메뉴 건너뛰기




Volumn 11, Issue 7, 2015, Pages

Characterization of a Prefusion-Specific Antibody That Recognizes a Quaternary, Cleavage-Dependent Epitope on the RSV Fusion Glycoprotein

Author keywords

[No Author keywords available]

Indexed keywords

EPITOPE; GLYCOPROTEIN; HYBRID PROTEIN; IMMUNOGLOBULIN G; NEUTRALIZING ANTIBODY; RESPIRATORY SYNCYTIAL VIRUS ANTIBODY; VIRUS ANTIBODY; VIRUS ANTIGEN;

EID: 84938801217     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1005035     Document Type: Article
Times cited : (107)

References (52)
  • 1
    • 0022589125 scopus 로고
    • Risk of primary infection and reinfection with respiratory syncytial virus
    • Glezen WP, Taber LH, Frank AL, Kasel JA, Risk of primary infection and reinfection with respiratory syncytial virus. Am J Dis Child. 1986;140(6): 543–546. 3706232
    • (1986) Am J Dis Child , vol.140 , Issue.6 , pp. 543-546
    • Glezen, W.P.1    Taber, L.H.2    Frank, A.L.3    Kasel, J.A.4
  • 2
    • 84871036375 scopus 로고    scopus 로고
    • Global and regional mortality from 235 causes of death for 20 age groups in 1990 and 2010: a systematic analysis for the Global Burden of Disease Study 2010
    • Lozano R, Naghavi M, Foreman K, Lim S, Shibuya K, Aboyans V, et al. Global and regional mortality from 235 causes of death for 20 age groups in 1990 and 2010: a systematic analysis for the Global Burden of Disease Study 2010. Lancet. 2012;380(9859): 2095–2128. doi: 10.1016/S0140-6736(12)61728-0 23245604
    • (2012) Lancet , vol.380 , Issue.9859 , pp. 2095-2128
    • Lozano, R.1    Naghavi, M.2    Foreman, K.3    Lim, S.4    Shibuya, K.5    Aboyans, V.6
  • 3
    • 84920405800 scopus 로고    scopus 로고
    • Respiratory syncytial virus-associated mortality in hospitalized infants and young children
    • Byington CL, Wilkes J, Korgenski K, Sheng X, Respiratory syncytial virus-associated mortality in hospitalized infants and young children. Pediatrics. 2015;135(1): e24–31. doi: 10.1542/peds.2014-2151 25489019
    • (2015) Pediatrics , vol.135 , Issue.1 , pp. e24-31
    • Byington, C.L.1    Wilkes, J.2    Korgenski, K.3    Sheng, X.4
  • 4
    • 0344153462 scopus 로고    scopus 로고
    • Recent trends in severe respiratory syncytial virus (RSV) among US infants, 1997 to 2000
    • Leader S, Kohlhase K, Recent trends in severe respiratory syncytial virus (RSV) among US infants, 1997 to 2000. J Pediatr. 2003;143(5 Suppl): S127–132. 14615711
    • (2003) J Pediatr , vol.143 , pp. S127-132
    • Leader, S.1    Kohlhase, K.2
  • 5
    • 84938368964 scopus 로고    scopus 로고
    • Effectiveness of Palivizumab in Preventing RSV Hospitalization in High Risk Children: A Real-World Perspective
    • Homaira N, Rawlinson W, Snelling TL, Jaffe A, Effectiveness of Palivizumab in Preventing RSV Hospitalization in High Risk Children: A Real-World Perspective. Int J Pediatr. 2014;2014: 571609. doi: 10.1155/2014/571609 25548575
    • (2014) Int J Pediatr , vol.2014 , pp. 571609
    • Homaira, N.1    Rawlinson, W.2    Snelling, T.L.3    Jaffe, A.4
  • 6
    • 0031683919 scopus 로고    scopus 로고
    • Palivizumab, a humanized respiratory syncytial virus monoclonal antibody, reduces hospitalization from respiratory syncytial virus infection in high-risk infants
