-
1
-
-
84957818744
-
Coronaviruses-drug discovery and therapeutic options
-
Zumla A, Chan JF, Azhar EI, Hui DS, Yuen KY. 2016. Coronaviruses-drug discovery and therapeutic options. Nat Rev Drug Discov 15:327-347. https://doi.org/10.1038/nrd.2015.37
-
(2016)
Nat Rev Drug Discov
, vol.15
, pp. 327-347
-
-
Zumla, A.1
Chan, J.F.2
Azhar, E.I.3
Hui, D.S.4
Yuen, K.Y.5
-
2
-
-
84957045369
-
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
-
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
-
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
-
5
-
-
84881479703
-
Molecular basis of binding between novel human coronavirus MERS-CoV and its receptor CD26
-
Lu G, Hu Y, Wang Q, Qi J, Gao F, Li Y, Zhang Y, Zhang W, Yuan Y, Bao J, Zhang B, Shi Y, Yan J, Gao GF. 2013. Molecular basis of binding between novel human coronavirus MERS-CoV and its receptor CD26. Nature 500:227-231. https://doi.org/10.1038/nature12328
-
(2013)
Nature
, vol.500
, pp. 227-231
-
-
Lu, G.1
Hu, Y.2
Wang, Q.3
Qi, J.4
Gao, F.5
Li, Y.6
Zhang, Y.7
Zhang, W.8
Yuan, Y.9
Bao, J.10
Zhang, B.11
Shi, Y.12
Yan, J.13
Gao, G.F.14
-
6
-
-
84962487236
-
SARS-like WIV1-CoV poised for human emergence
-
Menachery VD, Yount BL, Jr, Sims AC, Debbink K, Agnihothram SS, Gralinski LE, Graham RL, Scobey T, Plante JA, Royal SR, Swanstrom J, Sheahan TP, Pickles RJ, Corti D, Randell SH, Lanzavecchia A, Marasco WA, Baric RS. 2016. SARS-like WIV1-CoV poised for human emergence. Proc Natl Acad Sci U S A 113:3048-3053. https://doi.org/10 .1073/pnas.1517719113
-
(2016)
Proc Natl Acad Sci U S A
, vol.113
, pp. 3048-3053
-
-
Menachery, V.D.1
Yount, B.L.2
Sims, A.C.3
Debbink, K.4
Agnihothram, S.S.5
Gralinski, L.E.6
Graham, R.L.7
Scobey, T.8
Plante, J.A.9
Royal, S.R.10
Swanstrom, J.11
Sheahan, T.P.12
Pickles, R.J.13
Corti, D.14
Randell, S.H.15
Lanzavecchia, A.16
Marasco, W.A.17
Baric, R.S.18
-
7
-
-
84889573658
-
Isolation and characterization of a bat SARS-like coronavirus that uses the ACE2 receptor
-
Ge XY, Li JL, Yang XL, Chmura AA, Zhu G, Epstein JH, Mazet JK, Hu B, Zhang W, Peng C, Zhang YJ, Luo CM, Tan B, Wang N, Zhu Y, Crameri G, Zhang SY, Wang LF, Daszak P, Shi ZL. 2013. Isolation and characterization of a bat SARS-like coronavirus that uses the ACE2 receptor. Nature 503:535-538. https://doi.org/10.1038/nature12711
-
(2013)
Nature
, vol.503
, pp. 535-538
-
-
Ge, X.Y.1
Li, J.L.2
Yang, X.L.3
Chmura, A.A.4
Zhu, G.5
Epstein, J.H.6
Mazet, J.K.7
Hu, B.8
Zhang, W.9
Peng, C.10
Zhang, Y.J.11
Luo, C.M.12
Tan, B.13
Wang, N.14
Zhu, Y.15
Crameri, G.16
Zhang, S.Y.17
Wang, L.F.18
Daszak, P.19
Shi, Z.L.20
more..
