메뉴 건너뛰기




Volumn 9, Issue 8, 2013, Pages

Structure of the Parainfluenza Virus 5 (PIV5) Hemagglutinin-Neuraminidase (HN) Ectodomain

Author keywords

[No Author keywords available]

Indexed keywords

DIMER; HN PROTEIN; SIALIC ACID; SIALIDASE;

EID: 84883271554     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1003534     Document Type: Article
Times cited : (64)

References (56)
  • 1
    • 34547601896 scopus 로고    scopus 로고
    • Paramyxoviridae: The viruses and their replication
    • Knipe DM, Howley PM, editors, Philadelphia: Lippincott Williams & Wilkins
    • Lamb RA, Parks GD (2007) Paramyxoviridae: The viruses and their replication. In: Knipe DM, Howley PM, editors. Fields Virology (Fifth Edition). Philadelphia: Lippincott Williams & Wilkins. pp. 1449-1496.
    • (2007) Fields Virology (Fifth Edition) , pp. 1449-1496
    • Lamb, R.A.1    Parks, G.D.2
  • 2
    • 0019501239 scopus 로고
    • Inhibition of the neuraminidase of paramyxoviruses by halide ions: a possible means of modulating the two activities of the HN protein
    • Merz DC, Prehm P, Scheid A, Choppin PW, (1981) Inhibition of the neuraminidase of paramyxoviruses by halide ions: a possible means of modulating the two activities of the HN protein. Virology 112: 296-305.
    • (1981) Virology , vol.112 , pp. 296-305
    • Merz, D.C.1    Prehm, P.2    Scheid, A.3    Choppin, P.W.4
  • 3
    • 30144436116 scopus 로고    scopus 로고
    • Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation
    • Yin HS, Wen X, Paterson RG, Lamb RA, Jardetzky TS, (2006) Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation. Nature 439: 38-44.
    • (2006) Nature , vol.439 , pp. 38-44
    • Yin, H.S.1    Wen, X.2    Paterson, R.G.3    Lamb, R.A.4    Jardetzky, T.S.5
  • 4
    • 84861315738 scopus 로고    scopus 로고
    • Structure of the human metapneumovirus fusion protein with neutralizing antibody identifies a pneumovirus antigenic site
    • Wen X, Krause JC, Leser GP, Cox RG, Lamb RA, et al. (2012) Structure of the human metapneumovirus fusion protein with neutralizing antibody identifies a pneumovirus antigenic site. Nat Struct Mol Biol 19: 461-463.
    • (2012) Nat Struct Mol Biol , vol.19 , pp. 461-463
    • Wen, X.1    Krause, J.C.2    Leser, G.P.3    Cox, R.G.4    Lamb, R.A.5
  • 5
    • 84867351430 scopus 로고    scopus 로고
    • Structure of the cleavage-activated prefusion form of the parainfluenza virus 5 fusion protein
    • Welch BD, Liu Y, Kors CA, Leser GP, Jardetzky TS, et al. (2012) Structure of the cleavage-activated prefusion form of the parainfluenza virus 5 fusion protein. Proc Nat Acad Sci USA 109: 16672-16677.
    • (2012) Proc Nat Acad Sci USA , vol.109 , pp. 16672-16677
    • Welch, B.D.1    Liu, Y.2    Kors, C.A.3    Leser, G.P.4    Jardetzky, T.S.5
  • 6
  • 7
    • 0034687711 scopus 로고    scopus 로고
    • Structural characterization of the human respiratory syncytial virus fusion protein core
    • Zhao X, Singh M, Malashkevich VN, Kim PS, (2000) Structural characterization of the human respiratory syncytial virus fusion protein core. Proc Natl Acad Sci USA 97: 14172-14177.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 14172-14177
    • Zhao, X.1    Singh, M.2    Malashkevich, V.N.3    Kim, P.S.4
  • 8
    • 77953021928 scopus 로고    scopus 로고
    • Structure of the Newcastle disease virus F protein in the post-fusion conformation
    • Swanson K, Wen X, Leser GP, Paterson RG, Lamb RA, et al. (2010) Structure of the Newcastle disease virus F protein in the post-fusion conformation. Virology 402: 372-379.
