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Volumn 22, Issue 12, 2016, Pages 1456-1464

Molecular-level analysis of the serum antibody repertoire in young adults before and after seasonal influenza vaccination

(35)  Lee, Jiwon a   Boutz, Daniel R b   Chromikova, Veronika c   Joyce, M Gordon d   Vollmers, Christopher e   Leung, Kwanyee d   Horton, Andrew P b   DeKosky, Brandon J a,d   Lee, Chang Han a   Lavinder, Jason J a   Murrin, Ellen M a   Chrysostomou, Constantine a,f   Hoi, Kam Hon a   Tsybovsky, Yaroslav a   Thomas, Paul V a   Druz, Aliaksandr d   Zhang, Baoshan d   Zhang, Yi d   Wang, Lingshu d   Kong, Wing Pui a   more..


Author keywords

[No Author keywords available]

Indexed keywords

B LYMPHOCYTE RECEPTOR; CROSS REACTING ANTIBODY; IMMUNOGLOBULIN G; IMMUNOGLOBULIN KAPPA CHAIN; INFLUENZA VACCINE; INFLUENZA VIRUS HEMAGGLUTININ; RECOMBINANT ANTIBODY; EPITOPE; LYMPHOCYTE ANTIGEN RECEPTOR; MESSENGER RNA; VIRUS ANTIBODY;

EID: 84994591811     PISSN: 10788956     EISSN: 1546170X     Source Type: Journal    
DOI: 10.1038/nm.4224     Document Type: Article
Times cited : (243)

References (59)
  • 1
    • 34249938743 scopus 로고    scopus 로고
    • The annual impact of seasonal influenza in the US: Measuring disease burden and costs
    • Molinari, N.-A. M. et al. The annual impact of seasonal influenza in the US: measuring disease burden and costs. Vaccine 25, 5086-5096 (2007).
    • (2007) Vaccine , vol.25 , pp. 5086-5096
    • Molinari, N.-A.M.1
  • 2
    • 78549241668 scopus 로고    scopus 로고
    • Influenza vaccines for the future
    • Lambert, L. C., Fauci, A. S. Influenza vaccines for the future. N. Engl. J. Med. 363, 2036-2044 (2010).
    • (2010) N. Engl. J. Med. , vol.363 , pp. 2036-2044
    • Lambert, L.C.1    Fauci, A.S.2
  • 3
    • 51449110453 scopus 로고    scopus 로고
    • Correlates of protection: Novel generations of influenza vaccines
    • Rimmelzwaan, G. F., McElhaney, J. E. Correlates of protection: novel generations of influenza vaccines. Vaccine 26, D41-D44 (2008).
    • (2008) Vaccine , vol.26 , pp. D41-D44
    • Rimmelzwaan, G.F.1    McElhaney, J.E.2
  • 4
    • 84924060844 scopus 로고    scopus 로고
    • Advances in the development of influenza virus vaccines
    • Krammer, F., Palese, P. Advances in the development of influenza virus vaccines. Nat. Rev. Drug Discov. 14, 167-182 (2015).
    • (2015) Nat. Rev. Drug Discov. , vol.14 , pp. 167-182
    • Krammer, F.1    Palese, P.2
  • 5
    • 70349437154 scopus 로고    scopus 로고
    • Comparative efficacy of inactivated and live attenuated influenza vaccines
    • Monto, A. S. et al. Comparative efficacy of inactivated and live attenuated influenza vaccines. N. Engl. J. Med. 361, 1260-1267 (2009).
    • (2009) N. Engl. J. Med. , vol.361 , pp. 1260-1267
    • Monto, A.S.1
  • 6
    • 84155162558 scopus 로고    scopus 로고
    • Efficacy and effectiveness of influenza vaccines: A systematic review and meta-analysis
    • Osterholm, M. T., Kelley, N. S., Sommer, A., Belongia, E. A. Efficacy and effectiveness of influenza vaccines: a systematic review and meta-analysis. Lancet Infect. Dis. 12, 36-44 (2012).
