메뉴 건너뛰기




Volumn 5, Issue , 2012, Pages 290-311

Mechanisms of enveloped virus entry by membrane fusion

Author keywords

[No Author keywords available]

Indexed keywords

CELL MEMBRANES; CYTOLOGY; LIPID BILAYERS; MERGING; VIRUSES;

EID: 84882741550     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-374920-8.00524-5     Document Type: Chapter
Times cited : (2)

References (294)
  • 1
    • 0032431055 scopus 로고    scopus 로고
    • Coiled coils in both intracellular vesicle and viral membrane fusion
    • Skehel J.J., Wiley D.C. Coiled coils in both intracellular vesicle and viral membrane fusion. Cell 1998, 95(7):871-874.
    • (1998) Cell , vol.95 , Issue.7 , pp. 871-874
    • Skehel, J.J.1    Wiley, D.C.2
  • 3
    • 0032577550 scopus 로고    scopus 로고
    • HIV entry and its inhibition
    • Chan D.C., Kim P.S. HIV entry and its inhibition. Cell 1998, 93(5):681-684.
    • (1998) Cell , vol.93 , Issue.5 , pp. 681-684
    • Chan, D.C.1    Kim, P.S.2
  • 4
    • 34548824835 scopus 로고    scopus 로고
    • Structural basis of viral invasion: Lessons from paramyxovirus F
    • Lamb R.A., Jardetzky T.S. Structural basis of viral invasion: Lessons from paramyxovirus F. Curr. Opin. Struct. Biol. 2007, 17(4):427-436.
    • (2007) Curr. Opin. Struct. Biol. , vol.17 , Issue.4 , pp. 427-436
    • Lamb, R.A.1    Jardetzky, T.S.2
  • 5
    • 31344432402 scopus 로고    scopus 로고
    • Virus membrane-fusion proteins: More than one way to make a hairpin
    • Kielian M., Rey F.A. Virus membrane-fusion proteins: More than one way to make a hairpin. Nat. Rev. Microbiol. 2006, 4(1):67-76.
    • (2006) Nat. Rev. Microbiol. , vol.4 , Issue.1 , pp. 67-76
    • Kielian, M.1    Rey, F.A.2
  • 6
    • 44749085794 scopus 로고    scopus 로고
    • Structures of vesicular stomatitis virus glycoprotein: Membrane fusion revisited
    • Roche S., Albertini A.A., Lepault J., Bressanelli S., Gaudin Y. Structures of vesicular stomatitis virus glycoprotein: Membrane fusion revisited. Cell. Mol. Life Sci. 2008, 65(11):1716-1728.
    • (2008) Cell. Mol. Life Sci. , vol.65 , Issue.11 , pp. 1716-1728
    • Roche, S.1    Albertini, A.A.2    Lepault, J.3    Bressanelli, S.4    Gaudin, Y.5
  • 7
    • 46449100666 scopus 로고    scopus 로고
    • Viral membrane fusion
    • Harrison S.C. Viral membrane fusion. Nat. Struct. Mol. Biol. 2008, 15(7):690-698.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , Issue.7 , pp. 690-698
    • Harrison, S.C.1
  • 8
  • 10
    • 59849107898 scopus 로고    scopus 로고
    • Common principles and intermediates of viral protein-mediated fusion: The HIV-1 paradigm
    • Melikyan G.B. Common principles and intermediates of viral protein-mediated fusion: The HIV-1 paradigm. Retrovirology 2008, 5(1):111.
    • (2008) Retrovirology , vol.5 , Issue.1 , pp. 111
    • Melikyan, G.B.1
  • 12
    • 45849108331 scopus 로고    scopus 로고
    • Structures and mechanisms of viral membrane fusion proteins: Multiple variations on a common theme
    • White J.M., Delos S.E., Brecher M., Schornberg K. Structures and mechanisms of viral membrane fusion proteins: Multiple variations on a common theme. Crit. Rev. Biochem. Mol. Biol. 2008, 43(3):189-219.
    • (2008) Crit. Rev. Biochem. Mol. Biol. , vol.43 , Issue.3 , pp. 189-219
    • White, J.M.1    Delos, S.E.2    Brecher, M.3    Schornberg, K.4
  • 13
    • 0038825375 scopus 로고    scopus 로고
    • Hypothesis: Spring-loaded boomerang mechanism of influenza hemagglutinin-mediated membrane fusion
    • Tamm L.K. Hypothesis: Spring-loaded boomerang mechanism of influenza hemagglutinin-mediated membrane fusion. Biochim. Biophys. Acta 2003, 1614(1):14-23.
    • (2003) Biochim. Biophys. Acta , vol.1614 , Issue.1 , pp. 14-23
    • Tamm, L.K.1
  • 14
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution
    • Wilson I.A., Skehel J.J., Wiley D.C. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution. Nature 1981, 289(5796):366-373.
    • (1981) Nature , vol.289 , Issue.5796 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 16
    • 18844470928 scopus 로고    scopus 로고
    • Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation
    • Chen J., Lee K.H., Steinhauer D.A., Stevens D.J., Skehel J.J., Wiley D.C. Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation. Cell 1998, 95:409-417.
    • (1998) Cell , vol.95 , pp. 409-417
    • Chen, J.1    Lee, K.H.2    Steinhauer, D.A.3    Stevens, D.J.4    Skehel, J.J.5    Wiley, D.C.6
  • 17
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough P.A., Hughson F.M., Skehel J.J., Wiley D.C. Structure of influenza haemagglutinin at the pH of membrane fusion. Nature 1994, 371:37-43.
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 18
    • 0033106334 scopus 로고    scopus 로고
    • Structural basis for paramyxovirus-mediated membrane fusion
    • Baker K.A., Dutch R.E., Lamb R.A., Jardetzky T.S. Structural basis for paramyxovirus-mediated membrane fusion. Mol. Cell 1999, 3:309-319.
    • (1999) Mol. Cell , vol.3 , pp. 309-319
    • Baker, K.A.1    Dutch, R.E.2    Lamb, R.A.3    Jardetzky, T.S.4
  • 19
    • 77953021928 scopus 로고    scopus 로고
    • Structure of the Newcastle disease virus F protein in the post-fusion conformation
    • Swanson K., Wen X., Leser G.P., Paterson R.G., Lamb R.A., Jardetzky T.S. Structure of the Newcastle disease virus F protein in the post-fusion conformation. Virology 2010, 402(2):372-379.
    • (2010) Virology , vol.402 , Issue.2 , pp. 372-379
    • Swanson, K.1    Wen, X.2    Leser, G.P.3    Paterson, R.G.4    Lamb, R.A.5    Jardetzky, T.S.6
  • 20
    • 21544470513 scopus 로고    scopus 로고
    • Structure of the uncleaved ectodomain of the paramyxovirus (hPIV3) fusion protein
    • Yin H.S., Paterson R.G., Wen X., Lamb R.A., Jardetzky T.S. Structure of the uncleaved ectodomain of the paramyxovirus (hPIV3) fusion protein. Proc. Natl. Acad. Sci. USA 2005, 102(26):9288-9293.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , Issue.26 , pp. 9288-9293
    • Yin, H.S.1    Paterson, R.G.2    Wen, X.3    Lamb, R.A.4    Jardetzky, T.S.5
  • 21
    • 77954059555 scopus 로고    scopus 로고
    • Crystal structure of HIV-1 gp41 including both fusion peptide and membrane proximal external regions
    • Buzon V., Natrajan G., Schibli D., Campelo F., Kozlov M.M., Weissenhorn W. Crystal structure of HIV-1 gp41 including both fusion peptide and membrane proximal external regions. PLoS Pathog. 2010, 6(5):e1000880.
    • (2010) PLoS Pathog. , vol.6 , Issue.5
    • Buzon, V.1    Natrajan, G.2    Schibli, D.3    Campelo, F.4    Kozlov, M.M.5    Weissenhorn, W.6
  • 22
    • 0030970693 scopus 로고    scopus 로고
    • Core structure of gp41 from the HIV envelope glycoprotein
    • Chan D.C., Fass D., Berger J.M., Kim P.S. Core structure of gp41 from the HIV envelope glycoprotein. Cell 1997, 89:263-273.
    • (1997) Cell , vol.89 , pp. 263-273
    • Chan, D.C.1    Fass, D.2    Berger, J.M.3    Kim, P.S.4
  • 24
    • 41349112506 scopus 로고    scopus 로고
    • The flavivirus precursor membrane-envelope protein complex: Structure and maturation
    • Li L., Lok S.M., Yu I.M., Zhang Y., Kuhn R.J., Chen J., Rossmann M.G. The flavivirus precursor membrane-envelope protein complex: Structure and maturation. Science 2008, 319(5871):1830-1834.
    • (2008) Science , vol.319 , Issue.5871 , pp. 1830-1834
    • Li, L.1    Lok, S.M.2    Yu, I.M.3    Zhang, Y.4    Kuhn, R.J.5    Chen, J.6    Rossmann, M.G.7
  • 26
  • 27
    • 1642499388 scopus 로고    scopus 로고
    • Structure of the dengue virus envelope protein after membrane fusion
    • Modis Y., Ogata S., Clements D., Harrison S.C. Structure of the dengue virus envelope protein after membrane fusion. Nature 2004, 427(6972):313-319.
    • (2004) Nature , vol.427 , Issue.6972 , pp. 313-319
    • Modis, Y.1    Ogata, S.2    Clements, D.3    Harrison, S.C.4
  • 28
    • 33745974537 scopus 로고    scopus 로고
    • Crystal structure of the low-pH form of the vesicular stomatitis virus glycoprotein G
    • Roche S., Bressanelli S., Rey F.A., Gaudin Y. Crystal structure of the low-pH form of the vesicular stomatitis virus glycoprotein G. Science 2006, 313(5784):187-191.
    • (2006) Science , vol.313 , Issue.5784 , pp. 187-191
    • Roche, S.1    Bressanelli, S.2    Rey, F.A.3    Gaudin, Y.4
  • 29
    • 33846959065 scopus 로고    scopus 로고
    • Structure of the prefusion form of the vesicular stomatitis virus glycoprotein G
    • Roche S., Rey F.A., Gaudin Y., Bressanelli S. Structure of the prefusion form of the vesicular stomatitis virus glycoprotein G. Science 2007, 315(5813):843-848.
    • (2007) Science , vol.315 , Issue.5813 , pp. 843-848
    • Roche, S.1    Rey, F.A.2    Gaudin, Y.3    Bressanelli, S.4
  • 30
    • 53549088587 scopus 로고    scopus 로고
    • The postfusion structure of baculovirus gp64 supports a unified view of viral fusion machines
    • Kadlec J., Loureiro S., Abrescia N.G., Stuart D.I., Jones I.M. The postfusion structure of baculovirus gp64 supports a unified view of viral fusion machines. Nat. Struct. Mol. Biol. 2008, 15(10):1024-1030.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , Issue.10 , pp. 1024-1030
    • Kadlec, J.1    Loureiro, S.2    Abrescia, N.G.3    Stuart, D.I.4    Jones, I.M.5
  • 31
    • 32944473016 scopus 로고    scopus 로고
    • Virus entry: Open sesame
    • Marsh M., Helenius A. Virus entry: Open sesame. Cell 2006, 124(4):729-740.
    • (2006) Cell , vol.124 , Issue.4 , pp. 729-740
    • Marsh, M.1    Helenius, A.2
  • 32
    • 1842534392 scopus 로고    scopus 로고
    • How viruses enter animal cells
    • Smith A.E., Helenius A. How viruses enter animal cells. Science 2004, 304(5668):237-242.
    • (2004) Science , vol.304 , Issue.5668 , pp. 237-242
    • Smith, A.E.1    Helenius, A.2
  • 33
    • 1842509971 scopus 로고    scopus 로고
    • Low pH is required for avian sarcoma and leukosis virus Env-induced hemifusion and fusion pore formation but not for pore growth
    • Melikyan G.B., Barnard R.J., Markosyan R.M., Young J.A., Cohen F.S. Low pH is required for avian sarcoma and leukosis virus Env-induced hemifusion and fusion pore formation but not for pore growth. J. Virol. 2004, 78(7):3753-3762.
    • (2004) J. Virol. , vol.78 , Issue.7 , pp. 3753-3762
    • Melikyan, G.B.1    Barnard, R.J.2    Markosyan, R.M.3    Young, J.A.4    Cohen, F.S.5
  • 34
    • 0033697734 scopus 로고    scopus 로고
    • Retroviral entry mediated by receptor priming and low pH triggering of an envelope glycoprotein
    • Mothes W., Boerger A.L., Narayan S., Cunningham J.M., Young J.A. Retroviral entry mediated by receptor priming and low pH triggering of an envelope glycoprotein. Cell 2000, 103(4):679-689.
    • (2000) Cell , vol.103 , Issue.4 , pp. 679-689
    • Mothes, W.1    Boerger, A.L.2    Narayan, S.3    Cunningham, J.M.4    Young, J.A.5
  • 35
    • 0001914545 scopus 로고    scopus 로고
    • Chemokine receptors and HIV entry
    • Doms R.W. Chemokine receptors and HIV entry. AIDS 2001, 15(Suppl 1):S34-S35.
    • (2001) AIDS , vol.15 , Issue.SUPPL.1
    • Doms, R.W.1
  • 36
    • 0033012398 scopus 로고    scopus 로고
    • Chemokine receptors as HIV-1 coreceptors: Roles in viral entry, tropism, and disease
    • Berger E.A., Murphy P.M., Farber J.M. Chemokine receptors as HIV-1 coreceptors: Roles in viral entry, tropism, and disease. Annu. Rev. Immunol. 1999, 17:657-700.
    • (1999) Annu. Rev. Immunol. , vol.17 , pp. 657-700
    • Berger, E.A.1    Murphy, P.M.2    Farber, J.M.3
  • 37
    • 40449125013 scopus 로고    scopus 로고
    • Filoviruses: Interactions with the host cell
    • Dolnik O., Kolesnikova L., Becker S. Filoviruses: Interactions with the host cell. Cell. Mol. Life Sci. 2008, 65(5):756-776.
    • (2008) Cell. Mol. Life Sci. , vol.65 , Issue.5 , pp. 756-776
    • Dolnik, O.1    Kolesnikova, L.2    Becker, S.3
  • 38
    • 33645788357 scopus 로고    scopus 로고
    • Role of endosomal cathepsins in entry mediated by the Ebola virus glycoprotein
    • Schornberg K., Matsuyama S., Kabsch K., Delos S., Bouton A., White J. Role of endosomal cathepsins in entry mediated by the Ebola virus glycoprotein. J. Virol. 2006, 80(8):4174-4178.
    • (2006) J. Virol. , vol.80 , Issue.8 , pp. 4174-4178
    • Schornberg, K.1    Matsuyama, S.2    Kabsch, K.3    Delos, S.4    Bouton, A.5    White, J.6
  • 39
    • 19144365133 scopus 로고    scopus 로고
    • Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection
    • Chandran K., Sullivan N.J., Felbor U., Whelan S.P., Cunningham J.M. Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection. Science 2005, 308(5728):1643-1645.
    • (2005) Science , vol.308 , Issue.5728 , pp. 1643-1645
    • Chandran, K.1    Sullivan, N.J.2    Felbor, U.3    Whelan, S.P.4    Cunningham, J.M.5
  • 40
    • 0001178028 scopus 로고    scopus 로고
    • Paramyxoviridae: The viruses and their replication
    • Lippincott Williams & Wilkins, Philadelphia
    • Lamb R.A., Parks G.D. Paramyxoviridae: The viruses and their replication. Fields Virology 2007, Vol. 1:1449-1496. Lippincott Williams & Wilkins, Philadelphia.
    • (2007) Fields Virology , vol.1 , pp. 1449-1496
    • Lamb, R.A.1    Parks, G.D.2
  • 41
    • 71949123985 scopus 로고    scopus 로고
    • Viral entry mechanisms: The increasing diversity of paramyxovirus entry
    • Smith E.C., Popa A., Chang A., Masante C., Dutch R.E. Viral entry mechanisms: The increasing diversity of paramyxovirus entry. FEBS J. 2009, 276(24):7217-7227.
    • (2009) FEBS J. , vol.276 , Issue.24 , pp. 7217-7227
    • Smith, E.C.1    Popa, A.2    Chang, A.3    Masante, C.4    Dutch, R.E.5
  • 42
    • 59449099994 scopus 로고    scopus 로고
    • A novel receptor-induced activation site in the Nipah virus attachment glycoprotein (G) involved in triggering the fusion glycoprotein (F)
    • Aguilar H.C., Ataman Z.A., Aspericueta V., Fang A.Q., Stroud M., Negrete O.A., Kammerer R.A., Lee B. A novel receptor-induced activation site in the Nipah virus attachment glycoprotein (G) involved in triggering the fusion glycoprotein (F). J. Biol. Chem. 2009, 284(3):1628-1635.
    • (2009) J. Biol. Chem. , vol.284 , Issue.3 , pp. 1628-1635
    • Aguilar, H.C.1    Ataman, Z.A.2    Aspericueta, V.3    Fang, A.Q.4    Stroud, M.5    Negrete, O.A.6    Kammerer, R.A.7    Lee, B.8
  • 43
    • 55549116002 scopus 로고    scopus 로고
    • Residues in the stalk domain of the Hendra virus G glycoprotein modulate conformational changes associated with receptor binding
    • Bishop K.A., Hickey A.C., Khetawat D., Patch J.R., Bossart K.N., Zhu Z., Wang L.F., Dimitrov D.S., Broder C.C. Residues in the stalk domain of the Hendra virus G glycoprotein modulate conformational changes associated with receptor binding. J. Virol. 2008, 82(22):11398-11409.