    • (2010) Virology , vol.402 , pp. 372-379
    • Swanson, K.1    Wen, X.2    Leser, G.P.3    Paterson, R.G.4    Lamb, R.A.5
  • 9
    • 34548824835 scopus 로고    scopus 로고
    • Structural basis of viral invasion: lessons from paramyxovirus F
    • Lamb RA, Jardetzky TS, (2007) Structural basis of viral invasion: lessons from paramyxovirus F. Curr Opin Struct Biol 17: 427-436.
    • (2007) Curr Opin Struct Biol , vol.17 , pp. 427-436
    • Lamb, R.A.1    Jardetzky, T.S.2
  • 10
    • 44849140504 scopus 로고    scopus 로고
    • Structural basis of Nipah and Hendra virus attachment to their cell-surface receptor ephrin-B2
    • Bowden TA, Aricescu AR, Gilbert RJ, Grimes JM, Jones EY, et al. (2008) Structural basis of Nipah and Hendra virus attachment to their cell-surface receptor ephrin-B2. Nat Struct Biol 15: 567-572.
    • (2008) Nat Struct Biol , vol.15 , pp. 567-572
    • Bowden, T.A.1    Aricescu, A.R.2    Gilbert, R.J.3    Grimes, J.M.4    Jones, E.Y.5
  • 11
    • 36849029202 scopus 로고    scopus 로고
    • Structure of the measles virus hemagglutinin
    • Colf LA, Juo ZS, Garcia KC, (2007) Structure of the measles virus hemagglutinin. Nat Struct Mol Biol 14: 1227-1228.
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 1227-1228
    • Colf, L.A.1    Juo, Z.S.2    Garcia, K.C.3
  • 12
    • 0033762350 scopus 로고    scopus 로고
    • Crystal structure of the multifunctional paramyxovirus hemagglutinin-neuraminidase
    • Crennell S, Takimoto T, Portner A, Taylor G, (2000) Crystal structure of the multifunctional paramyxovirus hemagglutinin-neuraminidase. Nat Struct Biol 7: 1068-1074.
    • (2000) Nat Struct Biol , vol.7 , pp. 1068-1074
    • Crennell, S.1    Takimoto, T.2    Portner, A.3    Taylor, G.4
  • 13
    • 37649006255 scopus 로고    scopus 로고
    • Crystal structure of measles virus hemagglutinin provides insight into effective vaccines
    • Hashiguchi T, Kajikawa M, Maita N, Takeda M, Kuroki K, et al. (2007) Crystal structure of measles virus hemagglutinin provides insight into effective vaccines. Proc Natl Acad Sci USA 104: 19535-19540.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 19535-19540
    • Hashiguchi, T.1    Kajikawa, M.2    Maita, N.3    Takeda, M.4    Kuroki, K.5
  • 14
    • 0346654073 scopus 로고    scopus 로고
    • Structure of the haemagglutinin-neuraminidase from human parainfluenza virus type III
    • Lawrence MC, Borg NA, Streltsov VA, Pilling PA, Epa VC, et al. (2004) Structure of the haemagglutinin-neuraminidase from human parainfluenza virus type III. J Mol Biol 335: 1343-1357.
    • (2004) J Mol Biol , vol.335 , pp. 1343-1357
    • Lawrence, M.C.1    Borg, N.A.2    Streltsov, V.A.3    Pilling, P.A.4    Epa, V.C.5
  • 15
    • 48249113696 scopus 로고    scopus 로고
    • Host cell recognition by the henipaviruses: crystal structures of the Nipah G attachment glycoprotein and its complex with ephrin-B3
    • Xu K, Rajashankar KR, Chan YP, Himanen JP, Broder CC, et al. (2008) Host cell recognition by the henipaviruses: crystal structures of the Nipah G attachment glycoprotein and its complex with ephrin-B3. Proc Natl Acad Sci USA 105: 9953-9958.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 9953-9958
    • Xu, K.1    Rajashankar, K.R.2    Chan, Y.P.3    Himanen, J.P.4    Broder, C.C.5
  • 16
    • 80052564183 scopus 로고    scopus 로고
    • Structure of the Newcastle disease virus hemagglutinin-neuraminidase (HN) ectodomain reveals a four-helix bundle stalk
    • Yuan P, Swanson KA, Leser GP, Paterson RG, Lamb RA, et al. (2011) Structure of the Newcastle disease virus hemagglutinin-neuraminidase (HN) ectodomain reveals a four-helix bundle stalk. Proc Nat Acad Sci USA 108: 14920-14925.
