메뉴 건너뛰기




Volumn 110, Issue 30, 2013, Pages

Thermodynamic origins of protein folding, allostery, and capsid formation in the human hepatitis B virus core protein

Author keywords

Capsid assembly; Energy landscape; Protein dynamics; Thermodynamic coupling

Indexed keywords

CORE PROTEIN; DIMER; MUTANT PROTEIN;

EID: 84880691749     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1308846110     Document Type: Article
Times cited : (66)

References (60)
  • 2
    • 0031815749 scopus 로고    scopus 로고
    • How do small single-domain proteins fold?
    • Jackson SE (1998) How do small single-domain proteins fold? Fold Des 3(4): R81-R91.
    • (1998) Fold Des , vol.3 , Issue.4
    • Jackson, S.E.1
  • 3
    • 13444304369 scopus 로고    scopus 로고
    • PFD: A database for the investigation of protein folding kinetics and stability
    • (Database issue
    • Fulton KF, et al. (2005) PFD: A database for the investigation of protein folding kinetics and stability. Nucleic Acids Res 33(Database issue):D279-D283.
    • (2005) Nucleic Acids Res , vol.33
    • Fulton, K.F.1
  • 4
    • 0037666888 scopus 로고    scopus 로고
    • Implications of protein flexibility for drug discovery
    • Teague SJ (2003) Implications of protein flexibility for drug discovery. Nat Rev Drug Discov 2(7):527-541.
    • (2003) Nat Rev Drug Discov , vol.2 , Issue.7 , pp. 527-541
    • Teague, S.J.1
  • 5
    • 71149084765 scopus 로고    scopus 로고
    • Hepatitis B vaccines: WHO position paper-Recommendations
    • World Health Organization Publication
    • World Health Organization Publication (2010) Hepatitis B vaccines: WHO position paper-Recommendations. Vaccine 28(3):589-590.
    • (2010) Vaccine , vol.28 , Issue.3 , pp. 589-590
  • 6
    • 84867411012 scopus 로고    scopus 로고
    • Are novel combination therapies needed for chronic hepatitis B?
    • Zoulim F (2012) Are novel combination therapies needed for chronic hepatitis B? Antiviral Res 96(2):256-259.
    • (2012) Antiviral Res , vol.96 , Issue.2 , pp. 256-259
    • Zoulim, F.1
  • 7
    • 0042692926 scopus 로고    scopus 로고
    • Nuclear import of hepatitis B virus capsids and release of the viral genome
    • Rabe B, Vlachou A, Panté N, Helenius A, Kann M (2003) Nuclear import of hepatitis B virus capsids and release of the viral genome. Proc Natl Acad Sci USA 100(17):9849-9854.
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.17 , pp. 9849-9854
    • Rabe, B.1    Vlachou, A.2    Panté, N.3    Helenius, A.4    Kann, M.5
  • 8
    • 78651384693 scopus 로고    scopus 로고
    • The arginine clusters of the carboxy-terminal domain of the core protein of hepatitis B virus make pleiotropic contributions to genome replication
    • Lewellyn EB, Loeb DD (2011) The arginine clusters of the carboxy-terminal domain of the core protein of hepatitis B virus make pleiotropic contributions to genome replication. J Virol 85(3):1298-1309.
    • (2011) J Virol , vol.85 , Issue.3 , pp. 1298-1309
    • Lewellyn, E.B.1    Loeb, D.D.2
  • 9
    • 0037213251 scopus 로고    scopus 로고
    • Mapping of amino acid side chains on the surface of hepatitis B virus capsids required for envelopment and virion formation
    • Ponsel D, Bruss V (2003) Mapping of amino acid side chains on the surface of hepatitis B virus capsids required for envelopment and virion formation. J Virol 77 (1):416-422.
    • (2003) J Virol , vol.77 , Issue.1 , pp. 416-422
    • Ponsel, D.1    Bruss, V.2
  • 10
    • 78650580448 scopus 로고    scopus 로고
    • Trapping of hepatitis B virus capsid assembly intermediates by phenylpropenamide assembly accelerators
    • Katen SP, Chirapu SR, Finn MG, Zlotnick A (2010) Trapping of hepatitis B virus capsid assembly intermediates by phenylpropenamide assembly accelerators. ACS Chem Biol 5(12):1125-1136.
