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Volumn 113, Issue 45, 2016, Pages 12768-12773

Structural flexibility at a major conserved antibody target on Hepatitis C virus E2 antigen

Author keywords

CD81 binding site; Conformational flexibility; E2; Hepatitis C virus; Protein dynamics

Indexed keywords

CD81 ANTIGEN; HEPATITIS C VIRUS E2 ANTIGEN; UNCLASSIFIED DRUG; VIRUS ANTIGEN;

EID: 84994545682     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1609780113     Document Type: Article
Times cited : (68)

References (72)
  • 1
    • 84921060015 scopus 로고    scopus 로고
    • Global distribution and prevalence of hepatitis C virus genotypes
    • Messina JP, et al. (2015) Global distribution and prevalence of hepatitis C virus genotypes. Hepatology 61(1):77-87.
    • (2015) Hepatology , vol.61 , Issue.1 , pp. 77-87
    • Messina, J.P.1
  • 2
    • 84891738607 scopus 로고    scopus 로고
    • HCV transmission in industrialized countries and resourceconstrained areas
    • Thursz M, Fontanet A (2014) HCV transmission in industrialized countries and resourceconstrained areas. Nat Rev Gastroenterol Hepatol 11(1):28-35.
    • (2014) Nat Rev Gastroenterol Hepatol , vol.11 , Issue.1 , pp. 28-35
    • Thursz, M.1    Fontanet, A.2
  • 3
    • 84903975871 scopus 로고    scopus 로고
    • Antiviral treatment of hepatitis C
    • Feeney ER, Chung RT (2014) Antiviral treatment of hepatitis C. BMJ 348:g3308.
    • (2014) BMJ , vol.348 , pp. g3308
    • Feeney, E.R.1    Chung, R.T.2
  • 4
    • 84934823081 scopus 로고    scopus 로고
    • From non-A, non-B hepatitis to hepatitis C virus cure
    • Pawlotsky JM, Feld JJ, Zeuzem S, Hoofnagle JH (2015) From non-A, non-B hepatitis to hepatitis C virus cure. J Hepatol 62(1, Suppl):S87-S99.
    • (2015) J Hepatol , vol.62 , Issue.1 , pp. S87-S99
    • Pawlotsky, J.M.1    Feld, J.J.2    Zeuzem, S.3    Hoofnagle, J.H.4
  • 5
    • 84893058008 scopus 로고    scopus 로고
    • Hepatitis C virus genotype diversity among intravenous drug users in Yunnan Province, Southwestern China
    • Zhang Z, et al. (2013) Hepatitis C virus genotype diversity among intravenous drug users in Yunnan Province, Southwestern China. PLoS One 8(12):e82598.
    • (2013) PLoS One , vol.8 , Issue.12 , pp. e82598
    • Zhang, Z.1
  • 6
    • 84857144025 scopus 로고    scopus 로고
    • The increasing burden of mortality from viral hepatitis in the United States between 1999 and 2007
    • Ly KN, et al. (2012) The increasing burden of mortality from viral hepatitis in the United States between 1999 and 2007. Ann Intern Med 156(4):271-278.
    • (2012) Ann Intern Med , vol.156 , Issue.4 , pp. 271-278
    • Ly, K.N.1
  • 7
    • 84879131244 scopus 로고    scopus 로고
    • Hepatitis C virus reinfection among prisoners with sustained virological response after treatment for chronic hepatitis C
    • Marco A, et al. (2013) Hepatitis C virus reinfection among prisoners with sustained virological response after treatment for chronic hepatitis C. J Hepatol 59(1):45-51.
    • (2013) J Hepatol , vol.59 , Issue.1 , pp. 45-51
    • Marco, A.1
  • 8
    • 84963649635 scopus 로고    scopus 로고
    • Hepatitis C reinfection after sustained virological response
    • Midgard H, et al. (2016) Hepatitis C reinfection after sustained virological response. J Hepatol 64(5):1020-1026.