    • (2008) J. Virol. , vol.82 , Issue.22 , pp. 11398-11409
    • Bishop, K.A.1    Hickey, A.C.2    Khetawat, D.3    Patch, J.R.4    Bossart, K.N.5    Zhu, Z.6    Wang, L.F.7    Dimitrov, D.S.8    Broder, C.C.9
  • 44
    • 0029006480 scopus 로고
    • Localization of a domain on the paramyxovirus attachment protein required for the promotion of cellular fusion by its homologous fusion protein spike
    • Deng R., Wang Z., Mirza A.M., Iorio R.M. Localization of a domain on the paramyxovirus attachment protein required for the promotion of cellular fusion by its homologous fusion protein spike. Virology 1995, 209:457-469.
    • (1995) Virology , vol.209 , pp. 457-469
    • Deng, R.1    Wang, Z.2    Mirza, A.M.3    Iorio, R.M.4
  • 45
    • 47749143663 scopus 로고    scopus 로고
    • Functional interaction between paramyxovirus fusion and attachment proteins
    • Lee J.K., Prussia A., Paal T., White L.K., Snyder J.P., Plemper R.K. Functional interaction between paramyxovirus fusion and attachment proteins. J. Biol. Chem. 2008, 283(24):16561-16572.
    • (2008) J. Biol. Chem. , vol.283 , Issue.24 , pp. 16561-16572
    • Lee, J.K.1    Prussia, A.2    Paal, T.3    White, L.K.4    Snyder, J.P.5    Plemper, R.K.6
  • 46
    • 30344467852 scopus 로고    scopus 로고
    • Addition of N-glycans in the stalk of the Newcastle disease virus HN protein blocks its interaction with the F protein and prevents fusion
    • Melanson V.R., Iorio R.M. Addition of N-glycans in the stalk of the Newcastle disease virus HN protein blocks its interaction with the F protein and prevents fusion. J. Virol. 2006, 80(2):623-633.
    • (2006) J. Virol. , vol.80 , Issue.2 , pp. 623-633
    • Melanson, V.R.1    Iorio, R.M.2
  • 47
    • 0028308332 scopus 로고
    • Site-directed mutagenesis of a conserved hexapeptide in the paramyxovirus hemagglutinin-neuraminidae glycoprotein: Effects on antigenic structure and function
    • Mirza A.M., Deng R., Iorio R.M. Site-directed mutagenesis of a conserved hexapeptide in the paramyxovirus hemagglutinin-neuraminidae glycoprotein: Effects on antigenic structure and function. J. Virol. 1994, 68:5093-5099.
    • (1994) J. Virol. , vol.68 , pp. 5093-5099
    • Mirza, A.M.1    Deng, R.2    Iorio, R.M.3
  • 48
    • 0037333844 scopus 로고    scopus 로고
    • Triggering of human parainfluenza virus 3 fusion protein (F) by the hemagglutinin-neuraminidase (HN) protein: An HN mutation diminishes the rate of F activation and fusion
    • Porotto M., Murrell M., Greengard O., Moscona A. Triggering of human parainfluenza virus 3 fusion protein (F) by the hemagglutinin-neuraminidase (HN) protein: An HN mutation diminishes the rate of F activation and fusion. J. Virol. 2003, 77(6):3647-3654.
    • (2003) J. Virol. , vol.77 , Issue.6 , pp. 3647-3654
    • Porotto, M.1    Murrell, M.2    Greengard, O.3    Moscona, A.4
  • 49
    • 0027286406 scopus 로고
    • The attachment function of the Newcastle disease virus hemagglutinin-neuraminidase protein can be separated from fusion promotion by mutation
    • Sergel T., McGinnes L.W., Peeples M.E., Morrison T.G. The attachment function of the Newcastle disease virus hemagglutinin-neuraminidase protein can be separated from fusion promotion by mutation. Virology 1993, 193:717-726.
    • (1993) Virology , vol.193 , pp. 717-726
    • Sergel, T.1    McGinnes, L.W.2    Peeples, M.E.3    Morrison, T.G.4
  • 50
    • 0029836433 scopus 로고    scopus 로고
    • Functional interaction of paramyxovirus glycoproteins: Identification of a domain in Sendai virus HN which promotes cell fusion
    • Tanabayashi K., Compans R.W. Functional interaction of paramyxovirus glycoproteins: Identification of a domain in Sendai virus HN which promotes cell fusion. J. Virol. 1996, 70:6112-6118.
    • (1996) J. Virol. , vol.70 , pp. 6112-6118
    • Tanabayashi, K.1    Compans, R.W.2
  • 51
    • 71949107259 scopus 로고    scopus 로고
    • Viral entry mechanisms: Cellular and viral mediators of herpes simplex virus entry
    • Akhtar J., Shukla D. Viral entry mechanisms: Cellular and viral mediators of herpes simplex virus entry. FEBS J. 2009, 276(24):7228-7236.
    • (2009) FEBS J. , vol.276 , Issue.24 , pp. 7228-7236
    • Akhtar, J.1    Shukla, D.2
  • 52
    • 44749091723 scopus 로고    scopus 로고
    • Entry of herpesviruses into mammalian cells
    • Heldwein E.E., Krummenacher C. Entry of herpesviruses into mammalian cells. Cell. Mol. Life Sci. 2008, 65(11):1653-1668.
    • (2008) Cell. Mol. Life Sci. , vol.65 , Issue.11 , pp. 1653-1668
    • Heldwein, E.E.1    Krummenacher, C.2
  • 53
    • 1842850945 scopus 로고    scopus 로고
    • Herpes simplex virus: Receptors and ligands for cell entry
    • Spear P.G. Herpes simplex virus: Receptors and ligands for cell entry. Cell. Microbiol. 2004, 6(5):401-410.
    • (2004) Cell. Microbiol. , vol.6 , Issue.5 , pp. 401-410
    • Spear, P.G.1
  • 54
    • 0034665214 scopus 로고    scopus 로고
    • Three classes of cell surface receptors for alphaherpesvirus entry
    • Spear P.G., Eisenberg R.J., Cohen G.H. Three classes of cell surface receptors for alphaherpesvirus entry. Virology 2000, 275(1):1-8.
    • (2000) Virology , vol.275 , Issue.1 , pp. 1-8
    • Spear, P.G.1    Eisenberg, R.J.2    Cohen, G.H.3
  • 55
    • 0034991840 scopus 로고    scopus 로고
    • Plasma membrane requirements for cell fusion induced by herpes simplex virus type 1 glycoproteins gB, gD, gH and gL
    • Browne H., Bruun B., Minson T. Plasma membrane requirements for cell fusion induced by herpes simplex virus type 1 glycoproteins gB, gD, gH and gL. J. Gen. Virol. 2001, 82(Pt 6):1419-1422.
    • (2001) J. Gen. Virol. , vol.82 , Issue.PT 6 , pp. 1419-1422
    • Browne, H.1    Bruun, B.2    Minson, T.3
  • 58
    • 67449093075 scopus 로고    scopus 로고
    • Glycoprotein B of herpes simplex virus associates with target membranes via its fusion loops
    • Hannah B.P., Cairns T.M., Bender F.C., Whitbeck J.C., Lou H., Eisenberg R.J., Cohen G.H. Glycoprotein B of herpes simplex virus associates with target membranes via its fusion loops. J. Virol. 2009, 83(13):6825-6836.
    • (2009) J. Virol. , vol.83 , Issue.13 , pp. 6825-6836
    • Hannah, B.P.1    Cairns, T.M.2    Bender, F.C.3    Whitbeck, J.C.4    Lou, H.5    Eisenberg, R.J.6    Cohen, G.H.7
  • 59
    • 34548778580 scopus 로고    scopus 로고
    • Random linker-insertion mutagenesis to identify functional domains of herpes simplex virus type 1 glycoprotein B
    • Lin E., Spear P.G. Random linker-insertion mutagenesis to identify functional domains of herpes simplex virus type 1 glycoprotein B. Proc. Natl. Acad. Sci. USA 2007, 104(32):13140-13145.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , Issue.32 , pp. 13140-13145
    • Lin, E.1    Spear, P.G.2
  • 60
    • 33847295240 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 mediates fusion through a hemifusion intermediate by sequential activity of glycoproteins D, H, L, and B
    • Subramanian R.P., Geraghty R.J. Herpes simplex virus type 1 mediates fusion through a hemifusion intermediate by sequential activity of glycoproteins D, H, L, and B. Proc. Natl. Acad. Sci. USA 2007, 104(8):2903-2908.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , Issue.8 , pp. 2903-2908
    • Subramanian, R.P.1    Geraghty, R.J.2
  • 61
    • 0034676041 scopus 로고    scopus 로고
    • The transmembrane domain of influenza hemagglutinin exhibits a stringent length requirement to support the hemifusion to fusion transition
    • Armstrong R.T., Kushnir A.S., White J.M. The transmembrane domain of influenza hemagglutinin exhibits a stringent length requirement to support the hemifusion to fusion transition. J. Cell Biol. 2000, 151(2):425-437.
    • (2000) J. Cell Biol. , vol.151 , Issue.2 , pp. 425-437
    • Armstrong, R.T.1    Kushnir, A.S.2    White, J.M.3
  • 62
    • 2942635759 scopus 로고    scopus 로고
    • The energetics of membrane fusion from binding, through hemifusion, pore formation, and pore enlargement
    • Cohen F.S., Melikyan G.B. The energetics of membrane fusion from binding, through hemifusion, pore formation, and pore enlargement. J. Membr. Biol. 2004, 199(1):1-14.
    • (2004) J. Membr. Biol. , vol.199 , Issue.1 , pp. 1-14
    • Cohen, F.S.1    Melikyan, G.B.2
  • 63
    • 0034675886 scopus 로고    scopus 로고
    • Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion
    • Melikyan G.B., Markosyan R.M., Hemmati H., Delmedico M.K., Lambert D.M., Cohen F.S. Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion. J. Cell Biol. 2000, 151(2):413-424.
    • (2000) J. Cell Biol. , vol.151 , Issue.2 , pp. 413-424
    • Melikyan, G.B.1    Markosyan, R.M.2    Hemmati, H.3    Delmedico, M.K.4    Lambert, D.M.5    Cohen, F.S.6
  • 64
    • 0034120341 scopus 로고    scopus 로고
    • Membrane fusion mediated by coiled coils: A hypothesis
    • Bentz J. Membrane fusion mediated by coiled coils: A hypothesis. Biophys. J. 2000, 78(2):886-900.
    • (2000) Biophys. J. , vol.78 , Issue.2 , pp. 886-900
    • Bentz, J.1
  • 65
    • 0031678678 scopus 로고    scopus 로고
    • A mechanism of protein-mediated fusion: Coupling between refolding of the influenza hemagglutinin and lipid rearrangements
    • Kozlov M.M., Chernomordik L.V. A mechanism of protein-mediated fusion: Coupling between refolding of the influenza hemagglutinin and lipid rearrangements. Biophys. J. 1998, 75(3):1384-1396.
    • (1998) Biophys. J. , vol.75 , Issue.3 , pp. 1384-1396
    • Kozlov, M.M.1    Chernomordik, L.V.2
  • 66
    • 0029156059 scopus 로고
    • Structure and function of fusion pores in exocytosis and ectoplasmic membrane fusion
    • Lindau M., Almers W. Structure and function of fusion pores in exocytosis and ectoplasmic membrane fusion. Curr. Opin. Cell Biol. 1995, 7(4):509-517.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , Issue.4 , pp. 509-517
    • Lindau, M.1    Almers, W.2
  • 67
    • 0041320883 scopus 로고    scopus 로고
    • A new mechanism of model membrane fusion determined from Monte Carlo simulation
    • Muller M., Katsov K., Schick M. A new mechanism of model membrane fusion determined from Monte Carlo simulation. Biophys. J. 2003, 85(3):1611-1623.
    • (2003) Biophys. J. , vol.85 , Issue.3 , pp. 1611-1623
    • Muller, M.1    Katsov, K.2    Schick, M.3
  • 68
    • 0042631498 scopus 로고    scopus 로고
    • Membrane permeability changes at early stages of influenza hemagglutinin-mediated fusion
    • Frolov V.A., Dunina-Barkovskaya A.Y., Samsonov A.V., Zimmerberg J. Membrane permeability changes at early stages of influenza hemagglutinin-mediated fusion. Biophys. J. 2003, 85(3):1725-1733.
    • (2003) Biophys. J. , vol.85 , Issue.3 , pp. 1725-1733
    • Frolov, V.A.1    Dunina-Barkovskaya, A.Y.2    Samsonov, A.V.3    Zimmerberg, J.4
  • 69
    • 0034092235 scopus 로고    scopus 로고
    • Membrane perturbation and fusion pore formation in influenza hemagglutinin-mediated membrane fusion: A new model for fusion
    • Bonnafous P., Stegmann T. Membrane perturbation and fusion pore formation in influenza hemagglutinin-mediated membrane fusion: A new model for fusion. J. Biol. Chem. 2000, 275(9):6160-6166.
    • (2000) J. Biol. Chem. , vol.275 , Issue.9 , pp. 6160-6166
    • Bonnafous, P.1    Stegmann, T.2
  • 70
    • 33646024277 scopus 로고    scopus 로고
    • Cell entry of hepatitis C virus
    • Bartosch B., Cosset F.L. Cell entry of hepatitis C virus. Virology 2006, 348(1):1-12.
    • (2006) Virology , vol.348 , Issue.1 , pp. 1-12
    • Bartosch, B.1    Cosset, F.L.2
  • 71
    • 38549086984 scopus 로고    scopus 로고
    • Hepatitis C virus entry into host cells
    • Helle F., Dubuisson J. Hepatitis C virus entry into host cells. Cell. Mol. Life Sci. 2008, 65(1):100-112.
    • (2008) Cell. Mol. Life Sci. , vol.65 , Issue.1 , pp. 100-112
    • Helle, F.1    Dubuisson, J.2
  • 72
    • 42949118005 scopus 로고    scopus 로고
    • Hepatitis C virus entry
    • von Hahn T., Rice C.M. Hepatitis C virus entry. J. Biol. Chem. 2008, 283:3689-3693.
    • (2008) J. Biol. Chem. , vol.283 , pp. 3689-3693
    • von Hahn, T.1    Rice, C.M.2
  • 73
    • 29144460894 scopus 로고    scopus 로고
    • Paramyxovirus membrane fusion: Lessons from the F and HN atomic structures
    • Lamb R.A., Paterson R.G., Jardetzky T.S. Paramyxovirus membrane fusion: Lessons from the F and HN atomic structures. Virology 2006, 344(1):30-37.
    • (2006) Virology , vol.344 , Issue.1 , pp. 30-37
    • Lamb, R.A.1    Paterson, R.G.2    Jardetzky, T.S.3
  • 74
    • 77950528480 scopus 로고    scopus 로고
    • Architecture of a nascent viral fusion pore
    • Lee K.K. Architecture of a nascent viral fusion pore. EMBO J. 2010, 29(7):1299-1311.
    • (2010) EMBO J. , vol.29 , Issue.7 , pp. 1299-1311
    • Lee, K.K.1
  • 75
    • 0028783783 scopus 로고
    • The fusion kinetics of influenza hemagglutinin expressing cells to planar bilayer membranes is affected by HA density and host cell surface
    • Melikyan G.B., Niles W.D., Cohen F.S. The fusion kinetics of influenza hemagglutinin expressing cells to planar bilayer membranes is affected by HA density and host cell surface. J. Gen. Physiol. 1995, 106:783-802.
    • (1995) J. Gen. Physiol. , vol.106 , pp. 783-802
    • Melikyan, G.B.1    Niles, W.D.2    Cohen, F.S.3
  • 77
    • 34447311691 scopus 로고    scopus 로고
    • Rapid membrane fusion of individual virus particles with supported lipid bilayers
    • Wessels L., Elting M.W., Scimeca D., Weninger K. Rapid membrane fusion of individual virus particles with supported lipid bilayers. Biophys. J. 2007, 93(2):526-538.
    • (2007) Biophys. J. , vol.93 , Issue.2 , pp. 526-538
    • Wessels, L.1    Elting, M.W.2    Scimeca, D.3    Weninger, K.4
  • 78
    • 0020338520 scopus 로고
    • Membrane fusion activity of influenza virus
    • White J., Kartenbeck J., Helenius A. Membrane fusion activity of influenza virus. EMBO J. 1982, 1(2):217-222.
    • (1982) EMBO J. , vol.1 , Issue.2 , pp. 217-222
    • White, J.1    Kartenbeck, J.2    Helenius, A.3
  • 79
    • 0024195940 scopus 로고
    • Molecular mechanisms of membrane fusion and applications of membrane fusion techniques
    • Wilschut J., Scholma J., Stegmann T. Molecular mechanisms of membrane fusion and applications of membrane fusion techniques. Adv. Exp. Med. Biol. 1988, 238:105-126.
    • (1988) Adv. Exp. Med. Biol. , vol.238 , pp. 105-126
    • Wilschut, J.1    Scholma, J.2    Stegmann, T.3
  • 81
    • 0036294842 scopus 로고    scopus 로고
    • Fluorescent lipid probes in the study of viral membrane fusion
    • Blumenthal R., Gallo S.A., Viard M., Raviv Y., Puri A. Fluorescent lipid probes in the study of viral membrane fusion. Chem. Phys. Lipids 2002, 116(1-2):39-55.
