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Volumn 92, Issue 4, 2018, Pages

Glycan shield and fusion activation of a deltacoronavirus spike glycoprotein fine-tuned for enteric infections

Author keywords

Coronaviruses; Cryo EM; Fusion proteins

Indexed keywords

AMINO ACID; GLYCAN; NEUTRALIZING ANTIBODY; PROTEINASE; VIRUS FUSION PROTEIN; VIRUS SPIKE PROTEIN; CORONAVIRUS SPIKE GLYCOPROTEIN; POLYSACCHARIDE;

EID: 85041238304     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.01628-17     Document Type: Article
Times cited : (120)

References (77)
  • 1
  • 2
    • 84957045369 scopus 로고    scopus 로고
    • Middle East respiratory syndrome and severe acute respiratory syndrome
    • Vijay R, Perlman S. 2016. Middle East respiratory syndrome and severe acute respiratory syndrome. Curr Opin Virol 16:70-76. https://doi.org/10.1016/j.coviro.2016.01.011
    • (2016) Curr Opin Virol , vol.16 , pp. 70-76
    • Vijay, R.1    Perlman, S.2
  • 3
    • 84894208443 scopus 로고    scopus 로고
    • Host adaptation and transmission of influenza A viruses in mammals
    • Schrauwen EJ, Fouchier RA. 2014. Host adaptation and transmission of influenza A viruses in mammals. Emerg Microbes Infect 3:e9. https://doi .org/10.1038/emi.2014.9
    • (2014) Emerg Microbes Infect , vol.3 , pp. e9
    • Schrauwen, E.J.1    Fouchier, R.A.2
  • 4
    • 24944498409 scopus 로고    scopus 로고
    • Structure of SARS coronavirus spike receptor-binding domain complexed with receptor
    • Li F, Li W, Farzan M, Harrison SC. 2005. Structure of SARS coronavirus spike receptor-binding domain complexed with receptor. Science 309: 1864-1868. https://doi.org/10.1126/science.1116480
    • (2005) Science , vol.309 , pp. 1864-1868
    • Li, F.1    Li, W.2    Farzan, M.3    Harrison, S.C.4
  • 8
    • 84906658079 scopus 로고    scopus 로고
    • Receptor usage and cell entry of bat coronavirus HKU4 provide insight into bat-to-human transmission of MERS coronavirus
    • Yang Y, Du L, Liu C, Wang L, Ma C, Tang J, Baric RS, Jiang S, Li F. 2014. Receptor usage and cell entry of bat coronavirus HKU4 provide insight into bat-to-human transmission of MERS coronavirus. Proc Natl Acad Sci U S A 111:12516-12521. https://doi.org/10.1073/pnas.1405889111
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 12516-12521
    • Yang, Y.1    Du, L.2    Liu, C.3    Wang, L.4    Ma, C.5    Tang, J.6    Baric, R.S.7    Jiang, S.8    Li, F.9
  • 10
    • 84930047858 scopus 로고    scopus 로고
    • Host cell proteases: critical determinants of coronavirus tropism and pathogenesis
    • Millet JK, Whittaker GR. 2015. Host cell proteases: critical determinants of coronavirus tropism and pathogenesis. Virus Res 202:120-134. https://doi.org/10.1016/j.virusres.2014.11.021
    • (2015) Virus Res , vol.202 , pp. 120-134
    • Millet, J.K.1    Whittaker, G.R.2
  • 11
    • 65249097210 scopus 로고    scopus 로고
    • Activation of the SARS coronavirus spike protein via sequential proteolytic cleavage at two distinct sites
    • Belouzard S, Chu VC, Whittaker GR. 2009. Activation of the SARS coronavirus spike protein via sequential proteolytic cleavage at two distinct sites. Proc Natl Acad Sci U S A 106:5871-5876. https://doi.org/10.1073/pnas.0809524106
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 5871-5876
    • Belouzard, S.1    Chu, V.C.2    Whittaker, G.R.3
  • 13