    • (2016) J Hepatol , vol.64 , Issue.5 , pp. 1020-1026
    • Midgard, H.1
  • 9
    • 84928945299 scopus 로고    scopus 로고
    • Capitalizing on knowledge of hepatitis C virus neutralizing epitopes for rational vaccine design
    • Kong L, Jackson KN, Wilson IA, Law M (2015) Capitalizing on knowledge of hepatitis C virus neutralizing epitopes for rational vaccine design. Curr Opin Virol 11:148-157.
    • (2015) Curr Opin Virol , vol.11 , pp. 148-157
    • Kong, L.1    Jackson, K.N.2    Wilson, I.A.3    Law, M.4
  • 10
    • 84938603864 scopus 로고    scopus 로고
    • Hepatitis C virus: Why do we need a vaccine to prevent a curable persistent infection?
    • Walker CM, Grakoui A (2015) Hepatitis C virus: Why do we need a vaccine to prevent a curable persistent infection? Curr Opin Immunol 35:137-143.
    • (2015) Curr Opin Immunol , vol.35 , pp. 137-143
    • Walker, C.M.1    Grakoui, A.2
  • 11
    • 84939817155 scopus 로고    scopus 로고
    • MEDICINE. Global control of hepatitis C virus
    • Cox AL (2015) MEDICINE. Global control of hepatitis C virus. Science 349(6250):790-791.
    • (2015) Science , vol.349 , Issue.6250 , pp. 790-791
    • Cox, A.L.1
  • 12
    • 84893943976 scopus 로고    scopus 로고
    • CD81-receptor associations. Impact for hepatitis C virus entry and antiviral therapies
    • Zona L, et al. (2014) CD81-receptor associations. impact for hepatitis C virus entry and antiviral therapies. Viruses 6(2):875-892.
    • (2014) Viruses , vol.6 , Issue.2 , pp. 875-892
    • Zona, L.1
  • 14
    • 84888778890 scopus 로고    scopus 로고
    • Hepatitis C virus E2 envelope glycoprotein core structure
    • Kong L, et al. (2013) Hepatitis C virus E2 envelope glycoprotein core structure. Science 342(6162):1090-1094.
    • (2013) Science , vol.342 , Issue.6162 , pp. 1090-1094
    • Kong, L.1
  • 15
    • 33748673151 scopus 로고    scopus 로고
    • Identification of conserved residues in the E2 envelope glycoprotein of the hepatitis C virus that are critical for CD81 binding
    • Owsianka AM, et al. (2006) Identification of conserved residues in the E2 envelope glycoprotein of the hepatitis C virus that are critical for CD81 binding. J Virol 80(17):8695-8704.
    • (2006) J Virol , vol.80 , Issue.17 , pp. 8695-8704
    • Owsianka, A.M.1
  • 16
    • 0036839176 scopus 로고    scopus 로고
    • Identification of the hepatitis C virus E2 glycoprotein binding site on the large extracellular loop of CD81
    • Drummer HE, Wilson KA, Poumbourios P (2002) Identification of the hepatitis C virus E2 glycoprotein binding site on the large extracellular loop of CD81. J Virol 76(21):11143-11147.
    • (2002) J Virol , vol.76 , Issue.21 , pp. 11143-11147
    • Drummer, H.E.1    Wilson, K.A.2    Poumbourios, P.3
  • 17
    • 84869229723 scopus 로고    scopus 로고
    • Structure of hepatitis C virus envelope glycoprotein E2 antigenic site 412 to 423 in complex with antibody AP33
    • Kong L, et al. (2012) Structure of hepatitis C virus envelope glycoprotein E2 antigenic site 412 to 423 in complex with antibody AP33. J Virol 86(23):13085-13088.