    • (2002) Chem. Phys. Lipids , vol.116 , Issue.1-2 , pp. 39-55
    • Blumenthal, R.1    Gallo, S.A.2    Viard, M.3    Raviv, Y.4    Puri, A.5
  • 82
    • 0027434098 scopus 로고
    • Evaluation of viral membrane fusion assays. Comparison of the octadecylrhodamine dequenching assay with the pyrene excimer assay
    • Stegmann T., Schoen P., Bron R., Wey J., Bartoldus I., Ortiz A., Nieva J.L., Wilschut J. Evaluation of viral membrane fusion assays. Comparison of the octadecylrhodamine dequenching assay with the pyrene excimer assay. Biochemistry 1993, 32(42):11330-11337.
    • (1993) Biochemistry , vol.32 , Issue.42 , pp. 11330-11337
    • Stegmann, T.1    Schoen, P.2    Bron, R.3    Wey, J.4    Bartoldus, I.5    Ortiz, A.6    Nieva, J.L.7    Wilschut, J.8
  • 83
    • 3543106027 scopus 로고    scopus 로고
    • Evidence that rabies virus forms different kinds of fusion machines with different pH thresholds for fusion
    • Roche S., Gaudin Y. Evidence that rabies virus forms different kinds of fusion machines with different pH thresholds for fusion. J. Virol. 2004, 78(16):8746-8752.
    • (2004) J. Virol. , vol.78 , Issue.16 , pp. 8746-8752
    • Roche, S.1    Gaudin, Y.2
  • 84
    • 0025114776 scopus 로고
    • Fluorescence assays to monitor membrane fusion: Potential application in biliary lipid secretion and vesicle interactions
    • 3 PT 2
    • Hoekstra D. Fluorescence assays to monitor membrane fusion: Potential application in biliary lipid secretion and vesicle interactions. Hepatology 1990, 12(3 Pt 2):61S-66S.
    • (1990) Hepatology , vol.12
    • Hoekstra, D.1
  • 85
    • 77952000064 scopus 로고    scopus 로고
    • Conformational changes of the HIV-1 envelope protein during membrane fusion are inhibited by the replacement of its membrane-spanning domain
    • Kondo N., Miyauchi K., Meng F., Iwamoto A., Matsuda Z. Conformational changes of the HIV-1 envelope protein during membrane fusion are inhibited by the replacement of its membrane-spanning domain. J. Biol. Chem. 2010, 285(19):14681-14688.
    • (2010) J. Biol. Chem. , vol.285 , Issue.19 , pp. 14681-14688
    • Kondo, N.1    Miyauchi, K.2    Meng, F.3    Iwamoto, A.4    Matsuda, Z.5
  • 86
    • 68949187944 scopus 로고    scopus 로고
    • Monitoring of HIV-1 envelope-mediated membrane fusion using modified split green fluorescent proteins
    • Wang J., Kondo N., Long Y., Iwamoto A., Matsuda Z. Monitoring of HIV-1 envelope-mediated membrane fusion using modified split green fluorescent proteins. J. Virol. Methods 2009, 161(2):216-222.
    • (2009) J. Virol. Methods , vol.161 , Issue.2 , pp. 216-222
    • Wang, J.1    Kondo, N.2    Long, Y.3    Iwamoto, A.4    Matsuda, Z.5
  • 87
    • 1342300737 scopus 로고    scopus 로고
    • Alpha-complementation assay for HIV envelope glycoprotein-mediated fusion
    • Holland A.U., Munk C., Lucero G.R., Nguyen L.D., Landau N.R. Alpha-complementation assay for HIV envelope glycoprotein-mediated fusion. Virology 2004, 319(2):343-352.
    • (2004) Virology , vol.319 , Issue.2 , pp. 343-352
    • Holland, A.U.1    Munk, C.2    Lucero, G.R.3    Nguyen, L.D.4    Landau, N.R.5
  • 89
    • 0028587209 scopus 로고
    • Restricted movement of lipid and aqueous dyes through pores formed by influenza hemagglutinin during cell fusion
    • 6 PT 2
    • Zimmerberg J., Blumenthal R., Sarkar D.P., Curran M., Morris S.J. Restricted movement of lipid and aqueous dyes through pores formed by influenza hemagglutinin during cell fusion. J. Cell Biol. 1994, 127(6 Pt 2):1885-1894.
    • (1994) J. Cell Biol. , vol.127 , pp. 1885-1894
    • Zimmerberg, J.1    Blumenthal, R.2    Sarkar, D.P.3    Curran, M.4    Morris, S.J.5
  • 90
    • 0036121209 scopus 로고    scopus 로고
    • Altering expression levels of human immunodeficiency virus type 1 gp120-gp41 affects efficiency but not kinetics of cell-cell fusion
    • Lineberger J.E., Danzeisen R., Hazuda D.J., Simon A.J., Miller M.D. Altering expression levels of human immunodeficiency virus type 1 gp120-gp41 affects efficiency but not kinetics of cell-cell fusion. J. Virol. 2002, 76(7):3522-3533.
    • (2002) J. Virol. , vol.76 , Issue.7 , pp. 3522-3533
    • Lineberger, J.E.1    Danzeisen, R.2    Hazuda, D.J.3    Simon, A.J.4    Miller, M.D.5
  • 91
    • 0032559801 scopus 로고    scopus 로고
    • The pathway of membrane fusion catalyzed by influenza hemagglutinin: Restriction of lipids, hemifusion, and lipidic fusion pore formation
    • Chernomordik L.V., Frolov V.A., Leikina E., Bronk P., Zimmerberg J. The pathway of membrane fusion catalyzed by influenza hemagglutinin: Restriction of lipids, hemifusion, and lipidic fusion pore formation. J. Cell Biol. 1998, 140(6):1369-1382.
    • (1998) J. Cell Biol. , vol.140 , Issue.6 , pp. 1369-1382
    • Chernomordik, L.V.1    Frolov, V.A.2    Leikina, E.3    Bronk, P.4    Zimmerberg, J.5
  • 92
    • 43749109393 scopus 로고    scopus 로고
    • Vaccinia-based reporter gene cell-fusion assays to quantitate functional interactions of HIV envelope glycoprotein with receptors
    • Chapter 12, Unit 12.10
    • Dey B., Berger E.A. Vaccinia-based reporter gene cell-fusion assays to quantitate functional interactions of HIV envelope glycoprotein with receptors. Curr. Protoc. Immunol. 2003, Chapter 12, Unit 12.10.
    • (2003) Curr. Protoc. Immunol.
    • Dey, B.1    Berger, E.A.2
  • 93
    • 0030630237 scopus 로고    scopus 로고
    • Cell-cell fusion assay to study role of chemokine receptors in human immunodeficiency virus type 1 entry
    • Rucker J., Doranz B.J., Edinger A.L., Long D., Berson J.F., Doms R.W. Cell-cell fusion assay to study role of chemokine receptors in human immunodeficiency virus type 1 entry. Methods Enzymol. 1997, 288:118-133.
    • (1997) Methods Enzymol. , vol.288 , pp. 118-133
    • Rucker, J.1    Doranz, B.J.2    Edinger, A.L.3    Long, D.4    Berson, J.F.5    Doms, R.W.6
  • 94
    • 0242475091 scopus 로고    scopus 로고
    • Establishment of an HIV cell-cell fusion assay by using two genetically modified HeLa cell lines and reporter gene
    • Sakamoto T., Ushijima H., Okitsu S., Suzuki E., Sakai K., Morikawa S., Muller W.E. Establishment of an HIV cell-cell fusion assay by using two genetically modified HeLa cell lines and reporter gene. J. Virol. Methods 2003, 114(2):159-166.
    • (2003) J. Virol. Methods , vol.114 , Issue.2 , pp. 159-166
    • Sakamoto, T.1    Ushijima, H.2    Okitsu, S.3    Suzuki, E.4    Sakai, K.5    Morikawa, S.6    Muller, W.E.7
  • 95
    • 32444440783 scopus 로고    scopus 로고
    • Functional analysis of hepatitis C virus envelope proteins, using a cell-cell fusion assay
    • Kobayashi M., Bennett M.C., Bercot T., Singh I.R. Functional analysis of hepatitis C virus envelope proteins, using a cell-cell fusion assay. J. Virol. 2006, 80(4):1817-1825.
    • (2006) J. Virol. , vol.80 , Issue.4 , pp. 1817-1825
    • Kobayashi, M.1    Bennett, M.C.2    Bercot, T.3    Singh, I.R.4
  • 96
    • 0030894767 scopus 로고    scopus 로고
    • Host-derived ICAM-1 glycoproteins incorporated on human immunodeficiency virus type 1 are biologically active and enhance viral infectivity
    • Fortin J.F., Cantin R., Lamontagne G., Tremblay M. Host-derived ICAM-1 glycoproteins incorporated on human immunodeficiency virus type 1 are biologically active and enhance viral infectivity. J. Virol. 1997, 71(5):3588-3596.
    • (1997) J. Virol. , vol.71 , Issue.5 , pp. 3588-3596
    • Fortin, J.F.1    Cantin, R.2    Lamontagne, G.3    Tremblay, M.4
  • 97
    • 67449127600 scopus 로고    scopus 로고
    • HIV-1 interactions with cells: From viral binding to cell-cell transmission
    • Chapter 26, Unit 26.5
    • Janas A.M., Wu L. HIV-1 interactions with cells: From viral binding to cell-cell transmission. Curr. Protoc. Cell Biol. 2009, Chapter 26, Unit 26.5.
    • (2009) Curr. Protoc. Cell Biol.
    • Janas, A.M.1    Wu, L.2
  • 98
    • 13744252968 scopus 로고    scopus 로고
    • Involvement of clathrin-mediated endocytosis in human immunodeficiency virus type 1 entry
    • Daecke J., Fackler O.T., Dittmar M.T., Krausslich H.G. Involvement of clathrin-mediated endocytosis in human immunodeficiency virus type 1 entry. J. Virol. 2005, 79(3):1581-1594.
    • (2005) J. Virol. , vol.79 , Issue.3 , pp. 1581-1594
    • Daecke, J.1    Fackler, O.T.2    Dittmar, M.T.3    Krausslich, H.G.4
  • 99
    • 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., Aiken C. Nef does not affect the efficiency of human immunodeficiency virus type 1 fusion with target cells. J. Virol. 2003, 77(19):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
  • 100
    • 34247170928 scopus 로고    scopus 로고
    • Efficiency of human immunodeficiency virus type 1 postentry infection processes: Evidence against disproportionate numbers of defective virions
    • Thomas J.A., Ott D.E., Gorelick R.J. Efficiency of human immunodeficiency virus type 1 postentry infection processes: Evidence against disproportionate numbers of defective virions. J. Virol. 2007, 81(8):4367-4370.
    • (2007) J. Virol. , vol.81 , Issue.8 , pp. 4367-4370
    • Thomas, J.A.1    Ott, D.E.2    Gorelick, R.J.3
  • 101
    • 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., Greene W.C. A sensitive and specific enzyme-based assay detecting HIV-1 virion fusion in primary T lymphocytes. Nat. Biotechnol. 2002, 20(11):1151-1154.
    • (2002) Nat. Biotechnol. , vol.20 , Issue.11 , pp. 1151-1154
    • Cavrois, M.1    De Noronha, C.2    Greene, W.C.3
  • 102
    • 2342575708 scopus 로고    scopus 로고
    • Rapid and sensitive detection of retrovirus entry by using a novel luciferase-based content-mixing assay
    • Kolokoltsov A.A., Davey R.A. Rapid and sensitive detection of retrovirus entry by using a novel luciferase-based content-mixing assay. J. Virol. 2004, 78(10):5124-5132.
    • (2004) J. Virol. , vol.78 , Issue.10 , pp. 5124-5132
    • Kolokoltsov, A.A.1    Davey, R.A.2
  • 103
    • 33745142510 scopus 로고    scopus 로고
    • Novel, rapid assay for measuring entry of diverse enveloped viruses, including HIV and rabies
    • Saeed M.F., Kolokoltsov A.A., Davey R.A. Novel, rapid assay for measuring entry of diverse enveloped viruses, including HIV and rabies. J. Virol. Methods 2006, 135(2):143-150.
    • (2006) J. Virol. Methods , vol.135 , Issue.2 , pp. 143-150
    • Saeed, M.F.1    Kolokoltsov, A.A.2    Davey, R.A.3
  • 104
    • 65249139458 scopus 로고    scopus 로고
    • HIV enters cells via endocytosis and dynamin-dependent fusion with endosomes
    • Miyauchi K., Kim Y., Latinovic O., Morozov V., Melikyan G.B. HIV enters cells via endocytosis and dynamin-dependent fusion with endosomes. Cell 2009, 137(3):433-444.
    • (2009) Cell , vol.137 , Issue.3 , pp. 433-444
    • Miyauchi, K.1    Kim, Y.2    Latinovic, O.3    Morozov, V.4    Melikyan, G.B.5
  • 105
    • 70349677167 scopus 로고    scopus 로고
    • Early steps of HIV-1 fusion define the sensitivity to inhibitory peptides that block 6-helix bundle formation
    • Miyauchi K., Kozlov M.M., Melikyan G.B. Early steps of HIV-1 fusion define the sensitivity to inhibitory peptides that block 6-helix bundle formation. PLoS Pathog. 2009, 5(9):e1000585.
    • (2009) PLoS Pathog. , vol.5 , Issue.9
    • Miyauchi, K.1    Kozlov, M.M.2    Melikyan, G.B.3
  • 108
    • 0037066255 scopus 로고    scopus 로고
    • Single virus tracing: Visualization of the infection pathway of a virus into a living cell
    • Brauchle C., Seisenberger G., Endress T., Ried M.U., Buning H., Hallek M. Single virus tracing: Visualization of the infection pathway of a virus into a living cell. ChemPhysChem 2002, 3(3):299-303.
    • (2002) ChemPhysChem , vol.3 , Issue.3 , pp. 299-303
    • Brauchle, C.1    Seisenberger, G.2    Endress, T.3    Ried, M.U.4    Buning, H.5    Hallek, M.6
  • 111
    • 53649093082 scopus 로고    scopus 로고
    • Visualization of targeted transduction by engineered lentiviral vectors
    • Joo K.I., Wang P. Visualization of targeted transduction by engineered lentiviral vectors. Gene Ther. 2008, 15(20):1384-1396.
    • (2008) Gene Ther. , vol.15 , Issue.20 , pp. 1384-1396
    • Joo, K.I.1    Wang, P.2
  • 113
    • 0025192947 scopus 로고
    • Observation of single influenza virus-cell fusion and measurement by fluorescence video microscopy
    • Lowy R.J., Sarkar D.P., Chen Y., Blumenthal R. Observation of single influenza virus-cell fusion and measurement by fluorescence video microscopy. Proc. Natl. Acad. Sci. USA 1990, 87(5):1850-1854.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , Issue.5 , pp. 1850-1854
    • Lowy, R.J.1    Sarkar, D.P.2    Chen, Y.3    Blumenthal, R.4
  • 114
    • 28644442495 scopus 로고    scopus 로고
    • Time-resolved imaging of HIV-1 Env-mediated lipid and content mixing between a single virion and cell membrane
    • Markosyan R.M., Cohen F.S., Melikyan G.B. Time-resolved imaging of HIV-1 Env-mediated lipid and content mixing between a single virion and cell membrane. Mol. Biol. Cell 2005, 16(12):5502-5513.
    • (2005) Mol. Biol. Cell , vol.16 , Issue.12 , pp. 5502-5513
    • Markosyan, R.M.1    Cohen, F.S.2    Melikyan, G.B.3
  • 115
    • 20844457308 scopus 로고    scopus 로고
    • Imaging individual retroviral fusion events: From hemifusion to pore formation and growth
    • Melikyan G.B., Barnard R.J., Abrahamyan L.G., Mothes W., Young J.A. Imaging individual retroviral fusion events: From hemifusion to pore formation and growth. Proc. Natl. Acad. Sci. USA 2005, 102(24):8728-8733.
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , Issue.24 , pp. 8728-8733
    • Melikyan, G.B.1    Barnard, R.J.2    Abrahamyan, L.G.3    Mothes, W.4    Young, J.A.5
  • 117
    • 0036841175 scopus 로고    scopus 로고
    • Lipid intermediates in membrane fusion: Formation, structure, and decay of hemifusion diaphragm
    • Kozlovsky Y., Chernomordik L.V., Kozlov M.M. Lipid intermediates in membrane fusion: Formation, structure, and decay of hemifusion diaphragm. Biophys. J. 2002, 83(5):2634-2651.
    • (2002) Biophys. J. , vol.83 , Issue.5 , pp. 2634-2651
    • Kozlovsky, Y.1    Chernomordik, L.V.2    Kozlov, M.M.3
  • 118
    • 0023636677 scopus 로고
    • Biomembrane fusion: A new concept derived from model studies using two interacting planar lipid bilayers
    • Chernomordik L.V., Melikyan G.B., Chizmadzhev Y.A. Biomembrane fusion: A new concept derived from model studies using two interacting planar lipid bilayers. Biochim. Biophys. Acta 1987, 906(3):309-352.