    • 84908065761 scopus 로고    scopus 로고
    • Host cell entry of Middle East respiratory syndrome coronavirus after two-step, furin-mediated activation of the spike protein
    • Millet JK, Whittaker GR. 2014. Host cell entry of Middle East respiratory syndrome coronavirus after two-step, furin-mediated activation of the spike protein. Proc Natl Acad Sci U S A 111:15214-15219. https://doi .org/10.1073/pnas.1407087111
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 15214-15219
    • Millet, J.K.1    Whittaker, G.R.2
  • 14
    • 84938933311 scopus 로고    scopus 로고
    • Two mutations were critical for bat-to-human transmission of Middle East respiratory syndrome coronavirus
    • Yang Y, Liu C, Du L, Jiang S, Shi Z, Baric RS, Li F. 2015. Two mutations were critical for bat-to-human transmission of Middle East respiratory syndrome coronavirus. J Virol 89:9119-9123. https://doi.org/10.1128/JVI .01279-15
    • (2015) J Virol , vol.89 , pp. 9119-9123
    • Yang, Y.1    Liu, C.2    Du, L.3    Jiang, S.4    Shi, Z.5    Baric, R.S.6    Li, F.7
  • 15
    • 50149113012 scopus 로고    scopus 로고
    • Cathepsin L functionally cleaves the severe acute respiratory syndrome coronavirus class I fusion protein upstream of rather than adjacent to the fusion peptide
    • Bosch BJ, Bartelink W, Rottier PJ. 2008. Cathepsin L functionally cleaves the severe acute respiratory syndrome coronavirus class I fusion protein upstream of rather than adjacent to the fusion peptide. J Virol 82: 8887-8890. https://doi.org/10.1128/JVI.00415-08
    • (2008) J Virol , vol.82 , pp. 8887-8890
    • Bosch, B.J.1    Bartelink, W.2    Rottier, P.J.3
  • 16
    • 84904637027 scopus 로고    scopus 로고
    • Proteolytic activation of the porcine epidemic diarrhea coronavirus spike fusion protein by trypsin in cell culture
    • Wicht O, Li W, Willems L, Meuleman TJ, Wubbolts RW, van Kuppeveld FJ, Rottier PJ, Bosch BJ. 2014. Proteolytic activation of the porcine epidemic diarrhea coronavirus spike fusion protein by trypsin in cell culture. J Virol 88:7952-7961. https://doi.org/10.1128/JVI.00297-14
    • (2014) J Virol , vol.88 , pp. 7952-7961
    • Wicht, O.1    Li, W.2    Willems, L.3    Meuleman, T.J.4    Wubbolts, R.W.5    van Kuppeveld, F.J.6    Rottier, P.J.7    Bosch, B.J.8
  • 20
    • 81555228650 scopus 로고    scopus 로고
    • A review of Nipah and Hendra viruses with an historical aside
    • Ksiazek TG, Rota PA, Rollin PE. 2011. A review of Nipah and Hendra viruses with an historical aside. Virus Res 162:173-183. https://doi.org/10.1016/j.virusres.2011.09.026
    • (2011) Virus Res , vol.162 , pp. 173-183
    • Ksiazek, T.G.1    Rota, P.A.2    Rollin, P.E.3
  • 23
    • 85017378927 scopus 로고    scopus 로고
    • Cryo-EM structures of MERS-CoV and SARS-CoV spike glycoproteins reveal the dynamic receptor binding domains
    • Yuan Y, Cao D, Zhang Y, Ma J, Qi J, Wang Q, Lu G, Wu Y, Yan J, Shi Y, Zhang X, Gao GF. 2017. Cryo-EM structures of MERS-CoV and SARS-CoV spike glycoproteins reveal the dynamic receptor binding domains. Nat Commun 8:15092. https://doi.org/10.1038/ncomms15092
    • (2017) Nat Commun , vol.8 , pp. 15092
    • Yuan, Y.1    Cao, D.2    Zhang, Y.3    Ma, J.4    Qi, J.5    Wang, Q.6    Lu, G.7    Wu, Y.8    Yan, J.9    Shi, Y.10    Zhang, X.11    Gao, G.F.12
  • 24
    • 85007247657 scopus 로고    scopus 로고