    • (2012) J Virol , vol.86 , Issue.23 , pp. 13085-13088
    • Kong, L.1
  • 18
    • 84862177880 scopus 로고    scopus 로고
    • Structural basis of hepatitis C virus neutralization by broadly neutralizing antibody HCV1
    • Kong L, et al. (2012) Structural basis of hepatitis C virus neutralization by broadly neutralizing antibody HCV1. Proc Natl Acad Sci USA 109(24):9499-9504.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.24 , pp. 9499-9504
    • Kong, L.1
  • 19
    • 84869233037 scopus 로고    scopus 로고
    • Toward a hepatitis C virus vaccine: The structural basis of hepatitis C virus neutralization by AP33, a broadly neutralizing antibody
    • Potter JA, et al. (2012) Toward a hepatitis C virus vaccine: The structural basis of hepatitis C virus neutralization by AP33, a broadly neutralizing antibody. J Virol 86(23):12923-12932.
    • (2012) J Virol , vol.86 , Issue.23 , pp. 12923-12932
    • Potter, J.A.1
  • 20
    • 84877720407 scopus 로고    scopus 로고
    • Glycan shifting on hepatitis C virus (HCV) E2 glycoprotein is a mechanism for escape from broadly neutralizing antibodies
    • Pantua H, et al. (2013) Glycan shifting on hepatitis C virus (HCV) E2 glycoprotein is a mechanism for escape from broadly neutralizing antibodies. J Mol Biol 425(11):1899-1914.
    • (2013) J Mol Biol , vol.425 , Issue.11 , pp. 1899-1914
    • Pantua, H.1
  • 21
    • 84921684956 scopus 로고    scopus 로고
    • Structural flexibility of a conserved antigenic region in hepatitis C virus glycoprotein E2 recognized by broadly neutralizing antibodies
    • Meola A, et al. (2015) Structural flexibility of a conserved antigenic region in hepatitis C virus glycoprotein E2 recognized by broadly neutralizing antibodies. J Virol 89(4):2170-2181.
    • (2015) J Virol , vol.89 , Issue.4 , pp. 2170-2181
    • Meola, A.1
  • 22
    • 84927920900 scopus 로고    scopus 로고
    • Structural basis for penetration of the glycan shield of hepatitis C virus E2 glycoprotein by a broadly neutralizing human antibody
    • Li Y, et al. (2015) Structural basis for penetration of the glycan shield of hepatitis C virus E2 glycoprotein by a broadly neutralizing human antibody. J Biol Chem 290(16):10117-10125.
    • (2015) J Biol Chem , vol.290 , Issue.16 , pp. 10117-10125
    • Li, Y.1
  • 23
    • 84878472445 scopus 로고    scopus 로고
    • Structural basis of HCV neutralization by human monoclonal antibodies resistant to viral neutralization escape
    • Krey T, et al. (2013) Structural basis of HCV neutralization by human monoclonal antibodies resistant to viral neutralization escape. PLoS Pathog 9(5):e1003364.
    • (2013) PLoS Pathog , vol.9 , Issue.5 , pp. e1003364
    • Krey, T.1
  • 24
    • 84876942110 scopus 로고    scopus 로고
    • Structural evidence for a bifurcated mode of action in the antibody-mediated neutralization of hepatitis C virus
    • Deng L, et al. (2013) Structural evidence for a bifurcated mode of action in the antibody-mediated neutralization of hepatitis C virus. Proc Natl Acad Sci USA 110(18):7418-7422.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.18 , pp. 7418-7422
    • Deng, L.1
  • 25
    • 38049083122 scopus 로고    scopus 로고
    • Broadly neutralizing antibodies protect against hepatitis C virus quasispecies challenge
    • Law M, et al. (2008) Broadly neutralizing antibodies protect against hepatitis C virus quasispecies challenge. Nat Med 14(1):25-27.