    • (2012) Lancet Infect. Dis. , vol.12 , pp. 36-44
    • Osterholm, M.T.1    Kelley, N.S.2    Sommer, A.3    Belongia, E.A.4
  • 7
    • 0015452705 scopus 로고
    • The role of serum haemagglutination-inhibiting antibody in protection against challenge infection with influenza A2 and B viruses
    • Hobson, D., Curry, R. L., Beare, A. S., Ward-Gardner, A. The role of serum haemagglutination-inhibiting antibody in protection against challenge infection with influenza A2 and B viruses. J. Hyg. (Lond. ) 70, 767-777 (1972).
    • (1972) J. Hyg. (Lond. ) , vol.70 , pp. 767-777
    • Hobson, D.1    Curry, R.L.2    Beare, A.S.3    Ward-Gardner, A.4
  • 8
    • 2442440593 scopus 로고    scopus 로고
    • And protective efficacy of influenza vaccination
    • Hannoun, C., Megas, F., Piercy, J. Immunogenicity and protective efficacy of influenza vaccination. Virus Res. 103, 133-138 (2004).
    • (2004) Virus Res. , vol.103 , pp. 133-138
    • Hannoun, C.1    Megas, F.2    Immunogenicity, P.J.3
  • 9
    • 0027471177 scopus 로고
    • A common neutralizing epitope conserved between the hemagglutinins of influenza A virus H1 and H2 strains
    • Okuno, Y., Isegawa, Y., Sasao, F., Ueda, S. A common neutralizing epitope conserved between the hemagglutinins of influenza A virus H1 and H2 strains. J. Virol. 67, 2552-2558 (1993).
    • (1993) J. Virol. , vol.67 , pp. 2552-2558
    • Okuno, Y.1    Isegawa, Y.2    Sasao, F.3    Ueda, S.4
  • 10
    • 80051670323 scopus 로고    scopus 로고
    • A neutralizing antibody selected from plasma cells that binds to group 1 and group 2 influenza A hemagglutinins
    • Corti, D. et al. A neutralizing antibody selected from plasma cells that binds to group 1 and group 2 influenza A hemagglutinins. Science 333, 850-856 (2011).
    • (2011) Science , vol.333 , pp. 850-856
    • Corti, D.1
  • 11
    • 84866122029 scopus 로고    scopus 로고
    • Highly conserved protective epitopes on influenza B viruses
    • Dreyfus, C. et al. Highly conserved protective epitopes on influenza B viruses. Science 337, 1343-1348 (2012).
    • (2012) Science , vol.337 , pp. 1343-1348
    • Dreyfus, C.1
  • 12
    • 84861872090 scopus 로고    scopus 로고
    • Pandemic H1N1 influenza vaccine induces a recall response in humans that favors broadly cross-reactive memory B cells
    • Li, G.-M. et al. Pandemic H1N1 influenza vaccine induces a recall response in humans that favors broadly cross-reactive memory B cells. Proc. Natl. Acad. Sci. USA 109, 9047-9052 (2012).
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 9047-9052
    • Li, G.-M.1
  • 13
    • 44449118948 scopus 로고    scopus 로고
    • Rapid cloning of high-affinity human monoclonal antibodies against influenza virus
    • Wrammert, J. et al. Rapid cloning of high-affinity human monoclonal antibodies against influenza virus. Nature 453, 667-671 (2008).
    • (2008) Nature , vol.453 , pp. 667-671
    • Wrammert, J.1
  • 14
    • 80054780343 scopus 로고    scopus 로고
    • H3N2 influenza infection elicits more cross-reactive and less clonally expanded anti-hemagglutinin antibodies than influenza vaccination
    • Moody, M. A. et al. H3N2 influenza infection elicits more cross-reactive and less clonally expanded anti-hemagglutinin antibodies than influenza vaccination. PLoS One 6, e25797 (2011).