    • Cryoelectron microscopy structures of the SARS-CoV spike glycoprotein reveal a prerequisite conformational state for receptor binding
    • Gui M, Song W, Zhou H, Xu J, Chen S, Xiang Y, Wang X. 2017. Cryoelectron microscopy structures of the SARS-CoV spike glycoprotein reveal a prerequisite conformational state for receptor binding. Cell Res 27:119-129. https://doi.org/10.1038/cr.2016.152
    • (2017) Cell Res , vol.27 , pp. 119-129
    • Gui, M.1    Song, W.2    Zhou, H.3    Xu, J.4    Chen, S.5    Xiang, Y.6    Wang, X.7
  • 28
    • 84928039266 scopus 로고    scopus 로고
    • Isolation and characterization of porcine deltacoronavirus from pigs with diarrhea in the United States
    • Hu H, Jung K, Vlasova AN, Chepngeno J, Lu Z, Wang Q, Saif LJ. 2015. Isolation and characterization of porcine deltacoronavirus from pigs with diarrhea in the United States. J Clin Microbiol 53:1537-1548. https://doi.org/10.1128/JCM.00031-15
    • (2015) J Clin Microbiol , vol.53 , pp. 1537-1548
    • Hu, H.1    Jung, K.2    Vlasova, A.N.3    Chepngeno, J.4    Lu, Z.5    Wang, Q.6    Saif, L.J.7
  • 29
    • 84861307149 scopus 로고    scopus 로고
    • Discovery of seven novel mammalian and avian coronaviruses in the genus Deltacoronavirus supports bat coronaviruses as the gene source of Alphacoronavirus and Betacoronavirus and avian coronaviruses as the gene source of Gammacoronavirus and Deltacoronavirus
    • Woo PC, Lau SK, Lam CS, Lau CC, Tsang AK, Lau JH, Bai R, Teng JL, Tsang CC, Wang M, Zheng BJ, Chan KH, Yuen KY. 2012. Discovery of seven novel mammalian and avian coronaviruses in the genus Deltacoronavirus supports bat coronaviruses as the gene source of Alphacoronavirus and Betacoronavirus and avian coronaviruses as the gene source of Gammacoronavirus and Deltacoronavirus. J Virol 86:3995-4008. https://doi.org/10.1128/JVI.06540-11
    • (2012) J Virol , vol.86 , pp. 3995-4008
    • Woo, P.C.1    Lau, S.K.2    Lam, C.S.3    Lau, C.C.4    Tsang, A.K.5    Lau, J.H.6    Bai, R.7    Teng, J.L.8    Tsang, C.C.9    Wang, M.10    Zheng, B.J.11    Chan, K.H.12    Yuen, K.Y.13
  • 30
    • 84991734851 scopus 로고    scopus 로고
    • Crucial steps in the structure determination of a coronavirus spike glycoprotein using cryo-electron microscopy
    • Walls A, Tortorici MA, Bosch BJ, Frenz B, Rottier PJ, DiMaio F, Rey FA, Veesler D. 2017. Crucial steps in the structure determination of a coronavirus spike glycoprotein using cryo-electron microscopy. Protein Sci 26:113-121. https://doi.org/10.1002/pro.3048
    • (2017) Protein Sci , vol.26 , pp. 113-121
    • Walls, A.1    Tortorici, M.A.2    Bosch, B.J.3    Frenz, B.4    Rottier, P.J.5    DiMaio, F.6    Rey, F.A.7    Veesler, D.8
  • 31
    • 85013932755 scopus 로고    scopus 로고
    • Vitrification after multiple rounds of sample application and blotting improves particle density on cryo-electron microscopy grids
    • Snijder J, Borst AJ, Dosey A, Walls AC, Burrell A, Reddy VS, Kollman JM, Veesler D. 2017. Vitrification after multiple rounds of sample application and blotting improves particle density on cryo-electron microscopy grids. J Struct Biol 198:38-42. https://doi.org/10.1016/j.jsb.2017.02.008
    • (2017) J Struct Biol , vol.198 , pp. 38-42
    • Snijder, J.1    Borst, A.J.2    Dosey, A.3    Walls, A.C.4    Burrell, A.5    Reddy, V.S.6    Kollman, J.M.7    Veesler, D.8
  • 34
    • 84874601328 scopus 로고    scopus 로고