-
8
-
-
84906658079
-
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
-
9
-
-
84907681989
-
Bat origins of MERS-CoV supported by bat coronavirus HKU4 usage of human receptor CD26
-
Wang Q, Qi J, Yuan Y, Xuan Y, Han P, Wan Y, Ji W, Li Y, Wu Y, Wang J, Iwamoto A, Woo PC, Yuen KY, Yan J, Lu G, Gao GF. 2014. Bat origins of MERS-CoV supported by bat coronavirus HKU4 usage of human receptor CD26. Cell Host Microbe 16:328-337. https://doi.org/10.1016/j.chom .2014.08.009
-
(2014)
Cell Host Microbe
, vol.16
, pp. 328-337
-
-
Wang, Q.1
Qi, J.2
Yuan, Y.3
Xuan, Y.4
Han, P.5
Wan, Y.6
Ji, W.7
Li, Y.8
Wu, Y.9
Wang, J.10
Iwamoto, A.11
Woo, P.C.12
Yuen, K.Y.13
Yan, J.14
Lu, G.15
Gao, G.F.16
-
10
-
-
84930047858
-
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
-
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
-
12
-
-
84912120721
-
Coronavirus cell entry occurs through the endo-/lysosomal pathway in a proteolysis-dependent manner
-
Burkard C, Verheije MH, Wicht O, van Kasteren SI, van Kuppeveld FJ, Haagmans BL, Pelkmans L, Rottier PJ, Bosch BJ, de Haan CA. 2014. Coronavirus cell entry occurs through the endo-/lysosomal pathway in a proteolysis-dependent manner. PLoS Pathog 10:e1004502. https://doi .org/10.1371/journal.ppat.1004502
-
(2014)
PLoS Pathog
, vol.10
-
-
Burkard, C.1
Verheije, M.H.2
Wicht, O.3
van Kasteren, S.I.4
van Kuppeveld, F.J.5
Haagmans, B.L.6
Pelkmans, L.7
Rottier, P.J.8
Bosch, B.J.9
de Haan, C.A.10
-
13
-
-
84908065761
-
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
-
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
-
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
-
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
-
17
-
-
84952951392
-
Co-circulation of three camel coronavirus species and recombination of MERS-CoVs in Saudi Arabia
-
Sabir JS, Lam TT, Ahmed MM, Li L, Shen Y, Abo-Aba SE, Qureshi MI, Abu-Zeid M, Zhang Y, Khiyami MA, Alharbi NS, Hajrah NH, Sabir MJ, Mutwakil MH, Kabli SA, Alsulaimany FA, Obaid AY, Zhou B, Smith DK, Holmes EC, Zhu H, Guan Y. 2016. Co-circulation of three camel coronavirus species and recombination of MERS-CoVs in Saudi Arabia. Science 351:81-84. https://doi.org/10.1126/science.aac8608
-
(2016)
Science
, vol.351
, pp. 81-84
-
-
Sabir, J.S.1
Lam, T.T.2
Ahmed, M.M.3
Li, L.4
Shen, Y.5
Abo-Aba, S.E.6
Qureshi, M.I.7
Abu-Zeid, M.8
Zhang, Y.9
Khiyami, M.A.10
Alharbi, N.S.11
Hajrah, N.H.12
Sabir, M.J.13
Mutwakil, M.H.14
Kabli, S.A.15
Alsulaimany, F.A.16
Obaid, A.Y.17
Zhou, B.18
Smith, D.K.19
Holmes, E.C.20
Zhu, H.21
Guan, Y.22
more..