    • The IMpact-RSV Study Group. Palivizumab, a humanized respiratory syncytial virus monoclonal antibody, reduces hospitalization from respiratory syncytial virus infection in high-risk infants. Pediatrics. 1998;102(3 Pt 1): 531–537. 9738173
    • (1998) Pediatrics , vol.102 , Issue.3 , pp. 531-537
  • 7
    • 0036821671 scopus 로고    scopus 로고
    • Economic analyses of respiratory syncytial virus immunoprophylaxis in high-risk infants: a systematic review
    • Kamal-Bahl S, Doshi J, Campbell J, Economic analyses of respiratory syncytial virus immunoprophylaxis in high-risk infants: a systematic review. Arch Pediatr Adolesc Med. 2002;156(10): 1034–1041. 12361451
    • (2002) Arch Pediatr Adolesc Med , vol.156 , Issue.10 , pp. 1034-1041
    • Kamal-Bahl, S.1    Doshi, J.2    Campbell, J.3
  • 8
    • 0031457568 scopus 로고    scopus 로고
    • Respiratory syncytial virus (RSV) SH and G proteins are not essential for viral replication in vitro: clinical evaluation and molecular characterization of a cold-passaged, attenuated RSV subgroup B mutant
    • Karron RA, Buonagurio DA, Georgiu AF, Whitehead SS, Adamus JE, Clements-Mann ML, et al. Respiratory syncytial virus (RSV) SH and G proteins are not essential for viral replication in vitro: clinical evaluation and molecular characterization of a cold-passaged, attenuated RSV subgroup B mutant. Proc Natl Acad Sci U S A. 1997;94(25): 13961–13966. 9391135
    • (1997) Proc Natl Acad Sci U S A , vol.94 , Issue.25 , pp. 13961-13966
    • Karron, R.A.1    Buonagurio, D.A.2    Georgiu, A.F.3    Whitehead, S.S.4    Adamus, J.E.5    Clements-Mann, M.L.6
  • 9
    • 0024320889 scopus 로고
    • Neutralization epitopes of the F glycoprotein of respiratory syncytial virus: effect of mutation upon fusion function
    • Beeler JA, van Wyke Coelingh K, Neutralization epitopes of the F glycoprotein of respiratory syncytial virus: effect of mutation upon fusion function. J Virol. 1989;63(7): 2941–2950. 2470922
    • (1989) J Virol , vol.63 , Issue.7 , pp. 2941-2950
    • Beeler, J.A.1    van Wyke Coelingh, K.2
  • 10
    • 16944363559 scopus 로고    scopus 로고
    • Development of a humanized monoclonal antibody (MEDI-493) with potent in vitro and in vivo activity against respiratory syncytial virus
    • Johnson S, Oliver C, Prince GA, Hemming VG, Pfarr DS, Wang SC, et al. Development of a humanized monoclonal antibody (MEDI-493) with potent in vitro and in vivo activity against respiratory syncytial virus. J Infect Dis. 1997;176(5): 1215–1224. 9359721
    • (1997) J Infect Dis , vol.176 , Issue.5 , pp. 1215-1224
    • Johnson, S.1    Oliver, C.2    Prince, G.A.3    Hemming, V.G.4    Pfarr, D.S.5    Wang, S.C.6
  • 11
    • 76349122922 scopus 로고    scopus 로고
    • Structural basis of respiratory syncytial virus neutralization by motavizumab
    • McLellan JS, Chen M, Kim A, Yang Y, Graham BS, Kwong PD, Structural basis of respiratory syncytial virus neutralization by motavizumab. Nat Struct Mol Biol. 2010;17(2): 248–250. doi: 10.1038/nsmb.1723 20098425
    • (2010) Nat Struct Mol Biol , vol.17 , Issue.2 , pp. 248-250
    • McLellan, J.S.1    Chen, M.2    Kim, A.3    Yang, Y.4    Graham, B.S.5    Kwong, P.D.6
  • 12
    • 17844362436 scopus 로고    scopus 로고
    • Comparison of affinity chromatography and adsorption to vaccinia virus recombinant infected cells for depletion of antibodies directed against respiratory syncytial virus glycoproteins present in a human immunoglobulin preparation