    • (2011) Proc Nat Acad Sci USA , vol.108 , pp. 14920-14925
    • Yuan, P.1    Swanson, K.A.2    Leser, G.P.3    Paterson, R.G.4    Lamb, R.A.5
  • 17
    • 18944375873 scopus 로고    scopus 로고
    • Structural studies of the parainfluenza virius 5 hemagglutinin-neuraminidase tetramer in complex with its receptor, sialyllactose
    • Yuan P, Thompson T, Wurzburg BA, Paterson RG, Lamb RA, et al. (2005) Structural studies of the parainfluenza virius 5 hemagglutinin-neuraminidase tetramer in complex with its receptor, sialyllactose. Structure 13: 1-13.
    • (2005) Structure , vol.13 , pp. 1-13
    • Yuan, P.1    Thompson, T.2    Wurzburg, B.A.3    Paterson, R.G.4    Lamb, R.A.5
  • 18
    • 0025342516 scopus 로고
    • Different roles of individual N-linked oligosaccharide chains in folding, assembly, and transport of the simian virus 5 hemagglutinin-neuraminidase
    • Ng DT, Hiebert SW, Lamb RA, (1990) Different roles of individual N-linked oligosaccharide chains in folding, assembly, and transport of the simian virus 5 hemagglutinin-neuraminidase. Mol Cell Biol 10: 1989-2001.
    • (1990) Mol Cell Biol , vol.10 , pp. 1989-2001
    • Ng, D.T.1    Hiebert, S.W.2    Lamb, R.A.3
  • 19
    • 49049109230 scopus 로고    scopus 로고
    • Domain architecture and oligomerization properties of the paramyxovirus PIV5 hemagglutinin-neuraminidase (HN) protein
    • Yuan P, Leser GP, Demeler B, Lamb RA, Jardetzky TS, (2008) Domain architecture and oligomerization properties of the paramyxovirus PIV5 hemagglutinin-neuraminidase (HN) protein. Virology 378: 282-291.
    • (2008) Virology , vol.378 , pp. 282-291
    • Yuan, P.1    Leser, G.P.2    Demeler, B.3    Lamb, R.A.4    Jardetzky, T.S.5
  • 20
    • 0025155169 scopus 로고
    • Folding and oligomerization properties of a soluble and secreted form of the paramyxovirus hemagglutinin-neuraminidase glycoprotein
    • Parks GD, Lamb RA, (1990) Folding and oligomerization properties of a soluble and secreted form of the paramyxovirus hemagglutinin-neuraminidase glycoprotein. Virology 178: 498-508.
    • (1990) Virology , vol.178 , pp. 498-508
    • Parks, G.D.1    Lamb, R.A.2
  • 21
    • 84855845971 scopus 로고    scopus 로고
    • Structure and mutagenesis of the parainfluenza virus 5 hemagglutinin-neuraminidase stalk domain reveals a four-helix bundle and the role of the stalk in fusion promotion
    • Bose S, Welch BD, Kors CA, Yuan P, Jardetzky TS, et al. (2011) Structure and mutagenesis of the parainfluenza virus 5 hemagglutinin-neuraminidase stalk domain reveals a four-helix bundle and the role of the stalk in fusion promotion. J Virol 85: 12855-12866.
    • (2011) J Virol , vol.85 , pp. 12855-12866
    • Bose, S.1    Welch, B.D.2    Kors, C.A.3    Yuan, P.4    Jardetzky, T.S.5
  • 22
    • 84869204459 scopus 로고    scopus 로고
    • Regulation of paramyxovirus fusion activation: the hemagglutinin-neuraminidase protein stabilizes the fusion protein in a pre-triggered state
    • Porotto M, Salah ZW, Gui L, Devito I, Jurgens EM, et al. (2012) Regulation of paramyxovirus fusion activation: the hemagglutinin-neuraminidase protein stabilizes the fusion protein in a pre-triggered state. J Virol 86: 12838-12848.
