
    • (2001) Biochemistry , vol.40 , Issue.9 , pp. 2797-2807
    • Liu, J.1    Shu, W.2    Fagan, M.B.3    Nunberg, J.H.4    Lu, M.5
  • 29
    • 0028229632 scopus 로고
    • The intracytoplasmic domain of gp41 mediates polarized budding of human immunodeficiency virus type 1 in MDCK cells
    • Lodge R., Gottlinger H., Gabuzda D., Cohen E.A., and Lemay G. The intracytoplasmic domain of gp41 mediates polarized budding of human immunodeficiency virus type 1 in MDCK cells. J. Virol. 68 8 (1994) 4857-4861
    • (1994) J. Virol. , vol.68 , Issue.8 , pp. 4857-4861
    • Lodge, R.1    Gottlinger, H.2    Gabuzda, D.3    Cohen, E.A.4    Lemay, G.5
  • 30
    • 0031039756 scopus 로고    scopus 로고
    • The membrane-proximal intracytoplasmic tyrosine residue of HIV-1 envelope glycoprotein is critical for basolateral targeting of viral budding in MDCK cells
    • Lodge R., Lalonde J.P., Lemay G., and Cohen E.A. The membrane-proximal intracytoplasmic tyrosine residue of HIV-1 envelope glycoprotein is critical for basolateral targeting of viral budding in MDCK cells. EMBO J. 16 4 (1997) 695-705
    • (1997) EMBO J. , vol.16 , Issue.4 , pp. 695-705
    • Lodge, R.1    Lalonde, J.P.2    Lemay, G.3    Cohen, E.A.4
  • 31
    • 0034759947 scopus 로고    scopus 로고
    • Structural and functional analysis of interhelical interactions in the human immunodeficiency virus type 1 gp41 envelope glycoprotein by alanine-scanning mutagenesis
    • Lu M., Stoller M.O., Wang S., Liu J., Fagan M.B., and Nunberg J.H. Structural and functional analysis of interhelical interactions in the human immunodeficiency virus type 1 gp41 envelope glycoprotein by alanine-scanning mutagenesis. J. Virol. 75 22 (2001) 11146-11156
    • (2001) J. Virol. , vol.75 , Issue.22 , pp. 11146-11156
    • Lu, M.1    Stoller, M.O.2    Wang, S.3    Liu, J.4    Fagan, M.B.5    Nunberg, J.H.6
  • 32
    • 0033730718 scopus 로고    scopus 로고
    • A point mutation in the transmembrane domain of the hemagglutinin of influenza virus stabilizes a hemifusion intermediate that can transit to fusion
    • Melikyan G.B., Markosyan R.M., Roth M.G., and Cohen F.S. A point mutation in the transmembrane domain of the hemagglutinin of influenza virus stabilizes a hemifusion intermediate that can transit to fusion. Mol. Biol. Cell. 11 11 (2000) 3765-3775
    • (2000) Mol. Biol. Cell. , vol.11 , Issue.11 , pp. 3765-3775
    • Melikyan, G.B.1    Markosyan, R.M.2    Roth, M.G.3    Cohen, F.S.4
  • 33
    • 0028865392 scopus 로고
    • GPI-anchored influenza hemagglutinin induces hemifusion to both red blood cell and planar bilayer membranes
    • Melikyan G.B., White J.M., and Cohen F.S. GPI-anchored influenza hemagglutinin induces hemifusion to both red blood cell and planar bilayer membranes. J. Cell. Biol. 131 3 (1995) 679-691
    • (1995) J. Cell. Biol. , vol.131 , Issue.3 , pp. 679-691
    • Melikyan, G.B.1    White, J.M.2    Cohen, F.S.3
  • 34
    • 16244410802 scopus 로고    scopus 로고
    • Role of the specific amino acid sequence of the membrane-spanning domain of human immunodeficiency virus type 1 in membrane fusion
    • Miyauchi K., Komano J., Yokomaku Y., Sugiura W., Yamamoto N., and Matsuda Z. Role of the specific amino acid sequence of the membrane-spanning domain of human immunodeficiency virus type 1 in membrane fusion. J. Virol. 79 8 (2005) 4720-4729
    • (2005) J. Virol. , vol.79 , Issue.8 , pp. 4720-4729
    • Miyauchi, K.1    Komano, J.2    Yokomaku, Y.3    Sugiura, W.4    Yamamoto, N.5    Matsuda, Z.6
  • 35
    • 0030874794 scopus 로고    scopus 로고
    • Influence of membrane anchoring and cytoplasmic domains on the fusogenic activity of vesicular stomatitis virus glycoprotein G
    • Odell D., Wanas E., Yan J., and Ghosh H.P. Influence of membrane anchoring and cytoplasmic domains on the fusogenic activity of vesicular stomatitis virus glycoprotein G. J. Virol. 71 10 (1997) 7996-8000
    • (1997) J. Virol. , vol.71 , Issue.10 , pp. 7996-8000
    • Odell, D.1    Wanas, E.2    Yan, J.3    Ghosh, H.P.4
  • 36
    • 0028180109 scopus 로고