-
18
-
-
0141889936
-
Isolation and characterization of viruses related to the SARS coronavirus from animals in southern China
-
Guan Y, Zheng BJ, He YQ, Liu XL, Zhuang ZX, Cheung CL, Luo SW, Li PH, Zhang LJ, Guan YJ, Butt KM, Wong KL, Chan KW, Lim W, Shortridge KF, Yuen KY, Peiris JS, Poon LL. 2003. Isolation and characterization of viruses related to the SARS coronavirus from animals in southern China. Science 302:276-278. https://doi.org/10.1126/science.1087139
-
(2003)
Science
, vol.302
, pp. 276-278
-
-
Guan, Y.1
Zheng, B.J.2
He, Y.Q.3
Liu, X.L.4
Zhuang, Z.X.5
Cheung, C.L.6
Luo, S.W.7
Li, P.H.8
Zhang, L.J.9
Guan, Y.J.10
Butt, K.M.11
Wong, K.L.12
Chan, K.W.13
Lim, W.14
Shortridge, K.F.15
Yuen, K.Y.16
Peiris, J.S.17
Poon, L.L.18
-
19
-
-
67649538978
-
Origins and evolutionary genomics of the 2009 swine-origin H1N1 influenza A epidemic
-
Smith GJ, Vijaykrishna D, Bahl J, Lycett SJ, Worobey M, Pybus OG, Ma SK, Cheung CL, Raghwani J, Bhatt S, Peiris JS, Guan Y, Rambaut A. 2009. Origins and evolutionary genomics of the 2009 swine-origin H1N1 influenza A epidemic. Nature 459:1122-1125. https://doi.org/10.1038/nature08182
-
(2009)
Nature
, vol.459
, pp. 1122-1125
-
-
Smith, G.J.1
Vijaykrishna, D.2
Bahl, J.3
Lycett, S.J.4
Worobey, M.5
Pybus, O.G.6
Ma, S.K.7
Cheung, C.L.8
Raghwani, J.9
Bhatt, S.10
Peiris, J.S.11
Guan, Y.12
Rambaut, A.13
-
20
-
-
81555228650
-
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
-
21
-
-
84960090603
-
Cryo-electron microscopy structure of a coronavirus spike glycoprotein trimer
-
Walls AC, Tortorici MA, Bosch BJ, Frenz B, Rottier PJ, DiMaio F, Rey FA, Veesler D. 2016. Cryo-electron microscopy structure of a coronavirus spike glycoprotein trimer. Nature 531:114-117. https://doi.org/10.1038/nature16988
-
(2016)
Nature
, vol.531
, pp. 114-117
-
-
Walls, A.C.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
-
22
-
-
84987652828
-
Glycan shield and epitope masking of a coronavirus spike protein observed by cryo-electron microscopy
-
Walls AC, Tortorici MA, Frenz B, Snijder J, Li W, Rey FA, DiMaio F, Bosch BJ, Veesler D. 2016. Glycan shield and epitope masking of a coronavirus spike protein observed by cryo-electron microscopy. Nat Struct Mol Biol 23:899-905. https://doi.org/10.1038/nsmb.3293
-
(2016)
Nat Struct Mol Biol
, vol.23
, pp. 899-905
-
-
Walls, A.C.1
Tortorici, M.A.2
Frenz, B.3
Snijder, J.4
Li, W.5
Rey, F.A.6
DiMaio, F.7
Bosch, B.J.8
Veesler, D.9
-
23
-
-
85017378927
-
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
-
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
-
25
-
-
84960173062
-
Pre-fusion structure of a human coronavirus spike protein
-
Kirchdoerfer RN, Cottrell CA, Wang N, Pallesen J, Yassine HM, Turner HL, Corbett KS, Graham BS, McLellan JS, Ward AB. 2016. Pre-fusion structure of a human coronavirus spike protein. Nature 531:118-121. https://doi .org/10.1038/nature17200
-
(2016)
Nature
, vol.531
, pp. 118-121
-
-
Kirchdoerfer, R.N.1
Cottrell, C.A.2
Wang, N.3
Pallesen, J.4
Yassine, H.M.5
Turner, H.L.6
Corbett, K.S.7
Graham, B.S.8
McLellan, J.S.9
Ward, A.B.10
-
26
-
-
85028522287
-
Immunogenicity and structures of a rationally designed prefusion MERSCoV spike antigen