    • Unambiguous phosphosite localization using electron-transfer/higher-energy collision dissociation (EThcD)
    • Frese CK, Zhou H, Taus T, Altelaar AF, Mechtler K, Heck AJ, Mohammed S. 2013. Unambiguous phosphosite localization using electron-transfer/higher-energy collision dissociation (EThcD). J Proteome Res 12: 1520-1525. https://doi.org/10.1021/pr301130k
    • (2013) J Proteome Res , vol.12 , pp. 1520-1525
    • Frese, C.K.1    Zhou, H.2    Taus, T.3    Altelaar, A.F.4    Mechtler, K.5    Heck, A.J.6    Mohammed, S.7
  • 38
    • 77956625296 scopus 로고    scopus 로고
    • A single asparagine-linked glycosylation site of the severe acute respiratory syndrome coronavirus spike glycoprotein facilitates inhibition by mannose-binding lectin through multiple mechanisms
    • Zhou Y, Lu K, Pfefferle S, Bertram S, Glowacka I, Drosten C, Pohlmann S, Simmons G. 2010. A single asparagine-linked glycosylation site of the severe acute respiratory syndrome coronavirus spike glycoprotein facilitates inhibition by mannose-binding lectin through multiple mechanisms. J Virol 84:8753-8764. https://doi.org/10.1128/JVI.00554-10
    • (2010) J Virol , vol.84 , pp. 8753-8764
    • Zhou, Y.1    Lu, K.2    Pfefferle, S.3    Bertram, S.4    Glowacka, I.5    Drosten, C.6    Pohlmann, S.7    Simmons, G.8
  • 40
    • 84934434228 scopus 로고    scopus 로고
    • Human coronavirus 229E can use CD209L (L-SIGN) to enter cells
    • Jeffers SA, Hemmila EM, Holmes KV. 2006. Human coronavirus 229E can use CD209L (L-SIGN) to enter cells. Adv Exp Med Biol 581:265-269. https://doi.org/10.1007/978-0-387-33012-9_44
    • (2006) Adv Exp Med Biol , vol.581 , pp. 265-269
    • Jeffers, S.A.1    Hemmila, E.M.2    Holmes, K.V.3
  • 41
    • 0033957648 scopus 로고    scopus 로고
    • Characterization of the sialic acid binding activity of transmissible gastroenteritis coronavirus by analysis of haemagglutination-deficient mutants
    • Krempl C, Ballesteros ML, Zimmer G, Enjuanes L, Klenk HD, Herrler G. 2000. Characterization of the sialic acid binding activity of transmissible gastroenteritis coronavirus by analysis of haemagglutination-deficient mutants. J Gen Virol 81:489-496. https://doi.org/10.1099/0022-1317-81-2-489
    • (2000) J Gen Virol , vol.81 , pp. 489-496
    • Krempl, C.1    Ballesteros, M.L.2    Zimmer, G.3    Enjuanes, L.4    Klenk, H.D.5    Herrler, G.6
  • 42
    • 0026788417 scopus 로고
    • Genetic evolution and tropism of transmissible gastroenteritis coronaviruses
    • Sanchez CM, Gebauer F, Sune C, Mendez A, Dopazo J, Enjuanes L. 1992. Genetic evolution and tropism of transmissible gastroenteritis coronaviruses. Virology 190:92-105. https://doi.org/10.1016/0042-6822(92)91195-Z
    • (1992) Virology , vol.190 , pp. 92-105
    • Sanchez, C.M.1    Gebauer, F.2    Sune, C.3    Mendez, A.4    Dopazo, J.5    Enjuanes, L.6
  • 43
    • 84931053998 scopus 로고    scopus 로고
    • Human coronavirus HKU1 spike protein uses o-acetylated sialic acid as an attachment receptor determinant and employs hemagglutinin-esterase protein as a receptordestroying enzyme
    • Huang X, Dong W, Milewska A, Golda A, Qi Y, Zhu QK, Marasco WA, Baric RS, Sims AC, Pyrc K, Li W, Sui J. 2015. Human coronavirus HKU1 spike protein uses o-acetylated sialic acid as an attachment receptor determinant and employs hemagglutinin-esterase protein as a receptordestroying enzyme. J Virol 89:7202-7213. https://doi.org/10.1128/JVI .00854-15