    • Uncoupled expression of Moloney murine leukemia virus envelope polypeptides SU and TM: a functional analysis of the role of TM domains in viral entry
    • Ragheb J.A., and Anderson W.F. Uncoupled expression of Moloney murine leukemia virus envelope polypeptides SU and TM: a functional analysis of the role of TM domains in viral entry. J. Virol. 68 5 (1994) 3207-3219
    • (1994) J. Virol. , vol.68 , Issue.5 , pp. 3207-3219
    • Ragheb, J.A.1    Anderson, W.F.2
  • 37
    • 0033749617 scopus 로고    scopus 로고
    • Cooperative subunit interactions within the oligomeric envelope glycoprotein of HIV-1: functional complementation of specific defects in gp120 and gp41
    • Salzwedel K., and Berger E.A. Cooperative subunit interactions within the oligomeric envelope glycoprotein of HIV-1: functional complementation of specific defects in gp120 and gp41. Proc. Natl. Acad. Sci. U.S.A. 97 23 (2000) 12794-12799
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , Issue.23 , pp. 12794-12799
    • Salzwedel, K.1    Berger, E.A.2
  • 38
    • 0027249613 scopus 로고
    • Expression and characterization of glycophospholipid-anchored human immunodeficiency virus type 1 envelope glycoproteins
    • Salzwedel K., Johnston P.B., Roberts S.J., Dubay J.W., and Hunter E. Expression and characterization of glycophospholipid-anchored human immunodeficiency virus type 1 envelope glycoproteins. J. Virol. 67 9 (1993) 5279-5288
    • (1993) J. Virol. , vol.67 , Issue.9 , pp. 5279-5288
    • Salzwedel, K.1    Johnston, P.B.2    Roberts, S.J.3    Dubay, J.W.4    Hunter, E.5
  • 39
    • 0034443994 scopus 로고    scopus 로고
    • The role of the transmembrane and of the intraviral domain of glycoproteins in membrane fusion of enveloped viruses
    • Schroth-Diez B., Ludwig K., Baljinnyam B., Kozerski C., Huang Q., and Herrmann A. The role of the transmembrane and of the intraviral domain of glycoproteins in membrane fusion of enveloped viruses. Biosci. Rep. 20 6 (2000) 571-595
    • (2000) Biosci. Rep. , vol.20 , Issue.6 , pp. 571-595
    • Schroth-Diez, B.1    Ludwig, K.2    Baljinnyam, B.3    Kozerski, C.4    Huang, Q.5    Herrmann, A.6
  • 41
    • 0141744628 scopus 로고    scopus 로고
    • Nef does not affect the efficiency of human immunodeficiency virus type 1 fusion with target cells
    • Tobiume M., Lineberger J.E., Lundquist C.A., Miller M.D., and Aiken C. Nef does not affect the efficiency of human immunodeficiency virus type 1 fusion with target cells. J. Virol. 77 19 (2003) 10645-10650
    • (2003) J. Virol. , vol.77 , Issue.19 , pp. 10645-10650
    • Tobiume, M.1    Lineberger, J.E.2    Lundquist, C.A.3    Miller, M.D.4    Aiken, C.5
  • 42
    • 0035795721 scopus 로고    scopus 로고
    • Amino acid distributions in integral membrane protein structures
    • Ulmschneider M.B., and Sansom M.S. Amino acid distributions in integral membrane protein structures. Biochim. Biophys. Acta 1512 1 (2001) 1-14
    • (2001) Biochim. Biophys. Acta , vol.1512 , Issue.1 , pp. 1-14
    • Ulmschneider, M.B.1    Sansom, M.S.2
  • 43
    • 0028861290 scopus 로고
    • Megaprimer method for in vitro mutagenesis using parallel templates
    • 32
    • Upender M., Raj L., and Weir M. Megaprimer method for in vitro mutagenesis using parallel templates. Biotechniques 18 1 (1995) 29-30 32
    • (1995) Biotechniques , vol.18 , Issue.1 , pp. 29-30
    • Upender, M.1    Raj, L.2    Weir, M.3
  • 44
    • 0037062578 scopus 로고    scopus 로고
    • Interhelical interactions in the gp41 core: implications for activation of HIV-1 membrane fusion
    • Wang S., York J., Shu W., Stoller M.O., Nunberg J.H., and Lu M. Interhelical interactions in the gp41 core: implications for activation of HIV-1 membrane fusion. Biochemistry 41 23 (2002) 7283-7292
    • (2002) Biochemistry , vol.41 , Issue.23 , pp. 7283-7292
    • Wang, S.1    York, J.2    Shu, W.3    Stoller, M.O.4    Nunberg, J.H.5    Lu, M.6
  • 45
    • 0027483786 scopus 로고
    • Characterization of stable Chinese hamster ovary cells expressing wild-type, secreted, and glycosylphosphatidylinositol-anchored human immunodeficiency virus type 1 envelope glycoprotein