    • (2011) PLoS One , vol.6 , pp. e25797
    • Moody, M.A.1
  • 15
    • 84880427552 scopus 로고    scopus 로고
    • An in vivo human-plasmablast-enrichment technique allows rapid identification of therapeutic influenza A antibodies
    • Nakamura, G. et al. An in vivo human-plasmablast-enrichment technique allows rapid identification of therapeutic influenza A antibodies. Cell Host Microbe 14, 93-103 (2013).
    • (2013) Cell Host Microbe , vol.14 , pp. 93-103
    • Nakamura, G.1
  • 17
    • 84906996647 scopus 로고    scopus 로고
    • Induction of broadly cross-reactive antibody responses to the influenza HA stem region following H5N1 vaccination in humans
    • Ellebedy, A. H. et al. Induction of broadly cross-reactive antibody responses to the influenza HA stem region following H5N1 vaccination in humans. Proc. Natl. Acad. Sci. USA 111, 13133-13138 (2014).
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 13133-13138
    • Ellebedy, A.H.1
  • 18
    • 84896917279 scopus 로고    scopus 로고
    • Flow cytometry reveals that H5N1 vaccination elicits cross-reactive stem-directed antibodies from multiple Ig heavy-chain lineages
    • Whittle, J. R. R. et al. Flow cytometry reveals that H5N1 vaccination elicits cross-reactive stem-directed antibodies from multiple Ig heavy-chain lineages. J. Virol. 88, 4047-4057 (2014).
    • (2014) J. Virol. , vol.88 , pp. 4047-4057
    • Whittle, J.R.R.1
  • 19
    • 84862554454 scopus 로고    scopus 로고
    • Seroconversion to seasonal influenza viruses after A(H1N1)pdm09 virus infection, Quebec, Canada
    • Baz, M. et al. Seroconversion to seasonal influenza viruses after A(H1N1)pdm09 virus infection, Quebec, Canada. Emerging Infect. Dis. 18, 1132-1134 (2012).
    • (2012) Emerging Infect. Dis. , vol.18 , pp. 1132-1134
    • Baz, M.1
  • 20
    • 84956934982 scopus 로고    scopus 로고
    • Broadly neutralizing anti-influenza antibodies require Fc receptor engagement for in vivo protection
    • DiLillo, D. J., Palese, P., Wilson, P. C., Ravetch, J. V. Broadly neutralizing anti-influenza antibodies require Fc receptor engagement for in vivo protection. J. Clin. Invest. 126, 605-610 (2016).
    • (2016) J. Clin. Invest. , vol.126 , pp. 605-610
    • DiLillo, D.J.1    Palese, P.2    Wilson, P.C.3    Ravetch, J.V.4
  • 21
    • 84973488141 scopus 로고    scopus 로고
    • Both neutralizing and non-neutralizing human H7N9 influenza vaccine-induced monoclonal antibodies confer protection
    • Henry Dunand, C. J. et al. Both neutralizing and non-neutralizing human H7N9 influenza vaccine-induced monoclonal antibodies confer protection. Cell Host Microbe 19, 800-813 (2016).
    • (2016) Cell Host Microbe , vol.19 , pp. 800-813
    • Henry Dunand, C.J.1
  • 23
    • 84954162891 scopus 로고    scopus 로고
    • Hemagglutinin stalk-and neuraminidase-specific monoclonal antibodies protect against lethal H10N8 influenza virus infection in mice
    • Wohlbold, T. J. et al. Hemagglutinin stalk-and neuraminidase-specific monoclonal antibodies protect against lethal H10N8 influenza virus infection in mice. J. Virol. 90, 851-861 (2015).