    • (2015) J Virol , vol.89 , pp. 7202-7213
    • Huang, X.1    Dong, W.2    Milewska, A.3    Golda, A.4    Qi, Y.5    Zhu, Q.K.6    Marasco, W.A.7    Baric, R.S.8    Sims, A.C.9    Pyrc, K.10    Li, W.11    Sui, J.12
  • 44
    • 0001515909 scopus 로고
    • Human and bovine coronaviruses recognize sialic acid-containing receptors similar to those of influenza C viruses
    • Vlasak R, Luytjes W, Spaan W, Palese P. 1988. Human and bovine coronaviruses recognize sialic acid-containing receptors similar to those of influenza C viruses. Proc Natl Acad Sci U S A 85:4526-4529. https://doi.org/10.1073/pnas.85.12.4526
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 4526-4529
    • Vlasak, R.1    Luytjes, W.2    Spaan, W.3    Palese, P.4
  • 45
    • 84871290676 scopus 로고    scopus 로고
    • Crystal structure of bovine coronavirus spike protein lectin domain
    • Peng G, Xu L, Lin YL, Chen L, Pasquarella JR, Holmes KV, Li F. 2012. Crystal structure of bovine coronavirus spike protein lectin domain. J Biol Chem 287:41931-41938. https://doi.org/10.1074/jbc.M112.418210
    • (2012) J Biol Chem , vol.287 , pp. 41931-41938
    • Peng, G.1    Xu, L.2    Lin, Y.L.3    Chen, L.4    Pasquarella, J.R.5    Holmes, K.V.6    Li, F.7
  • 46
    • 73949110051 scopus 로고    scopus 로고
    • Crystal structure of NL63 respiratory coronavirus receptor-binding domain complexed with its human receptor
    • Wu K, Li W, Peng G, Li F. 2009. Crystal structure of NL63 respiratory coronavirus receptor-binding domain complexed with its human receptor. Proc Natl Acad Sci U S A 106:19970-19974. https://doi.org/10.1073/pnas.0908837106
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 19970-19974
    • Wu, K.1    Li, W.2    Peng, G.3    Li, F.4
  • 47
    • 84866168715 scopus 로고    scopus 로고
    • Structural bases of coronavirus attachment to host aminopeptidase N and its inhibition by neutralizing antibodies
    • Reguera J, Santiago C, Mudgal G, Ordono D, Enjuanes L, Casasnovas JM. 2012. Structural bases of coronavirus attachment to host aminopeptidase N and its inhibition by neutralizing antibodies. PLoS Pathog 8:e1002859. https://doi.org/10.1371/journal.ppat.1002859
    • (2012) PLoS Pathog , vol.8
    • Reguera, J.1    Santiago, C.2    Mudgal, G.3    Ordono, D.4    Enjuanes, L.5    Casasnovas, J.M.6
  • 48
    • 84941788522 scopus 로고    scopus 로고
    • Junctional and allele-specific residues are critical for MERS-CoV neutralization by an exceptionally potent germline-like antibody
    • Ying T, Prabakaran P, Du L, Shi W, Feng Y, Wang Y, Wang L, Li W, Jiang S, Dimitrov DS, Zhou T. 2015. Junctional and allele-specific residues are critical for MERS-CoV neutralization by an exceptionally potent germline-like antibody. Nat Commun 6:8223. https://doi.org/10.1038/ncomms9223
    • (2015) Nat Commun , vol.6 , pp. 8223
    • Ying, T.1    Prabakaran, P.2    Du, L.3    Shi, W.4    Feng, Y.5    Wang, Y.6    Wang, L.7    Li, W.8    Jiang, S.9    Dimitrov, D.S.10    Zhou, T.11
  • 49
    • 33744910870 scopus 로고    scopus 로고
    • Structure of severe acute respiratory syndrome coronavirus receptor-binding domain complexed with neutralizing antibody
    • Prabakaran P, Gan J, Feng Y, Zhu Z, Choudhry V, Xiao X, Ji X, Dimitrov DS. 2006. Structure of severe acute respiratory syndrome coronavirus receptor-binding domain complexed with neutralizing antibody. J Biol Chem 281:15829-15836. https://doi.org/10.1074/jbc.M600697200