    • (1987) Biochim. Biophys. Acta , vol.906 , Issue.3 , pp. 309-352
    • Chernomordik, L.V.1    Melikyan, G.B.2    Chizmadzhev, Y.A.3
  • 119
    • 0028865392 scopus 로고
    • GPI-anchored influenza hemagglutinin induces hemifusion to both red blood cell and planar bilayer membranes
    • Melikyan G.B., White J.M., Cohen F.S. GPI-anchored influenza hemagglutinin induces hemifusion to both red blood cell and planar bilayer membranes. J. Cell Biol. 1995, 131(3):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
  • 121
    • 16344374383 scopus 로고    scopus 로고
    • Field theoretic study of bilayer membrane fusion: I. Hemifusion mechanism
    • Katsov K., Muller M., Schick M. Field theoretic study of bilayer membrane fusion: I. Hemifusion mechanism. Biophys. J. 2004, 87(5):3277-3290.
    • (2004) Biophys. J. , vol.87 , Issue.5 , pp. 3277-3290
    • Katsov, K.1    Muller, M.2    Schick, M.3
  • 122
    • 41449085212 scopus 로고    scopus 로고
    • Calculation of free energy barriers to the fusion of small vesicles
    • Lee J.Y., Schick M. Calculation of free energy barriers to the fusion of small vesicles. Biophys. J. 2008, 94(5):1699-1706.
    • (2008) Biophys. J. , vol.94 , Issue.5 , pp. 1699-1706
    • Lee, J.Y.1    Schick, M.2
  • 123
    • 0038290760 scopus 로고    scopus 로고
    • Protein-lipid interplay in fusion and fission of biological membranes
    • Chernomordik L.V., Kozlov M.M. Protein-lipid interplay in fusion and fission of biological membranes. Annu. Rev. Biochem. 2003, 72:175-207.
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 175-207
    • Chernomordik, L.V.1    Kozlov, M.M.2
  • 124
    • 0038468973 scopus 로고    scopus 로고
    • The process of membrane fusion: Nipples, hemifusion, pores, and pore growth
    • Cohen F.S., Markosyan R.M., Melikyan G.B. The process of membrane fusion: Nipples, hemifusion, pores, and pore growth. Curr. Top. Membr. 2002, 52:501-529.
    • (2002) Curr. Top. Membr. , vol.52 , pp. 501-529
    • Cohen, F.S.1    Markosyan, R.M.2    Melikyan, G.B.3
  • 126
    • 0036158070 scopus 로고    scopus 로고
    • Membrane fusion: Stalk model revisited
    • Markin V.S., Albanesi J.P. Membrane fusion: Stalk model revisited. Biophys. J. 2002, 82(2):693-712.
    • (2002) Biophys. J. , vol.82 , Issue.2 , pp. 693-712
    • Markin, V.S.1    Albanesi, J.P.2
  • 128
  • 129
    • 84943997802 scopus 로고
    • Elastic properties of lipid bilayers: Theory and possible experiments
    • Helfrich W. Elastic properties of lipid bilayers: Theory and possible experiments. Z. Naturforsch. 1973, 28c:693-703.
    • (1973) Z. Naturforsch. , vol.28 c , pp. 693-703
    • Helfrich, W.1
  • 131
    • 0030899232 scopus 로고    scopus 로고
    • Inner but not outer membrane leaflets control the transition from glycosylphosphatidylinositol-anchored influenza hemagglutinin-induced hemifusion to full fusion
    • Melikyan G.B., Brener S.A., Ok D.C., Cohen F.S. Inner but not outer membrane leaflets control the transition from glycosylphosphatidylinositol-anchored influenza hemagglutinin-induced hemifusion to full fusion. J. Cell Biol. 1997, 136:995-1005.
    • (1997) J. Cell Biol. , vol.136 , pp. 995-1005
    • Melikyan, G.B.1    Brener, S.A.2    Ok, D.C.3    Cohen, F.S.4
  • 132
    • 27544473312 scopus 로고    scopus 로고
    • Membrane hemifusion: Crossing a chasm in two leaps
    • Chernomordik L.V., Kozlov M.M. Membrane hemifusion: Crossing a chasm in two leaps. Cell 2005, 123(3):375-382.
    • (2005) Cell , vol.123 , Issue.3 , pp. 375-382
    • Chernomordik, L.V.1    Kozlov, M.M.2
  • 133
    • 0035839477 scopus 로고    scopus 로고
    • Early intermediates in HIV-1 envelope glycoprotein-mediated fusion triggered by CD4 and co-receptor complexes
    • Dimitrov A.S., Xiao X., Dimitrov D.S., Blumenthal R. Early intermediates in HIV-1 envelope glycoprotein-mediated fusion triggered by CD4 and co-receptor complexes. J. Biol. Chem. 2001, 276(32):30335-30341.
    • (2001) J. Biol. Chem. , vol.276 , Issue.32 , pp. 30335-30341
    • Dimitrov, A.S.1    Xiao, X.2    Dimitrov, D.S.3    Blumenthal, R.4
  • 134
    • 0038496834 scopus 로고    scopus 로고
    • The membrane proteins of flaviviruses form ion-permeable pores in the target membrane after fusion: Identification of the pores and analysis of their possible role in virus infection
    • Koschinski A., Wengler G., Wengler G., Repp H. The membrane proteins of flaviviruses form ion-permeable pores in the target membrane after fusion: Identification of the pores and analysis of their possible role in virus infection. J. Gen. Virol. 2003, 84(Pt 7):1711-1721.
    • (2003) J. Gen. Virol. , vol.84 , Issue.PT 7 , pp. 1711-1721
    • Koschinski, A.1    Wengler, G.2    Wengler, G.3    Repp, H.4
  • 135
    • 0032812477 scopus 로고    scopus 로고
    • A specific point mutant at position 1 of the influenza hemagglutinin fusion peptide displays a hemifusion phenotype
    • Qiao H., Armstrong R.T., Melikyan G.B., Cohen F.S., White J.M. A specific point mutant at position 1 of the influenza hemagglutinin fusion peptide displays a hemifusion phenotype. Mol. Biol. Cell 1999, 10(8):2759-2769.
    • (1999) Mol. Biol. Cell , vol.10 , Issue.8 , pp. 2759-2769
    • Qiao, H.1    Armstrong, R.T.2    Melikyan, G.B.3    Cohen, F.S.4    White, J.M.5
  • 136
    • 0033017030 scopus 로고    scopus 로고
    • Amino acid sequence requirements of the transmembrane and cytoplasmic domains of influenza virus hemagglutinin for viable membrane fusion
    • Melikyan G.B., Lin S., Roth M.G., Cohen F.S. Amino acid sequence requirements of the transmembrane and cytoplasmic domains of influenza virus hemagglutinin for viable membrane fusion. Mol. Biol. Cell 1999, 10(6):1821-1836.
    • (1999) Mol. Biol. Cell , vol.10 , Issue.6 , pp. 1821-1836
    • Melikyan, G.B.1    Lin, S.2    Roth, M.G.3    Cohen, F.S.4
  • 137
    • 28044453310 scopus 로고    scopus 로고
    • Rare earth ions block the ion pores generated by the class II fusion proteins of alphaviruses and allow analysis of the biological functions of these pores
    • Koschinski A., Wengler G., Wengler G., Repp H. Rare earth ions block the ion pores generated by the class II fusion proteins of alphaviruses and allow analysis of the biological functions of these pores. J. Gen. Virol. 2005, 86(Pt 12):3311-3320.
    • (2005) J. Gen. Virol. , vol.86 , Issue.PT 12 , pp. 3311-3320
    • Koschinski, A.1    Wengler, G.2    Wengler, G.3    Repp, H.4
  • 138
    • 0028864309 scopus 로고
    • Inhibition of influenza-induced membrane fusion by lysophosphatidylcholine
    • Günther-Ausborn S., Praetor A., Stegmann T. Inhibition of influenza-induced membrane fusion by lysophosphatidylcholine. J. Biol. Chem. 1995, 270(49):29279-29285.
    • (1995) J. Biol. Chem. , vol.270 , Issue.49 , pp. 29279-29285
    • Günther-Ausborn, S.1    Praetor, A.2    Stegmann, T.3
  • 139
    • 16344374327 scopus 로고    scopus 로고
    • A study of low pH-induced refolding of Env of avian sarcoma and leukosis virus into a six-helix bundle
    • Markosyan R.M., Bates P., Cohen F.S., Melikyan G.B. A study of low pH-induced refolding of Env of avian sarcoma and leukosis virus into a six-helix bundle. Biophys. J. 2004, 87(5):3291-3298.
    • (2004) Biophys. J. , vol.87 , Issue.5 , pp. 3291-3298
    • Markosyan, R.M.1    Bates, P.2    Cohen, F.S.3    Melikyan, G.B.4
  • 140
    • 33645230933 scopus 로고    scopus 로고
    • Membrane-anchored inhibitory peptides capture human immunodeficiency virus type 1 gp41 conformations that engage the target membrane prior to fusion
    • Melikyan G.B., Egelhofer M., von Laer D. Membrane-anchored inhibitory peptides capture human immunodeficiency virus type 1 gp41 conformations that engage the target membrane prior to fusion. J. Virol. 2006, 80(7):3249-3258.
    • (2006) J. Virol. , vol.80 , Issue.7 , pp. 3249-3258
    • Melikyan, G.B.1    Egelhofer, M.2    von Laer, D.3
  • 141
    • 0034617991 scopus 로고    scopus 로고
    • Rabies virus-induced membrane fusion pathway
    • Gaudin Y. Rabies virus-induced membrane fusion pathway. J. Cell Biol. 2000, 150(3):601-612.
    • (2000) J. Cell Biol. , vol.150 , Issue.3 , pp. 601-612
    • Gaudin, Y.1
  • 142
    • 17644377288 scopus 로고    scopus 로고
    • Class II fusion protein of alphaviruses drives membrane fusion through the same pathway as class I proteins
    • Zaitseva E., Mittal A., Griffin D.E., Chernomordik L.V. Class II fusion protein of alphaviruses drives membrane fusion through the same pathway as class I proteins. J. Cell Biol. 2005, 169(1):167-177.
    • (2005) J. Cell Biol. , vol.169 , Issue.1 , pp. 167-177
    • Zaitseva, E.1    Mittal, A.2    Griffin, D.E.3    Chernomordik, L.V.4
  • 143
    • 0026389193 scopus 로고
    • A dissection of steps leading to viral envelope protein-mediated membrane fusion
    • Blumenthal R., Schoch C., Puri A., Clague M.J. A dissection of steps leading to viral envelope protein-mediated membrane fusion. Ann. N. Y. Acad. Sci. 1991, 635:285-296.
    • (1991) Ann. N. Y. Acad. Sci. , vol.635 , pp. 285-296
    • Blumenthal, R.1    Schoch, C.2    Puri, A.3    Clague, M.J.4
  • 144
    • 0026737264 scopus 로고
    • A long-lived state for influenza virus-erythrocyte complexes committed to fusion at neutral pH
    • Schoch C., Blumenthal R., Clague M.J. A long-lived state for influenza virus-erythrocyte complexes committed to fusion at neutral pH. FEBS Lett. 1992, 311(3):221-225.
    • (1992) FEBS Lett. , vol.311 , Issue.3 , pp. 221-225
    • Schoch, C.1    Blumenthal, R.2    Clague, M.J.3
  • 145
    • 0033916032 scopus 로고    scopus 로고
    • Reversible merger of membranes at the early stage of influenza hemagglutinin-mediated fusion
    • Leikina E., Chernomordik L.V. Reversible merger of membranes at the early stage of influenza hemagglutinin-mediated fusion. Mol. Biol. Cell 2000, 11(7):2359-2371.
    • (2000) Mol. Biol. Cell , vol.11 , Issue.7 , pp. 2359-2371
    • Leikina, E.1    Chernomordik, L.V.2
  • 146
    • 0037340005 scopus 로고    scopus 로고
    • HIV-1 envelope proteins complete their folding into six-helix bundles immediately after fusion pore formation
    • Markosyan R.M., Cohen F.S., Melikyan G.B. HIV-1 envelope proteins complete their folding into six-helix bundles immediately after fusion pore formation. Mol. Biol. Cell 2003, 14(3):926-938.
    • (2003) Mol. Biol. Cell , vol.14 , Issue.3 , pp. 926-938
    • Markosyan, R.M.1    Cohen, F.S.2    Melikyan, G.B.3
  • 147
    • 0027441876 scopus 로고
    • Lysophosphatidylcholine reversibly arrests exocytosis and viral fusion at a stage between triggering and membrane merger
    • Vogel S.S., Leikina E.A., Chernomordik L.V. Lysophosphatidylcholine reversibly arrests exocytosis and viral fusion at a stage between triggering and membrane merger. J. Biol. Chem. 1993, 268(34):25764-25768.
    • (1993) J. Biol. Chem. , vol.268 , Issue.34 , pp. 25764-25768
    • Vogel, S.S.1    Leikina, E.A.2    Chernomordik, L.V.3
  • 148
    • 0021984076 scopus 로고
    • Membrane fusion activity of the influenza virus hemagglutinin: The low pH-induced conformational change
    • Doms R.W., Helenius A., White J. Membrane fusion activity of the influenza virus hemagglutinin: The low pH-induced conformational change. J. Biol. Chem. 1985, 260(5):2973-2981.
    • (1985) J. Biol. Chem. , vol.260 , Issue.5 , pp. 2973-2981
    • Doms, R.W.1    Helenius, A.2    White, J.3
  • 149
    • 0032583172 scopus 로고    scopus 로고
    • Membrane fusion mediated by baculovirus gp64 involves assembly of stable gp64 TRIMERS into multiprotein aggregates
    • Markovic I., Pulyaeva H., Sokoloff A., Chernomordik L.V. Membrane fusion mediated by baculovirus gp64 involves assembly of stable gp64 TRIMERS into multiprotein aggregates. J. Cell Biol. 1998, 143(5):1155-1166.
    • (1998) J. Cell Biol. , vol.143 , Issue.5 , pp. 1155-1166
    • Markovic, I.1    Pulyaeva, H.2    Sokoloff, A.3    Chernomordik, L.V.4
  • 150
    • 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., 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 2000, 11(11):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
  • 151
    • 0023574003 scopus 로고
    • Anti-peptide antibodies detect steps in a protein conformational change: Low-pH activation of the influenza virus hemagglutinin
    • 6 PT 2
    • White J.M., Wilson I.A. Anti-peptide antibodies detect steps in a protein conformational change: Low-pH activation of the influenza virus hemagglutinin. J. Cell Biol. 1987, 105(6 Pt 2):2887-2896.
    • (1987) J. Cell Biol. , vol.105 , pp. 2887-2896
    • White, J.M.1    Wilson, I.A.2
  • 152
    • 0025647464 scopus 로고
    • Intermediates in influenza induced membrane fusion
    • Stegmann T., White J.M., Helenius A. Intermediates in influenza induced membrane fusion. EMBO J. 1990, 9(13):4231-4241.
    • (1990) EMBO J. , vol.9 , Issue.13 , pp. 4231-4241
    • Stegmann, T.1    White, J.M.2    Helenius, A.3
  • 153
    • 24944493173 scopus 로고    scopus 로고
    • Conformational changes in HIV-1 gp41 in the course of HIV-1 envelope glycoprotein-mediated fusion and inactivation
    • Dimitrov A.S., Louis J.M., Bewley C.A., Clore G.M., Blumenthal R. Conformational changes in HIV-1 gp41 in the course of HIV-1 envelope glycoprotein-mediated fusion and inactivation. Biochemistry 2005, 44(37):12471-12479.
    • (2005) Biochemistry , vol.44 , Issue.37 , pp. 12471-12479
    • Dimitrov, A.S.1    Louis, J.M.2    Bewley, C.A.3    Clore, G.M.4    Blumenthal, R.5
  • 154
    • 0034759248 scopus 로고    scopus 로고
    • Antigenic properties of the human immunodeficiency virus envelope during cell-cell fusion
    • Finnegan C.M., Berg W., Lewis G.K., DeVico A.L. Antigenic properties of the human immunodeficiency virus envelope during cell-cell fusion. J. Virol. 2001, 75(22):11096-11105.
    • (2001) J. Virol. , vol.75 , Issue.22 , pp. 11096-11105
    • Finnegan, C.M.1    Berg, W.2    Lewis, G.K.3    DeVico, A.L.4
  • 155
    • 0036889127 scopus 로고    scopus 로고
    • Antigenic properties of the human immunodeficiency virus transmembrane glycoprotein during cell-cell fusion
    • Finnegan C.M., Berg W., Lewis G.K., DeVico A.L. Antigenic properties of the human immunodeficiency virus transmembrane glycoprotein during cell-cell fusion. J. Virol. 2002, 76(23):12123-12134.
    • (2002) J. Virol. , vol.76 , Issue.23 , pp. 12123-12134
    • Finnegan, C.M.1    Berg, W.2    Lewis, G.K.3    DeVico, A.L.4
  • 156
    • 33947408272 scopus 로고    scopus 로고
    • Time frames for neutralization during the human immunodeficiency virus type 1 entry phase, as monitored in synchronously infected cell cultures
    • Haim H., Steiner I., Panet A. Time frames for neutralization during the human immunodeficiency virus type 1 entry phase, as monitored in synchronously infected cell cultures. J. Virol. 2007, 81(7):3525-3534.
