메뉴 건너뛰기




Volumn 84, Issue 3, 2003, Pages 1926-1939

Investigation of pathways for the low-pH conformational transition in influenza hemagglutinin

Author keywords

[No Author keywords available]

Indexed keywords

HEMAGGLUTININ; PEPTIDE; PROTEIN PRECURSOR;

EID: 0037340698     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(03)75001-2     Document Type: Article
Times cited : (17)

References (64)
  • 1
    • 0001568871 scopus 로고    scopus 로고
    • Calculation of conformational transitions and barriers in solvated systems: Application to the alanine dipeptide in water
    • Apostolakis, J., P. Ferrara, and A. Caflisch. 1999. Calculation of conformational transitions and barriers in solvated systems: application to the alanine dipeptide in water. J. Chem. Phys. 110:2099-2108.
    • (1999) J. Chem. Phys. , vol.110 , pp. 2099-2108
    • Apostolakis, J.1    Ferrara, P.2    Caflisch, A.3
  • 2
    • 0035142899 scopus 로고    scopus 로고
    • Implicit solvent model studies of the interactions of the influenza hemagglutinin fusion peptide with lipid bilayers
    • Bechor, D., and N. Ben-Tal. 2001. Implicit solvent model studies of the interactions of the influenza hemagglutinin fusion peptide with lipid bilayers. Biophys. J. 80:643-655.
    • (2001) Biophys. J. , vol.80 , pp. 643-655
    • Bechor, D.1    Ben-Tal, N.2
  • 3
    • 0026782108 scopus 로고
    • Intermediates and kinetics of membrane fusion
    • Bentz, J. 1992. Intermediates and kinetics of membrane fusion. Biophys. J. 63:448-459.
    • (1992) Biophys. J. , vol.63 , pp. 448-459
    • Bentz, J.1
  • 4
    • 0034120341 scopus 로고    scopus 로고
    • Membrane fusion mediated by coiled coils: A hypothesis
    • Bentz, J. 2000. Membrane fusion mediated by coiled coils: a hypothesis. Biophys. J. 78:886-900.
    • (2000) Biophys. J. , vol.78 , pp. 886-900
    • Bentz, J.1
  • 5
    • 0025639178 scopus 로고
    • An architecture for the fusion site of influenza hemagglutinin
    • Bentz, J., H. Ellens, and D. Alford. 1990. An architecture for the fusion site of influenza hemagglutinin. FEBS Lett. 276:1-5.
    • (1990) FEBS Lett. , vol.276 , pp. 1-5
    • Bentz, J.1    Ellens, H.2    Alford, D.3
  • 6
    • 0036175994 scopus 로고    scopus 로고
    • Nanoseconds MD simulation of primary mechanical energy transfer steps in F1-ATP synthase
    • Bockmann, R. A., and H. Grubmuller. 2002. Nanoseconds MD simulation of primary mechanical energy transfer steps in F1-ATP synthase. Nature Str. Biol. 9:198-202.
    • (2002) Nature Str. Biol. , vol.9 , pp. 198-202
    • Bockmann, R.A.1    Grubmuller, H.2
  • 7
    • 0034092235 scopus 로고    scopus 로고
    • Membrane perturbation and fusion pore formation in influenza hemagglutinin-mediated membrane fusion
    • Bonnafous, P., and T. Stegmann. 2000. Membrane perturbation and fusion pore formation in influenza hemagglutinin-mediated membrane fusion. J. Biol. Chem. 275:6160-6166.
    • (2000) J. Biol. Chem. , vol.275 , pp. 6160-6166
    • Bonnafous, P.1    Stegmann, T.2
  • 8
    • 0037738967 scopus 로고    scopus 로고
    • Structure of influenza hemagglutinin at neutral and at fusogenic pH by electron cryo-microscopy
    • Böttcher, C., K. Ludwig, A. Herrmann, M. V. Heel, and H. Stark. 1999. Structure of influenza hemagglutinin at neutral and at fusogenic pH by electron cryo-microscopy. FEBS Lett. 463:255-259.