    • (2012) J Virol , vol.86 , pp. 12838-12848
    • Porotto, M.1    Salah, Z.W.2    Gui, L.3    Devito, I.4    Jurgens, E.M.5
  • 23
    • 84869027005 scopus 로고    scopus 로고
    • Membrane fusion triggering: three modules with different structure and function in the upper half of the measles virus attachment protein stalk
    • Navaratnarajah CK, Negi S, Braun W, Cattaneo R, (2012) Membrane fusion triggering: three modules with different structure and function in the upper half of the measles virus attachment protein stalk. J Biol Chem 287: 38543-38551.
    • (2012) J Biol Chem , vol.287 , pp. 38543-38551
    • Navaratnarajah, C.K.1    Negi, S.2    Braun, W.3    Cattaneo, R.4
  • 24
    • 84863995623 scopus 로고    scopus 로고
    • Cysteines in the stalk of the Nipah virus G glycoprotein are located in a distinct subdomain critical for fusion activation
    • Maar D, Harmon B, Chu D, Schulz B, Aguilar HC, et al. (2012) Cysteines in the stalk of the Nipah virus G glycoprotein are located in a distinct subdomain critical for fusion activation. J Virol 86: 6632-6642.
    • (2012) J Virol , vol.86 , pp. 6632-6642
    • Maar, D.1    Harmon, B.2    Chu, D.3    Schulz, B.4    Aguilar, H.C.5
  • 25
    • 78049490873 scopus 로고    scopus 로고
    • Blue native PAGE and biomolecular complementation reveal a tetrameric or higher-order oligomer organization of the physiological measles virus attachment protein H
    • Brindley MA, Plemper RK, (2010) Blue native PAGE and biomolecular complementation reveal a tetrameric or higher-order oligomer organization of the physiological measles virus attachment protein H. J Virol 84: 12174-12184.
    • (2010) J Virol , vol.84 , pp. 12174-12184
    • Brindley, M.A.1    Plemper, R.K.2
  • 26
    • 84860844283 scopus 로고    scopus 로고
    • Structural rearrangements of the central region of the morbillivirus attachment protein stalk domain trigger F protein refolding for membrane fusion
    • Ader N, Brindley MA, Avila M, Origgi FC, Langedijk J, et al. (2012) Structural rearrangements of the central region of the morbillivirus attachment protein stalk domain trigger F protein refolding for membrane fusion. J Biol Chem 287: 16324-16334.
    • (2012) J Biol Chem , vol.287 , pp. 16324-16334
    • Ader, N.1    Brindley, M.A.2    Avila, M.3    Origgi, F.C.4    Langedijk, J.5
  • 27
    • 70349747076 scopus 로고    scopus 로고
    • Probing the spatial organization of measles virus fusion complexes
    • Paal T, Brindley MA, St Clair C, Prussia A, Gaus D, et al. (2009) Probing the spatial organization of measles virus fusion complexes. J Virol 83: 10480-10493.
    • (2009) J Virol , vol.83 , pp. 10480-10493
    • Paal, T.1    Brindley, M.A.2    St Clair, C.3    Prussia, A.4    Gaus, D.5
  • 28
    • 55549116002 scopus 로고    scopus 로고
    • Residues in the stalk domain of the Hendra virus G glycoprotein modulate conformational changes associated with receptor binding
    • Bishop KA, Hickey AC, Khetawat D, Patch JR, Bossart KN, et al. (2008) Residues in the stalk domain of the Hendra virus G glycoprotein modulate conformational changes associated with receptor binding. J Virol 82: 11398-11409.
    • (2008) J Virol , vol.82 , pp. 11398-11409
    • Bishop, K.A.1    Hickey, A.C.2    Khetawat, D.3    Patch, J.R.4    Bossart, K.N.5
  • 29
    • 0028076285 scopus 로고
    • Regions on the hemagglutinin-neuraminidase proteins of human parainfluenza virus type-1 and Sendai virus important for membrane fusion
    • Bousse T, Takimoto T, Gorman WL, Takahashi T, Portner A, (1994) Regions on the hemagglutinin-neuraminidase proteins of human parainfluenza virus type-1 and Sendai virus important for membrane fusion. Virology 204: 506-514.