    • Sastre P, Melero JA, Garcia-Barreno B, Palomo C, Comparison of affinity chromatography and adsorption to vaccinia virus recombinant infected cells for depletion of antibodies directed against respiratory syncytial virus glycoproteins present in a human immunoglobulin preparation. J Med Virol. 2005;76(2): 248–255. 15834867
    • (2005) J Med Virol , vol.76 , Issue.2 , pp. 248-255
    • Sastre, P.1    Melero, J.A.2    Garcia-Barreno, B.3    Palomo, C.4
  • 13
    • 0035859824 scopus 로고    scopus 로고
    • Cleavage of the human respiratory syncytial virus fusion protein at two distinct sites is required for activation of membrane fusion
    • Gonzalez-Reyes L, Ruiz-Arguello MB, Garcia-Barreno B, Calder L, Lopez JA, Albar JP, et al. Cleavage of the human respiratory syncytial virus fusion protein at two distinct sites is required for activation of membrane fusion. Proc Natl Acad Sci U S A. 2001;98(17): 9859–9864. 11493675
    • (2001) Proc Natl Acad Sci U S A , vol.98 , Issue.17 , pp. 9859-9864
    • Gonzalez-Reyes, L.1    Ruiz-Arguello, M.B.2    Garcia-Barreno, B.3    Calder, L.4    Lopez, J.A.5    Albar, J.P.6
  • 14
    • 0033876915 scopus 로고    scopus 로고
    • Cleavage of the respiratory syncytial virus fusion protein is required for its surface expression: role of furin
    • Bolt G, Pedersen LO, Birkeslund HH, Cleavage of the respiratory syncytial virus fusion protein is required for its surface expression: role of furin. Virus Res. 2000;68(1): 25–33. 10930660
    • (2000) Virus Res , vol.68 , Issue.1 , pp. 25-33
    • Bolt, G.1    Pedersen, L.O.2    Birkeslund, H.H.3
  • 15
    • 0036376658 scopus 로고    scopus 로고
    • Effect of proteolytic processing at two distinct sites on shape and aggregation of an anchorless fusion protein of human respiratory syncytial virus and fate of the intervening segment
    • Begona Ruiz-Arguello M, Gonzalez-Reyes L, Calder LJ, Palomo C, Martin D, Saiz MJ, et al. Effect of proteolytic processing at two distinct sites on shape and aggregation of an anchorless fusion protein of human respiratory syncytial virus and fate of the intervening segment. Virology. 2002;298(2): 317–326. 12127793
    • (2002) Virology , vol.298 , Issue.2 , pp. 317-326
    • Begona Ruiz-Arguello, M.1    Gonzalez-Reyes, L.2    Calder, L.J.3    Palomo, C.4    Martin, D.5    Saiz, M.J.6
  • 16
    • 0017404533 scopus 로고
    • Two disulfide-linked polypeptide chains constitute the active F protein of paramyxoviruses
    • Scheid A, Choppin PW, Two disulfide-linked polypeptide chains constitute the active F protein of paramyxoviruses. Virology. 1977;80(1): 54–66. 195398
    • (1977) Virology , vol.80 , Issue.1 , pp. 54-66
    • Scheid, A.1    Choppin, P.W.2
  • 17
    • 79959338198 scopus 로고    scopus 로고
    • Structural basis for immunization with postfusion respiratory syncytial virus fusion F glycoprotein (RSV F) to elicit high neutralizing antibody titers
    • Swanson KA, Settembre EC, Shaw CA, Dey AK, Rappuoli R, Mandl CW, et al. Structural basis for immunization with postfusion respiratory syncytial virus fusion F glycoprotein (RSV F) to elicit high neutralizing antibody titers. Proc Natl Acad Sci U S A. 2011;108(23): 9619–9624. doi: 10.1073/pnas.1106536108 21586636