    • (2007) J. Virol. , vol.81 , Issue.7 , pp. 3525-3534
    • Haim, H.1    Steiner, I.2    Panet, A.3
  • 157
    • 0028107685 scopus 로고
    • Probing the structure of the human immunodeficiency virus surface glycoprotein gp120 with a panel of monoclonal antibodies
    • Moore J.P., Sattentau Q.J., Wyatt R., Sodroski J. Probing the structure of the human immunodeficiency virus surface glycoprotein gp120 with a panel of monoclonal antibodies. J. Virol. 1994, 68(1):469-484.
    • (1994) J. Virol. , vol.68 , Issue.1 , pp. 469-484
    • Moore, J.P.1    Sattentau, Q.J.2    Wyatt, R.3    Sodroski, J.4
  • 158
    • 0025866185 scopus 로고
    • Conformational changes induced in the human immunodeficiency virus envelope glycoprotein by soluble CD4 binding
    • Sattentau Q.J., Moore J.P. Conformational changes induced in the human immunodeficiency virus envelope glycoprotein by soluble CD4 binding. J. Exp. Med. 1991, 174(2):407-415.
    • (1991) J. Exp. Med. , vol.174 , Issue.2 , pp. 407-415
    • Sattentau, Q.J.1    Moore, J.P.2
  • 159
    • 0033988632 scopus 로고    scopus 로고
    • Sequential CD4-coreceptor interactions in human immunodeficiency virus type 1 Env function: Soluble CD4 activates Env for coreceptor-dependent fusion and reveals blocking activities of antibodies against cryptic conserved epitopes on gp120
    • Salzwedel K., Smith E.D., Dey B., Berger E.A. Sequential CD4-coreceptor interactions in human immunodeficiency virus type 1 Env function: Soluble CD4 activates Env for coreceptor-dependent fusion and reveals blocking activities of antibodies against cryptic conserved epitopes on gp120. J. Virol. 2000, 74(1):326-333.
    • (2000) J. Virol. , vol.74 , Issue.1 , pp. 326-333
    • Salzwedel, K.1    Smith, E.D.2    Dey, B.3    Berger, E.A.4
  • 160
  • 161
    • 36348931103 scopus 로고    scopus 로고
    • A monoclonal Fab derived from a human nonimmune phage library reveals a new epitope on gp41 and neutralizes diverse human immunodeficiency virus type 1 strains
    • Gustchina E., Louis J.M., Lam S.N., Bewley C.A., Clore G.M. A monoclonal Fab derived from a human nonimmune phage library reveals a new epitope on gp41 and neutralizes diverse human immunodeficiency virus type 1 strains. J. Virol. 2007, 81(23):12946-12953.
    • (2007) J. Virol. , vol.81 , Issue.23 , pp. 12946-12953
    • Gustchina, E.1    Louis, J.M.2    Lam, S.N.3    Bewley, C.A.4    Clore, G.M.5
  • 164
    • 40849136223 scopus 로고    scopus 로고
    • The membrane-proximal external region of the human immunodeficiency virus type 1 envelope: dominant site of antibody neutralization and target for vaccine design
    • Montero M., van Houten N.E., Wang X., Scott J.K. The membrane-proximal external region of the human immunodeficiency virus type 1 envelope: dominant site of antibody neutralization and target for vaccine design. Microbiol. Mol. Biol. Rev. 2008, 72(1):54-84.
    • (2008) Microbiol. Mol. Biol. Rev. , vol.72 , Issue.1 , pp. 54-84
    • Montero, M.1    van Houten, N.E.2    Wang, X.3    Scott, J.K.4
  • 166
    • 1242342052 scopus 로고    scopus 로고
    • Binding of the 2F5 monoclonal antibody to native and fusion-intermediate forms of human immunodeficiency virus type 1 gp41: Implications for fusion-inducing conformational changes
    • de Rosny E., Vassell R., Jiang S., Kunert R., Weiss C.D. Binding of the 2F5 monoclonal antibody to native and fusion-intermediate forms of human immunodeficiency virus type 1 gp41: Implications for fusion-inducing conformational changes. J. Virol. 2004, 78(5):2627-2631.
    • (2004) J. Virol. , vol.78 , Issue.5 , pp. 2627-2631
    • de Rosny, E.1    Vassell, R.2    Jiang, S.3    Kunert, R.4    Weiss, C.D.5
  • 167
    • 0035900003 scopus 로고    scopus 로고
    • HIV-1 gp41 six-helix bundle formation occurs rapidly after the engagement of gp120 by CXCR4 in the HIV-1 Env-mediated fusion process
    • Gallo S.A., Puri A., Blumenthal R. HIV-1 gp41 six-helix bundle formation occurs rapidly after the engagement of gp120 by CXCR4 in the HIV-1 Env-mediated fusion process. Biochemistry 2001, 40(41):12231-12236.
    • (2001) Biochemistry , vol.40 , Issue.41 , pp. 12231-12236
    • Gallo, S.A.1    Puri, A.2    Blumenthal, R.3
  • 168
    • 23844479503 scopus 로고    scopus 로고
    • Ternary complex formation of human immunodeficiency virus type 1 Env, CD4, and chemokine receptor captured as an intermediate of membrane fusion
    • Mkrtchyan S.R., Markosyan R.M., Eadon M.T., Moore J.P., Melikyan G.B., Cohen F.S. Ternary complex formation of human immunodeficiency virus type 1 Env, CD4, and chemokine receptor captured as an intermediate of membrane fusion. J. Virol. 2005, 79(17):11161-11169.
    • (2005) J. Virol. , vol.79 , Issue.17 , pp. 11161-11169
    • Mkrtchyan, S.R.1    Markosyan, R.M.2    Eadon, M.T.3    Moore, J.P.4    Melikyan, G.B.5    Cohen, F.S.6
  • 169
    • 26444506252 scopus 로고    scopus 로고
    • Domain III from class II fusion proteins functions as a dominant-negative inhibitor of virus membrane fusion
    • Liao M., Kielian M. Domain III from class II fusion proteins functions as a dominant-negative inhibitor of virus membrane fusion. J. Cell Biol. 2005, 171(1):111-120.
    • (2005) J. Cell Biol. , vol.171 , Issue.1 , pp. 111-120
    • Liao, M.1    Kielian, M.2
  • 170
    • 23744446349 scopus 로고    scopus 로고
    • Peptide inhibitors of dengue virus and West Nile virus infectivity
    • Hrobowski Y.M., Garry R.F., Michael S.F. Peptide inhibitors of dengue virus and West Nile virus infectivity. Virol. J. 2005, 2:49.
    • (2005) Virol. J. , vol.2 , pp. 49
    • Hrobowski, Y.M.1    Garry, R.F.2    Michael, S.F.3
  • 171
    • 77954044356 scopus 로고    scopus 로고
    • Peptide inhibitors of dengue-virus entry target a late-stage fusion intermediate
    • Schmidt A.G., Yang P.L., Harrison S.C. Peptide inhibitors of dengue-virus entry target a late-stage fusion intermediate. PLoS Pathog. 2010, 6(4):e1000851.
    • (2010) PLoS Pathog. , vol.6 , Issue.4
    • Schmidt, A.G.1    Yang, P.L.2    Harrison, S.C.3
  • 172
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • Eckert D.M., Kim P.S. Mechanisms of viral membrane fusion and its inhibition. Annu. Rev. Biochem. 2001, 70:777-810.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 173
    • 10044241596 scopus 로고    scopus 로고
    • Heptad repeat 2-based peptides inhibit avian sarcoma and leukosis virus subgroup a infection and identify a fusion intermediate
    • Netter R.C., Amberg S.M., Balliet J.W., Biscone M.J., Vermeulen A., Earp L.J., White J.M., Bates P. Heptad repeat 2-based peptides inhibit avian sarcoma and leukosis virus subgroup a infection and identify a fusion intermediate. J. Virol. 2004, 78(24):13430-13439.
    • (2004) J. Virol. , vol.78 , Issue.24 , pp. 13430-13439
    • Netter, R.C.1    Amberg, S.M.2    Balliet, J.W.3    Biscone, M.J.4    Vermeulen, A.5    Earp, L.J.6    White, J.M.7    Bates, P.8
  • 174
    • 0035421959 scopus 로고    scopus 로고
    • Membrane fusion machines of paramyxoviruses: Capture of intermediates of fusion
    • Russell C.J., Jardetzky T.S., Lamb R.A. Membrane fusion machines of paramyxoviruses: Capture of intermediates of fusion. EMBO J. 2001, 20(15):4024-4034.
    • (2001) EMBO J. , vol.20 , Issue.15 , pp. 4024-4034
    • Russell, C.J.1    Jardetzky, T.S.2    Lamb, R.A.3
  • 177
    • 0027502083 scopus 로고
    • Low-pH conformational changes of rabies virus glycoprotein and their role in membrane fusion
    • Gaudin Y., Ruigrok R.W., Knossow M., Flamand A. Low-pH conformational changes of rabies virus glycoprotein and their role in membrane fusion. J. Virol. 1993, 67(3):1365-1372.
    • (1993) J. Virol. , vol.67 , Issue.3 , pp. 1365-1372
    • Gaudin, Y.1    Ruigrok, R.W.2    Knossow, M.3    Flamand, A.4
  • 178
    • 0023950102 scopus 로고
    • Activation of vesicular stomatitis virus fusion with cells by pretreatment at low pH
    • Puri A., Winick J., Lowy R.J., Covell D., Eidelman O., Walter A., Blumenthal R. Activation of vesicular stomatitis virus fusion with cells by pretreatment at low pH. J. Biol. Chem. 1988, 263(10):4749-4753.
    • (1988) J. Biol. Chem. , vol.263 , Issue.10 , pp. 4749-4753
    • Puri, A.1    Winick, J.2    Lowy, R.J.3    Covell, D.4    Eidelman, O.5    Walter, A.6    Blumenthal, R.7
  • 179
    • 0023645644 scopus 로고
    • PH-dependent fusion of vesicular stomatitis virus with Vero cells: Measurement by dequenching of octadecyl rhodamine fluorescence
    • Blumenthal R., Bali-Puri A., Walter A., Covell D., Eidelman O. pH-dependent fusion of vesicular stomatitis virus with Vero cells: Measurement by dequenching of octadecyl rhodamine fluorescence. J. Biol. Chem. 1987, 262(28):13614-13619.
    • (1987) J. Biol. Chem. , vol.262 , Issue.28 , pp. 13614-13619
    • Blumenthal, R.1    Bali-Puri, A.2    Walter, A.3    Covell, D.4    Eidelman, O.5
  • 180
  • 181
    • 0030593483 scopus 로고    scopus 로고
    • Reversible pH-dependent conformational change of reconstituted influenza hemagglutinin
    • Tatulian S.A., Tamm L.K. Reversible pH-dependent conformational change of reconstituted influenza hemagglutinin. J. Mol. Biol. 1996, 260(3):312-316.
    • (1996) J. Mol. Biol. , vol.260 , Issue.3 , pp. 312-316
    • Tatulian, S.A.1    Tamm, L.K.2
  • 182
    • 0036846370 scopus 로고    scopus 로고
    • Reversible stages of the low-pH-triggered conformational change in influenza virus hemagglutinin
    • Leikina E., Ramos C., Markovic I., Zimmerberg J., Chernomordik L.V. Reversible stages of the low-pH-triggered conformational change in influenza virus hemagglutinin. EMBO J. 2002, 21(21):5701-5710.
    • (2002) EMBO J. , vol.21 , Issue.21 , pp. 5701-5710
    • Leikina, E.1    Ramos, C.2    Markovic, I.3    Zimmerberg, J.4    Chernomordik, L.V.5
  • 183
    • 0029795282 scopus 로고    scopus 로고
    • Structural requirements for low-pH-induced rearrangements in the envelope glycoprotein of tick-borne encephalitis virus
    • Stiasny K., Allison S.L., Marchler-Bauer A., Kunz C., Heinz F.X. Structural requirements for low-pH-induced rearrangements in the envelope glycoprotein of tick-borne encephalitis virus. J. Virol. 1996, 70(11):8142-8147.
    • (1996) J. Virol. , vol.70 , Issue.11 , pp. 8142-8147
    • Stiasny, K.1    Allison, S.L.2    Marchler-Bauer, A.3    Kunz, C.4    Heinz, F.X.5
  • 184
    • 0024455501 scopus 로고
    • The heterodimeric association between the membrane proteins of Semliki Forest virus changes its sensitivity to low pH during virus maturation
    • Wahlberg J.M., Boere W.A., Garoff H. The heterodimeric association between the membrane proteins of Semliki Forest virus changes its sensitivity to low pH during virus maturation. J. Virol. 1989, 63(12):4991-4997.
    • (1989) J. Virol. , vol.63 , Issue.12 , pp. 4991-4997
    • Wahlberg, J.M.1    Boere, W.A.2    Garoff, H.3
  • 185
    • 0030808221 scopus 로고    scopus 로고
    • Conformational changes and fusion activity of vesicular stomatitis virus glycoprotein: [125I]iodonaphthyl azide photolabeling studies in biological membranes
    • Pak C.C., Puri A., Blumenthal R. Conformational changes and fusion activity of vesicular stomatitis virus glycoprotein: [125I]iodonaphthyl azide photolabeling studies in biological membranes. Biochemistry 1997, 36(29):8890-8896.
    • (1997) Biochemistry , vol.36 , Issue.29 , pp. 8890-8896
    • Pak, C.C.1    Puri, A.2    Blumenthal, R.3
  • 186
    • 0141429172 scopus 로고    scopus 로고
    • Visualization of the target-membrane-inserted fusion protein of Semliki Forest virus by combined electron microscopy and crystallography
    • Gibbons D.L., Erk I., Reilly B., Navaza J., Kielian M., Rey F.A., Lepault J. Visualization of the target-membrane-inserted fusion protein of Semliki Forest virus by combined electron microscopy and crystallography. Cell 2003, 114(5):573-583.
    • (2003) Cell , vol.114 , Issue.5 , pp. 573-583
    • Gibbons, D.L.1    Erk, I.2    Reilly, B.3    Navaza, J.4    Kielian, M.5    Rey, F.A.6    Lepault, J.7
  • 188
    • 0032478191 scopus 로고    scopus 로고
    • Receptor-triggered membrane association of a model retroviral glycoprotein
    • Damico R.L., Crane J., Bates P. Receptor-triggered membrane association of a model retroviral glycoprotein. Proc. Natl. Acad. Sci. USA 1998, 95(5):2580-2585.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , Issue.5 , pp. 2580-2585
    • Damico, R.L.1    Crane, J.2    Bates, P.3
  • 189
    • 14744272823 scopus 로고    scopus 로고
    • Receptor-induced conformational changes in the SU subunit of the avian sarcoma/leukosis virus A envelope protein: Implications for fusion activation
    • Delos S.E., Godby J.A., White J.M. Receptor-induced conformational changes in the SU subunit of the avian sarcoma/leukosis virus A envelope protein: Implications for fusion activation. J. Virol. 2005, 79(6):3488-3499.
    • (2005) J. Virol. , vol.79 , Issue.6 , pp. 3488-3499
    • Delos, S.E.1    Godby, J.A.2    White, J.M.3
  • 190
    • 0031959601 scopus 로고    scopus 로고
    • Capture of an early fusion-active conformation of HIV-1 gp41
    • Furuta R.A., Wild C.T., Weng Y., Weiss C.D. Capture of an early fusion-active conformation of HIV-1 gp41. Nat. Struct. Biol. 1998, 5(4):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
  • 191
    • 0037470227 scopus 로고    scopus 로고
    • The prefusogenic intermediate of HIV-1 gp41 contains exposed C-peptide regions
    • Koshiba T., Chan D.C. The prefusogenic intermediate of HIV-1 gp41 contains exposed C-peptide regions. J. Biol. Chem. 2002, 278:7573-7579.
    • (2002) J. Biol. Chem. , vol.278 , pp. 7573-7579
    • Koshiba, T.1    Chan, D.C.2
  • 192
    • 0038467539 scopus 로고    scopus 로고
    • Direct evidence that C-peptide inhibitors of human immunodeficiency virus type 1 entry bind to the gp41 N-helical domain in receptor-activated viral envelope
    • Kilgore N.R., Salzwedel K., Reddick M., Allaway G.P., Wild C.T. Direct evidence that C-peptide inhibitors of human immunodeficiency virus type 1 entry bind to the gp41 N-helical domain in receptor-activated viral envelope. J. Virol. 2003, 77(13):7669-7672.
    • (2003) J. Virol. , vol.77 , Issue.13 , pp. 7669-7672
    • Kilgore, N.R.1    Salzwedel, K.2    Reddick, M.3    Allaway, G.P.4    Wild, C.T.5
  • 193
    • 0030010945 scopus 로고    scopus 로고
    • +-induced membrane insertion of influenza virus hemagglutinin involves the HA2 amino-terminal fusion peptide but not the coiled coil region
    • +-induced membrane insertion of influenza virus hemagglutinin involves the HA2 amino-terminal fusion peptide but not the coiled coil region. J. Biol. Chem. 1996, 271(23):13417-13421.
    • (1996) J. Biol. Chem. , vol.271 , Issue.23 , pp. 13417-13421
    • Durrer, P.1    Galli, C.2    Hoenke, S.3    Corti, C.4    Gluck, R.5    Vorherr, T.6    Brunner, J.7
  • 194
    • 0029143629 scopus 로고
    • Photolabeling identifies a putative fusion domain in the envelope glycoprotein of rabies and vesicular stomatitis viruses
    • Durrer P., Gaudin Y., Ruigrok R.W., Graf R., Brunner J. Photolabeling identifies a putative fusion domain in the envelope glycoprotein of rabies and vesicular stomatitis viruses. J. Biol. Chem. 1995, 270(29):17575-17581.
