메뉴 건너뛰기




Volumn 90, Issue 1, 2016, Pages 575-585

PH-dependent formation and disintegration of the influenza A virus protein scaffold to provide tension for membrane fusion

Author keywords

[No Author keywords available]

Indexed keywords

COAT PROTEIN; MATRIX PROTEIN; MONOMER; RIBONUCLEOPROTEIN; LIPID BILAYER; M1 PROTEIN, INFLUENZA A VIRUS; PROTEIN BINDING;

EID: 84953911279     PISSN: 0022538X     EISSN: 10985514     Source Type: Journal    
DOI: 10.1128/JVI.01539-15     Document Type: Article
Times cited : (41)

References (61)
  • 1
    • 0001178029 scopus 로고    scopus 로고
    • Orthomyxoviridae: the viruses and their replication
    • Knipe DM, Howley PM, Griffin DE, Lamb RA, Martin MA, Roizman B, Straus SE (ed), 4th ed Lippincott Williams & Wilkins, Philadelphia, PA
    • Lamb RA, Krug RM. 2001. Orthomyxoviridae: the viruses and their replication, p 1487-1532. In Knipe DM, Howley PM, Griffin DE, Lamb RA, Martin MA, Roizman B, Straus SE (ed), Fields virology, 4th ed. Lippincott Williams & Wilkins, Philadelphia, PA.
    • (2001) Fields virology , pp. 1487-1532
    • Lamb, R.A.1    Krug, R.M.2
  • 2
    • 0020696905 scopus 로고
    • The structure and replication of influenza virus
    • Lamb RA, Choppin PW. 1983. The structure and replication of influenza virus. Annu Rev Biochem 52:467-506. http://dx.doi.org/10.1146/annurev.bi.52.070183.002343.
    • (1983) Annu Rev Biochem , vol.52 , pp. 467-506
    • Lamb, R.A.1    Choppin, P.W.2
  • 3
    • 84953852865 scopus 로고    scopus 로고
    • Entry of influenza virus
    • Poehlmann S, Simmons G (ed), Springer Science & Business Media, LLC, New York, NY
    • Sun X, Whittaker GR. 2006. Entry of influenza virus, p 72-82. In Poehlmann S, Simmons G (ed), Viral entry into host cells. Springer Science & Business Media, LLC, New York, NY.
    • (2006) Viral entry into host cells , pp. 72-82
    • Sun, X.1    Whittaker, G.R.2
  • 4
    • 0041422345 scopus 로고    scopus 로고
    • Visualizing infection of individual influenza viruses
    • Lakadamyali M, Rust MJ, Babcock HP, Zhuang X. 2003. Visualizing infection of individual influenza viruses. Proc Natl Acad Sci U S A 100: 9280-9285. http://dx.doi.org/10.1073/pnas.0832269100.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 9280-9285
    • Lakadamyali, M.1    Rust, M.J.2    Babcock, H.P.3    Zhuang, X.4
  • 5
    • 84908377302 scopus 로고    scopus 로고
    • + concentration is required for efficient uncoating of influenza A virus cores after penetration
    • + concentration is required for efficient uncoating of influenza A virus cores after penetration. J Virol 88:13029-13046. http://dx.doi.org/10.1128/JVI.01430-14.
    • (2014) J Virol , vol.88 , pp. 13029-13046
    • Stauffer, S.1    Feng, Y.2    Nebioglu, F.3    Heilig, R.4    Picotti, P.5    Helenius, A.6
  • 6
    • 0026006258 scopus 로고
    • Nuclear transport of influenza virus ribonucleoproteins: the viral matrix protein (M1) promotes export and inhibits import
    • Martin K, Helenius A. 1991. Nuclear transport of influenza virus ribonucleoproteins: the viral matrix protein (M1) promotes export and inhibits import. Cell 67:117-130. http://dx.doi.org/10.1016/0092-8674(91)90576-K.
    • (1991) Cell , vol.67 , pp. 117-130
    • Martin, K.1    Helenius, A.2
  • 7
    • 0026664025 scopus 로고
    • Unpacking the incoming influenza virus
    • Helenius A. 1992. Unpacking the incoming influenza virus. Cell 69:577-578. http://dx.doi.org/10.1016/0092-8674(92)90219-3.