    • (2011) Proc Natl Acad Sci U S A , vol.108 , Issue.23 , pp. 9619-9624
    • Swanson, K.A.1    Settembre, E.C.2    Shaw, C.A.3    Dey, A.K.4    Rappuoli, R.5    Mandl, C.W.6
  • 18
    • 79960387921 scopus 로고    scopus 로고
    • Structure of respiratory syncytial virus fusion glycoprotein in the postfusion conformation reveals preservation of neutralizing epitopes
    • McLellan JS, Yang Y, Graham BS, Kwong PD, Structure of respiratory syncytial virus fusion glycoprotein in the postfusion conformation reveals preservation of neutralizing epitopes. J Virol. 2011;85(15): 7788–7796. doi: 10.1128/JVI.00555-11 21613394
    • (2011) J Virol , vol.85 , Issue.15 , pp. 7788-7796
    • McLellan, J.S.1    Yang, Y.2    Graham, B.S.3    Kwong, P.D.4
  • 19
    • 84878349946 scopus 로고    scopus 로고
    • Structure of RSV fusion glycoprotein trimer bound to a prefusion-specific neutralizing antibody
    • McLellan JS, Chen M, Leung S, Graepel KW, Du X, Yang Y, et al. Structure of RSV fusion glycoprotein trimer bound to a prefusion-specific neutralizing antibody. Science. 2013;340(6136): 1113–1117. doi: 10.1126/science.1234914 23618766
    • (2013) Science , vol.340 , Issue.6136 , pp. 1113-1117
    • McLellan, J.S.1    Chen, M.2    Leung, S.3    Graepel, K.W.4    Du, X.5    Yang, Y.6
  • 20
    • 84892747352 scopus 로고    scopus 로고
    • Structure and function of respiratory syncytial virus surface glycoproteins
    • McLellan JS, Ray WC, Peeples ME, Structure and function of respiratory syncytial virus surface glycoproteins. Curr Top Microbiol Immunol. 2013;372: 83–104. doi: 10.1007/978-3-642-38919-1_4 24362685
    • (2013) Curr Top Microbiol Immunol , vol.372 , pp. 83-104
    • McLellan, J.S.1    Ray, W.C.2    Peeples, M.E.3
  • 21
    • 84879707555 scopus 로고    scopus 로고
    • Architecture of respiratory syncytial virus revealed by electron cryotomography
    • Liljeroos L, Krzyzaniak MA, Helenius A, Butcher SJ, Architecture of respiratory syncytial virus revealed by electron cryotomography. Proc Natl Acad Sci U S A. 2013;110(27): 11133–11138. doi: 10.1073/pnas.1309070110 23776214
    • (2013) Proc Natl Acad Sci U S A , vol.110 , Issue.27 , pp. 11133-11138
    • Liljeroos, L.1    Krzyzaniak, M.A.2    Helenius, A.3    Butcher, S.J.4
  • 22
    • 78049495019 scopus 로고    scopus 로고
    • Structure of a major antigenic site on the respiratory syncytial virus fusion glycoprotein in complex with neutralizing antibody 101F
    • McLellan JS, Chen M, Chang JS, Yang Y, Kim A, Graham BS, et al. Structure of a major antigenic site on the respiratory syncytial virus fusion glycoprotein in complex with neutralizing antibody 101F. J Virol. 2010;84(23): 12236–12244. doi: 10.1128/JVI.01579-10 20881049
    • (2010) J Virol , vol.84 , Issue.23 , pp. 12236-12244
    • McLellan, J.S.1    Chen, M.2    Chang, J.S.3    Yang, Y.4    Kim, A.5    Graham, B.S.6
  • 23
    • 73849116425 scopus 로고    scopus 로고
    • Generation of stable monoclonal antibody-producing B cell receptor-positive human memory B cells by genetic programming
    • Kwakkenbos MJ, Diehl SA, Yasuda E, Bakker AQ, van Geelen CM, Lukens MV, et al. Generation of stable monoclonal antibody-producing B cell receptor-positive human memory B cells by genetic programming. Nat Med. 2010;16(1): 123–128. doi: 10.1038/nm.2071 20023635