    • (2010) ACS Chem Biol , vol.5 , Issue.12 , pp. 1125-1136
    • Katen, S.P.1    Chirapu, S.R.2    Finn, M.G.3    Zlotnick, A.4
  • 11
    • 0347928672 scopus 로고    scopus 로고
    • Inhibition of hepatitis B virus replication by drug-induced depletion of nucleocapsids
    • Deres K, et al. (2003) Inhibition of hepatitis B virus replication by drug-induced depletion of nucleocapsids. Science 299(5608):893-896.
    • (2003) Science , vol.299 , Issue.5608 , pp. 893-896
    • Deres, K.1
  • 12
    • 33750704335 scopus 로고    scopus 로고
    • Global structural changes in hepatitis B virus capsids induced by the assembly effector HAP1
    • Bourne CR, Finn MG, Zlotnick A (2006) Global structural changes in hepatitis B virus capsids induced by the assembly effector HAP1. J Virol 80(22):11055-11061.
    • (2006) J Virol , vol.80 , Issue.22 , pp. 11055-11061
    • Bourne, C.R.1    Finn, M.G.2    Zlotnick, A.3
  • 13
    • 20444421508 scopus 로고    scopus 로고
    • A heteroaryldihydropyrimidine activates and can misdirect hepatitis B virus capsid assembly
    • Stray SJ, et al. (2005) A heteroaryldihydropyrimidine activates and can misdirect hepatitis B virus capsid assembly. Proc Natl Acad Sci USA 102(23):8138-8143.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.23 , pp. 8138-8143
    • Stray, S.J.1
  • 14
    • 0028928193 scopus 로고
    • Selection of peptide inhibitors of interactions involved in complex protein assemblies: Association of the core and surface antigens of hepatitis B virus
    • Dyson MR, Murray K (1995) Selection of peptide inhibitors of interactions involved in complex protein assemblies: Association of the core and surface antigens of hepatitis B virus. Proc Natl Acad Sci USA 92(6):2194-2198.
    • (1995) Proc Natl Acad Sci USA , vol.92 , Issue.6 , pp. 2194-2198
    • Dyson, M.R.1    Murray, K.2
  • 15
    • 56949095876 scopus 로고    scopus 로고
    • Moving towards highresolution descriptions of the molecular interactions and structural rearrangements of the human hepatitis B core protein
    • Freund SM, Johnson CM, Jaulent AM, Ferguson N (2008) Moving towards highresolution descriptions of the molecular interactions and structural rearrangements of the human hepatitis B core protein. J Mol Biol 384(5):1301-1313.
    • (2008) J Mol Biol , vol.384 , Issue.5 , pp. 1301-1313
    • Freund, S.M.1    Johnson, C.M.2    Jaulent, A.M.3    Ferguson, N.4
  • 16
    • 0029950758 scopus 로고    scopus 로고
    • Dimorphism of hepatitis B virus capsids is strongly influenced by the C-terminus of the capsid protein
    • Zlotnick A, et al. (1996) Dimorphism of hepatitis B virus capsids is strongly influenced by the C-terminus of the capsid protein. Biochemistry 35(23):7412-7421.
    • (1996) Biochemistry , vol.35 , Issue.23 , pp. 7412-7421
    • Zlotnick, A.1
  • 17
    • 26944499478 scopus 로고    scopus 로고
    • Structure, assembly, and antigenicity of hepatitis B virus capsid proteins
    • Steven AC, et al. (2005) Structure, assembly, and antigenicity of hepatitis B virus capsid proteins. Adv Virus Res 64:125-164.
    • (2005) Adv Virus Res , vol.64 , pp. 125-164
    • Steven, A.C.1
  • 18
    • 84866941201 scopus 로고    scopus 로고
    • Structural organization of pregenomic RNA and the carboxy-terminal domain of the capsid protein of hepatitis B virus
    • Wang JC, Dhason MS, Zlotnick A (2012) Structural organization of pregenomic RNA and the carboxy-terminal domain of the capsid protein of hepatitis B virus. PLoS Pathog 8(9):e1002919.