    • (1999) FEBS Lett. , vol.463 , pp. 255-259
    • Böttcher, C.1    Ludwig, K.2    Herrmann, A.3    Heel, M.V.4    Stark, H.5
  • 9
    • 0040952847 scopus 로고    scopus 로고
    • Oblique membrane insertion of viral fusion peptide probed by neutron diffraction
    • Bradshaw, J. P., M. J. M. Darkes, T. A. Harroun, J. Katsaras, and R. M. Epand. 2000. Oblique membrane insertion of viral fusion peptide probed by neutron diffraction. Biochemistry. 39:6581-6585.
    • (2000) Biochemistry , vol.39 , pp. 6581-6585
    • Bradshaw, J.P.1    Darkes, M.J.M.2    Harroun, T.A.3    Katsaras, J.4    Epand, R.M.5
  • 10
    • 0030965850 scopus 로고    scopus 로고
    • Peptides in membranes: Tipping the balance of membrane stability
    • Brasseur, R., T. Pillot, L. Lins, J. Vandekerckhove, and M. Rosseneu. 1997. Peptides in membranes: tipping the balance of membrane stability. TIBS. 22:167-171.
    • (1997) TIBS , vol.22 , pp. 167-171
    • Brasseur, R.1    Pillot, T.2    Lins, L.3    Vandekerckhove, J.4    Rosseneu, M.5
  • 12
    • 0028023726 scopus 로고
    • Structure of influenza hemagglutinin at the pH of membrane fusion
    • Bullough, P. A., F. M. Hughson, J. J. Skehel, and D. C. Wiley. 1994. Structure of influenza hemagglutinin at the pH of membrane fusion. Nature. 371:37-43.
    • (1994) Nature , vol.371 , pp. 37-43
    • Bullough, P.A.1    Hughson, F.M.2    Skehel, J.J.3    Wiley, D.C.4
  • 13
    • 0031460632 scopus 로고    scopus 로고
    • Influenza hemagglutinin is spring-loaded by a metastable native configuration
    • Carr, C. M., C. Chaudhry, and P. S. Kim. 1997. Influenza hemagglutinin is spring-loaded by a metastable native configuration. Proc. Natl. Acad. Sci. USA. 94:14306-14313.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 14306-14313
    • Carr, C.M.1    Chaudhry, C.2    Kim, P.S.3
  • 14
    • 0027253445 scopus 로고
    • A spring-loaded mechanism for the conformational change of influenza hemagglutinin
    • Carr, C. M., and P. S. Kim. 1993. A spring-loaded mechanism for the conformational change of influenza hemagglutinin. Cell. 73:823-832.
    • (1993) Cell , vol.73 , pp. 823-832
    • Carr, C.M.1    Kim, P.S.2
  • 15
    • 18844470928 scopus 로고    scopus 로고
    • Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation
    • Chen, J., K. H. Lee, D. A. Steinhauer, D. J. Stevens, J. J. Skehel, and D. C. Wiley. 1998. Structure of the hemagglutinin precursor cleavage site, a determinant of influenza pathogenicity and the origin of the labile conformation. Cell. 95:409-417.
    • (1998) Cell , vol.95 , pp. 409-417
    • Chen, J.1    Lee, K.H.2    Steinhauer, D.A.3    Stevens, D.J.4    Skehel, J.J.5    Wiley, D.C.6
  • 16
    • 0033529752 scopus 로고    scopus 로고
    • 2 subunit to form an N-cap that terminates the triple-stranded coiled coil
    • 2 subunit to form an N-cap that terminates the triple-stranded coiled coil. Proc. Natl. Acad. Sci. USA. 96:8967-8972.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 8967-8972
    • Chen, J.1    Skehel, J.J.2    Wiley, D.C.3
  • 18
    • 0032559801 scopus 로고    scopus 로고
    • The pathway of membrane fusion catalyzed by influenza hemagglutinin: Restriction of lipids, hemifusion, and lipidic fusion pore formation
    • Chemomordik, L. V., E. Leikina, V. Frolov, P. Bronk, and J. Zimmerberg. 1998. The pathway of membrane fusion catalyzed by influenza hemagglutinin: restriction of lipids, hemifusion, and lipidic fusion pore formation. J. Cell Biol. 140:1369-1382.