    • (1992) Cell , vol.69 , pp. 577-578
    • Helenius, A.1
  • 9
    • 0028179011 scopus 로고
    • Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion
    • Kemble GW, Danieli T, White JM. 1994. Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion. Cell 76:383-391. http://dx.doi.org/10.1016/0092-8674(94)90344-1.
    • (1994) Cell , vol.76 , pp. 383-391
    • Kemble, G.W.1    Danieli, T.2    White, J.M.3
  • 10
    • 77950528480 scopus 로고    scopus 로고
    • Architecture of a nascent viral fusion pore
    • Lee KK. 2010. Architecture of a nascent viral fusion pore. EMBO J 29: 1299-1311. http://dx.doi.org/10.1038/emboj.2010.13.
    • (2010) EMBO J , vol.29 , pp. 1299-1311
    • Lee, K.K.1
  • 11
    • 0021750873 scopus 로고
    • Changes in the morphology of influenza particles induced at low pH
    • Ruigrok RWH, Cremers AFM, Beyer WEP, Ronde-Verloop FM. 1984. Changes in the morphology of influenza particles induced at low pH. Arch Virol 82:181-194. http://dx.doi.org/10.1007/BF01311162.
    • (1984) Arch Virol , vol.82 , pp. 181-194
    • Ruigrok, R.W.H.1    Cremers, A.F.M.2    Beyer, W.E.P.3    Ronde-Verloop, F.M.4
  • 12
    • 84877324091 scopus 로고    scopus 로고
    • At low pH, influenza virus matrix protein M1 undergoes a conformational change prior to dissociating from the membrane
    • Fontana J, Steven AC. 2013. At low pH, influenza virus matrix protein M1 undergoes a conformational change prior to dissociating from the membrane. J Virol 87:5621-5628. http://dx.doi.org/10.1128/JVI.00276-13.
    • (2013) J Virol , vol.87 , pp. 5621-5628
    • Fontana, J.1    Steven, A.C.2
  • 13
    • 2042418996 scopus 로고    scopus 로고
    • The mechanisms of lipid-protein rearrangements during viral infection
    • Chizmadzhev YA. 2004. The mechanisms of lipid-protein rearrangements during viral infection. Bioelectrochemistry 63:129-136. http://dx.doi.org/10.1016/j.bioelechem.2003.10.016.
    • (2004) Bioelectrochemistry , vol.63 , pp. 129-136
    • Chizmadzhev, Y.A.1
  • 14
    • 0031039724 scopus 로고    scopus 로고
    • Structure of a bifunctional membrane-RNA binding protein, influenza virus matrix protein M1
    • Sha B, Luo M. 1997. Structure of a bifunctional membrane-RNA binding protein, influenza virus matrix protein M1. Nat Struct Biol 4:239-244. http://dx.doi.org/10.1038/nsb0397-239.
    • (1997) Nat Struct Biol , vol.4 , pp. 239-244
    • Sha, B.1    Luo, M.2
  • 15
    • 0035840794 scopus 로고    scopus 로고
    • The crystal structure of the influenza matrix protein M1 at neutral pH: M1-M1 protein interfaces can rotate in the oligomeric structures of M1
    • Harris AF, Forouhar SQ, Sha B, Luo M. 2001. The crystal structure of the influenza matrix protein M1 at neutral pH: M1-M1 protein interfaces can rotate in the oligomeric structures of M1. Virology 289:34-44. http://dx.doi.org/10.1006/viro.2001.1119.
    • (2001) Virology , vol.289 , pp. 34-44
    • Harris, A.F.1    Forouhar, S.Q.2    Sha, B.3    Luo, M.4
  • 16
    • 84907720555 scopus 로고    scopus 로고
    • Crystal structures of influenza A virus matrix protein M1: variations on a theme
    • Safo MK, Musayev FN, Mosier PD, Zhou Q, Xie H, Desai UR. 2014. Crystal structures of influenza A virus matrix protein M1: variations on a theme. PLoS One 9:e109510. http://dx.doi.org/10.1371/journal.pone.0109510.