    • (2010) Nat Med , vol.16 , Issue.1 , pp. 123-128
    • Kwakkenbos, M.J.1    Diehl, S.A.2    Yasuda, E.3    Bakker, A.Q.4    van Geelen, C.M.5    Lukens, M.V.6
  • 24
    • 84857410882 scopus 로고    scopus 로고
    • Neutralizing antibodies against the preactive form of respiratory syncytial virus fusion protein offer unique possibilities for clinical intervention
    • Magro M, Mas V, Chappell K, Vazquez M, Cano O, Luque D, et al. Neutralizing antibodies against the preactive form of respiratory syncytial virus fusion protein offer unique possibilities for clinical intervention. Proc Natl Acad Sci U S A. 2012;109(8): 3089–3094. doi: 10.1073/pnas.1115941109 22323598
    • (2012) Proc Natl Acad Sci U S A , vol.109 , Issue.8 , pp. 3089-3094
    • Magro, M.1    Mas, V.2    Chappell, K.3    Vazquez, M.4    Cano, O.5    Luque, D.6
  • 25
    • 84884413000 scopus 로고    scopus 로고
    • Cross-neutralization of four paramyxoviruses by a human monoclonal antibody
    • Corti D, Bianchi S, Vanzetta F, Minola A, Perez L, Agatic G, et al. Cross-neutralization of four paramyxoviruses by a human monoclonal antibody. Nature. 2013;501(7467): 439–443. doi: 10.1038/nature12442 23955151
    • (2013) Nature , vol.501 , Issue.7467 , pp. 439-443
    • Corti, D.1    Bianchi, S.2    Vanzetta, F.3    Minola, A.4    Perez, L.5    Agatic, G.6
  • 26
    • 84887277978 scopus 로고    scopus 로고
    • Structure-based design of a fusion glycoprotein vaccine for respiratory syncytial virus
    • McLellan JS, Chen M, Joyce MG, Sastry M, Stewart-Jones GB, Yang Y, et al. Structure-based design of a fusion glycoprotein vaccine for respiratory syncytial virus. Science. 2013;342(6158): 592–598. doi: 10.1126/science.1243283 24179220
    • (2013) Science , vol.342 , Issue.6158 , pp. 592-598
    • McLellan, J.S.1    Chen, M.2    Joyce, M.G.3    Sastry, M.4    Stewart-Jones, G.B.5    Yang, Y.6
  • 27
    • 84907916697 scopus 로고    scopus 로고
    • A monomeric uncleaved respiratory syncytial virus F antigen retains prefusion-specific neutralizing epitopes
    • Swanson KA, Balabanis K, Xie Y, Aggarwal Y, Palomo C, Mas V, et al. A monomeric uncleaved respiratory syncytial virus F antigen retains prefusion-specific neutralizing epitopes. J Virol. 2014;88(20): 11802–11810. doi: 10.1128/JVI.01225-14 25078705
    • (2014) J Virol , vol.88 , Issue.20 , pp. 11802-11810
    • Swanson, K.A.1    Balabanis, K.2    Xie, Y.3    Aggarwal, Y.4    Palomo, C.5    Mas, V.6
  • 28
    • 20244381798 scopus 로고    scopus 로고
    • A direct comparison of the activities of two humanized respiratory syncytial virus monoclonal antibodies: MEDI-493 and RSHZl9
    • Johnson S, Griego SD, Pfarr DS, Doyle ML, Woods R, Carlin D, et al. A direct comparison of the activities of two humanized respiratory syncytial virus monoclonal antibodies: MEDI-493 and RSHZl9. J Infect Dis. 1999;180(1): 35–40. 10353858
    • (1999) J Infect Dis , vol.180 , Issue.1 , pp. 35-40
    • Johnson, S.1    Griego, S.D.2    Pfarr, D.S.3    Doyle, M.L.4    Woods, R.5    Carlin, D.6
  • 29
    • 84900467984 scopus 로고    scopus 로고
    • Structural delineation of a quaternary, cleavage-dependent epitope at the gp41-gp120 interface on intact HIV-1 Env trimers