    • (1998) J. Cell Biol. , vol.140 , pp. 1369-1382
    • Chemomordik, L.V.1    Leikina, E.2    Frolov, V.3    Bronk, P.4    Zimmerberg, J.5
  • 19
    • 0034890642 scopus 로고    scopus 로고
    • Implications of a fusion peptide structure
    • Cohen, F. S., and G. B. Melikyan. 2001. Implications of a fusion peptide structure. Nat. Struct. Biol. 8:653-655.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 653-655
    • Cohen, F.S.1    Melikyan, G.B.2
  • 20
    • 0020955303 scopus 로고
    • Analyses of the antigenicity of influenza hemagglutinin at the pH optimum for virus-mediated membrane fusion
    • Daniels, R. S., A. R. Douglas, J. J. Skehel, and D. C. Wiley. 1983. Analyses of the antigenicity of influenza hemagglutinin at the pH optimum for virus-mediated membrane fusion. J. Gen. Virol. 64:1657-1662.
    • (1983) J. Gen. Virol. , vol.64 , pp. 1657-1662
    • Daniels, R.S.1    Douglas, A.R.2    Skehel, J.J.3    Wiley, D.C.4
  • 21
    • 0242618314 scopus 로고    scopus 로고
    • Calculation of pathways for the conformational transition between the GTP- and GDP-bound states of the HA-ras-p21 protein: Calculations with explicit solvent simulations and comparison with calculations in vacuum
    • Diaz, J., J. Wroblowski, J. Schlitter, and Y. Engelborghs. 1997. Calculation of pathways for the conformational transition between the GTP- and GDP-bound states of the HA-ras-p21 protein: calculations with explicit solvent simulations and comparison with calculations in vacuum. Proteins. 28:434-451.
    • (1997) Proteins , vol.28 , pp. 434-451
    • Diaz, J.1    Wroblowski, J.2    Schlitter, J.3    Engelborghs, Y.4
  • 22
    • 84961985307 scopus 로고    scopus 로고
    • Development of a generalized Born model parameterization for proteins and nucleic acids
    • Dominy, B. N., and C. L. Brooks, III. 1999. Development of a generalized Born model parameterization for proteins and nucleic acids. J. Phys. Chem. B. 103:3765-3773.
    • (1999) J. Phys. Chem. B , vol.103 , pp. 3765-3773
    • Dominy, B.N.1    Brooks C.L. III2
  • 23
    • 0021984076 scopus 로고
    • Membrane fusion activity of influenza virus hemagglutinin
    • Doms, R. W., A. Helenius, and J. White. 1985. Membrane fusion activity of influenza virus hemagglutinin. J. Biol. Chem. 260:2973-2981.
    • (1985) J. Biol. Chem. , vol.260 , pp. 2973-2981
    • Doms, R.W.1    Helenius, A.2    White, J.3
  • 24
    • 0030682144 scopus 로고    scopus 로고
    • What studies of fusion peptides tell us about viral envelope glycoprotein-mediated membrane fusion
    • Durell, S. R., I. Martin, J. M. Ruysschaert, Y. Shai, and R. Blumenthal. 1997. What studies of fusion peptides tell us about viral envelope glycoprotein-mediated membrane fusion. Mol. Membr. Biol. 14:97-112.
    • (1997) Mol. Membr. Biol. , vol.14 , pp. 97-112
    • Durell, S.R.1    Martin, I.2    Ruysschaert, J.M.3    Shai, Y.4    Blumenthal, R.5
  • 25
    • 0034924823 scopus 로고    scopus 로고
    • Mechanisms of viral membrane fusion and its inhibition
    • Eckert, D. M., and P. S. Kim. 2001. Mechanisms of viral membrane fusion and its inhibition. Annu. Rev. Biochem. 70:777-810.