    • (2006) J Biol Chem , vol.281 , pp. 15829-15836
    • Prabakaran, P.1    Gan, J.2    Feng, Y.3    Zhu, Z.4    Choudhry, V.5    Xiao, X.6    Ji, X.7    Dimitrov, D.S.8
  • 50
    • 33845922896 scopus 로고    scopus 로고
    • Structural basis of neutralization by a human anti-severe acute respiratory syndrome spike protein antibody, 80R
    • Hwang WC, Lin Y, Santelli E, Sui J, Jaroszewski L, Stec B, Farzan M, Marasco WA, Liddington RC. 2006. Structural basis of neutralization by a human anti-severe acute respiratory syndrome spike protein antibody, 80R. J Biol Chem 281:34610-34616. https://doi.org/10.1074/jbc.M603275200
    • (2006) J Biol Chem , vol.281 , pp. 34610-34616
    • Hwang, W.C.1    Lin, Y.2    Santelli, E.3    Sui, J.4    Jaroszewski, L.5    Stec, B.6    Farzan, M.7    Marasco, W.A.8    Liddington, R.C.9
  • 54
    • 84892475040 scopus 로고    scopus 로고
    • A novel activation mechanism of avian influenza virus H9N2 by furin
    • Tse LV, Hamilton AM, Friling T, Whittaker GR. 2014. A novel activation mechanism of avian influenza virus H9N2 by furin. J Virol 88:1673-1683. https://doi.org/10.1128/JVI.02648-13
    • (2014) J Virol , vol.88 , pp. 1673-1683
    • Tse, L.V.1    Hamilton, A.M.2    Friling, T.3    Whittaker, G.R.4
  • 55
    • 0021741381 scopus 로고
    • Is virulence of H5N2 influenza viruses in chickens associated with loss of carbohydrate from the hemagglutinin?
    • Kawaoka Y, Naeve CW, Webster RG. 1984. Is virulence of H5N2 influenza viruses in chickens associated with loss of carbohydrate from the hemagglutinin? Virology 139:303-316. https://doi.org/10.1016/0042-6822(84) 90376-3
    • (1984) Virology , vol.139 , pp. 303-316
    • Kawaoka, Y.1    Naeve, C.W.2    Webster, R.G.3
  • 56
    • 33845961570 scopus 로고    scopus 로고
    • Core structure of S2 from the human coronavirus NL63 spike glycoprotein
    • Zheng Q, Deng Y, Liu J, van der Hoek L, Berkhout B, Lu M. 2006. Core structure of S2 from the human coronavirus NL63 spike glycoprotein. Biochemistry 45:15205-15215. https://doi.org/10.1021/bi061686w
    • (2006) Biochemistry , vol.45 , pp. 15205-15215
    • Zheng, Q.1    Deng, Y.2    Liu, J.3    van der Hoek, L.4    Berkhout, B.5    Lu, M.6
  • 57
    • 24644441711 scopus 로고    scopus 로고
    • Proteasemediated enhancement of severe acute respiratory syndrome coronavirus infection
    • Matsuyama S, Ujike M, Morikawa S, Tashiro M, Taguchi F. 2005. Proteasemediated enhancement of severe acute respiratory syndrome coronavirus infection. Proc Natl Acad Sci U S A 102:12543-12547. https://doi .org/10.1073/pnas.0503203102
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 12543-12547
    • Matsuyama, S.1    Ujike, M.2    Morikawa, S.3    Tashiro, M.4    Taguchi, F.5
  • 58
    • 70350322417 scopus 로고    scopus 로고
    • Two-step conformational changes in a coronavirus envelope glycoprotein mediated by receptor binding and proteolysis
    • Matsuyama S, Taguchi F. 2009. Two-step conformational changes in a coronavirus envelope glycoprotein mediated by receptor binding and proteolysis. J Virol 83:11133-11141. https://doi.org/10.1128/JVI .00959-09
    • (2009) J Virol , vol.83 , pp. 11133-11141
    • Matsuyama, S.1    Taguchi, F.2
  • 59
    • 0032509096 scopus 로고    scopus 로고