    • (1994) Virology , vol.204 , pp. 506-514
    • Bousse, T.1    Takimoto, T.2    Gorman, W.L.3    Takahashi, T.4    Portner, A.5
  • 30
    • 35348888403 scopus 로고    scopus 로고
    • Mutations in the stalk of the measles virus hemagglutinin protein decrease fusion but do not interfere with virus-specific interaction with the homologous fusion protein
    • Corey EA, Iorio RM, (2007) Mutations in the stalk of the measles virus hemagglutinin protein decrease fusion but do not interfere with virus-specific interaction with the homologous fusion protein. J Virol 81: 9900-9910.
    • (2007) J Virol , vol.81 , pp. 9900-9910
    • Corey, E.A.1    Iorio, R.M.2
  • 31
    • 0033524341 scopus 로고    scopus 로고
    • Mutations in the Newcastle disease virus hemagglutinin-neuraminidase protein that interfere with its ability to interact with the homologous F protein in the promotion of fusion
    • Deng R, Wang Z, Mahon PJ, Marinello M, Mirza A, et al. (1999) Mutations in the Newcastle disease virus hemagglutinin-neuraminidase protein that interfere with its ability to interact with the homologous F protein in the promotion of fusion. Virology 253: 43-54.
    • (1999) Virology , vol.253 , pp. 43-54
    • Deng, R.1    Wang, Z.2    Mahon, P.J.3    Marinello, M.4    Mirza, A.5
  • 32
    • 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 AM, Iorio RM, (1995) Localization of a domain on the paramyxovirus attachment protein required for the promotion of cellular fusion by its homologous fusion protein spike. Virology 209: 457-469.
    • (1995) Virology , vol.209 , pp. 457-469
    • Deng, R.1    Wang, Z.2    Mirza, A.M.3    Iorio, R.M.4
  • 33
    • 8644256749 scopus 로고    scopus 로고
    • Amino acid substitutions in the F-specific domain in the stalk of the Newcastle disease virus HN protein modulate fusion and interfere with its interaction with the F protein
    • Melanson VR, Iorio RM, (2004) Amino acid substitutions in the F-specific domain in the stalk of the Newcastle disease virus HN protein modulate fusion and interfere with its interaction with the F protein. J Virol 78: 13053-13061.
    • (2004) J Virol , vol.78 , pp. 13053-13061
    • Melanson, V.R.1    Iorio, R.M.2
  • 34
    • 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 VR, Iorio RM, (2006) 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 80: 623-633.
    • (2006) J Virol , vol.80 , pp. 623-633
    • Melanson, V.R.1    Iorio, R.M.2
  • 35
    • 77957199952 scopus 로고    scopus 로고
    • Mutations in the stalk region of the measles virus hemagglutinin inhibit syncytium formation but not virus entry
    • Ennis MK, Hu C, Naik SK, Hallak LK, Peng KW, et al. (2010) Mutations in the stalk region of the measles virus hemagglutinin inhibit syncytium formation but not virus entry. J Virol 84: 10913-10917.
    • (2010) J Virol , vol.84 , pp. 10913-10917
    • Ennis, M.K.1    Hu, C.2    Naik, S.K.3    Hallak, L.K.4    Peng, K.W.5
  • 36
    • 0032899490 scopus 로고    scopus 로고
    • Mutational analysis of heptad repeats in the membrane-proximal region of Newcastle disease virus HN protein
    • Stone-Hulslander J, Morrison TG, (1999) Mutational analysis of heptad repeats in the membrane-proximal region of Newcastle disease virus HN protein. J Virol 73: 3630-3637.
    • (1999) J Virol , vol.73 , pp. 3630-3637
    • Stone-Hulslander, J.1    Morrison, T.G.2
  • 37
    • 47749143663 scopus 로고    scopus 로고
    • Functional interaction between paramyxovirus fusion and attachment proteins
    • Lee JK, Prussia A, Paal T, White LK, Snyder JP, et al. (2008) Functional interaction between paramyxovirus fusion and attachment proteins. J Biol Chem 283: 16561-16572.