    • (2001) Annu. Rev. Biochem. , vol.70 , pp. 777-810
    • Eckert, D.M.1    Kim, P.S.2
  • 26
    • 0034657550 scopus 로고    scopus 로고
    • Computer simulations of protein folding by targeted molecular dynamics
    • Ferrara, P., J. Apostolakis, and A. Caflisch. 2000a. Computer simulations of protein folding by targeted molecular dynamics. Proteins. 39:252-260.
    • (2000) Proteins , vol.39 , pp. 252-260
    • Ferrara, P.1    Apostolakis, J.2    Caflisch, A.3
  • 27
    • 0001744683 scopus 로고    scopus 로고
    • Targeted molecular dynamics simulations of protein unfolding
    • Ferrara, P., J. Apostolakis, and A. Caflisch. 2000b. Targeted molecular dynamics simulations of protein unfolding. J. Phys. Chem. B. 104:4511-4518.
    • (2000) J. Phys. Chem. B , vol.104 , pp. 4511-4518
    • Ferrara, P.1    Apostolakis, J.2    Caflisch, A.3
  • 28
    • 0022619527 scopus 로고
    • Studies on the mechanism of membrane fusion: Site-specific mutagenesis of the hemagglutinin of influenza virus
    • Gething, M. J., R. W. Doms, D. York, and J. White. 1986. Studies on the mechanism of membrane fusion: site-specific mutagenesis of the hemagglutinin of influenza virus. J. Cell Biol. 102:11-23.
    • (1986) J. Cell Biol. , vol.102 , pp. 11-23
    • Gething, M.J.1    Doms, R.W.2    York, D.3    White, J.4
  • 29
    • 0026560161 scopus 로고
    • Introduction of intersubunit disulfide bonds in the membrane-distal region of the influenza hemagglutinin abolishes membrane fusion activity
    • Godley, L., J. Pfeifer, D. Steinhauer, B. Ely, G. Shaw, R. Kaufmann, E. Suchanek, C. Pabo, J. J. Skehel, D. C. Wiley, and S. Wharton. 1992. Introduction of intersubunit disulfide bonds in the membrane-distal region of the influenza hemagglutinin abolishes membrane fusion activity. Cell. 68:635-645.
    • (1992) Cell , vol.68 , pp. 635-645
    • Godley, L.1    Pfeifer, J.2    Steinhauer, D.3    Ely, B.4    Shaw, G.5    Kaufmann, R.6    Suchanek, E.7    Pabo, C.8    Skehel, J.J.9    Wiley, D.C.10    Wharton, S.11
  • 30
    • 0034892952 scopus 로고    scopus 로고
    • Membrane structure and fusion-triggering conformational change of the fusion domain from influenza hemagglutinin
    • Han, X., J. H. Bushweller, D. S. Cafiso, and L. K. Tamm. 2001. Membrane structure and fusion-triggering conformational change of the fusion domain from influenza hemagglutinin. Nat. Struct. Biol. 8:715-720.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 715-720
    • Han, X.1    Bushweller, J.H.2    Cafiso, D.S.3    Tamm, L.K.4
  • 31
    • 0034700147 scopus 로고    scopus 로고
    • A host-guest system to study structure-function relationships of membrane fusion peptides
    • Han, X., and L. K. Tamm. 2000. A host-guest system to study structure-function relationships of membrane fusion peptides. Proc. Natl. Acad. Sci. USA. 97:13097-13102.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 13097-13102
    • Han, X.1    Tamm, L.K.2
  • 33
    • 0031240001 scopus 로고    scopus 로고
    • Enveloped viruses: A common mode of membrane fusion?
    • Hughson, F. M. 1997. Enveloped viruses: a common mode of membrane fusion? Curr. Biol. 7:R565-R569.