    • (2008) Nat Med , vol.14 , Issue.1 , pp. 25-27
    • Law, M.1
  • 26
    • 84859965965 scopus 로고    scopus 로고
    • Human broadly neutralizing antibodies to the envelope glycoprotein complex of hepatitis C virus
    • Giang E, et al. (2012) Human broadly neutralizing antibodies to the envelope glycoprotein complex of hepatitis C virus. Proc Natl Acad Sci USA 109(16):6205-6210.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.16 , pp. 6205-6210
    • Giang, E.1
  • 27
    • 77955659499 scopus 로고    scopus 로고
    • Characterization of antibodies induced by vaccination with hepatitis C virus envelope glycoproteins
    • Ray R, et al. (2010) Characterization of antibodies induced by vaccination with hepatitis C virus envelope glycoproteins. J Infect Dis 202(6):862-866.
    • (2010) J Infect Dis , vol.202 , Issue.6 , pp. 862-866
    • Ray, R.1
  • 28
    • 80051923476 scopus 로고    scopus 로고
    • A weak neutralizing antibody response to hepatitis C virus envelope glycoprotein enhances virus infection
    • Meyer K, Banerjee A, Frey SE, Belshe RB, Ray R (2011) A weak neutralizing antibody response to hepatitis C virus envelope glycoprotein enhances virus infection. PLoS One 6(8):e23699.
    • (2011) PLoS One , vol.6 , Issue.8 , pp. e23699
    • Meyer, K.1    Banerjee, A.2    Frey, S.E.3    Belshe, R.B.4    Ray, R.5
  • 29
    • 34347253229 scopus 로고    scopus 로고
    • Hepatitis C virus epitope-specific neutralizing antibodies in Igs prepared from human plasma
    • Zhang P, et al. (2007) Hepatitis C virus epitope-specific neutralizing antibodies in Igs prepared from human plasma. Proc Natl Acad Sci USA 104(20):8449-8454.
    • (2007) Proc Natl Acad Sci USA , vol.104 , Issue.20 , pp. 8449-8454
    • Zhang, P.1
  • 30
    • 84906330457 scopus 로고    scopus 로고
    • Fine mapping of murine antibody responses to immunization with a novel soluble form of hepatitis C virus envelope glycoprotein complex
    • Ruwona TB, Giang E, Nieusma T, Law M (2014) Fine mapping of murine antibody responses to immunization with a novel soluble form of hepatitis C virus envelope glycoprotein complex. J Virol 88(18):10459-10471.
    • (2014) J Virol , vol.88 , Issue.18 , pp. 10459-10471
    • Ruwona, T.B.1    Giang, E.2    Nieusma, T.3    Law, M.4
  • 31
    • 84896977436 scopus 로고    scopus 로고
    • The past, present and future of neutralizing antibodies for hepatitis C virus
    • Ball JK, Tarr AW, McKeating JA (2014) The past, present and future of neutralizing antibodies for hepatitis C virus. Antiviral Res 105:100-111.
    • (2014) Antiviral Res , vol.105 , pp. 100-111
    • Ball, J.K.1    Tarr, A.W.2    McKeating, J.A.3
  • 32
    • 0036145390 scopus 로고    scopus 로고
    • Binding of hepatitis C virus-like particles derived from infectious clone H77C to defined human cell lines
    • Wellnitz S, et al. (2002) Binding of hepatitis C virus-like particles derived from infectious clone H77C to defined human cell lines. J Virol 76(3):1181-1193.
    • (2002) J Virol , vol.76 , Issue.3 , pp. 1181-1193
    • Wellnitz, S.1
  • 33
    • 0036302087 scopus 로고    scopus 로고
    • Structural features of envelope proteins on hepatitis C viruslike particles as determined by anti-envelope monoclonal antibodies and CD81 binding
    • Triyatni M, et al. (2002) Structural features of envelope proteins on hepatitis C viruslike particles as determined by anti-envelope monoclonal antibodies and CD81 binding. Virology 298(1):124-132.
    • (2002) Virology , vol.298 , Issue.1 , pp. 124-132
    • Triyatni, M.1
  • 34
    • 83455254775 scopus 로고    scopus 로고
    • Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9
    • McLellan JS, et al. (2011) Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9. Nature 480(7377):336-343.