    • (2012) PLoS Pathog , vol.8 , Issue.9
    • Wang, J.C.1    Dhason, M.S.2    Zlotnick, A.3
  • 19
    • 0033152857 scopus 로고    scopus 로고
    • The crystal structure of the human hepatitis B virus capsid
    • Wynne SA, Crowther RA, Leslie AG (1999) The crystal structure of the human hepatitis B virus capsid. Mol Cell 3(6):771-780.
    • (1999) Mol Cell , vol.3 , Issue.6 , pp. 771-780
    • Wynne, S.A.1    Crowther, R.A.2    Leslie, A.G.3
  • 20
    • 34648846409 scopus 로고    scopus 로고
    • Cryo-electron microscopy of hepatitis B virions reveals variability in envelope capsid interactions
    • Seitz S, Urban S, Antoni C, Böttcher B (2007) Cryo-electron microscopy of hepatitis B virions reveals variability in envelope capsid interactions. EMBO J 26(18):4160-4167.
    • (2007) EMBO J , vol.26 , Issue.18 , pp. 4160-4167
    • Seitz, S.1    Urban, S.2    Antoni, C.3    Böttcher, B.4
  • 21
    • 73949118464 scopus 로고    scopus 로고
    • Conformational changes in the hepatitis B virus core protein are consistent with a role for allostery in virus assembly
    • Packianathan C, Katen SP, Dann CE, 3rd, Zlotnick A (2010) Conformational changes in the hepatitis B virus core protein are consistent with a role for allostery in virus assembly. J Virol 84(3):1607-1615.
    • (2010) J Virol , vol.84 , Issue.3 , pp. 1607-1615
    • Packianathan, C.1    Katen, S.P.2    Dann III, C.E.3    Zlotnick, A.4
  • 23
    • 31344442517 scopus 로고    scopus 로고
    • High plasticity of the hepatitis B virus capsid revealed by conformational stress
    • Böttcher B, Vogel M, Ploss M, Nassal M (2006) High plasticity of the hepatitis B virus capsid revealed by conformational stress. J Mol Biol 356(3):812-822.
    • (2006) J Mol Biol , vol.356 , Issue.3 , pp. 812-822
    • Böttcher, B.1    Vogel, M.2    Ploss, M.3    Nassal, M.4
  • 24
    • 0036786867 scopus 로고    scopus 로고
    • Weak protein-protein interactions are sufficient to drive assembly of hepatitis B virus capsids
    • Ceres P, Zlotnick A (2002) Weak protein-protein interactions are sufficient to drive assembly of hepatitis B virus capsids. Biochemistry 41(39):11525-11531.
    • (2002) Biochemistry , vol.41 , Issue.39 , pp. 11525-11531
    • Ceres, P.1    Zlotnick, A.2
  • 25
    • 4143143115 scopus 로고    scopus 로고
    • Hepatitis B virus capsid assembly is enhanced by naturally occurring mutation F97L
    • Ceres P, Stray SJ, Zlotnick A (2004) Hepatitis B virus capsid assembly is enhanced by naturally occurring mutation F97L. J Virol 78(17):9538-9543.
    • (2004) J Virol , vol.78 , Issue.17 , pp. 9538-9543
    • Ceres, P.1    Stray, S.J.2    Zlotnick, A.3
  • 26
    • 0026553768 scopus 로고
    • The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability
    • Serrano L, Kellis JT, Jr., Cann P, Matouschek A, Fersht AR (1992) The folding of an enzyme. II. Substructure of barnase and the contribution of different interactions to protein stability. J Mol Biol 224(3):783-804.
    • (1992) J Mol Biol , vol.224 , Issue.3 , pp. 783-804
    • Serrano, L.1    Kellis Jr., J.T.2    Cann, P.3    Matouschek, A.4    Fersht, A.R.5
  • 27
    • 0028947257 scopus 로고
    • Funnels, pathways, and the energy landscape of protein folding: A synthesis
    • Bryngelson JD, Onuchic JN, Socci ND, Wolynes PG (1995) Funnels, pathways, and the energy landscape of protein folding: A synthesis. Proteins 21(3):167-195.