    • (2015) J. Virol. , vol.90 , pp. 851-861
    • Wohlbold, T.J.1
  • 24
    • 80052184942 scopus 로고    scopus 로고
    • Broadly neutralizing human antibody that recognizes the receptor-binding pocket of influenza virus hemagglutinin
    • Whittle, J. R. R. et al. Broadly neutralizing human antibody that recognizes the receptor-binding pocket of influenza virus hemagglutinin. Proc. Natl. Acad. Sci. USA 108, 14216-14221 (2011).
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 14216-14221
    • Whittle, J.R.R.1
  • 25
    • 84911404794 scopus 로고    scopus 로고
    • Receptor mimicry by antibody F045-092 facilitates universal binding to the H3 subtype of influenza virus
    • Lee, P. S. et al. Receptor mimicry by antibody F045-092 facilitates universal binding to the H3 subtype of influenza virus. Nat. Commun. 5, 3614 (2014).
    • (2014) Nat. Commun. , vol.5 , pp. 3614
    • Lee, P.S.1
  • 26
    • 80053474133 scopus 로고    scopus 로고
    • A broadly neutralizing human monoclonal antibody that recognizes a conserved, novel epitope on the globular head of the influenza H1N1 virus hemagglutinin
    • Krause, J. C. et al. A broadly neutralizing human monoclonal antibody that recognizes a conserved, novel epitope on the globular head of the influenza H1N1 virus hemagglutinin. J. Virol. 85, 10905-10908 (2011).
    • (2011) J. Virol. , vol.85 , pp. 10905-10908
    • Krause, J.C.1
  • 27
    • 84904263671 scopus 로고    scopus 로고
    • Human responses to influenza vaccination show seroconversion signatures and convergent antibody rearrangements
    • Jackson, K. J. L. et al. Human responses to influenza vaccination show seroconversion signatures and convergent antibody rearrangements. Cell Host Microbe 16, 105-114 (2014).
    • (2014) Cell Host Microbe , vol.16 , pp. 105-114
    • Jackson, K.J.L.1
  • 28
    • 84911428207 scopus 로고    scopus 로고
    • Antibody landscapes after influenza virus infection or vaccination
    • Fonville, J. M. et al. Antibody landscapes after influenza virus infection or vaccination. Science 346, 996-1000 (2014).
    • (2014) Science , vol.346 , pp. 996-1000
    • Fonville, J.M.1
  • 29
    • 84920982264 scopus 로고    scopus 로고
    • Variation in the human immune system is largely driven by nonheritable influences
    • Brodin, P. et al. Variation in the human immune system is largely driven by nonheritable influences. Cell 160, 37-47 (2015).
    • (2015) Cell , vol.160 , pp. 37-47
    • Brodin, P.1
  • 30
    • 84954245342 scopus 로고    scopus 로고
    • Immune history profoundly affects broadly protective B cell responses to influenza
    • Andrews, S. F. et al. Immune history profoundly affects broadly protective B cell responses to influenza. Sci. Transl. Med. 7, 316ra192 (2015).
    • (2015) Sci. Transl. Med. , vol.7 , pp. 316-392
    • Andrews, S.F.1
  • 31
  • 32
    • 84893840611 scopus 로고    scopus 로고
    • Identification and characterization of the constituent human serum antibodies elicited by vaccination
    • Lavinder, J. J. et al. Identification and characterization of the constituent human serum antibodies elicited by vaccination. Proc. Natl. Acad. Sci. USA 111, 2259-2264 (2014).
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 2259-2264
    • Lavinder, J.J.1
  • 33
    • 84893831480 scopus 로고    scopus 로고
    • The promise and challenge of high-throughput sequencing of the antibody repertoire
    • Georgiou, G. et al. The promise and challenge of high-throughput sequencing of the antibody repertoire. Nat. Biotechnol. 32, 158-168 (2014).