    • (2011) Nature , vol.480 , Issue.7377 , pp. 336-343
    • McLellan, J.S.1
  • 35
    • 33750320427 scopus 로고    scopus 로고
    • Hydrogen exchange and mass spectrometry: A historical perspective
    • Englander SW (2006) Hydrogen exchange and mass spectrometry: A historical perspective. J Am Soc Mass Spectrom 17(11):1481-1489.
    • (2006) J Am Soc Mass Spectrom , vol.17 , Issue.11 , pp. 1481-1489
    • Englander, S.W.1
  • 36
    • 79951887389 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry for studying protein structure and dynamics
    • Konermann L, Pan J, Liu YH (2011) Hydrogen exchange mass spectrometry for studying protein structure and dynamics. Chem Soc Rev 40(3):1224-1234.
    • (2011) Chem Soc Rev , vol.40 , Issue.3 , pp. 1224-1234
    • Konermann, L.1    Pan, J.2    Liu, Y.H.3
  • 37
    • 82555169314 scopus 로고    scopus 로고
    • Ebola virus glycoprotein needs an additional trigger, beyond proteolytic priming for membrane fusion
    • Bale S, et al. (2011) Ebola virus glycoprotein needs an additional trigger, beyond proteolytic priming for membrane fusion. PLoS Negl Trop Dis 5(11):e1395.
    • (2011) PLoS Negl Trop Dis , vol.5 , Issue.11 , pp. e1395
    • Bale, S.1
  • 38
    • 77956819789 scopus 로고    scopus 로고
    • Local conformational stability of HIV-1 gp120 in unliganded and CD4-bound states as defined by amide hydrogen/deuterium exchange
    • Kong L, et al. (2010) Local conformational stability of HIV-1 gp120 in unliganded and CD4-bound states as defined by amide hydrogen/deuterium exchange. J Virol 84(19):10311-10321.
    • (2010) J Virol , vol.84 , Issue.19 , pp. 10311-10321
    • Kong, L.1
  • 39
    • 70450182950 scopus 로고    scopus 로고
    • Structural basis of immune evasion at the site of CD4 attachment on HIV-1 gp120
    • Chen L, et al. (2009) Structural basis of immune evasion at the site of CD4 attachment on HIV-1 gp120. Science 326(5956):1123-1127.
    • (2009) Science , vol.326 , Issue.5956 , pp. 1123-1127
    • Chen, L.1
  • 41
    • 84900798422 scopus 로고    scopus 로고
    • Structure of the core ectodomain of the hepatitis C virus envelope glycoprotein 2
    • Khan AG, et al. (2014) Structure of the core ectodomain of the hepatitis C virus envelope glycoprotein 2. Nature 509(7500):381-384.
    • (2014) Nature , vol.509 , Issue.7500 , pp. 381-384
    • Khan, A.G.1
  • 42
    • 84904609849 scopus 로고    scopus 로고
    • Discrete conformations of epitope II on the hepatitis C virus E2 protein for antibody-mediated neutralization and nonneutralization
    • Deng L, et al. (2014) Discrete conformations of epitope II on the hepatitis C virus E2 protein for antibody-mediated neutralization and nonneutralization. Proc Natl Acad Sci USA 111(29):10690-10695.
    • (2014) Proc Natl Acad Sci USA , vol.111 , Issue.29 , pp. 10690-10695
    • Deng, L.1
  • 43
    • 35648936537 scopus 로고    scopus 로고
    • A structural hypothesis for the transition between bent and extended conformations of the leukocyte-À2 integrins
    • Shi M, et al. (2007) A structural hypothesis for the transition between bent and extended conformations of the leukocyte-À2 integrins. J Biol Chem 282(41):30198-30206.
    • (2007) J Biol Chem , vol.282 , Issue.41 , pp. 30198-30206
    • Shi, M.1
  • 44
    • 77958477970 scopus 로고    scopus 로고
    • Modulation of integrin activation by an entropic spring in the -À-knee
    • Smagghe BJ, Huang PS, Ban YE, Baker D, Springer TA (2010) Modulation of integrin activation by an entropic spring in the -À-knee. J Biol Chem 285(43):32954-32966.