    • (2008) J Biol Chem , vol.283 , pp. 16561-16572
    • Lee, J.K.1    Prussia, A.2    Paal, T.3    White, L.K.4    Snyder, J.P.5
  • 38
    • 84866859065 scopus 로고    scopus 로고
    • Fusion activation by a headless parainfluenza virus 5 hemagglutinin-neuraminidase stalk suggests a modular mechanism for triggering
    • Bose S, Zokarkar A, Welch BD, Leser GP, Jardetzky TS, et al. (2012) Fusion activation by a headless parainfluenza virus 5 hemagglutinin-neuraminidase stalk suggests a modular mechanism for triggering. Proc Nat Acad Sci USA 109: E2625-E2634.
    • (2012) Proc Nat Acad Sci USA , vol.109
    • Bose, S.1    Zokarkar, A.2    Welch, B.D.3    Leser, G.P.4    Jardetzky, T.S.5
  • 39
    • 79551638780 scopus 로고    scopus 로고
    • Structure of the measles virus hemagglutinin bound to its cellular receptor SLAM
    • Hashiguchi T, Ose T, Kubota M, Maita N, Kamishikiryo J, et al. (2011) Structure of the measles virus hemagglutinin bound to its cellular receptor SLAM. Nat Struct Biol 18: 135-141.
    • (2011) Nat Struct Biol , vol.18 , pp. 135-141
    • Hashiguchi, T.1    Ose, T.2    Kubota, M.3    Maita, N.4    Kamishikiryo, J.5
  • 40
    • 84866152545 scopus 로고    scopus 로고
    • Structure of the Ulster strain Newcastle disease virus hemagglutinin-neuraminidase reveals auto-inhibitory interactions associated with low virulence
    • Yuan P, Paterson RG, Leser GP, Lamb RA, Jardetzky TS, (2012) Structure of the Ulster strain Newcastle disease virus hemagglutinin-neuraminidase reveals auto-inhibitory interactions associated with low virulence. PLoS Pathog 8: e1002855.
    • (2012) PLoS Pathog , vol.8
    • Yuan, P.1    Paterson, R.G.2    Leser, G.P.3    Lamb, R.A.4    Jardetzky, T.S.5
  • 42
    • 58149521444 scopus 로고    scopus 로고
    • Measles virus glycoprotein complex assembly, receptor attachment, and cell entry
    • Navaratnarajah CK, Leonard VH, Cattaneo R, (2009) Measles virus glycoprotein complex assembly, receptor attachment, and cell entry. Curr Top Microbiol Immunol 329: 59-76.
    • (2009) Curr Top Microbiol Immunol , vol.329 , pp. 59-76
    • Navaratnarajah, C.K.1    Leonard, V.H.2    Cattaneo, R.3
  • 43
    • 79551621397 scopus 로고    scopus 로고
    • The heads of the measles virus attachment protein move to transmit the fusion-triggering signal
    • Navaratnarajah CK, Oezguen N, Rupp L, Kay L, Leonard VH, et al. (2011) The heads of the measles virus attachment protein move to transmit the fusion-triggering signal. Nat Struct Mol Biol 18: 128-134.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 128-134
    • Navaratnarajah, C.K.1    Oezguen, N.2    Rupp, L.3    Kay, L.4    Leonard, V.H.5
  • 44
    • 55249102446 scopus 로고    scopus 로고
    • Engineered intermonomeric disulfide bonds in the globular domain of Newcastle disease virus hemagglutinin-neuraminidase protein: implications for the mechanism of fusion promotion
    • Mahon PJ, Mirza AM, Musich TA, Iorio RM, (2008) Engineered intermonomeric disulfide bonds in the globular domain of Newcastle disease virus hemagglutinin-neuraminidase protein: implications for the mechanism of fusion promotion. J Virol 82: 10386-10396.
    • (2008) J Virol , vol.82 , pp. 10386-10396
    • Mahon, P.J.1    Mirza, A.M.2    Musich, T.A.3    Iorio, R.M.4
  • 45
    • 79551652616 scopus 로고    scopus 로고
    • Measles virus fusion shifts into gear
    • Saphire EO, Oldstone MB, (2011) Measles virus fusion shifts into gear. Nat Struct Biol 18: 115-116.