    • (2014) PLoS One , vol.9
    • Safo, M.K.1    Musayev, F.N.2    Mosier, P.D.3    Zhou, Q.4    Xie, H.5    Desai, U.R.6
  • 17
    • 0035864293 scopus 로고    scopus 로고
    • Combined results from solution studies on intact influenza virusM1 protein and from a new crystal form of its N-terminal domain show that M1 is an elongated monomer
    • Arzt S, Baudin F, Barge A, Timmins P, Burmeister WP, Ruigrok RW. 2001. Combined results from solution studies on intact influenza virusM1 protein and from a new crystal form of its N-terminal domain show that M1 is an elongated monomer. Virology 279:439-446. http://dx.doi.org/10.1006/viro.2000.0727.
    • (2001) Virology , vol.279 , pp. 439-446
    • Arzt, S.1    Baudin, F.2    Barge, A.3    Timmins, P.4    Burmeister, W.P.5    Ruigrok, R.W.6
  • 19
    • 84861358303 scopus 로고    scopus 로고
    • Dissection of influenza A virus M1 protein: pH-dependent oligomerization of N-terminal domain and dimerization of C-terminal domain
    • Zhang K, Wang Z, Liu X, Yin C, Basit Z, Xia B, Liu W. 2012. Dissection of influenza A virus M1 protein: pH-dependent oligomerization of N-terminal domain and dimerization of C-terminal domain. PLoS One 7:e37786. http://dx.doi.org/10.1371/journal.pone.0037786.
    • (2012) PLoS One , vol.7
    • Zhang, K.1    Wang, Z.2    Liu, X.3    Yin, C.4    Basit, Z.5    Xia, B.6    Liu, W.7
  • 20
    • 0015963126 scopus 로고
    • Association of the internal membrane protein with the lipid bilayer in influenza virus. A study with the fluorescent probe 12-(9-anthroyl)-stearic acid
    • Lenard J, Wong CY, Compans RW. 1974. Association of the internal membrane protein with the lipid bilayer in influenza virus. A study with the fluorescent probe 12-(9-anthroyl)-stearic acid. Biochim Biophys Acta 332:341-349.
    • (1974) Biochim Biophys Acta , vol.332 , pp. 341-349
    • Lenard, J.1    Wong, C.Y.2    Compans, R.W.3
  • 22
    • 0019851016 scopus 로고
    • Insertion of influenza M protein into the viral lipid bilayer and localization of site of insertion
    • Gregoriades A, Frangione B. 1981. Insertion of influenza M protein into the viral lipid bilayer and localization of site of insertion. J Virol 40:323-328.
    • (1981) J Virol , vol.40 , pp. 323-328
    • Gregoriades, A.1    Frangione, B.2
  • 24
    • 0029905294 scopus 로고    scopus 로고
    • Membrane association of influenza virus matrix protein does not require specific hydrophobic domains or the viral glycoproteins
    • Kretzschmar E, Bui M, Rose JK. 1996. Membrane association of influenza virus matrix protein does not require specific hydrophobic domains or the viral glycoproteins. Virology 220:37-45. http://dx.doi.org/10.1006/viro.1996.0283.
    • (1996) Virology , vol.220 , pp. 37-45
    • Kretzschmar, E.1    Bui, M.2    Rose, J.K.3
  • 28
    • 66649116586 scopus 로고    scopus 로고
    • Intermolecular interactions of influenza M1 proteins on the model lipid membrane surface: a study using the inner field compensation method
    • Knyazev DG, Radyuhin VA, Sokolov VS. 2009. Intermolecular interactions of influenza M1 proteins on the model lipid membrane surface: a study using the inner field compensation method. Biochemistry (Mosc) Suppl Ser A Membr Cell Biol 3:81-89.
    • (2009) Biochemistry (Mosc) Suppl Ser A Membr Cell Biol , vol.3 , pp. 81-89
    • Knyazev, D.G.1    Radyuhin, V.A.2    Sokolov, V.S.3
  • 30
    • 0026517512 scopus 로고
    • Isolation of matrix protein M1 from influenza viruses by acid-dependent extraction with nonionic detergent
    • Zhirnov O. 1992. Isolation of matrix protein M1 from influenza viruses by acid-dependent extraction with nonionic detergent. Virology 186:324-330. http://dx.doi.org/10.1016/0042-6822(92)90090-C.