    • (2010) J Biol Chem , vol.285 , Issue.43 , pp. 32954-32966
    • Smagghe, B.J.1    Huang, P.S.2    Ban, Y.E.3    Baker, D.4    Springer, T.A.5
  • 45
    • 33745726737 scopus 로고    scopus 로고
    • Lessons in stability from thermophilic proteins
    • Razvi A, Scholtz JM (2006) Lessons in stability from thermophilic proteins. Protein Sci 15(7):1569-1578.
    • (2006) Protein Sci , vol.15 , Issue.7 , pp. 1569-1578
    • Razvi, A.1    Scholtz, J.M.2
  • 46
    • 84884678235 scopus 로고    scopus 로고
    • A next-generation cleaved, soluble HIV-1 Env trimer, BG505 SOSIP. 664 gp140, expresses multiple epitopes for broadly neutralizing but not nonneutralizing antibodies
    • Sanders RW, et al. (2013) A next-generation cleaved, soluble HIV-1 Env trimer, BG505 SOSIP. 664 gp140, expresses multiple epitopes for broadly neutralizing but not nonneutralizing antibodies. PLoS Pathog 9(9):e1003618.
    • (2013) PLoS Pathog , vol.9 , Issue.9 , pp. e1003618
    • Sanders, R.W.1
  • 47
    • 0036684445 scopus 로고    scopus 로고
    • Thermal denaturation of influenza virus and its relationship to membrane fusion
    • Epand RM, Epand RF (2002) Thermal denaturation of influenza virus and its relationship to membrane fusion. Biochem J 365(Pt 3):841-848.
    • (2002) Biochem J , vol.365 , pp. 841-848
    • Epand, R.M.1    Epand, R.F.2
  • 48
    • 77949537282 scopus 로고    scopus 로고
    • Naturally occurring variability in the envelope glycoprotein of HIV-1 and development of cell entry inhibitors
    • Brower ET, Schon A, Freire E (2010) Naturally occurring variability in the envelope glycoprotein of HIV-1 and development of cell entry inhibitors. Biochemistry 49(11):2359-2367.
    • (2010) Biochemistry , vol.49 , Issue.11 , pp. 2359-2367
    • Brower, E.T.1    Schon, A.2    Freire, E.3
  • 49
    • 84958055228 scopus 로고    scopus 로고
    • Differential scanning calorimetry (DSC) for biopharmaceutical development: Old concepts, new applications
    • Morar-Mitrica S, Nesta D, Crotts G (2013) Differential scanning calorimetry (DSC) for biopharmaceutical development: Old concepts, new applications. Biopharma Asia 2(4):44-55.
    • (2013) Biopharma Asia , vol.2 , Issue.4 , pp. 44-55
    • Morar-Mitrica, S.1    Nesta, D.2    Crotts, G.3
  • 51
    • 0034255034 scopus 로고    scopus 로고
    • Energetics of the HIV gp120-CD4 binding reaction
    • Myszka DG, et al. (2000) Energetics of the HIV gp120-CD4 binding reaction. Proc Natl Acad Sci USA 97(16):9026-9031.
    • (2000) Proc Natl Acad Sci USA , vol.97 , Issue.16 , pp. 9026-9031
    • Myszka, D.G.1
  • 52
    • 84960970619 scopus 로고    scopus 로고
    • Generation and characterization of monoclonal antibodies against a cyclic variant of hepatitis C virus E2 epitope 412-422
    • Sandomenico A, et al. (2016) Generation and characterization of monoclonal antibodies against a cyclic variant of hepatitis C virus E2 epitope 412-422. J Virol 90(7):3745-3759.
    • (2016) J Virol , vol.90 , Issue.7 , pp. 3745-3759
    • Sandomenico, A.1
  • 53
    • 84887277978 scopus 로고    scopus 로고
    • Structure-based design of a fusion glycoprotein vaccine for respiratory syncytial virus
    • McLellan JS, et al. (2013) Structure-based design of a fusion glycoprotein vaccine for respiratory syncytial virus. Science 342(6158):592-598.