    • (1995) Proteins , vol.21 , Issue.3 , pp. 167-195
    • Bryngelson, J.D.1    Onuchic, J.N.2    Socci, N.D.3    Wolynes, P.G.4
  • 28
    • 0032718386 scopus 로고    scopus 로고
    • Salt-induced detour through compact regions of the protein folding landscape
    • Otzen DE, Oliveberg M (1999) Salt-induced detour through compact regions of the protein folding landscape. Proc Natl Acad Sci USA 96(21):11746-11751.
    • (1999) Proc Natl Acad Sci USA , vol.96 , Issue.21 , pp. 11746-11751
    • Otzen, D.E.1    Oliveberg, M.2
  • 29
    • 79952762072 scopus 로고    scopus 로고
    • On the role of frustration in the energy landscapes of allosteric proteins
    • Ferreiro DU, Hegler JA, Komives EA, Wolynes PG (2011) On the role of frustration in the energy landscapes of allosteric proteins. Proc Natl Acad Sci USA 108(9):3499-3503.
    • (2011) Proc Natl Acad Sci USA , vol.108 , Issue.9 , pp. 3499-3503
    • Ferreiro, D.U.1    Hegler, J.A.2    Komives, E.A.3    Wolynes, P.G.4
  • 30
    • 0026684254 scopus 로고
    • Topological analysis of the hepatitis B virus core particle by cysteine-cysteine cross-linking
    • Nassal M, Rieger A, Steinau O (1992) Topological analysis of the hepatitis B virus core particle by cysteine-cysteine cross-linking. J Mol Biol 225(4):1013-1025.
    • (1992) J Mol Biol , vol.225 , Issue.4 , pp. 1013-1025
    • Nassal, M.1    Rieger, A.2    Steinau, O.3
  • 31
    • 0028820703 scopus 로고
    • Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
    • Myers JK, Pace CN, Scholtz JM (1995) Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding. Protein Sci 4(10): 2138-2148.
    • (1995) Protein Sci , vol.4 , Issue.10 , pp. 2138-2148
    • Myers, J.K.1    Pace, C.N.2    Scholtz, J.M.3
  • 32
    • 0028953769 scopus 로고
    • Hepatitis core antigen produced in Escherichia coli: Subunit composition, conformational analysis, and in vitro capsid assembly
    • Wingfield PT, Stahl SJ, Williams RW, Steven AC (1995) Hepatitis core antigen produced in Escherichia coli: Subunit composition, conformational analysis, and in vitro capsid assembly. Biochemistry 34(15):4919-4932.
    • (1995) Biochemistry , vol.34 , Issue.15 , pp. 4919-4932
    • Wingfield, P.T.1    Stahl, S.J.2    Williams, R.W.3    Steven, A.C.4
  • 34
    • 84867498176 scopus 로고    scopus 로고
    • Label-free microscale thermophoresis discriminates sites and affinity of protein-ligand binding
    • Seidel SA, et al. (2012) Label-free microscale thermophoresis discriminates sites and affinity of protein-ligand binding. Angew Chem Int Ed Engl 51(42):10656-10659.
    • (2012) Angew Chem Int Ed Engl , vol.51 , Issue.42 , pp. 10656-10659
    • Seidel, S.A.1
  • 35
    • 0016292941 scopus 로고
    • Urea and guanidine hydrochloride denaturation of ribonuclease, lysozyme, alpha-chymotrypsin, and beta-lactoglobulin
    • Greene RF, Jr., Pace CN (1974) Urea and guanidine hydrochloride denaturation of ribonuclease, lysozyme, alpha-chymotrypsin, and beta-lactoglobulin. J Biol Chem 249(17):5388-5393.
    • (1974) J Biol Chem , vol.249 , Issue.17 , pp. 5388-5393
    • Greene Jr., R.F.1    Pace, C.N.2
  • 36
    • 0033517792 scopus 로고    scopus 로고
    • A theoretical model successfully identifies features of hepatitis B virus capsid assembly
    • Zlotnick A, Johnson JM, Wingfield PW, Stahl SJ, Endres D (1999) A theoretical model successfully identifies features of hepatitis B virus capsid assembly. Biochemistry 38(44):14644-14652.
    • (1999) Biochemistry , vol.38 , Issue.44 , pp. 14644-14652
    • Zlotnick, A.1    Johnson, J.M.2    Wingfield, P.W.3    Stahl, S.J.4    Endres, D.5
  • 37
    • 65249135887 scopus 로고    scopus 로고
    • Folding and association of thermophilic dimeric and trimeric DsrEFH proteins: Tm0979 and Mth1491
    • Galvagnion C, et al. (2009) Folding and association of thermophilic dimeric and trimeric DsrEFH proteins: Tm0979 and Mth1491. Biochemistry 48(13):2891-2906.