    • Crystal structure of GCN4-pIQI, a trimeric coiled coil with buried polar residues
    • Eckert DM, Malashkevich VN, Kim PS. 1998. Crystal structure of GCN4-pIQI, a trimeric coiled coil with buried polar residues. J Mol Biol 284: 859-865. https://doi.org/10.1006/jmbi.1998.2214
    • (1998) J Mol Biol , vol.284 , pp. 859-865
    • Eckert, D.M.1    Malashkevich, V.N.2    Kim, P.S.3
  • 60
    • 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. https://doi.org/10.1038/nature04322
    • (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
  • 62
    • 25644458666 scopus 로고    scopus 로고
    • Automated electron microscope tomography using robust prediction of specimen movements
    • Mastronarde DN. 2005. Automated electron microscope tomography using robust prediction of specimen movements. J Struct Biol 152: 36-51. https://doi.org/10.1016/j.jsb.2005.07.007
    • (2005) J Struct Biol , vol.152 , pp. 36-51
    • Mastronarde, D.N.1
  • 63
    • 85014129582 scopus 로고    scopus 로고
    • MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy
    • Zheng SQ, Palovcak E, Armache JP, Verba KA, Cheng Y, Agard DA. 2017. MotionCor2: anisotropic correction of beam-induced motion for improved cryo-electron microscopy. Nat Methods 14:331-332. https://doi .org/10.1038/nmeth.4193
    • (2017) Nat Methods , vol.14 , pp. 331-332
    • Zheng, S.Q.1    Palovcak, E.2    Armache, J.P.3    Verba, K.A.4    Cheng, Y.5    Agard, D.A.6
  • 64
    • 84955216953 scopus 로고    scopus 로고
    • Gctf: real-time CTF determination and correction
    • Zhang K. 2016. Gctf: real-time CTF determination and correction. J Struct Biol 193:1-12. https://doi.org/10.1016/j.jsb.2015.11.003
    • (2016) J Struct Biol , vol.193 , pp. 1-12
    • Zhang, K.1
  • 65
    • 84946488108 scopus 로고    scopus 로고
    • CTFFIND4: fast and accurate defocus estimation from electron micrographs
    • Rohou A, Grigorieff N. 2015. CTFFIND4: fast and accurate defocus estimation from electron micrographs. J Struct Biol 192:216-221. https://doi.org/10.1016/j.jsb.2015.08.008
    • (2015) J Struct Biol , vol.192 , pp. 216-221
    • Rohou, A.1    Grigorieff, N.2
  • 66
    • 63649113687 scopus 로고    scopus 로고
    • DoG Picker and TiltPicker: software tools to facilitate particle selection in single particle electron microscopy
    • Voss NR, Yoshioka CK, Radermacher M, Potter CS, Carragher B. 2009. DoG Picker and TiltPicker: software tools to facilitate particle selection in single particle electron microscopy. J Struct Biol 166:205-213. https://doi.org/10.1016/j.jsb.2009.01.004
    • (2009) J Struct Biol , vol.166 , pp. 205-213
    • Voss, N.R.1    Yoshioka, C.K.2    Radermacher, M.3    Potter, C.S.4    Carragher, B.5
  • 67
    • 85009208040 scopus 로고    scopus 로고
    • Accelerated cryo-EM structure determination with parallelisation using GPUs in RELION-2
    • Kimanius D, Forsberg BO, Scheres SH, Lindahl E. 2016. Accelerated cryo-EM structure determination with parallelisation using GPUs in RELION-2. eLife 5:e18722
    • (2016) ELife , vol.5
    • Kimanius, D.1    Forsberg, B.O.2    Scheres, S.H.3    Lindahl, E.4
  • 68
    • 84868444740 scopus 로고    scopus 로고
    • RELION: implementation of a Bayesian approach to cryo-EM structure determination
    • Scheres SH. 2012. RELION: implementation of a Bayesian approach to cryo-EM structure determination. J Struct Biol 180:519-530. https://doi .org/10.1016/j.jsb.2012.09.006