    • (2014) Nat. Biotechnol. , vol.32 , pp. 158-168
    • Georgiou, G.1
  • 34
    • 84925284996 scopus 로고    scopus 로고
    • In-depth determination and analysis of the human paired heavy-and light-chain antibody repertoire
    • DeKosky, B. J. et al. In-depth determination and analysis of the human paired heavy-and light-chain antibody repertoire. Nat. Med. 21, 86-91 (2015).
    • (2015) Nat. Med. , vol.21 , pp. 86-91
    • DeKosky, B.J.1
  • 35
    • 84901253129 scopus 로고    scopus 로고
    • Proteomic identification of monoclonal antibodies from serum
    • Boutz, D. R. et al. Proteomic identification of monoclonal antibodies from serum. Anal. Chem. 86, 4758-4766 (2014).
    • (2014) Anal. Chem. , vol.86 , pp. 4758-4766
    • Boutz, D.R.1
  • 36
    • 84936880720 scopus 로고    scopus 로고
    • Serology in the 21st century: The molecular-level analysis of the serum antibody repertoire
    • Wine, Y., Horton, A. P., Ippolito, G. C., Georgiou, G. Serology in the 21st century: the molecular-level analysis of the serum antibody repertoire. Curr. Opin. Immunol. 35, 89-97 (2015).
    • (2015) Curr. Opin. Immunol. , vol.35 , pp. 89-97
    • Wine, Y.1    Horton, A.P.2    Ippolito, G.C.3    Georgiou, G.4
  • 37
    • 52149124652 scopus 로고    scopus 로고
    • Influence of prior influenza vaccination on antibody and B cell responses
    • Sasaki, S. et al. Influence of prior influenza vaccination on antibody and B cell responses. PLoS One 3, e2975 (2008).
    • (2008) PLoS One , vol.3 , pp. e2975
    • Sasaki, S.1
  • 38
    • 84923172329 scopus 로고    scopus 로고
    • High pre-existing serological antibody levels correlate with diversification of the influenza vaccine response
    • Andrews, S. F. et al. High pre-existing serological antibody levels correlate with diversification of the influenza vaccine response. J. Virol. 89, 3308-3317 (2015).
    • (2015) J. Virol. , vol.89 , pp. 3308-3317
    • Andrews, S.F.1
  • 39
    • 84941023600 scopus 로고    scopus 로고
    • Hemagglutinin-stem nanoparticles generate heterosubtypic influenza protection
    • Yassine, H. M. et al. Hemagglutinin-stem nanoparticles generate heterosubtypic influenza protection. Nat. Med. 21, 1065-1070 (2015).
    • (2015) Nat. Med. , vol.21 , pp. 1065-1070
    • Yassine, H.M.1
  • 40
    • 84930083052 scopus 로고    scopus 로고
    • Viral receptor-binding site antibodies with diverse germline origins
    • Schmidt, A. G. et al. Viral receptor-binding site antibodies with diverse germline origins. Cell 161, 1026-1034 (2015).
    • (2015) Cell , vol.161 , pp. 1026-1034
    • Schmidt, A.G.1
  • 41
    • 0026560161 scopus 로고
    • Introduction of intersubunit disulfide bonds in the membrane-distal region of the influenza hemagglutinin abolishes membrane fusion activity
    • Godley, L. et al. Introduction of intersubunit disulfide bonds in the membrane-distal region of the influenza hemagglutinin abolishes membrane fusion activity. Cell 68, 635-645 (1992).
    • (1992) Cell , vol.68 , pp. 635-645
    • Godley, L.1
  • 42
    • 84901981487 scopus 로고    scopus 로고
    • Conserved neutralizing epitope at globular head of hemagglutinin in H3N2 influenza viruses
    • Iba, Y. et al. Conserved neutralizing epitope at globular head of hemagglutinin in H3N2 influenza viruses. J. Virol. 88, 7130-7144 (2014).