    • (2009) Biochemistry , vol.48 , Issue.13 , pp. 2891-2906
    • Galvagnion, C.1
  • 38
    • 61849163979 scopus 로고    scopus 로고
    • The thermodynamics of virus capsid assembly
    • Katen S, Zlotnick A (2009) The thermodynamics of virus capsid assembly. Methods Enzymol 455:395-417.
    • (2009) Methods Enzymol , vol.455 , pp. 395-417
    • Katen, S.1    Zlotnick, A.2
  • 39
    • 0027362677 scopus 로고
    • Disulfide bonds and the stability of globular proteins
    • Betz SF (1993) Disulfide bonds and the stability of globular proteins. Protein Sci 2(10): 1551-1558.
    • (1993) Protein Sci , vol.2 , Issue.10 , pp. 1551-1558
    • Betz, S.F.1
  • 40
    • 13844255609 scopus 로고    scopus 로고
    • Folding studies on a knotted protein
    • Mallam AL, Jackson SE (2005) Folding studies on a knotted protein. J Mol Biol 346(5): 1409-1421.
    • (2005) J Mol Biol , vol.346 , Issue.5 , pp. 1409-1421
    • Mallam, A.L.1    Jackson, S.E.2
  • 41
    • 84868237181 scopus 로고    scopus 로고
    • Evidence for the preservation of native inter-and intramolecular hydrogen bonds in the desolvated FK-binding protein FK506 complex produced by electrospray ionization
    • Hopper JT, et al. (2012) Evidence for the preservation of native inter-and intramolecular hydrogen bonds in the desolvated FK-binding protein FK506 complex produced by electrospray ionization. J Am Soc Mass Spectrom 23(10): 1757-1767.
    • (2012) J Am Soc Mass Spectrom , vol.23 , Issue.10 , pp. 1757-1767
    • Hopper, J.T.1
  • 42
    • 70349108740 scopus 로고    scopus 로고
    • Collision induced unfolding of protein ions in the gas phase studied by ion mobility-mass spectrometry: The effect of ligand binding on conformational stability
    • Hopper JT, Oldham NJ (2009) Collision induced unfolding of protein ions in the gas phase studied by ion mobility-mass spectrometry: The effect of ligand binding on conformational stability. J Am Soc Mass Spectrom 20(10):1851-1858.
    • (2009) J Am Soc Mass Spectrom , vol.20 , Issue.10 , pp. 1851-1858
    • Hopper, J.T.1    Oldham, N.J.2
  • 43
    • 79960579141 scopus 로고    scopus 로고
    • Bound anions differentially stabilize multiprotein complexes in the absence of bulk solvent
    • Han L, Hyung SJ, Mayers JJ, Ruotolo BT (2011) Bound anions differentially stabilize multiprotein complexes in the absence of bulk solvent. J Am Chem Soc 133(29): 11358-11367.
    • (2011) J Am Chem Soc , vol.133 , Issue.29 , pp. 11358-11367
    • Han, L.1    Hyung, S.J.2    Mayers, J.J.3    Ruotolo, B.T.4
  • 44
    • 84861639125 scopus 로고    scopus 로고
    • Bound cations significantly stabilize the structure of multiprotein complexes in the gas phase
    • Han L, Hyung SJ, Ruotolo BT (2012) Bound cations significantly stabilize the structure of multiprotein complexes in the gas phase. Angew Chem Int Ed Engl 51(23): 5692-5695.
    • (2012) Angew Chem Int Ed Engl , vol.51 , Issue.23 , pp. 5692-5695
    • Han, L.1    Hyung, S.J.2    Ruotolo, B.T.3
  • 45
    • 84865726963 scopus 로고    scopus 로고
    • Conformational isomers of calcineurin follow distinct dissociation pathways
    • Kükrer B, et al. (2012) Conformational isomers of calcineurin follow distinct dissociation pathways. J Am Soc Mass Spectrom 23(9):1534-1543.