-
Pallesen J, Wang N, Corbett KS, Wrapp D, Kirchdoerfer RN, Turner HL, Cottrell CA, Becker MM, Wang L, Shi W, Kong WP, Andres EL, Kettenbach AN, Denison MR, Chappell JD, Graham BS, Ward AB, McLellan JS. 2017. Immunogenicity and structures of a rationally designed prefusion MERSCoV spike antigen. Proc Natl Acad Sci U S A 114:E7348-E7357. https://doi.org/10.1073/pnas.1707304114
-
(2017)
Proc Natl Acad Sci U S A
, vol.114
, pp. E7348-E7357
-
-
Pallesen, J.1
Wang, N.2
Corbett, K.S.3
Wrapp, D.4
Kirchdoerfer, R.N.5
Turner, H.L.6
Cottrell, C.A.7
Becker, M.M.8
Wang, L.9
Shi, W.10
Kong, W.P.11
Andres, E.L.12
Kettenbach, A.N.13
Denison, M.R.14
Chappell, J.D.15
Graham, B.S.16
Ward, A.B.17
McLellan, J.S.18
-
27
-
-
84929648712
-
Receptor usage and cell entry of porcine epidemic diarrhea coronavirus
-
Liu C, Tang J, Ma Y, Liang X, Yang Y, Peng G, Qi Q, Jiang S, Li J, Du L, Li F. 2015. Receptor usage and cell entry of porcine epidemic diarrhea coronavirus. J Virol 89:6121-6125. https://doi.org/10.1128/JVI.00430-15
-
(2015)
J Virol
, vol.89
, pp. 6121-6125
-
-
Liu, C.1
Tang, J.2
Ma, Y.3
Liang, X.4
Yang, Y.5
Peng, G.6
Qi, Q.7
Jiang, S.8
Li, J.9
Du, L.10
Li, F.11
-
28
-
-
84928039266
-
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
-
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
-
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
-
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
-
33
-
-
84926520440
-
Atomic-accuracy models from 4.5-A cryo-electron microscopy data with density-guided iterative local refinement
-
DiMaio F, Song Y, Li X, Brunner MJ, Xu C, Conticello V, Egelman E, Marlovits TC, Cheng Y, Baker D. 2015. Atomic-accuracy models from 4.5-A cryo-electron microscopy data with density-guided iterative local refinement. Nat Methods 12:361-365. https://doi.org/10.1038/nmeth .3286
-
(2015)
Nat Methods
, vol.12
, pp. 361-365
-
-
DiMaio, F.1
Song, Y.2
Li, X.3
Brunner, M.J.4
Xu, C.5
Conticello, V.6
Egelman, E.7
Marlovits, T.C.8
Cheng, Y.9
Baker, D.10
-
34
-
-
84874601328
-
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
-
35
-
-
84963936310
-
Trimeric HIV-1-Env structures define glycan shields from clades A, B, and G
-
Stewart-Jones GB, Soto C, Lemmin T, Chuang GY, Druz A, Kong R, Thomas PV, Wagh K, Zhou T, Behrens AJ, Bylund T, Choi CW, Davison JR, Georgiev IS, Joyce MG, Kwon YD, Pancera M, Taft J, Yang Y, Zhang B, Shivatare SS, Shivatare VS, Lee CD, Wu CY, Bewley CA, Burton DR, Koff WC, Connors M, Crispin M, Baxa U, Korber BT, Wong CH, Mascola JR, Kwong PD. 2016. Trimeric HIV-1-Env structures define glycan shields from clades A, B, and G. Cell 165:813-826. https://doi.org/10.1016/j.cell .2016.04.010
-
(2016)
Cell
, vol.165
, pp. 813-826
-
-
Stewart-Jones, G.B.1
Soto, C.2
Lemmin, T.3
Chuang, G.Y.4
Druz, A.5
Kong, R.6
Thomas, P.V.7
Wagh, K.8
Zhou, T.9
Behrens, A.J.10
Bylund, T.11
Choi, C.W.12
Davison, J.R.13
Georgiev, I.S.14
Joyce, M.G.15
Kwon, Y.D.16
Pancera, M.17
Taft, J.18
Yang, Y.19
Zhang, B.20
Shivatare, S.S.21
Shivatare, V.S.22
Lee, C.D.23
Wu, C.Y.24
Bewley, C.A.25
Burton, D.R.26
Koff, W.C.27
Connors, M.28
Crispin, M.29
Baxa, U.30
Korber, B.T.31
Wong, C.H.32
Mascola, J.R.33
Kwong, P.D.34
more..