    • (1992) Virology , vol.186 , pp. 324-330
    • Zhirnov, O.1
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685. http://dx.doi.org/10.1038/227680a0.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 32
    • 33947480633 scopus 로고
    • Methods for the formation of single bimolecular lipid membranes in aqueous solution
    • Mueller P, Rudin DO, Tien HT, Wescott WC. 1963. Methods for the formation of single bimolecular lipid membranes in aqueous solution. J Phys Chem 67:534-535. http://dx.doi.org/10.1021/j100796a529.
    • (1963) J Phys Chem , vol.67 , pp. 534-535
    • Mueller, P.1    Rudin, D.O.2    Tien, H.T.3    Wescott, W.C.4
  • 33
    • 0018812824 scopus 로고
    • Measurement of the differences in the surface potentials of bilayer membranes according to the second harmonic of a capacitance current
    • (In Russian.)
    • Sokolov VS, Kuz'min VG. 1980. Measurement of the differences in the surface potentials of bilayer membranes according to the second harmonic of a capacitance current. Biofizika 25:170-172. (In Russian.)
    • (1980) Biofizika , vol.25 , pp. 170-172
    • Sokolov, V.S.1    Kuz'min, V.G.2
  • 34
    • 58849140864 scopus 로고    scopus 로고
    • Membrane transport of singlet oxygen monitored by dipole potential measurements
    • Sokolov VS, Pohl P. 2009. Membrane transport of singlet oxygen monitored by dipole potential measurements. Biophys J 96:77-85. http://dx.doi.org/10.1529/biophysj.108.135145.
    • (2009) Biophys J , vol.96 , pp. 77-85
    • Sokolov, V.S.1    Pohl, P.2
  • 35
    • 0342901416 scopus 로고
    • Distribution of the interfacial potential drop in a situation when ionic solution components enter a surface-layer of finite thickness with fixed spacecharge
    • Vorotyntsev MA, Ermakov YA, Markin VS, Rubashkin AA. 1993. Distribution of the interfacial potential drop in a situation when ionic solution components enter a surface-layer of finite thickness with fixed spacecharge. Russ J Electrochem 29:730-748.
    • (1993) Russ J Electrochem , vol.29 , pp. 730-748
    • Vorotyntsev, M.A.1    Ermakov, Y.A.2    Markin, V.S.3    Rubashkin, A.A.4
  • 36
    • 0032542056 scopus 로고    scopus 로고
    • Interaction of the effector domain of MARCKS and MARCKS-related protein with lipid membranes revealed by electric potential measurements
    • Bähr G, Diederich A, Vergeres G, Winterhalter M. 1998. Interaction of the effector domain of MARCKS and MARCKS-related protein with lipid membranes revealed by electric potential measurements. Biochemistry 37:16252-16261. http://dx.doi.org/10.1021/bi981765a.
    • (1998) Biochemistry , vol.37 , pp. 16252-16261
    • Bähr, G.1    Diederich, A.2    Vergeres, G.3    Winterhalter, M.4
  • 39
    • 0000555535 scopus 로고
    • Sur la constitution de la charge électrique à la surface d'un électrolyte
    • (In French.)
    • Gouy M. 1910. Sur la constitution de la charge électrique à la surface d'un électrolyte. J Phys Theor Appl 9:457-468. (In French.) http://dx.doi.org/10.1051/jphystap:019100090045700.
    • (1910) J Phys Theor Appl , vol.9 , pp. 457-468
    • Gouy, M.1
  • 40
    • 0000264109 scopus 로고
    • A contribution to the theory of electrocapillarity
    • Chapman DL. 1913. A contribution to the theory of electrocapillarity. Philos Mag Ser 6 25:475-481. http://dx.doi.org/10.1080/14786440408634187.
    • (1913) Philos Mag Ser 6 , vol.25 , pp. 475-481
    • Chapman, D.L.1
  • 42
    • 83455172388 scopus 로고    scopus 로고
    • Removing material using atomic force microscopy with single-and multiple-tip sources
    • Tseng AA. 2011. Removing material using atomic force microscopy with single-and multiple-tip sources. Small 7:3409-3427. http://dx.doi.org/10.1002/smll.201100486.