    • Blattner C, Lee JH, Sliepen K, Derking R, Falkowska E, de la Pena AT, et al. Structural delineation of a quaternary, cleavage-dependent epitope at the gp41-gp120 interface on intact HIV-1 Env trimers. Immunity. 2014;40(5): 669–680. doi: 10.1016/j.immuni.2014.04.008 24768348
    • (2014) Immunity , vol.40 , Issue.5 , pp. 669-680
    • Blattner, C.1    Lee, J.H.2    Sliepen, K.3    Derking, R.4    Falkowska, E.5    de la Pena, A.T.6
  • 30
    • 84921607768 scopus 로고    scopus 로고
    • Broad and potent HIV-1 neutralization by a human antibody that binds the gp41-gp120 interface
    • Huang J, Kang BH, Pancera M, Lee JH, Tong T, Feng Y, et al. Broad and potent HIV-1 neutralization by a human antibody that binds the gp41-gp120 interface. Nature. 2014;515(7525): 138–142. doi: 10.1038/nature13601 25186731
    • (2014) Nature , vol.515 , Issue.7525 , pp. 138-142
    • Huang, J.1    Kang, B.H.2    Pancera, M.3    Lee, J.H.4    Tong, T.5    Feng, Y.6
  • 31
    • 84883292796 scopus 로고    scopus 로고
    • Influenza A virus hemagglutinin trimerization completes monomer folding and antigenicity
    • Magadan JG, Khurana S, Das SR, Frank GM, Stevens J, Golding H, et al. Influenza A virus hemagglutinin trimerization completes monomer folding and antigenicity. J Virol. 2013;87(17): 9742–9753. doi: 10.1128/JVI.00471-13 23824811
    • (2013) J Virol , vol.87 , Issue.17 , pp. 9742-9753
    • Magadan, J.G.1    Khurana, S.2    Das, S.R.3    Frank, G.M.4    Stevens, J.5    Golding, H.6
  • 32
    • 84900517557 scopus 로고    scopus 로고
    • Broadly neutralizing HIV antibodies define a glycan-dependent epitope on the prefusion conformation of gp41 on cleaved envelope trimers
    • Falkowska E, Le KM, Ramos A, Doores KJ, Lee JH, Blattner C, et al. Broadly neutralizing HIV antibodies define a glycan-dependent epitope on the prefusion conformation of gp41 on cleaved envelope trimers. Immunity. 2014;40(5): 657–668. doi: 10.1016/j.immuni.2014.04.009 24768347
    • (2014) Immunity , vol.40 , Issue.5 , pp. 657-668
    • Falkowska, E.1    Le, K.M.2    Ramos, A.3    Doores, K.J.4    Lee, J.H.5    Blattner, C.6
  • 33
    • 0033869414 scopus 로고    scopus 로고
    • A neutralizing antibody Fab-influenza haemagglutinin complex with an unprecedented 2:1 stoichiometry: characterization and crystallization
    • Gigant B, Barbey-Martin C, Bizebard T, Fleury D, Daniels R, Skehel JJ, et al. A neutralizing antibody Fab-influenza haemagglutinin complex with an unprecedented 2:1 stoichiometry: characterization and crystallization. Acta Crystallogr D Biol Crystallogr. 2000;56(Pt 8): 1067–1069. 10944356
    • (2000) Acta Crystallogr D Biol Crystallogr , vol.56 , pp. 1067-1069
    • Gigant, B.1    Barbey-Martin, C.2    Bizebard, T.3    Fleury, D.4    Daniels, R.5    Skehel, J.J.6
  • 35
    • 84926366727 scopus 로고    scopus 로고
    • Recognition determinants of broadly neutralizing human antibodies against dengue viruses
    • Rouvinski A, Guardado-Calvo P, Barba-Spaeth G, Duquerroy S, Vaney MC, Kikuti CM, et al. Recognition determinants of broadly neutralizing human antibodies against dengue viruses. Nature. 2015;520(7545): 109–113. doi: 10.1038/nature14130 25581790
    • (2015) Nature , vol.520 , Issue.7545 , pp. 109-113
    • Rouvinski, A.1    Guardado-Calvo, P.2    Barba-Spaeth, G.3    Duquerroy, S.4    Vaney, M.C.5    Kikuti, C.M.6