    • (1995) J. Biol. Chem. , vol.270 , Issue.29 , pp. 17575-17581
    • Durrer, P.1    Gaudin, Y.2    Ruigrok, R.W.3    Graf, R.4    Brunner, J.5
  • 195
    • 0026062948 scopus 로고
    • The HA2 subunit of influenza hemagglutinin inserts into the target membrane prior to fusion
    • Stegmann T., Delfino J.M., Richards F.M., Helenius A. The HA2 subunit of influenza hemagglutinin inserts into the target membrane prior to fusion. J. Biol. Chem. 1991, 266(27):18404-18410.
    • (1991) J. Biol. Chem. , vol.266 , Issue.27 , pp. 18404-18410
    • Stegmann, T.1    Delfino, J.M.2    Richards, F.M.3    Helenius, A.4
  • 197
    • 4544371670 scopus 로고    scopus 로고
    • Low pH is required for avian sarcoma and leukosis virus Env-dependent viral penetration into the cytosol and not for viral uncoating
    • Barnard R.J., Narayan S., Dornadula G., Miller M.D., Young J.A. Low pH is required for avian sarcoma and leukosis virus Env-dependent viral penetration into the cytosol and not for viral uncoating. J. Virol. 2004, 78(19):10433-10441.
    • (2004) J. Virol. , vol.78 , Issue.19 , pp. 10433-10441
    • Barnard, R.J.1    Narayan, S.2    Dornadula, G.3    Miller, M.D.4    Young, J.A.5
  • 198
    • 0033529752 scopus 로고    scopus 로고
    • N- and C-terminal residues combine in the fusion-pH influenza hemagglutinin HA(2) subunit to form an N cap that terminates the triple-stranded coiled coil
    • Chen J., Skehel J.J., Wiley D.C. N- and C-terminal residues combine in the fusion-pH influenza hemagglutinin HA(2) subunit to form an N cap that terminates the triple-stranded coiled coil. Proc. Natl. Acad. Sci. USA 1999, 96(16):8967-8972.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , Issue.16 , pp. 8967-8972
    • Chen, J.1    Skehel, J.J.2    Wiley, D.C.3
  • 199
    • 0345059375 scopus 로고    scopus 로고
    • Leash in the groove mechanism of membrane fusion
    • Park H.E., Gruenke J.A., White J.M. Leash in the groove mechanism of membrane fusion. Nat. Struct. Biol. 2003, 10(12):1048-1053.
    • (2003) Nat. Struct. Biol. , vol.10 , Issue.12 , pp. 1048-1053
    • Park, H.E.1    Gruenke, J.A.2    White, J.M.3
  • 200
    • 0344120220 scopus 로고    scopus 로고
    • Completion of trimeric hairpin formation of influenza virus hemagglutinin promotes fusion pore opening and enlargement
    • Borrego-Diaz E., Peeples M.E., Markosyan R.M., Melikyan G.B., Cohen F.S. Completion of trimeric hairpin formation of influenza virus hemagglutinin promotes fusion pore opening and enlargement. Virology 2003, 316(2):234-244.
    • (2003) Virology , vol.316 , Issue.2 , pp. 234-244
    • Borrego-Diaz, E.1    Peeples, M.E.2    Markosyan, R.M.3    Melikyan, G.B.4    Cohen, F.S.5
  • 201
    • 43949135190 scopus 로고    scopus 로고
    • Importance of the membrane-perturbing properties of the membrane-proximal external region of human immunodeficiency virus type 1 gp41 to viral fusion
    • Vishwanathan S.A., Hunter E. Importance of the membrane-perturbing properties of the membrane-proximal external region of human immunodeficiency virus type 1 gp41 to viral fusion. J. Virol. 2008, 82(11):5118-5126.
    • (2008) J. Virol. , vol.82 , Issue.11 , pp. 5118-5126
    • Vishwanathan, S.A.1    Hunter, E.2
  • 202
    • 0032980413 scopus 로고    scopus 로고
    • A conserved tryptophan-rich motif in the membrane-proximal region of the human immunodeficiency virus type 1 gp41 ectodomain is important for Env-mediated fusion and virus infectivity
    • Salzwedel K., West J.T., Hunter E. A conserved tryptophan-rich motif in the membrane-proximal region of the human immunodeficiency virus type 1 gp41 ectodomain is important for Env-mediated fusion and virus infectivity. J. Virol. 1999, 73(3):2469-2480.
    • (1999) J. Virol. , vol.73 , Issue.3 , pp. 2469-2480
    • Salzwedel, K.1    West, J.T.2    Hunter, E.3
  • 203
    • 0343365487 scopus 로고    scopus 로고
    • Role of the membrane-proximal domain in the initial stages of human immunodeficiency virus type 1 envelope glycoprotein-mediated membrane fusion
    • Munoz-Barroso I., Salzwedel K., Hunter E., Blumenthal R. Role of the membrane-proximal domain in the initial stages of human immunodeficiency virus type 1 envelope glycoprotein-mediated membrane fusion. J. Virol. 1999, 73(7):6089-6092.
    • (1999) J. Virol. , vol.73 , Issue.7 , pp. 6089-6092
    • Munoz-Barroso, I.1    Salzwedel, K.2    Hunter, E.3    Blumenthal, R.4
  • 204
    • 34548170245 scopus 로고    scopus 로고
    • Functional links between the fusion peptide-proximal polar segment and membrane-proximal region of human immunodeficiency virus gp41 in distinct phases of membrane fusion
    • Bellamy-McIntyre A.K., Lay C.S., Baar S., Maerz A.L., Talbo G.H., Drummer H.E., Poumbourios P. Functional links between the fusion peptide-proximal polar segment and membrane-proximal region of human immunodeficiency virus gp41 in distinct phases of membrane fusion. J. Biol. Chem. 2007, 282(32):23104-23116.
    • (2007) J. Biol. Chem. , vol.282 , Issue.32 , pp. 23104-23116
    • Bellamy-McIntyre, A.K.1    Lay, C.S.2    Baar, S.3    Maerz, A.L.4    Talbo, G.H.5    Drummer, H.E.6    Poumbourios, P.7
  • 205
    • 46049107703 scopus 로고    scopus 로고
    • The membrane proximal external region of the HIV-1 envelope glycoprotein gp41 contributes to the stabilization of the six-helix bundle formed with a matching N' peptide
    • Noah E., Biron Z., Naider F., Arshava B., Anglister J. The membrane proximal external region of the HIV-1 envelope glycoprotein gp41 contributes to the stabilization of the six-helix bundle formed with a matching N' peptide. Biochemistry 2008, 47(26):6782-6792.
    • (2008) Biochemistry , vol.47 , Issue.26 , pp. 6782-6792
    • Noah, E.1    Biron, Z.2    Naider, F.3    Arshava, B.4    Anglister, J.5
  • 206
    • 77951985716 scopus 로고    scopus 로고
    • Studies of the 'chain reversal regions' of the avian sarcoma/leukosis virus (ASLV) and ebolavirus fusion proteins: Analogous residues are important, and a His residue unique to EnvA affects the pH dependence of ASLV entry
    • Delos S.E., La B., Gilmartin A., White J.M. Studies of the 'chain reversal regions' of the avian sarcoma/leukosis virus (ASLV) and ebolavirus fusion proteins: Analogous residues are important, and a His residue unique to EnvA affects the pH dependence of ASLV entry. J. Virol. 2010, 84(11):5687-5694.
    • (2010) J. Virol. , vol.84 , Issue.11 , pp. 5687-5694
    • Delos, S.E.1    La, B.2    Gilmartin, A.3    White, J.M.4
  • 207
    • 0033920211 scopus 로고    scopus 로고
    • Functional implications of the human T-lymphotropic virus type 1 transmembrane glycoprotein helical hairpin structure
    • Maerz A.L., Center R.J., Kemp B.E., Kobe B., Poumbourios P. Functional implications of the human T-lymphotropic virus type 1 transmembrane glycoprotein helical hairpin structure. J. Virol. 2000, 74(14):6614-6621.
    • (2000) J. Virol. , vol.74 , Issue.14 , pp. 6614-6621
    • Maerz, A.L.1    Center, R.J.2    Kemp, B.E.3    Kobe, B.4    Poumbourios, P.5
  • 208
    • 0242409119 scopus 로고    scopus 로고
    • The membrane-proximal region of vesicular stomatitis virus glycoprotein G ectodomain is critical for fusion and virus infectivity
    • Jeetendra E., Ghosh K., Odell D., Li J., Ghosh H.P., Whitt M.A. The membrane-proximal region of vesicular stomatitis virus glycoprotein G ectodomain is critical for fusion and virus infectivity. J. Virol. 2003, 77(23):12807-12818.
    • (2003) J. Virol. , vol.77 , Issue.23 , pp. 12807-12818
    • Jeetendra, E.1    Ghosh, K.2    Odell, D.3    Li, J.4    Ghosh, H.P.5    Whitt, M.A.6
  • 209
    • 33750724162 scopus 로고    scopus 로고
    • Functions of the stem region of the Semliki Forest virus fusion protein during virus fusion and assembly
    • Liao M., Kielian M. Functions of the stem region of the Semliki Forest virus fusion protein during virus fusion and assembly. J. Virol. 2006, 80(22):11362-11369.
    • (2006) J. Virol. , vol.80 , Issue.22 , pp. 11362-11369
    • Liao, M.1    Kielian, M.2
  • 210
    • 0028179011 scopus 로고
    • Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion
    • Kemble G.W., Danieli T., White J.M. Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion. Cell 1994, 76(2):383-391.
    • (1994) Cell , vol.76 , Issue.2 , pp. 383-391
    • Kemble, G.W.1    Danieli, T.2    White, J.M.3
  • 211
    • 0034630904 scopus 로고    scopus 로고
    • Oligomerization, secretion, and biological function of an anchor-free parainfluenza virus type 2 (PI2) fusion protein
    • Tong S., Compans R.W. Oligomerization, secretion, and biological function of an anchor-free parainfluenza virus type 2 (PI2) fusion protein. Virology 2000, 270(2):368-376.
    • (2000) Virology , vol.270 , Issue.2 , pp. 368-376
    • Tong, S.1    Compans, R.W.2
  • 212
    • 0034252335 scopus 로고    scopus 로고
    • Both hemifusion and fusion pores are induced by GPI-linked influenza hemagglutinin
    • Frolov V., Cho M., Reese T.S., Zimmerberg J. Both hemifusion and fusion pores are induced by GPI-linked influenza hemagglutinin. Traffic 2000, 1:622-630.
    • (2000) Traffic , vol.1 , pp. 622-630
    • Frolov, V.1    Cho, M.2    Reese, T.S.3    Zimmerberg, J.4
  • 213
    • 0242671942 scopus 로고    scopus 로고
    • Meta-stability of the hemifusion intermediate induced by glycosylphosphatidylinositol-anchored influenza hemagglutinin
    • Nüssler F., Clague M.J., Herrmann A. Meta-stability of the hemifusion intermediate induced by glycosylphosphatidylinositol-anchored influenza hemagglutinin. Biophys. J. 1997, 73(5):2280-2291.
    • (1997) Biophys. J. , vol.73 , Issue.5 , pp. 2280-2291
    • Nüssler, F.1    Clague, M.J.2    Herrmann, A.3
  • 214
    • 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., 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. 1993, 67(12):7060-7066.
    • (1993) J. Virol. , vol.67 , Issue.12 , pp. 7060-7066
    • Weiss, C.D.1    White, J.M.2
  • 215
    • 0034801792 scopus 로고    scopus 로고
    • Mutations within the putative membrane-spanning domain of the simian immunodeficiency virus transmembrane glycoprotein define the minimal requirements for fusion, incorporation, and infectivity
    • West J.T., Johnston P.B., Dubay S.R., Hunter E. Mutations within the putative membrane-spanning domain of the simian immunodeficiency virus transmembrane glycoprotein define the minimal requirements for fusion, incorporation, and infectivity. J. Virol. 2001, 75(20):9601-9612.
    • (2001) J. Virol. , vol.75 , Issue.20 , pp. 9601-9612
    • West, J.T.1    Johnston, P.B.2    Dubay, S.R.3    Hunter, E.4
  • 216
    • 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., 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. USA 1998, 95(7):3425-3430.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , Issue.7 , pp. 3425-3430
    • Cleverley, D.Z.1    Lenard, J.2
  • 217
    • 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., 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. 2005, 79(8):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
  • 218
    • 43949136434 scopus 로고    scopus 로고
    • Role of the membrane-spanning domain of human immunodeficiency virus type 1 envelope glycoprotein in cell-cell fusion and virus infection
    • Shang L., Yue L., Hunter E. Role of the membrane-spanning domain of human immunodeficiency virus type 1 envelope glycoprotein in cell-cell fusion and virus infection. J. Virol. 2008, 82(11):5417-5428.
    • (2008) J. Virol. , vol.82 , Issue.11 , pp. 5417-5428
    • Shang, L.1    Yue, L.2    Hunter, E.3
  • 219
    • 58549102514 scopus 로고    scopus 로고
    • Functional analysis of the transmembrane domain in paramyxovirus F protein-mediated membrane fusion
    • Bissonnette M.L., Donald J.E., DeGrado W.F., Jardetzky T.S., Lamb R.A. Functional analysis of the transmembrane domain in paramyxovirus F protein-mediated membrane fusion. J. Mol. Biol. 2009, 386(1):14-36.
    • (2009) J. Mol. Biol. , vol.386 , Issue.1 , pp. 14-36
    • Bissonnette, M.L.1    Donald, J.E.2    DeGrado, W.F.3    Jardetzky, T.S.4    Lamb, R.A.5
  • 220
    • 30144436116 scopus 로고    scopus 로고
    • Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation
    • Yin H.S., Wen X., Paterson R.G., Lamb R.A., Jardetzky T.S. Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation. Nature 2006, 439(7072):38-44.
    • (2006) Nature , vol.439 , Issue.7072 , pp. 38-44
    • Yin, H.S.1    Wen, X.2    Paterson, R.G.3    Lamb, R.A.4    Jardetzky, T.S.5
  • 221
    • 3042550474 scopus 로고    scopus 로고
    • Activation of a paramyxovirus fusion protein is modulated by inside-out signaling from the cytoplasmic tail
    • Waning D.L., Russell C.J., Jardetzky T.S., Lamb R.A. Activation of a paramyxovirus fusion protein is modulated by inside-out signaling from the cytoplasmic tail. Proc. Natl. Acad. Sci. USA 2004, 101(25):9217-9222.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , Issue.25 , pp. 9217-9222
    • Waning, D.L.1    Russell, C.J.2    Jardetzky, T.S.3    Lamb, R.A.4
  • 222
    • 77951490223 scopus 로고    scopus 로고
    • Syncytial phenotype of C-terminally truncated herpes simplex virus type 1 gB is associated with diminished membrane interactions
    • Chowdary T.K., Heldwein E.E. Syncytial phenotype of C-terminally truncated herpes simplex virus type 1 gB is associated with diminished membrane interactions. J. Virol. 2010, 84(10):4923-4935.
    • (2010) J. Virol. , vol.84 , Issue.10 , pp. 4923-4935
    • Chowdary, T.K.1    Heldwein, E.E.2
  • 223
    • 39749131003 scopus 로고    scopus 로고
    • Fusogenicity of Jaagsiekte sheep retrovirus envelope protein is dependent on low pH and is enhanced by cytoplasmic tail truncations
    • Cote M., Zheng Y.M., Albritton L.M., Liu S.L. Fusogenicity of Jaagsiekte sheep retrovirus envelope protein is dependent on low pH and is enhanced by cytoplasmic tail truncations. J. Virol. 2008, 82(5):2543-2554.
    • (2008) J. Virol. , vol.82 , Issue.5 , pp. 2543-2554
    • Cote, M.1    Zheng, Y.M.2    Albritton, L.M.3    Liu, S.L.4
  • 224
    • 0033858690 scopus 로고    scopus 로고
    • Modification of the cytoplasmic domain of influenza virus hemagglutinin affects enlargement of the fusion pore
    • Kozerski C., Ponimaskin E., Schroth-Diez B., Schmidt M.F., Herrmann A. Modification of the cytoplasmic domain of influenza virus hemagglutinin affects enlargement of the fusion pore. J. Virol. 2000, 74(16):7529-7537.
    • (2000) J. Virol. , vol.74 , Issue.16 , pp. 7529-7537
    • Kozerski, C.1    Ponimaskin, E.2    Schroth-Diez, B.3    Schmidt, M.F.4    Herrmann, A.5
  • 225
    • 0028788472 scopus 로고
    • The role of human immunodeficiency virus type 1 envelope glycoproteins in virus infection
    • Freed E.O., Martin M.A. The role of human immunodeficiency virus type 1 envelope glycoproteins in virus infection. J. Biol. Chem. 1995, 270(41):23883-23886.
    • (1995) J. Biol. Chem. , vol.270 , Issue.41 , pp. 23883-23886
    • Freed, E.O.1    Martin, M.A.2
  • 226
    • 10644267548 scopus 로고    scopus 로고
    • The cytoplasmic tail slows the folding of human immunodeficiency virus type 1 Env from a late prebundle configuration into the six-helix bundle
    • Abrahamyan L.G., Mkrtchyan S.R., Binley J., Lu M., Melikyan G.B., Cohen F.S. The cytoplasmic tail slows the folding of human immunodeficiency virus type 1 Env from a late prebundle configuration into the six-helix bundle. J. Virol. 2005, 79(1):106-115.