-
36
-
-
84987652813
-
Natively glycosylated HIV-1 Env structure reveals new mode for antibody recognition of the CD4-binding site
-
Gristick HB, von Boehmer L, West AP, Jr, Schamber M, Gazumyan A, Golijanin J, Seaman MS, Fatkenheuer G, Klein F, Nussenzweig MC, Bjorkman PJ. 2016. Natively glycosylated HIV-1 Env structure reveals new mode for antibody recognition of the CD4-binding site. Nat Struct Mol Biol 23:906-915. https://doi.org/10.1038/nsmb.3291
-
(2016)
Nat Struct Mol Biol
, vol.23
, pp. 906-915
-
-
Gristick, H.B.1
von Boehmer, L.2
West, A.P.3
Schamber, M.4
Gazumyan, A.5
Golijanin, J.6
Seaman, M.S.7
Fatkenheuer, G.8
Klein, F.9
Nussenzweig, M.C.10
Bjorkman, P.J.11
-
37
-
-
84871825774
-
Evolution of the receptor binding properties of the influenza A(H3N2) hemagglutinin
-
Lin YP, Xiong X, Wharton SA, Martin SR, Coombs PJ, Vachieri SG, Christodoulou E, Walker PA, Liu J, Skehel JJ, Gamblin SJ, Hay AJ, Daniels RS, McCauley JW. 2012. Evolution of the receptor binding properties of the influenza A(H3N2) hemagglutinin. Proc Natl Acad Sci U S A 109: 21474-21479. https://doi.org/10.1073/pnas.1218841110
-
(2012)
Proc Natl Acad Sci U S A
, vol.109
, pp. 21474-21479
-
-
Lin, Y.P.1
Xiong, X.2
Wharton, S.A.3
Martin, S.R.4
Coombs, P.J.5
Vachieri, S.G.6
Christodoulou, E.7
Walker, P.A.8
Liu, J.9
Skehel, J.J.10
Gamblin, S.J.11
Hay, A.J.12
Daniels, R.S.13
McCauley, J.W.14
-
38
-
-
77956625296
-
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
-
39
-
-
8144221600
-
CD209L (L-SIGN) is a receptor for severe acute respiratory syndrome coronavirus
-
Jeffers SA, Tusell SM, Gillim-Ross L, Hemmila EM, Achenbach JE, Babcock GJ, Thomas WD, Jr, Thackray LB, Young MD, Mason RJ, Ambrosino DM, Wentworth DE, Demartini JC, Holmes KV. 2004. CD209L (L-SIGN) is a receptor for severe acute respiratory syndrome coronavirus. Proc Natl Acad Sci U S A 101:15748-15753. https://doi .org/10.1073/pnas.0403812101
-
(2004)
Proc Natl Acad Sci U S A
, vol.101
, pp. 15748-15753
-
-
Jeffers, S.A.1
Tusell, S.M.2
Gillim-Ross, L.3
Hemmila, E.M.4
Achenbach, J.E.5
Babcock, G.J.6
Thomas, W.D.7
Thackray, L.B.8
Young, M.D.9
Mason, R.J.10
Ambrosino, D.M.11
Wentworth, D.E.12
Demartini, J.C.13
Holmes, K.V.14
-
40
-
-
84934434228
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
51
-
-
10744229285
-
Potent neutralization of severe acute respiratory syndrome (SARS) coronavirus by a human mAb to S1 protein that blocks receptor association
-
Sui J, Li W, Murakami A, Tamin A, Matthews LJ, Wong SK, Moore MJ, Tallarico AS, Olurinde M, Choe H, Anderson LJ, Bellini WJ, Farzan M, Marasco WA. 2004. Potent neutralization of severe acute respiratory syndrome (SARS) coronavirus by a human mAb to S1 protein that blocks receptor association. Proc Natl Acad Sci U S A 101:2536-2541. https://doi.org/10.1073/pnas.0307140101
-
(2004)
Proc Natl Acad Sci U S A
, vol.101
, pp. 2536-2541
-
-
Sui, J.1
Li, W.2
Murakami, A.3
Tamin, A.4
Matthews, L.J.5
Wong, S.K.6
Moore, M.J.7
Tallarico, A.S.8
Olurinde, M.9
Choe, H.10
Anderson, L.J.11
Bellini, W.J.12
Farzan, M.13
Marasco, W.A.14
-
52
-
-
34547500771
-
Potent cross-reactive neutralization of SARS coronavirus isolates by human monoclonal antibodies
-
Zhu Z, Chakraborti S, He Y, Roberts A, Sheahan T, Xiao X, Hensley LE, Prabakaran P, Rockx B, Sidorov IA, Corti D, Vogel L, Feng Y, Kim JO, Wang LF, Baric R, Lanzavecchia A, Curtis KM, Nabel GJ, Subbarao K, Jiang S, Dimitrov DS. 2007. Potent cross-reactive neutralization of SARS coronavirus isolates by human monoclonal antibodies. Proc Natl Acad Sci U S A 104:12123-12128. https://doi.org/10.1073/pnas.0701000104
-
(2007)
Proc Natl Acad Sci U S A
, vol.104
, pp. 12123-12128
-
-
Zhu, Z.1
Chakraborti, S.2
He, Y.3
Roberts, A.4
Sheahan, T.5
Xiao, X.6
Hensley, L.E.7
Prabakaran, P.8
Rockx, B.9
Sidorov, I.A.10
Corti, D.11
Vogel, L.12
Feng, Y.13
Kim, J.O.14
Wang, L.F.15
Baric, R.16
Lanzavecchia, A.17
Curtis, K.M.18
Nabel, G.J.19
Subbarao, K.20
Jiang, S.21
Dimitrov, D.S.22
more..