    • (2011) Small , vol.7 , pp. 3409-3427
    • Tseng, A.A.1
  • 43
    • 34047260546 scopus 로고    scopus 로고
    • Atomic force microscopy and force spectroscopy study of Langmuir-Blodgett films formed by heteroacid phospholipids of biological interest
    • Garcia-Manyes S, Domènech Ò, Sanz F, Montero MT, Hernandez-Borrell J. 2007. Atomic force microscopy and force spectroscopy study of Langmuir-Blodgett films formed by heteroacid phospholipids of biological interest. Biochim Biophys Acta 1768:1190-1198. http://dx.doi.org/10.1016/j.bbamem.2007.02.004.
    • (2007) Biochim Biophys Acta , vol.1768 , pp. 1190-1198
    • Garcia-Manyes, S.1    Domènech, Ò.2    Sanz, F.3    Montero, M.T.4    Hernandez-Borrell, J.5
  • 46
    • 0027182957 scopus 로고
    • Fusion assays monitoring intermixing of aqueous contents
    • Düzgüneş N, Wilschut J. 1993. Fusion assays monitoring intermixing of aqueous contents. Methods Enzymol 220:3-14. http://dx.doi.org/10.1016/0076-6879(93)20069-F.
    • (1993) Methods Enzymol , vol.220 , pp. 3-14
    • Düzgüneş, N.1    Wilschut, J.2
  • 47
    • 12444272525 scopus 로고
    • Adsorption of gases in multimolecular layers
    • Brunauer S, Emmet PH, Teller E. 1938. Adsorption of gases in multimolecular layers. J Am Chem Soc 60:309-319. http://dx.doi.org/10.1021/ja01269a023.
    • (1938) J Am Chem Soc , vol.60 , pp. 309-319
    • Brunauer, S.1    Emmet, P.H.2    Teller, E.3
  • 48
    • 72449188290 scopus 로고    scopus 로고
    • What is the correct form of BET isotherm for modeling liquid phase adsorption?
    • Ebadi A, Mohammadzadeh JSS, Khudiev A. 2009. What is the correct form of BET isotherm for modeling liquid phase adsorption? Adsorption 15:65-73. http://dx.doi.org/10.1007/s10450-009-9151-3.
    • (2009) Adsorption , vol.15 , pp. 65-73
    • Ebadi, A.1    Mohammadzadeh, J.S.S.2    Khudiev, A.3
  • 49
    • 0028047505 scopus 로고
    • Fine structure of influenza A virus observed by electron cryo-microscopy
    • Fujiyoshi Y, Kume NP, Sakata K, Sato SB. 1994. Fine structure of influenza A virus observed by electron cryo-microscopy. EMBO J 13: 318-326.
    • (1994) EMBO J , vol.13 , pp. 318-326
    • Fujiyoshi, Y.1    Kume, N.P.2    Sakata, K.3    Sato, S.B.4
  • 50
    • 49049152405 scopus 로고
    • Hydration forces between mica surfaces in aqueous electrolyte solutions electrolyte solutions
    • Pashley RM. 1981. Hydration forces between mica surfaces in aqueous electrolyte solutions electrolyte solutions. J Colloid Interface Sci 80:153-162. http://dx.doi.org/10.1016/0021-9797(81)90171-5.
    • (1981) J Colloid Interface Sci , vol.80 , pp. 153-162
    • Pashley, R.M.1
  • 51
    • 0018789682 scopus 로고
    • Adsorption of monovalent cations to bilayer membranes containing negative phospholipids
    • Eisenberg M, GresalfiT, Riccio T, McLaughlin S. 1979. Adsorption of monovalent cations to bilayer membranes containing negative phospholipids. Biochemistry 18:5213-5223. http://dx.doi.org/10.1021/bi00590a028.
    • (1979) Biochemistry , vol.18 , pp. 5213-5223
    • Eisenberg, M.1    Gresalfi, T.2    Riccio, T.3    McLaughlin, S.4
  • 52
    • 84877287665 scopus 로고    scopus 로고
    • The Ebola virus matrix protein deeply penetrates the plasma membrane: an important step in viral egress
    • Soni SP, Adu-GyamfiE, Yong SS, Jee CS, Stahelin RV. 2013. The Ebola virus matrix protein deeply penetrates the plasma membrane: an important step in viral egress. Biophys J 104:1940-1949. http://dx.doi.org/10.1016/j.bpj.2013.03.021.