    • (2005) J. Virol. , vol.79 , Issue.1 , pp. 106-115
    • Abrahamyan, L.G.1    Mkrtchyan, S.R.2    Binley, J.3    Lu, M.4    Melikyan, G.B.5    Cohen, F.S.6
  • 227
    • 0036187805 scopus 로고    scopus 로고
    • Truncation of the cytoplasmic domain induces exposure of conserved regions in the ectodomain of human immunodeficiency virus type 1 envelope protein
    • Edwards T.G., Wyss S., Reeves J.D., Zolla-Pazner S., Hoxie J.A., Doms R.W., Baribaud F. Truncation of the cytoplasmic domain induces exposure of conserved regions in the ectodomain of human immunodeficiency virus type 1 envelope protein. J. Virol. 2002, 76(6):2683-2691.
    • (2002) J. Virol. , vol.76 , Issue.6 , pp. 2683-2691
    • Edwards, T.G.1    Wyss, S.2    Reeves, J.D.3    Zolla-Pazner, S.4    Hoxie, J.A.5    Doms, R.W.6    Baribaud, F.7
  • 228
    • 0026713860 scopus 로고
    • Truncation of the human immunodeficiency virus type 1 transmembrane glycoprotein cytoplasmic domain blocks virus infectivity
    • Dubay J.W., Roberts S.J., Hahn B.H., Hunter E. Truncation of the human immunodeficiency virus type 1 transmembrane glycoprotein cytoplasmic domain blocks virus infectivity. J. Virol. 1992, 66(11):6616-6625.
    • (1992) J. Virol. , vol.66 , Issue.11 , pp. 6616-6625
    • Dubay, J.W.1    Roberts, S.J.2    Hahn, B.H.3    Hunter, E.4
  • 229
    • 39749162175 scopus 로고    scopus 로고
    • R-peptide cleavage potentiates fusion-controlling isomerization of the intersubunit disulfide in Moloney murine leukemia virus Env
    • Loving R., Li K., Wallin M., Sjoberg M., Garoff H. R-peptide cleavage potentiates fusion-controlling isomerization of the intersubunit disulfide in Moloney murine leukemia virus Env. J. Virol. 2008, 82(5):2594-2597.
    • (2008) J. Virol. , vol.82 , Issue.5 , pp. 2594-2597
    • Loving, R.1    Li, K.2    Wallin, M.3    Sjoberg, M.4    Garoff, H.5
  • 230
    • 35348908350 scopus 로고    scopus 로고
    • Maturation-dependent human immunodeficiency virus type 1 particle fusion requires a carboxyl-terminal region of the gp41 cytoplasmic tail
    • Jiang J., Aiken C. Maturation-dependent human immunodeficiency virus type 1 particle fusion requires a carboxyl-terminal region of the gp41 cytoplasmic tail. J. Virol. 2007, 81(18):9999-10008.
    • (2007) J. Virol. , vol.81 , Issue.18 , pp. 9999-10008
    • Jiang, J.1    Aiken, C.2
  • 231
    • 43949142437 scopus 로고    scopus 로고
    • An alteration of human immunodeficiency virus gp41 leads to reduced CCR5 dependence and CD4 independence
    • Taylor B.M., Foulke J.S., Flinko R., Heredia A., DeVico A., Reitz M. An alteration of human immunodeficiency virus gp41 leads to reduced CCR5 dependence and CD4 independence. J. Virol. 2008, 82(11):5460-5471.
    • (2008) J. Virol. , vol.82 , Issue.11 , pp. 5460-5471
    • Taylor, B.M.1    Foulke, J.S.2    Flinko, R.3    Heredia, A.4    DeVico, A.5    Reitz, M.6
  • 232
    • 0028112013 scopus 로고
    • Effects of cytoplasmic domain length on cell surface expression and syncytium-forming capacity of the simian immunodeficiency virus envelope glycoprotein
    • Spies C.P., Compans R.W. Effects of cytoplasmic domain length on cell surface expression and syncytium-forming capacity of the simian immunodeficiency virus envelope glycoprotein. Virology 1994, 203(1):8-19.
    • (1994) Virology , vol.203 , Issue.1 , pp. 8-19
    • Spies, C.P.1    Compans, R.W.2
  • 233
    • 1842457792 scopus 로고    scopus 로고
    • Coupling of human immunodeficiency virus type 1 fusion to virion maturation: A novel role of the gp41 cytoplasmic tail
    • Wyma D.J., Jiang J., Shi J., Zhou J., Lineberger J.E., Miller M.D., Aiken C. Coupling of human immunodeficiency virus type 1 fusion to virion maturation: A novel role of the gp41 cytoplasmic tail. J. Virol. 2004, 78(7):3429-3435.
    • (2004) J. Virol. , vol.78 , Issue.7 , pp. 3429-3435
    • Wyma, D.J.1    Jiang, J.2    Shi, J.3    Zhou, J.4    Lineberger, J.E.5    Miller, M.D.6    Aiken, C.7
  • 234
    • 25144488199 scopus 로고    scopus 로고
    • Regulation of human immunodeficiency virus type 1 envelope glycoprotein fusion by a membrane-interactive domain in the gp41 cytoplasmic tail
    • Wyss S., Dimitrov A.S., Baribaud F., Edwards T.G., Blumenthal R., Hoxie J.A. Regulation of human immunodeficiency virus type 1 envelope glycoprotein fusion by a membrane-interactive domain in the gp41 cytoplasmic tail. J. Virol. 2005, 79(19):12231-12241.
    • (2005) J. Virol. , vol.79 , Issue.19 , pp. 12231-12241
    • Wyss, S.1    Dimitrov, A.S.2    Baribaud, F.3    Edwards, T.G.4    Blumenthal, R.5    Hoxie, J.A.6
  • 235
    • 0036711683 scopus 로고    scopus 로고
    • Identification of R-peptides in envelope proteins of C-type retroviruses
    • Bobkova M., Stitz J., Engelstadter M., Cichutek K., Buchholz C.J. Identification of R-peptides in envelope proteins of C-type retroviruses. J. Gen. Virol. 2002, 83(Pt 9):2241-2246.
    • (2002) J. Gen. Virol. , vol.83 , Issue.PT 9 , pp. 2241-2246
    • Bobkova, M.1    Stitz, J.2    Engelstadter, M.3    Cichutek, K.4    Buchholz, C.J.5
  • 236
    • 0019844429 scopus 로고
    • Sequence-specific antibodies show that maturation of Moloney leukemia virus envelope polyprotein involves removal of a COOH-terminal peptide
    • Green N., Shinnick T.M., Witte O., Ponticelli A., Sutcliffe J.G., Lerner R.A. Sequence-specific antibodies show that maturation of Moloney leukemia virus envelope polyprotein involves removal of a COOH-terminal peptide. Proc. Natl. Acad. Sci. USA 1981, 78(10):6023-6027.
    • (1981) Proc. Natl. Acad. Sci. USA , vol.78 , Issue.10 , pp. 6023-6027
    • Green, N.1    Shinnick, T.M.2    Witte, O.3    Ponticelli, A.4    Sutcliffe, J.G.5    Lerner, R.A.6
  • 237
    • 0033988562 scopus 로고    scopus 로고
    • Role of the cytoplasmic tail of ecotropic Moloney murine leukemia virus Env protein in fusion pore formation
    • Melikyan G.B., Markosyan R.M., Brener S.A., Rozenberg Y., Cohen F.S. Role of the cytoplasmic tail of ecotropic Moloney murine leukemia virus Env protein in fusion pore formation. J. Virol. 2000, 74(1):447-455.
    • (2000) J. Virol. , vol.74 , Issue.1 , pp. 447-455
    • Melikyan, G.B.1    Markosyan, R.M.2    Brener, S.A.3    Rozenberg, Y.4    Cohen, F.S.5
  • 238
    • 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.N., Suss-Toby E., Nora E., Zimmerberg J. An amphipathic peptide from the C-terminal region of the human immunodeficiency virus envelope glycoprotein causes pore formation in membranes. J. Virol. 1994, 68(11):7115-7123.
    • (1994) J. Virol. , vol.68 , Issue.11 , pp. 7115-7123
    • Chernomordik, L.1    Chanturiya, A.N.2    Suss-Toby, E.3    Nora, E.4    Zimmerberg, J.5
  • 239
    • 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
    • Viard M., Ablan S.D., Zhou M., Veenstra T.D., Freed E.O., Raviv Y., Blumenthal R. 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 2008, 47(7):1977-1983.
    • (2008) Biochemistry , vol.47 , Issue.7 , pp. 1977-1983
    • Viard, M.1    Ablan, S.D.2    Zhou, M.3    Veenstra, T.D.4    Freed, E.O.5    Raviv, Y.6    Blumenthal, R.7
  • 240
    • 47749086305 scopus 로고    scopus 로고
    • Surface exposure of the HIV-1 env cytoplasmic tail LLP2 domain during the membrane fusion process: Interaction with gp41 fusion core
    • Lu L., Zhu Y., Huang J., Chen X., Yang H., Jiang S., Chen Y.H. Surface exposure of the HIV-1 env cytoplasmic tail LLP2 domain during the membrane fusion process: Interaction with gp41 fusion core. J. Biol. Chem. 2008, 283(24):16723-16731.
    • (2008) J. Biol. Chem. , vol.283 , Issue.24 , pp. 16723-16731
    • Lu, L.1    Zhu, Y.2    Huang, J.3    Chen, X.4    Yang, H.5    Jiang, S.6    Chen, Y.H.7
  • 241
    • 0031460632 scopus 로고    scopus 로고
    • Influenza hemagglutinin is spring-loaded by a metastable native conformation
    • Carr C.M., Chaudhry C., Kim P.S. Influenza hemagglutinin is spring-loaded by a metastable native conformation. Proc. Natl. Acad. Sci. USA 1997, 94(26):14306-14313.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , Issue.26 , pp. 14306-14313
    • Carr, C.M.1    Chaudhry, C.2    Kim, P.S.3
  • 242
    • 0034037991 scopus 로고    scopus 로고
    • The lipid-anchored ectodomain of influenza virus hemagglutinin (GPI-HA) is capable of inducing nonenlarging fusion pores
    • Markosyan R.M., Cohen F.S., Melikyan G.B. The lipid-anchored ectodomain of influenza virus hemagglutinin (GPI-HA) is capable of inducing nonenlarging fusion pores. Mol. Biol. Cell 2000, 11(4):1143-1152.
    • (2000) Mol. Biol. Cell , vol.11 , Issue.4 , pp. 1143-1152
    • Markosyan, R.M.1    Cohen, F.S.2    Melikyan, G.B.3
  • 243
    • 0029823936 scopus 로고    scopus 로고
    • Dilation of the influenza hemagglutinin fusion pore revealed by the kinetics of individual cell-cell fusion events
    • Blumenthal R., Sarkar D.P., Durell S., Howard D.E., Morris S.J. Dilation of the influenza hemagglutinin fusion pore revealed by the kinetics of individual cell-cell fusion events. J. Cell Biol. 1996, 135(1):63-71.
    • (1996) J. Cell Biol. , vol.135 , Issue.1 , pp. 63-71
    • Blumenthal, R.1    Sarkar, D.P.2    Durell, S.3    Howard, D.E.4    Morris, S.J.5
  • 244
    • 0029898564 scopus 로고    scopus 로고
    • Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers
    • Danieli T., Pelletier S.L., Henis Y.I., White J.M. Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers. J. Cell Biol. 1996, 133(3):559-569.
    • (1996) J. Cell Biol. , vol.133 , Issue.3 , pp. 559-569
    • Danieli, T.1    Pelletier, S.L.2    Henis, Y.I.3    White, J.M.4
  • 245
    • 0343621483 scopus 로고    scopus 로고
    • Role of hemagglutinin surface density in the initial stages of influenza virus fusion: Lack of evidence for cooperativity
    • Gunther-Ausborn S., Schoen P., Bartoldus I., Wilschut J., Stegmann T. Role of hemagglutinin surface density in the initial stages of influenza virus fusion: Lack of evidence for cooperativity. J. Virol. 2000, 74(6):2714-2720.
    • (2000) J. Virol. , vol.74 , Issue.6 , pp. 2714-2720
    • Gunther-Ausborn, S.1    Schoen, P.2    Bartoldus, I.3    Wilschut, J.4    Stegmann, T.5
  • 246
    • 0034031590 scopus 로고    scopus 로고
    • Minimal aggregate size and minimal fusion unit for the first fusion pore of influenza hemagglutinin-mediated membrane fusion
    • Bentz J. Minimal aggregate size and minimal fusion unit for the first fusion pore of influenza hemagglutinin-mediated membrane fusion. Biophys. J. 2000, 78(1):227-245.
    • (2000) Biophys. J. , vol.78 , Issue.1 , pp. 227-245
    • Bentz, J.1
  • 247
    • 0036309399 scopus 로고    scopus 로고
    • Characterization of the equilibrium between the native and fusion-inactive conformation of rabies virus glycoprotein indicates that the fusion complex is made of several trimers
    • Roche S., Gaudin Y. Characterization of the equilibrium between the native and fusion-inactive conformation of rabies virus glycoprotein indicates that the fusion complex is made of several trimers. Virology 2002, 297(1):128-135.
    • (2002) Virology , vol.297 , Issue.1 , pp. 128-135
    • Roche, S.1    Gaudin, Y.2
  • 248
    • 36048944421 scopus 로고    scopus 로고
    • Modeling how many envelope glycoprotein trimers per virion participate in human immunodeficiency virus infectivity and its neutralization by antibody
    • Klasse P.J. Modeling how many envelope glycoprotein trimers per virion participate in human immunodeficiency virus infectivity and its neutralization by antibody. Virology 2007, 369(2):245-262.
    • (2007) Virology , vol.369 , Issue.2 , pp. 245-262
    • Klasse, P.J.1
  • 250
    • 25144500649 scopus 로고    scopus 로고
    • Stoichiometry of envelope glycoprotein trimers in the entry of human immunodeficiency virus type 1
    • Yang X., Kurteva S., Ren X., Lee S., Sodroski J. Stoichiometry of envelope glycoprotein trimers in the entry of human immunodeficiency virus type 1. J. Virol. 2005, 79(19):12132-12147.
    • (2005) J. Virol. , vol.79 , Issue.19 , pp. 12132-12147
    • Yang, X.1    Kurteva, S.2    Ren, X.3    Lee, S.4    Sodroski, J.5
  • 251
    • 0035956421 scopus 로고    scopus 로고
    • Synchronized activation and refolding of influenza hemagglutinin in multimeric fusion machines
    • Markovic I., Leikina E., Zhukovsky M., Zimmerberg J., Chernomordik L.V. Synchronized activation and refolding of influenza hemagglutinin in multimeric fusion machines. J. Cell Biol. 2001, 155(5):833-844.
    • (2001) J. Cell Biol. , vol.155 , Issue.5 , pp. 833-844
    • Markovic, I.1    Leikina, E.2    Zhukovsky, M.3    Zimmerberg, J.4    Chernomordik, L.V.5
  • 252
    • 2942702017 scopus 로고    scopus 로고
    • Influenza hemagglutinins outside of the contact zone are necessary for fusion pore expansion
    • Leikina E., Mittal A., Cho M.S., Melikov K., Kozlov M.M., Chernomordik L.V. Influenza hemagglutinins outside of the contact zone are necessary for fusion pore expansion. J. Biol. Chem. 2004, 279(25):26526-26532.
    • (2004) J. Biol. Chem. , vol.279 , Issue.25 , pp. 26526-26532
    • Leikina, E.1    Mittal, A.2    Cho, M.S.3    Melikov, K.4    Kozlov, M.M.5    Chernomordik, L.V.6
  • 253
    • 0027180538 scopus 로고
    • Membrane flux through the pore formed by a fusogenic viral envelope protein during cell fusion
    • Tse F.W., Iwata A., Almers W. Membrane flux through the pore formed by a fusogenic viral envelope protein during cell fusion. J. Cell Biol. 1993, 121(3):543-552.
    • (1993) J. Cell Biol. , vol.121 , Issue.3 , pp. 543-552
    • Tse, F.W.1    Iwata, A.2    Almers, W.3
  • 255
    • 0021322137 scopus 로고
    • Characterization of three highly purified influenza virus strains by electron microscopy
    • Ruigrok R.W., Andree P.J., Hooft van Huysduynen R.A., Mellema J.E. Characterization of three highly purified influenza virus strains by electron microscopy. J. Gen. Virol. 1984, 65(Pt 4):799-802.
    • (1984) J. Gen. Virol. , vol.65 , Issue.PT 4 , pp. 799-802
    • Ruigrok, R.W.1    Andree, P.J.2    Hooft van Huysduynen, R.A.3    Mellema, J.E.4
  • 256
    • 0347364638 scopus 로고    scopus 로고
    • Electron tomography analysis of envelope glycoprotein trimers on HIV and simian immunodeficiency virus virions
    • Zhu P., Chertova E., Bess J., Lifson J.D., Arthur L.O., Liu J., Taylor K.A., Roux K.H. Electron tomography analysis of envelope glycoprotein trimers on HIV and simian immunodeficiency virus virions. Proc. Natl. Acad. Sci. USA 2003, 100(26):15812-15817.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , Issue.26 , pp. 15812-15817
    • Zhu, P.1    Chertova, E.2    Bess, J.3    Lifson, J.D.4    Arthur, L.O.5    Liu, J.6    Taylor, K.A.7    Roux, K.H.8
  • 257
    • 0021281777 scopus 로고
    • Endosome pH measured in single cells by dual fluorescence flow cytometry: Rapid acidification of insulin to pH 6
    • Murphy R.F., Powers S., Cantor C.R. Endosome pH measured in single cells by dual fluorescence flow cytometry: Rapid acidification of insulin to pH 6. J. Cell Biol. 1984, 98(5):1757-1762.