    • (2013) Science , vol.342 , Issue.6158 , pp. 592-598
    • McLellan, J.S.1
  • 54
    • 84923850343 scopus 로고    scopus 로고
    • Well-ordered trimeric HIV-1 subtype B and C soluble spike mimetics generated by negative selection display native-like properties
    • Guenaga J, et al. (2015) Well-ordered trimeric HIV-1 subtype B and C soluble spike mimetics generated by negative selection display native-like properties. PLoS Pathog 11(1):e1004570.
    • (2015) PLoS Pathog , vol.11 , Issue.1 , pp. e1004570
    • Guenaga, J.1
  • 55
    • 84976633087 scopus 로고    scopus 로고
    • Uncleaved prefusion-optimized gp140 trimers derived from analysis of HIV-1 envelope metastability
    • Kong L, et al. (2016) Uncleaved prefusion-optimized gp140 trimers derived from analysis of HIV-1 envelope metastability. Nat Commun 7:12040.
    • (2016) Nat Commun , vol.7 , pp. 12040
    • Kong, L.1
  • 56
    • 76049121502 scopus 로고    scopus 로고
    • A conserved MutS homolog connector domain interface interacts with MutL homologs
    • Mendillo ML, et al. (2009) A conserved MutS homolog connector domain interface interacts with MutL homologs. Proc Natl Acad Sci USA 106(52):22223-22228.
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.52 , pp. 22223-22228
    • Mendillo, M.L.1
  • 57
    • 78049233405 scopus 로고    scopus 로고
    • Allosteric inhibition of complement function by a staphylococcal immune evasion protein
    • Chen H, et al. (2010) Allosteric inhibition of complement function by a staphylococcal immune evasion protein. Proc Natl Acad Sci USA 107(41):17621-17626.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.41 , pp. 17621-17626
    • Chen, H.1
  • 58
    • 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(2):205-213.
    • (2009) J Struct Biol , vol.166 , Issue.2 , pp. 205-213
    • Voss, N.R.1    Yoshioka, C.K.2    Radermacher, M.3    Potter, C.S.4    Carragher, B.5
  • 59
    • 16244396466 scopus 로고    scopus 로고
    • Maximum-likelihood multi-reference refinement for electron microscopy images
    • Scheres SH, et al. (2005) Maximum-likelihood multi-reference refinement for electron microscopy images. J Mol Biol 348(1):139-149.
    • (2005) J Mol Biol , vol.348 , Issue.1 , pp. 139-149
    • Scheres, S.H.1
  • 60
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • Frank J, et al. (1996) SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields. J Struct Biol 116(1):190-199.
    • (1996) J Struct Biol , vol.116 , Issue.1 , pp. 190-199
    • Frank, J.1
  • 61
    • 0033377664 scopus 로고    scopus 로고
    • EMAN: Semiautomated software for high-resolution single-particle reconstructions
    • Ludtke SJ, Baldwin PR, Chiu W (1999) EMAN: Semiautomated software for high-resolution single-particle reconstructions. J Struct Biol 128(1):82-97.
    • (1999) J Struct Biol , vol.128 , Issue.1 , pp. 82-97
    • Ludtke, S.J.1    Baldwin, P.R.2    Chiu, W.3
  • 63
    • 0023682353 scopus 로고
    • Streptococcal protein G has affinity for both Fab- and Fc-fragments of human IgG
    • Erntell M, Myhre EB, Sjobring U, Bjorck L (1988) Streptococcal protein G has affinity for both Fab- and Fc-fragments of human IgG. Mol Immunol 25(2):121-126.