  • 36
    • 78650495030 scopus 로고    scopus 로고
    • Neutralization of West Nile virus by cross-linking of its surface proteins with Fab fragments of the human monoclonal antibody CR4354
    • Kaufmann B, Vogt MR, Goudsmit J, Holdaway HA, Aksyuk AA, Chipman PR, et al. Neutralization of West Nile virus by cross-linking of its surface proteins with Fab fragments of the human monoclonal antibody CR4354. Proc Natl Acad Sci U S A. 2010;107(44): 18950–18955. doi: 10.1073/pnas.1011036107 20956322
    • (2010) Proc Natl Acad Sci U S A , vol.107 , Issue.44 , pp. 18950-18955
    • Kaufmann, B.1    Vogt, M.R.2    Goudsmit, J.3    Holdaway, H.A.4    Aksyuk, A.A.5    Chipman, P.R.6
  • 37
    • 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, Structure of the parainfluenza virus 5 F protein in its metastable, prefusion conformation. Nature. 2006;439(7072): 38–44. 16397490
    • (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
  • 38
    • 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, Lamb RA, Structure of the cleavage-activated prefusion form of the parainfluenza virus 5 fusion protein. Proc Natl Acad Sci U S A. 2012;109(41): 16672–16677. doi: 10.1073/pnas.1213802109 23012473
    • (2012) Proc Natl Acad Sci U S A , vol.109 , Issue.41 , pp. 16672-16677
    • Welch, B.D.1    Liu, Y.2    Kors, C.A.3    Leser, G.P.4    Jardetzky, T.S.5    Lamb, R.A.6
  • 39
    • 0023006195 scopus 로고
    • Assembly of influenza hemagglutinin trimers and its role in intracellular transport
    • Copeland CS, Doms RW, Bolzau EM, Webster RG, Helenius A, Assembly of influenza hemagglutinin trimers and its role in intracellular transport. J Cell Biol. 1986;103(4): 1179–1191. 2429970
    • (1986) J Cell Biol , vol.103 , Issue.4 , pp. 1179-1191
    • Copeland, C.S.1    Doms, R.W.2    Bolzau, E.M.3    Webster, R.G.4    Helenius, A.5
  • 40
    • 0024296435 scopus 로고
    • Monoclonal antibodies localize events in the folding, assembly, and intracellular transport of the influenza virus hemagglutinin glycoprotein
    • Yewdell JW, Yellen A, Bachi T, Monoclonal antibodies localize events in the folding, assembly, and intracellular transport of the influenza virus hemagglutinin glycoprotein. Cell. 1988;52(6): 843–852. 2450677
    • (1988) Cell , vol.52 , Issue.6 , pp. 843-852
    • Yewdell, J.W.1    Yellen, A.2    Bachi, T.3
  • 41
    • 25644458666 scopus 로고    scopus 로고
    • Automated electron microscope tomography using robust prediction of specimen movements
    • Mastronarde DN, Automated electron microscope tomography using robust prediction of specimen movements. J Struct Biol. 2005;152(1): 36–51. 16182563
    • (2005) J Struct Biol , vol.152 , Issue.1 , pp. 36-51
    • Mastronarde, D.N.1
  • 42
    • 33845332754 scopus 로고    scopus 로고
    • EMAN2: an extensible image processing suite for electron microscopy
    • Tang G, Peng L, Baldwin PR, Mann DS, Jiang W, Rees I, et al. EMAN2: an extensible image processing suite for electron microscopy. J Struct Biol. 2007;157(1): 38–46. 16859925
    • (2007) J Struct Biol , vol.157 , Issue.1 , pp. 38-46
    • Tang, G.1    Peng, L.2    Baldwin, P.R.3    Mann, D.S.4    Jiang, W.5    Rees, I.6
  • 45
    • 84879367781 scopus 로고    scopus 로고
    • How good are my data and what is the resolution?