    • (1984) J. Cell Biol. , vol.98 , Issue.5 , pp. 1757-1762
    • Murphy, R.F.1    Powers, S.2    Cantor, C.R.3
  • 258
    • 0023603374 scopus 로고
    • Kinetics of endosome acidification in mutant and wild-type Chinese hamster ovary cells
    • 6 PT 1
    • Yamashiro D.J., Maxfield F.R. Kinetics of endosome acidification in mutant and wild-type Chinese hamster ovary cells. J. Cell Biol. 1987, 105(6 Pt 1):2713-2721.
    • (1987) J. Cell Biol. , vol.105 , pp. 2713-2721
    • Yamashiro, D.J.1    Maxfield, F.R.2
  • 259
    • 0033551150 scopus 로고    scopus 로고
    • Tamoxifen inhibits acidification in cells independent of the estrogen receptor
    • Altan N., Chen Y., Schindler M., Simon S.M. Tamoxifen inhibits acidification in cells independent of the estrogen receptor. Proc. Natl. Acad. Sci. USA 1999, 96(8):4432-4437.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , Issue.8 , pp. 4432-4437
    • Altan, N.1    Chen, Y.2    Schindler, M.3    Simon, S.M.4
  • 260
    • 0026637939 scopus 로고
    • Biological activity of paramyxovirus fusion proteins: Factors influencing formation of syncytia
    • Horvath C.M., Paterson R.G., Shaughnessy M.A., Wood R., Lamb R.A. Biological activity of paramyxovirus fusion proteins: Factors influencing formation of syncytia. J. Virol. 1992, 66:4564-4569.
    • (1992) J. Virol. , vol.66 , pp. 4564-4569
    • Horvath, C.M.1    Paterson, R.G.2    Shaughnessy, M.A.3    Wood, R.4    Lamb, R.A.5
  • 262
    • 0023954154 scopus 로고
    • Human immunodeficiency virus infection of CD4-bearing cells occurs by a pH-independent mechanism
    • McClure M.O., Marsh M., Weiss R.A. Human immunodeficiency virus infection of CD4-bearing cells occurs by a pH-independent mechanism. EMBO J. 1988, 7(2):513-518.
    • (1988) EMBO J. , vol.7 , Issue.2 , pp. 513-518
    • McClure, M.O.1    Marsh, M.2    Weiss, R.A.3
  • 263
    • 0025304589 scopus 로고
    • Human immunodeficiency virus envelope glycoprotein/CD4-mediated fusion of nonprimate cells with human cells
    • Ashorn P.A., Berger E.A., Moss B. Human immunodeficiency virus envelope glycoprotein/CD4-mediated fusion of nonprimate cells with human cells. J. Virol. 1990, 64(5):2149-2156.
    • (1990) J. Virol. , vol.64 , Issue.5 , pp. 2149-2156
    • Ashorn, P.A.1    Berger, E.A.2    Moss, B.3
  • 264
    • 0023644926 scopus 로고
    • PH-independent HIV entry into CD4-positive T cells via virus envelope fusion to the plasma membrane
    • Stein B.S., Gowda S.D., Lifson J.D., Penhallow R.C., Bensch K.G., Engleman E.G. pH-independent HIV entry into CD4-positive T cells via virus envelope fusion to the plasma membrane. Cell 1987, 49(5):659-668.
    • (1987) Cell , vol.49 , Issue.5 , pp. 659-668
    • Stein, B.S.1    Gowda, S.D.2    Lifson, J.D.3    Penhallow, R.C.4    Bensch, K.G.5    Engleman, E.G.6
  • 265
    • 0036827862 scopus 로고    scopus 로고
    • Inhibition of endosomal/lysosomal degradation increases the infectivity of human immunodeficiency virus
    • Fredericksen B.L., Wei B.L., Yao J., Luo T., Garcia J.V. Inhibition of endosomal/lysosomal degradation increases the infectivity of human immunodeficiency virus. J. Virol. 2002, 76(22):11440-11446.
    • (2002) J. Virol. , vol.76 , Issue.22 , pp. 11440-11446
    • Fredericksen, B.L.1    Wei, B.L.2    Yao, J.3    Luo, T.4    Garcia, J.V.5
  • 266
    • 0347003570 scopus 로고    scopus 로고
    • Compensatory link between fusion and endocytosis of human immunodeficiency virus type 1 in human CD4 T lymphocytes
    • Schaeffer E., Soros V.B., Greene W.C. Compensatory link between fusion and endocytosis of human immunodeficiency virus type 1 in human CD4 T lymphocytes. J. Virol. 2004, 78(3):1375-1383.
    • (2004) J. Virol. , vol.78 , Issue.3 , pp. 1375-1383
    • Schaeffer, E.1    Soros, V.B.2    Greene, W.C.3
  • 267
    • 34447273317 scopus 로고    scopus 로고
    • Small interfering RNA profiling reveals key role of clathrin-mediated endocytosis and early endosome formation for infection by respiratory syncytial virus
    • Kolokoltsov A.A., Deniger D., Fleming E.H., Roberts N.J., Karpilow J.M., Davey R.A. Small interfering RNA profiling reveals key role of clathrin-mediated endocytosis and early endosome formation for infection by respiratory syncytial virus. J. Virol. 2007, 81(14):7786-7800.
    • (2007) J. Virol. , vol.81 , Issue.14 , pp. 7786-7800
    • Kolokoltsov, A.A.1    Deniger, D.2    Fleming, E.H.3    Roberts, N.J.4    Karpilow, J.M.5    Davey, R.A.6
  • 268
    • 23244461734 scopus 로고    scopus 로고
    • Caveola-dependent endocytic entry of amphotropic murine leukemia virus
    • Beer C., Andersen D.S., Rojek A., Pedersen L. Caveola-dependent endocytic entry of amphotropic murine leukemia virus. J. Virol. 2005, 79(16):10776-10787.
    • (2005) J. Virol. , vol.79 , Issue.16 , pp. 10776-10787
    • Beer, C.1    Andersen, D.S.2    Rojek, A.3    Pedersen, L.4
  • 269
    • 0035039738 scopus 로고    scopus 로고
    • Infectious entry by amphotropic as well as ecotropic murine leukemia viruses occurs through an endocytic pathway
    • Katen L.J., Januszeski M.M., Anderson W.F., Hasenkrug K.J., Evans L.H. Infectious entry by amphotropic as well as ecotropic murine leukemia viruses occurs through an endocytic pathway. J. Virol. 2001, 75(11):5018-5026.
    • (2001) J. Virol. , vol.75 , Issue.11 , pp. 5018-5026
    • Katen, L.J.1    Januszeski, M.M.2    Anderson, W.F.3    Hasenkrug, K.J.4    Evans, L.H.5
  • 270
    • 2942635074 scopus 로고    scopus 로고
    • Actin cytoskeletal reorganizations and coreceptor-mediated activation of rac during human immunodeficiency virus-induced cell fusion
    • Pontow S.E., Heyden N.V., Wei S., Ratner L. Actin cytoskeletal reorganizations and coreceptor-mediated activation of rac during human immunodeficiency virus-induced cell fusion. J. Virol. 2004, 78(13):7138-7147.
    • (2004) J. Virol. , vol.78 , Issue.13 , pp. 7138-7147
    • Pontow, S.E.1    Heyden, N.V.2    Wei, S.3    Ratner, L.4
  • 271
    • 0033995518 scopus 로고    scopus 로고
    • Role for dynamin in late endosome dynamics and trafficking of the cation-independent mannose 6-phosphate receptor
    • Nicoziani P., Vilhardt F., Llorente A., Hilout L., Courtoy P.J., Sandvig K., van Deurs B. Role for dynamin in late endosome dynamics and trafficking of the cation-independent mannose 6-phosphate receptor. Mol. Biol. Cell 2000, 11(2):481-495.
    • (2000) Mol. Biol. Cell , vol.11 , Issue.2 , pp. 481-495
    • Nicoziani, P.1    Vilhardt, F.2    Llorente, A.3    Hilout, L.4    Courtoy, P.J.5    Sandvig, K.6    van Deurs, B.7
  • 272
    • 0742288598 scopus 로고    scopus 로고
    • The dynamin superfamily: Universal membrane tubulation and fission molecules?
    • Praefcke G.J., McMahon H.T. The dynamin superfamily: Universal membrane tubulation and fission molecules?. Nat. Rev. Mol. Cell Biol. 2004, 5(2):133-147.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , Issue.2 , pp. 133-147
    • Praefcke, G.J.1    McMahon, H.T.2
  • 273
    • 58149390171 scopus 로고    scopus 로고
    • Host cell factors and functions involved in vesicular stomatitis virus entry
    • Johannsdottir H.K., Mancini R., Kartenbeck J., Amato L., Helenius A. Host cell factors and functions involved in vesicular stomatitis virus entry. J. Virol. 2009, 83:440-453.
    • (2009) J. Virol. , vol.83 , pp. 440-453
    • Johannsdottir, H.K.1    Mancini, R.2    Kartenbeck, J.3    Amato, L.4    Helenius, A.5
  • 274
    • 67349158752 scopus 로고    scopus 로고
    • Molecular assemblies and membrane domains in multivesicular endosome dynamics
    • Falguieres T., Luyet P.P., Gruenberg J. Molecular assemblies and membrane domains in multivesicular endosome dynamics. Exp. Cell Res. 2009, 315(9):1567-1573.
    • (2009) Exp. Cell Res. , vol.315 , Issue.9 , pp. 1567-1573
    • Falguieres, T.1    Luyet, P.P.2    Gruenberg, J.3
  • 280
    • 0036684445 scopus 로고    scopus 로고
    • Thermal denaturation of influenza virus and its relationship to membrane fusion
    • Epand R.M., Epand R.F. Thermal denaturation of influenza virus and its relationship to membrane fusion. Biochem. J. 2002, 365(Pt 3):841-848.
    • (2002) Biochem. J. , vol.365 , Issue.PT 3 , pp. 841-848
    • Epand, R.M.1    Epand, R.F.2
  • 281
    • 0037065673 scopus 로고    scopus 로고
    • Acid-induced changes in thermal stability and fusion activity of influenza hemagglutinin
    • Remeta D.P., Krumbiegel M., Minetti C.A., Puri A., Ginsburg A., Blumenthal R. Acid-induced changes in thermal stability and fusion activity of influenza hemagglutinin. Biochemistry 2002, 41(6):2044-2054.
    • (2002) Biochemistry , vol.41 , Issue.6 , pp. 2044-2054
    • Remeta, D.P.1    Krumbiegel, M.2    Minetti, C.A.3    Puri, A.4    Ginsburg, A.5    Blumenthal, R.6
  • 282
    • 0032488623 scopus 로고    scopus 로고
    • The mechanism for low-pH-induced clustering of phospholipid vesicles carrying the HA2 ectodomain of influenza hemagglutinin
    • Kim C.H., Macosko J.C., Shin Y.K. The mechanism for low-pH-induced clustering of phospholipid vesicles carrying the HA2 ectodomain of influenza hemagglutinin. Biochemistry 1998, 37(1):137-144.
    • (1998) Biochemistry , vol.37 , Issue.1 , pp. 137-144
    • Kim, C.H.1    Macosko, J.C.2    Shin, Y.K.3
  • 283
    • 0034646448 scopus 로고    scopus 로고
    • Factors determining vesicular lipid mixing induced by shortened constructs of influenza hemagglutinin
    • LeDuc D.L., Shin Y.K., Epand R.F., Epand R.M. Factors determining vesicular lipid mixing induced by shortened constructs of influenza hemagglutinin. Biochemistry 2000, 39(10):2733-2739.
    • (2000) Biochemistry , vol.39 , Issue.10 , pp. 2733-2739
    • LeDuc, D.L.1    Shin, Y.K.2    Epand, R.F.3    Epand, R.M.4
  • 285
    • 63149141422 scopus 로고    scopus 로고
    • Reovirus FAST protein transmembrane domains function in a modular, primary sequence-independent manner to mediate cell-cell membrane fusion
    • Clancy E.K., Duncan R. Reovirus FAST protein transmembrane domains function in a modular, primary sequence-independent manner to mediate cell-cell membrane fusion. J. Virol. 2009, 83(7):2941-2950.
    • (2009) J. Virol. , vol.83 , Issue.7 , pp. 2941-2950
    • Clancy, E.K.1    Duncan, R.2
  • 286
    • 10944247048 scopus 로고    scopus 로고
    • Myristoylation, a protruding loop, and structural plasticity are essential features of a nonenveloped virus fusion peptide motif
    • Corcoran J.A., Syvitski R., Top D., Epand R.M., Epand R.F., Jakeman D., Duncan R. Myristoylation, a protruding loop, and structural plasticity are essential features of a nonenveloped virus fusion peptide motif. J. Biol. Chem. 2004, 279(49):51386-51394.
    • (2004) J. Biol. Chem. , vol.279 , Issue.49 , pp. 51386-51394
    • Corcoran, J.A.1    Syvitski, R.2    Top, D.3    Epand, R.M.4    Epand, R.F.5    Jakeman, D.6    Duncan, R.7
  • 287
    • 0034161496 scopus 로고    scopus 로고
    • A new class of fusion-associated small transmembrane (FAST) proteins encoded by the non-enveloped fusogenic reoviruses
    • Shmulevitz M., Duncan R. A new class of fusion-associated small transmembrane (FAST) proteins encoded by the non-enveloped fusogenic reoviruses. EMBO J. 2000, 19(5):902-912.
    • (2000) EMBO J. , vol.19 , Issue.5 , pp. 902-912
    • Shmulevitz, M.1    Duncan, R.2
  • 288
    • 0027967960 scopus 로고
    • Insertion of a coiled-coil peptide from influenza virus hemagglutinin into membranes
    • Yu Y.G., King D.S., Shin Y.K. Insertion of a coiled-coil peptide from influenza virus hemagglutinin into membranes. Science 1994, 266(5183):274-276.
    • (1994) Science , vol.266 , Issue.5183 , pp. 274-276
    • Yu, Y.G.1    King, D.S.2    Shin, Y.K.3
  • 289
    • 0038131038 scopus 로고    scopus 로고
    • Thermodynamics of fusion peptide-membrane interactions
    • Li Y., Han X., Tamm L.K. Thermodynamics of fusion peptide-membrane interactions. Biochemistry 2003, 42(23):7245-7251.
    • (2003) Biochemistry , vol.42 , Issue.23 , pp. 7245-7251
    • Li, Y.1    Han, X.2    Tamm, L.K.3
  • 290
    • 70349304444 scopus 로고    scopus 로고
    • A strong correlation between fusogenicity and membrane insertion depth of the HIV fusion peptide
    • Qiang W., Sun Y., Weliky D.P. A strong correlation between fusogenicity and membrane insertion depth of the HIV fusion peptide. Proc. Natl. Acad. Sci. USA 2009, 106(36):15314-15319.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , Issue.36 , pp. 15314-15319
    • Qiang, W.1    Sun, Y.2    Weliky, D.P.3
  • 291
    • 0034892952 scopus 로고    scopus 로고
    • Membrane structure and fusion-triggering conformational change of the fusion domain from influenza hemagglutinin
    • Han X., Bushweller J.H., Cafiso D.S., Tamm L.K. Membrane structure and fusion-triggering conformational change of the fusion domain from influenza hemagglutinin. Nat. Struct. Biol. 2001, 8(8):715-720.
    • (2001) Nat. Struct. Biol. , vol.8 , Issue.8 , pp. 715-720
    • Han, X.1    Bushweller, J.H.2    Cafiso, D.S.3    Tamm, L.K.4
  • 292
    • 27744577746 scopus 로고    scopus 로고
    • Properties and structures of the influenza and HIV fusion peptides on lipid membranes: Implications for a role in fusion
    • Haque M.E., Koppaka V., Axelsen P.H., Lentz B.R. Properties and structures of the influenza and HIV fusion peptides on lipid membranes: Implications for a role in fusion. Biophys. J. 2005, 89(5):3183-3194.
    • (2005) Biophys. J. , vol.89 , Issue.5 , pp. 3183-3194
    • Haque, M.E.1    Koppaka, V.2    Axelsen, P.H.3    Lentz, B.R.4
  • 293
    • 0028306273 scopus 로고
    • Interaction of fluorescently labeled analogues of the amino-terminal fusion peptide of Sendai virus with phospholipid membranes
    • Rapaport D., Shai Y. Interaction of fluorescently labeled analogues of the amino-terminal fusion peptide of Sendai virus with phospholipid membranes. J. Biol. Chem. 1994, 269(21):15124-15131.
    • (1994) J. Biol. Chem. , vol.269 , Issue.21 , pp. 15124-15131
    • Rapaport, D.1    Shai, Y.2
  • 294
    • 33745785300 scopus 로고    scopus 로고
    • Visualization of molecular interactions by fluorescence complementation
    • Kerppola T.K. Visualization of molecular interactions by fluorescence complementation. Nat. Rev. Mol. Cell Biol. 2006, 7(6):449-456.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , Issue.6 , pp. 449-456
    • Kerppola, T.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.