    • (1997) Curr. Biol. , vol.7
    • Hughson, F.M.1
  • 34
    • 0026772024 scopus 로고
    • Intermonomer disulfide bonds impair the fusion activity of influenza virus hemagglutinin
    • Kemble, G. W., D. L. Bodian, J. Rose, I. A. Wilson, and J. M. White. 1992. Intermonomer disulfide bonds impair the fusion activity of influenza virus hemagglutinin. J. Virol. 66:4940-4950.
    • (1992) J. Virol. , vol.66 , pp. 4940-4950
    • Kemble, G.W.1    Bodian, D.L.2    Rose, J.3    Wilson, I.A.4    White, J.M.5
  • 35
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., M. Billeter, and K. Wüthrich. 1996. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 14:51-55.
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 36
    • 0031678678 scopus 로고    scopus 로고
    • A mechanism of protein-mediated fusion: Coupling between refolding of the influenza hemagglutinin and lipid rearrangements
    • Kozlov, M. M., and L. V. Chemomordik. 1998. A mechanism of protein-mediated fusion: coupling between refolding of the influenza hemagglutinin and lipid rearrangements. Biophys. J. 75:1384-1396.
    • (1998) Biophys. J. , vol.75 , pp. 1384-1396
    • Kozlov, M.M.1    Chemomordik, L.V.2
  • 37
    • 0028053969 scopus 로고
    • Kinetics of the low pH-induced conformational changes and fusogenic activity of influenza hemagglutinin
    • Krumbiegel, M., A. Herrmann, and R. Blumenthal. 1994. Kinetics of the low pH-induced conformational changes and fusogenic activity of influenza hemagglutinin. Biophys. J. 67:2355-2360.
    • (1994) Biophys. J. , vol.67 , pp. 2355-2360
    • Krumbiegel, M.1    Herrmann, A.2    Blumenthal, R.3
  • 38
    • 0033135638 scopus 로고    scopus 로고
    • Effective energy function for proteins in solution
    • Lazaridis, T., and M. Karplus. 1999. Effective energy function for proteins in solution. Proteins. 35:133-152.
    • (1999) Proteins , vol.35 , pp. 133-152
    • Lazaridis, T.1    Karplus, M.2
  • 39
    • 0001940206 scopus 로고    scopus 로고
    • Microscopic basis of macromolecular thermodynamics
    • E. DiCera, editor. Oxford University Press, Oxford
    • Lazaridis, T., and M. Karplus. 2001. Microscopic basis of macromolecular thermodynamics. In Thermodynamics in Biology. E. DiCera, editor. Oxford University Press, Oxford. pp3-48.
    • (2001) Thermodynamics in Biology , pp. 3-48
    • Lazaridis, T.1    Karplus, M.2
  • 40
    • 0023654706 scopus 로고
    • Membrane binding and conformational properties of peptides representing the NH2 terminus of influenza HA2
    • Lear, J. D., and W. F. DeGrado. 1987. Membrane binding and conformational properties of peptides representing the NH2 terminus of influenza HA2. J. Biol. Chem. 262:6500-6505.
    • (1987) J. Biol. Chem. , vol.262 , pp. 6500-6505
    • Lear, J.D.1    DeGrado, W.F.2
  • 41
    • 0036073866 scopus 로고    scopus 로고
    • A dynamic analysis of the rotation mechanism for conformational change in F1-ATPase
    • Ma, J., T. C. Flynn, Q. Cui, A. G. W. Leslie, J. E. Walker, and M. Karplus. 2002. A dynamic analysis of the rotation mechanism for conformational change in F1-ATPase. Structure. 10:921-931.
    • (2002) Structure , vol.10 , pp. 921-931
    • Ma, J.1    Flynn, T.C.2    Cui, Q.3    Leslie, A.G.W.4    Walker, J.E.5    Karplus, M.6
  • 42
    • 0030711616 scopus 로고    scopus 로고
    • Molecular switch in signal transduction: Reaction paths of the conformational changes in ras p21
    • Ma, J., and M. Karplus. 1997. Molecular switch in signal transduction: reaction paths of the conformational changes in ras p21. Proc. Natl. Acad. Sci. USA. 94:11905-11910.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11905-11910
    • Ma, J.1    Karplus, M.2
  • 43
    • 0031576994 scopus 로고    scopus 로고
    • The membrane topology of the fusion peptide region of influenza hemagglutinin determined by spin-labeling EPR
    • Macosko, J. C., C.-H. Kim, and Y.-K. Shin. 1997. The membrane topology of the fusion peptide region of influenza hemagglutinin determined by spin-labeling EPR. J. Mol. Biol. 267:1139-1148.