    • Evans PR, Murshudov GN, How good are my data and what is the resolution? Acta Crystallogr D Biol Crystallogr. 2013;69(Pt 7): 1204–1214. doi: 10.1107/S0907444913000061 23793146
    • (2013) Acta Crystallogr D Biol Crystallogr , vol.69 , pp. 1204-1214
    • Evans, P.R.1    Murshudov, G.N.2
  • 47
    • 84865994337 scopus 로고    scopus 로고
    • Molecular basis for negative regulation of the glucagon receptor
    • Koth CM, Murray JM, Mukund S, Madjidi A, Minn A, Clarke HJ, et al. Molecular basis for negative regulation of the glucagon receptor. Proc Natl Acad Sci U S A. 2012;109(36): 14393–14398. doi: 10.1073/pnas.1206734109 22908259
    • (2012) Proc Natl Acad Sci U S A , vol.109 , Issue.36 , pp. 14393-14398
    • Koth, C.M.1    Murray, J.M.2    Mukund, S.3    Madjidi, A.4    Minn, A.5    Clarke, H.J.6
  • 48
    • 13244281317 scopus 로고    scopus 로고
    • Coot: model-building tools for molecular graphics
    • Emsley P, Cowtan K, Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr. 2004;60(Pt 12 Pt 1): 2126–2132. 15572765
    • (2004) Acta Crystallogr D Biol Crystallogr , vol.60 , pp. 2126-2132
    • Emsley, P.1    Cowtan, K.2
  • 50
    • 20444363121 scopus 로고    scopus 로고
    • Ultra-potent antibodies against respiratory syncytial virus: effects of binding kinetics and binding valence on viral neutralization
    • Wu H, Pfarr DS, Tang Y, An LL, Patel NK, Watkins JD, et al. Ultra-potent antibodies against respiratory syncytial virus: effects of binding kinetics and binding valence on viral neutralization. J Mol Biol. 2005;350(1): 126–144. 15907931
    • (2005) J Mol Biol , vol.350 , Issue.1 , pp. 126-144
    • Wu, H.1    Pfarr, D.S.2    Tang, Y.3    An, L.L.4    Patel, N.K.5    Watkins, J.D.6
  • 51
    • 2342563850 scopus 로고    scopus 로고
    • RhoA-derived peptide dimers share mechanistic properties with other polyanionic inhibitors of respiratory syncytial virus (RSV), including disruption of viral attachment and dependence on RSV G
    • Budge PJ, Li Y, Beeler JA, Graham BS, RhoA-derived peptide dimers share mechanistic properties with other polyanionic inhibitors of respiratory syncytial virus (RSV), including disruption of viral attachment and dependence on RSV G. J Virol. 2004;78(10): 5015–5022. 15113882
    • (2004) J Virol , vol.78 , Issue.10 , pp. 5015-5022
    • Budge, P.J.1    Li, Y.2    Beeler, J.A.3    Graham, B.S.4
  • 52
    • 77958456819 scopus 로고    scopus 로고
    • A flow cytometry-based assay to assess RSV-specific neutralizing antibody is reproducible, efficient and accurate
    • Chen M, Chang JS, Nason M, Rangel D, Gall JG, Graham BS, et al. A flow cytometry-based assay to assess RSV-specific neutralizing antibody is reproducible, efficient and accurate. J Immunol Methods. 2010;362(1–2): 180–184. doi: 10.1016/j.jim.2010.08.005 20727896
    • (2010) J Immunol Methods , vol.362 , Issue.1-2 , pp. 180-184
    • Chen, M.1    Chang, J.S.2    Nason, M.3    Rangel, D.4    Gall, J.G.5    Graham, B.S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.