    • (2011) Nat Struct Biol , vol.18 , pp. 115-116
    • Saphire, E.O.1    Oldstone, M.B.2
  • 46
    • 70350277403 scopus 로고    scopus 로고
    • Bimolecular complementation of paramyxovirus fusion and hemagglutinin-neuraminidase proteins enhances fusion: implications for the mechanism of fusion triggering
    • Connolly SA, Leser GP, Jardetzky TS, Lamb RA, (2009) Bimolecular complementation of paramyxovirus fusion and hemagglutinin-neuraminidase proteins enhances fusion: implications for the mechanism of fusion triggering. J Virol 83: 10857-10868.
    • (2009) J Virol , vol.83 , pp. 10857-10868
    • Connolly, S.A.1    Leser, G.P.2    Jardetzky, T.S.3    Lamb, R.A.4
  • 47
    • 84860234644 scopus 로고    scopus 로고
    • Paramyxovirus fusion and entry: multiple paths to a common end
    • Chang A, Dutch RE, (2012) Paramyxovirus fusion and entry: multiple paths to a common end. Viruses 4: 613-636.
    • (2012) Viruses , vol.4 , pp. 613-636
    • Chang, A.1    Dutch, R.E.2
  • 48
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • Carter J, C.W, Sweet RM, editors, San Diego: Academic Press, Inc
    • Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. In: Carter J, C.W, Sweet RM, editors. Methods in Enzymology. San Diego: Academic Press, Inc. pp. 307-326.
    • (1997) Methods in Enzymology , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 49
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P, Cowtan K, (2004) Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 60: 2126-2132.
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 52
    • 3242892054 scopus 로고    scopus 로고
    • MONSTER: inferring non-covalent interactions in macromolecular structures from atomic coordinate data
    • Salerno WJ, Seaver SM, Armstrong BR, Radhakrishnan I, (2004) MONSTER: inferring non-covalent interactions in macromolecular structures from atomic coordinate data. Nucleic Acids Res 32: W566-W568.
    • (2004) Nucleic Acids Res , vol.32
    • Salerno, W.J.1    Seaver, S.M.2    Armstrong, B.R.3    Radhakrishnan, I.4
  • 53
    • 58549102514 scopus 로고    scopus 로고
    • Functional analysis of the transmembrane domain in paramyxovirus F protein-mediated membrane fusion
    • Bissonnette ML, Donald JE, DeGrado WF, Jardetzky TS, Lamb RA, (2009) Functional analysis of the transmembrane domain in paramyxovirus F protein-mediated membrane fusion. J Mol Biol 386: 14-36.
    • (2009) J Mol Biol , vol.386 , pp. 14-36
    • Bissonnette, M.L.1    Donald, J.E.2    DeGrado, W.F.3    Jardetzky, T.S.4    Lamb, R.A.5
  • 54
  • 55
    • 34547559704 scopus 로고    scopus 로고
    • PDB2PQR: exapanding and upgrading automated preparation of biomolecular structures for molecular simulations
    • Dolinsky TJ, Czodrowski P, Nielsen JE, Klebe G, Baker NA, (2007) PDB2PQR: exapanding and upgrading automated preparation of biomolecular structures for molecular simulations. Nucleic Acids Res 35: W222-W225.
    • (2007) Nucleic Acids Res , vol.35
    • Dolinsky, T.J.1    Czodrowski, P.2    Nielsen, J.E.3    Klebe, G.4    Baker, N.A.5
  • 56
    • 3242886771 scopus 로고    scopus 로고
    • PDB2PQR: an automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations
    • Dolinsky TJ, Nielsen JE, McCammon JA, Baker NA, (2004) PDB2PQR: an automated pipeline for the setup of Poisson-Boltzmann electrostatics calculations. Nucleic Acids Res 32: W665-W667.
    • (2004) Nucleic Acids Res , vol.32
    • Dolinsky, T.J.1    Nielsen, J.E.2    McCammon, J.A.3    Baker, N.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.