    • (1997) J. Mol. Biol. , vol.267 , pp. 1139-1148
    • Macosko, J.C.1    Kim, C.-H.2    Shin, Y.-K.3
  • 44
    • 0034675886 scopus 로고    scopus 로고
    • Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion
    • Melikyan, G. B., R. M. Markosyan, H. Hemmati, M. K. Delmedico, D. M. Lambert, and F. S. Cohen. 2000. Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion. J. Cell Biol. 151:413-423.
    • (2000) J. Cell Biol. , vol.151 , pp. 413-423
    • Melikyan, G.B.1    Markosyan, R.M.2    Hemmati, H.3    Delmedico, M.K.4    Lambert, D.M.5    Cohen, F.S.6
  • 45
    • 0000036869 scopus 로고    scopus 로고
    • Simulation of activation free energies in molecular systems
    • Neria, E., S. Fischer, and M. Karplus. 1996. Simulation of activation free energies in molecular systems. J. Chem. Phys. 105:1902-1921.
    • (1996) J. Chem. Phys. , vol.105 , pp. 1902-1921
    • Neria, E.1    Fischer, S.2    Karplus, M.3
  • 47
    • 0032812477 scopus 로고    scopus 로고
    • A specific point mutant at position 1 of the influenza hemagglutinin fusion peptide displays a hemifusion phenotype
    • Qiao, H., R. T. Armstrong, G. B. Melikyan, F. S. Cohen, and J. M. White. 1999. A specific point mutant at position 1 of the influenza hemagglutinin fusion peptide displays a hemifusion phenotype. Mol. Biol. Cell. 10:2759-2769.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 2759-2769
    • Qiao, H.1    Armstrong, R.T.2    Melikyan, G.B.3    Cohen, F.S.4    White, J.M.5
  • 48
    • 0037065673 scopus 로고    scopus 로고
    • Acid-induced changes in thermal stability and fusion activity of influenza hemagglutinin
    • Remeta, D. P., M. Krumbiegel, C. A. S. A. Minetti, A. Puri, A. Ginsbur, and R. Blumenthal. 2002. Acid-induced changes in thermal stability and fusion activity of influenza hemagglutinin. Biochemistry. 41:2044-2054.
    • (2002) Biochemistry , vol.41 , pp. 2044-2054
    • Remeta, D.P.1    Krumbiegel, M.2    Minetti, C.A.S.A.3    Puri, A.4    Ginsbur, A.5    Blumenthal, R.6
  • 51
    • 0027794972 scopus 로고
    • Targeted molecular dynamics simulation of conformational change application to the T → R transition in insulin
    • Schlitter, J., M. Engels, P. Krüger, E. Jacoby, and A. Wollmer. 1993. Targeted molecular dynamics simulation of conformational change application to the T → R transition in insulin. Mol. Simul. 10:291-308.
    • (1993) Mol. Simul. , vol.10 , pp. 291-308
    • Schlitter, J.1    Engels, M.2    Krüger, P.3    Jacoby, E.4    Wollmer, A.5
  • 52
  • 54
    • 0033783032 scopus 로고    scopus 로고
    • Receptor binding and membrane fusion in virus entry: The influenza hemagglutinin
    • Skehel, J. J., and D. C. Wiley. 2000. Receptor binding and membrane fusion in virus entry: the influenza hemagglutinin. Annu. Rev. Biochem. 69:531-569.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 531-569
    • Skehel, J.J.1    Wiley, D.C.2
  • 55
    • 0025647464 scopus 로고
    • Intermediates in influenza induced membrane fusion
    • Stegmann, T., J. M. White, and A. Helenius. 1990. Intermediates in influenza induced membrane fusion. EMBO J. 9:4231-4241.