    • (2014) J. Virol. , vol.88 , pp. 7130-7144
    • Iba, Y.1
  • 43
    • 84866953140 scopus 로고    scopus 로고
    • Cross-neutralization of influenza A viruses mediated by a single antibody loop
    • Ekiert, D. C. et al. Cross-neutralization of influenza A viruses mediated by a single antibody loop. Nature 489, 526-532 (2012).
    • (2012) Nature , vol.489 , pp. 526-532
    • Ekiert, D.C.1
  • 44
    • 84890902002 scopus 로고    scopus 로고
    • Vaccine for prevention of mild and moderate-to-severe influenza in children
    • Jain, V. K. et al. Vaccine for prevention of mild and moderate-to-severe influenza in children. N. Engl. J. Med. 369, 2481-2491 (2013).
    • (2013) N. Engl. J. Med. , vol.369 , pp. 2481-2491
    • Jain, V.K.1
  • 45
    • 84896733461 scopus 로고    scopus 로고
    • Immunogenicity, reactogenicity and safety of inactivated quadrivalent influenza vaccine candidate versus inactivated trivalent influenza vaccine in healthy adults aged 18 years: A phase 3, randomized trial
    • Tinoco, J. C. et al. Immunogenicity, reactogenicity and safety of inactivated quadrivalent influenza vaccine candidate versus inactivated trivalent influenza vaccine in healthy adults aged 18 years: a phase 3, randomized trial. Vaccine 32, 1480-1487 (2014).
    • (2014) Vaccine , vol.32 , pp. 1480-1487
    • Tinoco, J.C.1
  • 47
    • 0006348842 scopus 로고
    • On the doctrine of original antigenic sin
    • Francis, T. J. On the doctrine of original antigenic sin. Proc. Am. Phil. Soc. 104, 572-578 (1960).
    • (1960) Proc. Am. Phil. Soc. , vol.104 , pp. 572-578
    • Francis, T.J.1
  • 48
    • 84893797938 scopus 로고    scopus 로고
    • Broadly neutralizing hemagglutinin stalk-specific antibodies require Fc-R interactions for protection against influenza virus in vivo
    • DiLillo, D. J., Tan, G. S., Palese, P., Ravetch, J. V. Broadly neutralizing hemagglutinin stalk-specific antibodies require Fc-R interactions for protection against influenza virus in vivo. Nat. Med. 20, 143-151 (2014).
    • (2014) Nat. Med. , vol.20 , pp. 143-151
    • DiLillo, D.J.1    Tan, G.S.2    Palese, P.3    Ravetch, J.V.4
  • 49
    • 84959350663 scopus 로고    scopus 로고
    • Ultra-high-throughput sequencing of the immune receptor repertoire from millions of lymphocytes
    • McDaniel, J. R., DeKosky, B. J., Tanno, H., Ellington, A. D., Georgiou, G. Ultra-high-throughput sequencing of the immune receptor repertoire from millions of lymphocytes. Nat. Protoc. 11, 429-442 (2016).
    • (2016) Nat. Protoc. , vol.11 , pp. 429-442
    • McDaniel, J.R.1    DeKosky, B.J.2    Tanno, H.3    Ellington, A.D.4    Georgiou, G.5
  • 50
    • 80052674536 scopus 로고    scopus 로고
    • Software lock mass by two-dimensional minimization of peptide mass errors
    • Cox, J., Michalski, A., Mann, M. Software lock mass by two-dimensional minimization of peptide mass errors. J. Am. Soc. Mass Spectrom. 22, 1373-1380 (2011).
    • (2011) J. Am. Soc. Mass Spectrom. , vol.22 , pp. 1373-1380
    • Cox, J.1    Michalski, A.2    Mann, M.3
  • 51
    • 1842432386 scopus 로고    scopus 로고
    • Selective modification of variable loops alters tropism and enhances immunogenicity of human immunodeficiency virus type 1 envelope
    • Yang, Z. Y. et al. Selective modification of variable loops alters tropism and enhances immunogenicity of human immunodeficiency virus type 1 envelope. J. Virol. 78, 4029-4036 (2004).