-
53
-
-
85031329007
-
Tectonic conformational changes of a coronavirus spike glycoprotein promote membrane fusion
-
Walls AC, Tortorici MA, Snijder J, Xiong X, Bosch B-J, Rey FA, Veesler D. 2017. Tectonic conformational changes of a coronavirus spike glycoprotein promote membrane fusion. Proc Natl Acad Sci U S A 114: 11157-11162. https://doi.org/10.1073/pnas.1708727114
-
(2017)
Proc Natl Acad Sci U S A
, vol.114
, pp. 11157-11162
-
-
Walls, A.C.1
Tortorici, M.A.2
Snijder, J.3
Xiong, X.4
Bosch, B.-J.5
Rey, F.A.6
Veesler, D.7
-
54
-
-
84892475040
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
61
-
-
34247846396
-
A versatile ligation-independent cloning method suitable for high-throughput expression screening applications
-
Berrow NS, Alderton D, Sainsbury S, Nettleship J, Assenberg R, Rahman N, Stuart DI, Owens RJ. 2007. A versatile ligation-independent cloning method suitable for high-throughput expression screening applications. Nucleic Acids Res 35:e45. https://doi.org/10.1093/nar/gkm047
-
(2007)
Nucleic Acids Res
, vol.35
, pp. e45
-
-
Berrow, N.S.1
Alderton, D.2
Sainsbury, S.3
Nettleship, J.4
Assenberg, R.5
Rahman, N.6
Stuart, D.I.7
Owens, R.J.8
-
62
-
-
25644458666
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
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
-
75
-
-
74549178560
-
MolProbity: all-atom structure validation for macromolecular crystallography
-
Chen VB, Arendall WB, III, Headd JJ, Keedy DA, Immormino RM, Kapral GJ, Murray LW, Richardson JS, Richardson DC. 2010. MolProbity: all-atom structure validation for macromolecular crystallography. Acta Crystallogr D Biol Crystallogr 66:12-21. https://doi.org/10.1107/S0907444909042073
-
(2010)
Acta Crystallogr D Biol Crystallogr
, vol.66
, pp. 12-21
-
-
Chen, V.B.1
Arendall, W.B.2
Headd, J.J.3
Keedy, D.A.4
Immormino, R.M.5
Kapral, G.J.6
Murray, L.W.7
Richardson, J.S.8
Richardson, D.C.9
-
76
-
-
84947945686
-
Privateer: software for the conformational validation of carbohydrate structures
-
Agirre J, Iglesias-Fernandez J, Rovira C, Davies GJ, Wilson KS, Cowtan KD. 2015. Privateer: software for the conformational validation of carbohydrate structures. Nat Struct Mol Biol 22:833-834. https://doi.org/10 .1038/nsmb.3115
-
(2015)
Nat Struct Mol Biol
, vol.22
, pp. 833-834
-
-
Agirre, J.1
Iglesias-Fernandez, J.2
Rovira, C.3
Davies, G.J.4
Wilson, K.S.5
Cowtan, K.D.6
-
77
-
-
84875521318
-
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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