    • (1988) Mol Immunol , vol.25 , Issue.2 , pp. 121-126
    • Erntell, M.1    Myhre, E.B.2    Sjobring, U.3    Bjorck, L.4
  • 64
    • 82755167958 scopus 로고    scopus 로고
    • Crystal structure of the Lassa virus nucleoprotein-RNA complex reveals a gating mechanism for RNA binding
    • Hastie KM, et al. (2011) Crystal structure of the Lassa virus nucleoprotein-RNA complex reveals a gating mechanism for RNA binding. Proc Natl Acad Sci USA 108(48):19365-19370.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.48 , pp. 19365-19370
    • Hastie, K.M.1
  • 65
    • 84881656622 scopus 로고    scopus 로고
    • Structural insights into fibrinogen dynamics using amide hydrogen/deuterium exchange mass spectrometry
    • Marsh JJ, et al. (2013) Structural insights into fibrinogen dynamics using amide hydrogen/deuterium exchange mass spectrometry. Biochemistry 52(32):5491-5502.
    • (2013) Biochemistry , vol.52 , Issue.32 , pp. 5491-5502
    • Marsh, J.J.1
  • 66
    • 20544468931 scopus 로고    scopus 로고
    • Automated molecular microscopy: The new Leginon system
    • Suloway C, et al. (2005) Automated molecular microscopy: The new Leginon system. J Struct Biol 151(1):41-60.
    • (2005) J Struct Biol , vol.151 , Issue.1 , pp. 41-60
    • Suloway, C.1
  • 67
    • 0029912748 scopus 로고    scopus 로고
    • Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids
    • Jorgensen WL, Maxwell DS, Tirado Rives J (1996) Development and testing of the OPLS all-atom force field on conformational energetics and properties of organic liquids. J Am Chem Soc 118:11225-11236.
    • (1996) J Am Chem Soc , vol.118 , pp. 11225-11236
    • Jorgensen, W.L.1    Maxwell, D.S.2    Tirado Rives, J.3
  • 68
    • 0035871686 scopus 로고    scopus 로고
    • A fast SHAKE: Algorithm to solve distance constraint equations for small molecules in molecular dynamics simulations
    • Krautler V, van Gunsteren WF, Hunenberger PH (2001) A fast SHAKE: Algorithm to solve distance constraint equations for small molecules in molecular dynamics simulations. J Comput Chem 22:501-508.
    • (2001) J Comput Chem , vol.22 , pp. 501-508
    • Krautler, V.1    Van Gunsteren, W.F.2    Hunenberger, P.H.3
  • 69
    • 36449003554 scopus 로고
    • Constant-pressure molecular-dynamics algorithms
    • Martyna GJ, Tobias DJ, Klein ML (1994) Constant-pressure molecular-dynamics algorithms. J Chem Phys 101:4177-4189.
    • (1994) J Chem Phys , vol.101 , pp. 4177-4189
    • Martyna, G.J.1    Tobias, D.J.2    Klein, M.L.3
  • 70
    • 0001538909 scopus 로고
    • Canonical dynamics: Equilibrium phase-space distributions
    • Hoover WG (1985) Canonical dynamics: Equilibrium phase-space distributions. Phys Rev A Gen Phys 31(3):1695-1697.
    • (1985) Phys Rev a Gen Phys , vol.31 , Issue.3 , pp. 1695-1697
    • Hoover, W.G.1
  • 71
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N'Elog (N) method for Ewald sums in large systems
    • Darden TA, York DM, Pedersen LG (1993) Particle mesh Ewald: An N'Elog (N) method for Ewald sums in large systems. J Chem Phys 98:10089-10092.
    • (1993) J Chem Phys , vol.98 , pp. 10089-10092
    • Darden, T.A.1    York, D.M.2    Pedersen, L.G.3
  • 72
    • 33646650705 scopus 로고
    • Reversible multiple time scale moleculardynamics
    • Tuckerman M, Berne BJ, Martyna GJ (1992) Reversible multiple time scale moleculardynamics. J Chem Phys 97:1990-2001.
    • (1992) J Chem Phys , vol.97 , pp. 1990-2001
    • Tuckerman, M.1    Berne, B.J.2    Martyna, G.J.3


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