    • (1990) EMBO J. , vol.9 , pp. 4231-4241
    • Stegmann, T.1    White, J.M.2    Helenius, A.3
  • 56
    • 0020530076 scopus 로고
    • Changes in the antigenicity of the hemagglutinin molecule of H3 influenza virus at acidic pH
    • Webster, R. G., L. E. Brown, and D. C. Jackson. 1983. Changes in the antigenicity of the hemagglutinin molecule of H3 influenza virus at acidic pH. Virology. 126:587-599.
    • (1983) Virology , vol.126 , pp. 587-599
    • Webster, R.G.1    Brown, L.E.2    Jackson, D.C.3
  • 58
    • 0026492542 scopus 로고
    • Membrane fusion
    • White, J. M. 1992. Membrane fusion. Science. 258:917-924.
    • (1992) Science , vol.258 , pp. 917-924
    • White, J.M.1
  • 59
    • 0023574003 scopus 로고
    • Anti-peptide antibodies detect steps in a protein conformational change: Low-pH activation of the influenza virus hemagglutinin
    • White, J. M., and I. A. Wilson. 1987. Anti-peptide antibodies detect steps in a protein conformational change: low-pH activation of the influenza virus hemagglutinin. J. Cell Biol. 105:2887-2896.
    • (1987) J. Cell Biol. , vol.105 , pp. 2887-2896
    • White, J.M.1    Wilson, I.A.2
  • 60
    • 0023082135 scopus 로고
    • The structure and function of the hemagglutinin membrane glycoprotein of influenza virus
    • Wiley, D. C., and J. J. Skehel. 1987. The structure and function of the hemagglutinin membrane glycoprotein of influenza virus. Annu. Rev. Biochem. 56:365-394.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 365-394
    • Wiley, D.C.1    Skehel, J.J.2
  • 61
    • 0019432165 scopus 로고
    • Structural identification of the antibody-binding sites of Hong Kong influenza hemagglutinin and their involvement in antigenic variation
    • Wiley, D. C., I. A. Wilson, and J. J. Skehel. 1981. Structural identification of the antibody-binding sites of Hong Kong influenza hemagglutinin and their involvement in antigenic variation. Nature. 289:373-378.
    • (1981) Nature , vol.289 , pp. 373-378
    • Wiley, D.C.1    Wilson, I.A.2    Skehel, J.J.3
  • 62
    • 0019890491 scopus 로고
    • Structure of the hemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution
    • Wilson, I. A., J. J. Skehel, and D. C. Wiley. 1981. Structure of the hemagglutinin membrane glycoprotein of influenza virus at 3 Å resolution. Nature. 289:366-373.
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 63
    • 0036295231 scopus 로고    scopus 로고
    • Polymerase β simulations suggest that Arg258 rotation is a slow step rather than large subdomain motions Per Se
    • Yang, L., W. A. Beard, S. H. Wilson, S. Broyde, and T. Schlick. 2002. Polymerase β simulations suggest that Arg258 rotation is a slow step rather than large subdomain motions Per Se. J. Mol. Biol. 317:651-671.
    • (2002) J. Mol. Biol. , vol.317 , pp. 651-671
    • Yang, L.1    Beard, W.A.2    Wilson, S.H.3    Broyde, S.4    Schlick, T.5
  • 64
    • 0020607461 scopus 로고
    • Monoclonal anti-hemagglutinin antibodies detect irreversible antigenic alterations that coincide with the acid activation of influenza virus A/PR/834-mediated hemolysis
    • Yewdell, J. W., W. Gerhard, and T. Bachi. 1983. Monoclonal anti-hemagglutinin antibodies detect irreversible antigenic alterations that coincide with the acid activation of influenza virus A/PR/834-mediated hemolysis. J. Virol. 48:239-248.
    • (1983) J. Virol. , vol.48 , pp. 239-248
    • Yewdell, J.W.1    Gerhard, W.2    Bachi, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.