    • Weiss C.D., and White J.M. Characterization of stable Chinese hamster ovary cells expressing wild-type, secreted, and glycosylphosphatidylinositol-anchored human immunodeficiency virus type 1 envelope glycoprotein. J. Virol. 67 12 (1993) 7060-7066
    • (1993) J. Virol. , vol.67 , Issue.12 , pp. 7060-7066
    • Weiss, C.D.1    White, J.M.2
  • 46
    • 0031798443 scopus 로고    scopus 로고
    • Mutational analysis of residues in the coiled-coil domain of human immunodeficiency virus type 1 transmembrane protein gp41
    • Weng Y., and Weiss C.D. Mutational analysis of residues in the coiled-coil domain of human immunodeficiency virus type 1 transmembrane protein gp41. J. Virol. 72 12 (1998) 9676-9682
    • (1998) J. Virol. , vol.72 , Issue.12 , pp. 9676-9682
    • Weng, Y.1    Weiss, C.D.2
  • 47
    • 0027692502 scopus 로고
    • A synthetic peptide from HIV-1 gp41 is a potent inhibitor of virus-mediated cell-cell fusion
    • Wild C., Greenwell T., and Matthews T. A synthetic peptide from HIV-1 gp41 is a potent inhibitor of virus-mediated cell-cell fusion. AIDS Res. Hum. Retroviruses 9 11 (1993) 1051-1053
    • (1993) AIDS Res. Hum. Retroviruses , vol.9 , Issue.11 , pp. 1051-1053
    • Wild, C.1    Greenwell, T.2    Matthews, T.3
  • 48
    • 0026465468 scopus 로고
    • A synthetic peptide inhibitor of human immunodeficiency virus replication: correlation between solution structure and viral inhibition
    • Wild C., Oas T., McDanal C., Bolognesi D., and Matthews T. A synthetic peptide inhibitor of human immunodeficiency virus replication: correlation between solution structure and viral inhibition. Proc. Natl. Acad. Sci. U.S.A. 89 21 (1992) 10537-10541
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , Issue.21 , pp. 10537-10541
    • Wild, C.1    Oas, T.2    McDanal, C.3    Bolognesi, D.4    Matthews, T.5
  • 49
    • 0029998948 scopus 로고    scopus 로고
    • Glycoprotein incorporation and HIV-1 infectivity despite exchange of the gp160 membrane-spanning domain
    • Wilk T., Pfeiffer T., Bukovsky A., Moldenhauer G., and Bosch V. Glycoprotein incorporation and HIV-1 infectivity despite exchange of the gp160 membrane-spanning domain. Virology 218 1 (1996) 269-274
    • (1996) Virology , vol.218 , Issue.1 , pp. 269-274
    • Wilk, T.1    Pfeiffer, T.2    Bukovsky, A.3    Moldenhauer, G.4    Bosch, V.5
  • 50
    • 0032546844 scopus 로고    scopus 로고
    • The HIV-1 envelope glycoproteins: fusogens, antigens, and immunogens
    • Wyatt R., and Sodroski J. The HIV-1 envelope glycoproteins: fusogens, antigens, and immunogens. Science 280 5371 (1998) 1884-1888
    • (1998) Science , vol.280 , Issue.5371 , pp. 1884-1888
    • Wyatt, R.1    Sodroski, J.2
  • 51
    • 0029044110 scopus 로고
    • Degradation of CD4 induced by human immunodeficiency virus type 1 Vpu protein: a predicted alpha-helix structure in the proximal cytoplasmic region of CD4 contributes to Vpu sensitivity
    • Yao X.J., Friborg J., Checroune F., Gratton S., Boisvert F., Sekaly R.P., and Cohen E.A. Degradation of CD4 induced by human immunodeficiency virus type 1 Vpu protein: a predicted alpha-helix structure in the proximal cytoplasmic region of CD4 contributes to Vpu sensitivity. Virology 209 2 (1995) 615-623
    • (1995) Virology , vol.209 , Issue.2 , pp. 615-623
    • Yao, X.J.1    Friborg, J.2    Checroune, F.3    Gratton, S.4    Boisvert, F.5    Sekaly, R.P.6    Cohen, E.A.7
  • 52
    • 0026715929 scopus 로고
    • Envelope glycoprotein and CD4 independence of vpu-facilitated human immunodeficiency virus type 1 capsid export
    • Yao X.J., Gottlinger H., Haseltine W.A., and Cohen E.A. Envelope glycoprotein and CD4 independence of vpu-facilitated human immunodeficiency virus type 1 capsid export. J. Virol. 66 8 (1992) 5119-5126
    • (1992) J. Virol. , vol.66 , Issue.8 , pp. 5119-5126
    • Yao, X.J.1    Gottlinger, H.2    Haseltine, W.A.3    Cohen, E.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.