    • (2012) J Am Soc Mass Spectrom , vol.23 , Issue.9 , pp. 1534-1543
    • Kükrer, B.1
  • 46
    • 84856111733 scopus 로고    scopus 로고
    • Gas-phase protein assemblies: Unfolding landscapes and preserving native-like structures using noncovalent adducts
    • Freeke J, Bush MF, Robinson CV, Ruotolo BT (2012) Gas-phase protein assemblies: Unfolding landscapes and preserving native-like structures using noncovalent adducts. Chem Phys Lett 524:1-9.
    • (2012) Chem Phys Lett , vol.524 , pp. 1-9
    • Freeke, J.1    Bush, M.F.2    Robinson, C.V.3    Ruotolo, B.T.4
  • 47
    • 79251613176 scopus 로고    scopus 로고
    • Interrogating viral capsid assembly with ion mobility-mass spectrometry
    • Uetrecht C, Barbu IM, Shoemaker GK, van Duijn E, Heck AJ (2011) Interrogating viral capsid assembly with ion mobility-mass spectrometry. Nat Chem 3(2):126-132.
    • (2011) Nat Chem , vol.3 , Issue.2 , pp. 126-132
    • Uetrecht, C.1    Barbu, I.M.2    Shoemaker, G.K.3    Van Duijn, E.4    Heck, A.J.5
  • 48
    • 77958098504 scopus 로고    scopus 로고
    • Subunit exchange rates in Hepatitis B virus capsids are geometry-and temperature-dependent
    • Uetrecht C, et al. (2010) Subunit exchange rates in Hepatitis B virus capsids are geometry-and temperature-dependent. Phys Chem Chem Phys 12(41):13368-13371.
    • (2010) Phys Chem Chem Phys , vol.12 , Issue.41 , pp. 13368-13371
    • Uetrecht, C.1
  • 49
    • 84880685741 scopus 로고    scopus 로고
    • Phi-value analysis of protein folding transition states
    • eds Lutz S, Bornscheuer UT (Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim, Germany)
    • Ferguson N, Fersht AR (2011) Phi-value analysis of protein folding transition states. Protein Engineering Handbook, eds Lutz S, Bornscheuer UT (Wiley-VCH Verlag GmbH & Co. KGaA, Weinheim, Germany), pp 1-47.
    • (2011) Protein Engineering Handbook , pp. 1-47
    • Ferguson, N.1    Fersht, A.R.2
  • 50
    • 64349101502 scopus 로고    scopus 로고
    • A mutant hepatitis B virus core protein mimics inhibitors of icosahedral capsid self-assembly
    • Bourne CR, Katen SP, Fulz MR, Packianathan C, Zlotnick A (2009) A mutant hepatitis B virus core protein mimics inhibitors of icosahedral capsid self-assembly. Biochemistry 48(8):1736-1742.
    • (2009) Biochemistry , vol.48 , Issue.8 , pp. 1736-1742
    • Bourne, C.R.1    Katen, S.P.2    Fulz, M.R.3    Packianathan, C.4    Zlotnick, A.5
  • 51
    • 0141834247 scopus 로고    scopus 로고
    • Subtype-independent immature secretion and subtypedependent replication deficiency of a highly frequent, naturally occurring mutation of human hepatitis B virus core antigen
    • Yuan TT, Tai PC, Shih C (1999) Subtype-independent immature secretion and subtypedependent replication deficiency of a highly frequent, naturally occurring mutation of human hepatitis B virus core antigen. J Virol 73(12):10122-10128.
    • (1999) J Virol , vol.73 , Issue.12 , pp. 10122-10128
    • Yuan, T.T.1    Tai, P.C.2    Shih, C.3
  • 52
    • 0033064976 scopus 로고    scopus 로고
    • The mechanism of an immature secretion phenotype of a highly frequent naturally occurring missense mutation at codon 97 of human hepatitis B virus core antigen
    • Yuan TTT, Sahu GK, Whitehead WE, Greenberg R, Shih C (1999) The mechanism of an immature secretion phenotype of a highly frequent naturally occurring missense mutation at codon 97 of human hepatitis B virus core antigen. J Virol 73(7): 5731-5740.