    • (2004) J. Virol. , vol.78 , pp. 4029-4036
    • Yang, Z.Y.1
  • 52
    • 33750071716 scopus 로고    scopus 로고
    • Emerging respiratory viruses: Challenges and vaccine strategies
    • Gillim-Ross, L., Subbarao, K. Emerging respiratory viruses: challenges and vaccine strategies. Clin. Microbiol. Rev. 19, 614-636 (2006).
    • (2006) Clin. Microbiol. Rev. , vol.19 , pp. 614-636
    • Gillim-Ross, L.1    Subbarao, K.2
  • 53
    • 0034252626 scopus 로고    scopus 로고
    • C3d enhancement of antibodies to hemagglutinin accelerates protection against influenza virus challenge
    • Ross, T. M., Xu, Y., Bright, R. A., Robinson, H. L. C3d enhancement of antibodies to hemagglutinin accelerates protection against influenza virus challenge. Nat. Immunol. 1, 127-131 (2000).
    • (2000) Nat. Immunol. , vol.1 , pp. 127-131
    • Ross, T.M.1    Xu, Y.2    Bright, R.A.3    Robinson, H.L.4
  • 54
    • 25644458666 scopus 로고    scopus 로고
    • Automated electron microscope tomography using robust prediction of specimen movements
    • Mastronarde, D. N. Automated electron microscope tomography using robust prediction of specimen movements. J. Structural Biology 152, 36-51 (2005).
    • (2005) J. Structural Biology , vol.152 , pp. 36-51
    • Mastronarde, D.N.1
  • 55
    • 33845332754 scopus 로고    scopus 로고
    • EMAN2: An extensible image processing suite for electron microscopy
    • Tang, G. et al. EMAN2: An extensible image processing suite for electron microscopy. Journal of Struct. Biol. 157, 38-46 (2007).
    • (2007) Journal of Struct. Biol. , vol.157 , pp. 38-46
    • Tang, G.1
  • 56
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3d electron microscopy and related fields
    • Frank, J. et al. SPIDER and WEB: processing and visualization of images in 3d electron microscopy and related fields. J. Struct. Biol. 116, 190-199 (1996).
    • (1996) J. Struct. Biol. , vol.116 , pp. 190-199
    • Frank, J.1
  • 57
    • 84985231782 scopus 로고
    • Three-dimensional reconstruction from a single-exposure random conical tilt series applied to the 50S ribosomal subunit of Escherichia coli
    • Radermacher, M., Wagenknecht, T., Verschoor, A., Frank, J. Three-dimensional reconstruction from a single-exposure, random conical tilt series applied to the 50S ribosomal subunit of Escherichia coli. J. Microsc. 146, 113-136 (1987).
    • (1987) J. Microsc. , vol.146 , pp. 113-136
    • Radermacher, M.1    Wagenknecht, T.2    Verschoor, A.3    Frank, J.4
  • 58
    • 4444221565 scopus 로고    scopus 로고
    • UCSF Chimera-a visualization system for exploratory research and analysis
    • Pettersen, E. F. et al. UCSF Chimera-a visualization system for exploratory research and analysis. J. Comput. Chem. 25, 1605-1612 (2004).
    • (2004) J. Comput. Chem. , vol.25 , pp. 1605-1612
    • Pettersen, E.F.1
  • 59
    • 58049204808 scopus 로고    scopus 로고
    • SPIDER image processing for single-particle reconstruction of biological macromolecules from electron micrographs
    • Shaikh, T. R. et al. SPIDER image processing for single-particle reconstruction of biological macromolecules from electron micrographs. Nat. Protoc. 3, 1941-1974 (2008).
    • (2008) Nat. Protoc. , vol.3 , pp. 1941-1974
    • Shaikh, T.R.1


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