    • (2012) J Struct Biol , vol.180 , pp. 519-530
    • Scheres, S.H.1
  • 69
    • 84866078359 scopus 로고    scopus 로고
    • Prevention of overfitting in cryo-EM structure determination
    • Scheres SH, Chen S. 2012. Prevention of overfitting in cryo-EM structure determination. Nat Methods 9:853-854. https://doi.org/10.1038/nmeth .2115
    • (2012) Nat Methods , vol.9 , pp. 853-854
    • Scheres, S.H.1    Chen, S.2
  • 70
    • 0142042865 scopus 로고    scopus 로고
    • Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy
    • Rosenthal PB, Henderson R. 2003. Optimal determination of particle orientation, absolute hand, and contrast loss in single-particle electron cryomicroscopy. J Mol Biol 333:721-745. https://doi.org/10.1016/j.jmb .2003.07.013
    • (2003) J Mol Biol , vol.333 , pp. 721-745
    • Rosenthal, P.B.1    Henderson, R.2
  • 71
    • 84880607763 scopus 로고    scopus 로고
    • High-resolution noise substitution to measure overfitting and validate resolution in 3D structure determination by single particle electron cryomicroscopy
    • Chen S, McMullan G, Faruqi AR, Murshudov GN, Short JM, Scheres SH, Henderson R. 2013. High-resolution noise substitution to measure overfitting and validate resolution in 3D structure determination by single particle electron cryomicroscopy. Ultramicroscopy 135:24-35. https://doi.org/10.1016/j.ultramic.2013.06.004
    • (2013) Ultramicroscopy , vol.135 , pp. 24-35
    • Chen, S.1    McMullan, G.2    Faruqi, A.R.3    Murshudov, G.N.4    Short, J.M.5    Scheres, S.H.6    Henderson, R.7
  • 72
    • 33845345287 scopus 로고    scopus 로고
    • Visualizing density maps with UCSF Chimera
    • Goddard TD, Huang CC, Ferrin TE. 2007. Visualizing density maps with UCSF Chimera. J Struct Biol 157:281-287. https://doi.org/10.1016/j.jsb .2006.06.010
    • (2007) J Struct Biol , vol.157 , pp. 281-287
    • Goddard, T.D.1    Huang, C.C.2    Ferrin, T.E.3
  • 73
    • 84921777915 scopus 로고    scopus 로고
    • Tools for macromolecular model building and refinement into electron cryo-microscopy reconstructions
    • Brown A, Long F, Nicholls RA, Toots J, Emsley P, Murshudov G. 2015. Tools for macromolecular model building and refinement into electron cryo-microscopy reconstructions. Acta Crystallogr D Biol Crystallogr 71: 136-153. https://doi.org/10.1107/S1399004714021683
    • (2015) Acta Crystallogr D Biol Crystallogr , vol.71 , pp. 136-153
    • Brown, A.1    Long, F.2    Nicholls, R.A.3    Toots, J.4    Emsley, P.5    Murshudov, G.6
  • 74
    • 79959458821 scopus 로고    scopus 로고
    • Modeling symmetric macromolecular structures in Rosetta3
    • DiMaio F, Leaver-Fay A, Bradley P, Baker D, Andre I. 2011. Modeling symmetric macromolecular structures in Rosetta3. PLoS One 6:e20450. https://doi.org/10.1371/journal.pone.0020450
    • (2011) PLoS One , vol.6
    • DiMaio, F.1    Leaver-Fay, A.2    Bradley, P.3    Baker, D.4    Andre, I.5
  • 77
    • 84875521318 scopus 로고    scopus 로고
    • Byonic: advanced peptide and protein identification software
    • Chapter 13, Unit 13.20
    • Bern M, Kil YJ, Becker C. 2012. Byonic: advanced peptide and protein identification software. Curr Protoc Bioinformatics Chapter 13:Unit 13.20
    • (2012) Curr Protoc Bioinformatics
    • Bern, M.1    Kil, Y.J.2    Becker, C.3


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