    • (1999) J Virol , vol.73 , Issue.7 , pp. 5731-5740
    • Yuan, T.T.T.1    Sahu, G.K.2    Whitehead, W.E.3    Greenberg, R.4    Shih, C.5
  • 53
    • 0029100703 scopus 로고
    • Naturally occurring hepatitis B virus core gene mutations
    • Akarca US, Lok ASF (1995) Naturally occurring hepatitis B virus core gene mutations. Hepatology 22(1):50-60.
    • (1995) Hepatology , vol.22 , Issue.1 , pp. 50-60
    • Akarca, U.S.1    Lok, A.S.F.2
  • 54
    • 0033808521 scopus 로고    scopus 로고
    • Low-level secretion of human hepatitis B virus virions caused by two independent, naturally occurring mutations (P5T and L60V) in the capsid protein
    • Le Pogam S, Yuan TT, Sahu GK, Chatterjee S, Shih C (2000) Low-level secretion of human hepatitis B virus virions caused by two independent, naturally occurring mutations (P5T and L60V) in the capsid protein. J Virol 74(19):9099-9105.
    • (2000) J Virol , vol.74 , Issue.19 , pp. 9099-9105
    • Le Pogam, S.1    Yuan, T.T.2    Sahu, G.K.3    Chatterjee, S.4    Shih, C.5
  • 55
    • 33748342130 scopus 로고    scopus 로고
    • Phosphorylation of hepatitis B virus Cp at Ser87 facilitates core assembly
    • Kang HY, et al. (2006) Phosphorylation of hepatitis B virus Cp at Ser87 facilitates core assembly. Biochem J 398(2):311-317.
    • (2006) Biochem J , vol.398 , Issue.2 , pp. 311-317
    • Kang, H.Y.1
  • 56
    • 0028606077 scopus 로고
    • Conformational stability of dimeric proteins: Quantitative studies by equilibrium denaturation
    • Neet KE, Timm DE (1994) Conformational stability of dimeric proteins: Quantitative studies by equilibrium denaturation. Protein Sci 3(12):2167-2174.
    • (1994) Protein Sci , vol.3 , Issue.12 , pp. 2167-2174
    • Neet, K.E.1    Timm, D.E.2
  • 57
    • 0031565728 scopus 로고    scopus 로고
    • The foldon universe: A survey of structural similarity and self-recognition of independently folding units
    • Panchenko AR, Luthey-Schulten Z, Cole R, Wolynes PG (1997) The foldon universe: A survey of structural similarity and self-recognition of independently folding units. J Mol Biol 272(1):95-105.
    • (1997) J Mol Biol , vol.272 , Issue.1 , pp. 95-105
    • Panchenko, A.R.1    Luthey-Schulten, Z.2    Cole, R.3    Wolynes, P.G.4
  • 58
    • 84872147905 scopus 로고    scopus 로고
    • Antigenic switching of hepatitis B virus by alternative dimerization of the capsid protein
    • DiMattia MA, et al. (2013) Antigenic switching of hepatitis B virus by alternative dimerization of the capsid protein. Structure 21(1):133-142.
    • (2013) Structure , vol.21 , Issue.1 , pp. 133-142
    • DiMattia, M.A.1
  • 59
    • 84877023961 scopus 로고    scopus 로고
    • Epitope-distal effects accompany the binding of two distinct antibodies to hepatitis B virus capsids
    • Bereszczak JZ, et al. (2013) Epitope-distal effects accompany the binding of two distinct antibodies to hepatitis B virus capsids. J Am Chem Soc 135(17):6504-6512.
    • (2013) J Am Chem Soc , vol.135 , Issue.17 , pp. 6504-6512
    • Bereszczak, J.Z.1
  • 60
    • 84884235758 scopus 로고    scopus 로고
    • Structure-based design and biochemical evaluation of sulfanilamide derivatives as hepatitis B virus capsid assembly inhibitors
    • 10.3109/14756366.2012
    • Cho MH, Song JS, Kim HJ, Park SG, Jung G (2012) Structure-based design and biochemical evaluation of sulfanilamide derivatives as hepatitis B virus capsid assembly inhibitors. J Enzyme Inhib Med Chem, 10.3109/14756366.2012.
    • J Enzyme Inhib Med Chem , vol.2012
    • Cho, M.H.1    Song, J.S.2    Kim, H.J.3    Park, S.G.4    Jung, G.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.