    • (2013) Biophys J , vol.104 , pp. 1940-1949
    • Soni, S.P.1    Adu-Gyamfi, E.2    Yong, S.S.3    Jee, C.S.4    Stahelin, R.V.5
  • 53
    • 84875459950 scopus 로고    scopus 로고
    • Surface plasmon resonance: a useful technique for cell biologists to characterize biomolecular interactions
    • Stahelin RV. 2013. Surface plasmon resonance: a useful technique for cell biologists to characterize biomolecular interactions. Mol Biol Cell 24:883-886. http://dx.doi.org/10.1091/mbc. E12-10-0713.
    • (2013) Mol Biol Cell , vol.24 , pp. 883-886
    • Stahelin, R.V.1
  • 54
    • 72149087966 scopus 로고    scopus 로고
    • Analysis of membrane binding equilibria of peripheral proteins: allowance for excluded area of bound protein
    • Minton AP. 2010. Analysis of membrane binding equilibria of peripheral proteins: allowance for excluded area of bound protein. Anal Biochem 397:247-249. http://dx.doi.org/10.1016/j.ab.2009.10.023.
    • (2010) Anal Biochem , vol.397 , pp. 247-249
    • Minton, A.P.1
  • 55
    • 77950789595 scopus 로고    scopus 로고
    • The lack of an inherent membrane targeting signal is responsible for the failure of the matrix (M1) protein of influenza A virus to bud into virus-like particles
    • Wang D, Harmon A, Jin J, Francis DH, Christopher-Hennings J, Nelson E, Montelaro RC, Li F. 2010. The lack of an inherent membrane targeting signal is responsible for the failure of the matrix (M1) protein of influenza A virus to bud into virus-like particles. J Virol 84:4673-4681. http://dx.doi.org/10.1128/JVI.02306-09.
    • (2010) J Virol , vol.84 , pp. 4673-4681
    • Wang, D.1    Harmon, A.2    Jin, J.3    Francis, D.H.4    Christopher-Hennings, J.5    Nelson, E.6    Montelaro, R.C.7    Li, F.8
  • 56
    • 84901989727 scopus 로고    scopus 로고
    • How cells tune viral mechanics-insights from biophysical measurements of influenza virus
    • Greber UF. 2014. How cells tune viral mechanics-insights from biophysical measurements of influenza virus. Biophys J 106:2317-2321. http://dx.doi.org/10.1016/j.bpj.2014.04.025.
    • (2014) Biophys J , vol.106 , pp. 2317-2321
    • Greber, U.F.1
  • 57
    • 0033932837 scopus 로고    scopus 로고
    • Effect of chain length and unsaturation on elasticity of lipid bilayers
    • Rawicz W, Olbrich KC, McIntosh T, Needham D, Evans E. 2000. Effect of chain length and unsaturation on elasticity of lipid bilayers. Biophys J 79:328-339. http://dx.doi.org/10.1016/S0006-3495(00)76295-3.
    • (2000) Biophys J , vol.79 , pp. 328-339
    • Rawicz, W.1    Olbrich, K.C.2    McIntosh, T.3    Needham, D.4    Evans, E.5
  • 58
    • 0027715108 scopus 로고
    • Influenza hemagglutinin-mediated fusion pores connecting cells to planar membranes: flickering to final expansion
    • Melikyan GB, Niles WD, Peeples ME, Cohen FS. 1993. Influenza hemagglutinin-mediated fusion pores connecting cells to planar membranes: flickering to final expansion. J Gen Physiol 102:1131-1149. http://dx.doi.org/10.1085/jgp.102.6.1131.
    • (1993) J Gen Physiol , vol.102 , pp. 1131-1149
    • Melikyan, G.B.1    Niles, W.D.2    Peeples, M.E.3    Cohen, F.S.4
  • 59
    • 0034252335 scopus 로고    scopus 로고
    • Multiple local contact sites are induced by GPI-linked influenza hemagglutinin during hemifusion and flickering pore formation
    • Frolov VA, Cho M-S, Bronk P, Reese TS, Zimmerberg J. 2000. Multiple local contact sites are induced by GPI-linked influenza hemagglutinin during hemifusion and flickering pore formation. Traffic 1:622-630. http://dx.doi.org/10.1034/j.1600-0854.2000.010806.x.
    • (2000) Traffic , vol.1 , pp. 622-630
    • Frolov, V.A.1    Cho, M.-S.2    Bronk, P.3    Reese, T.S.4    Zimmerberg, J.5
  • 60
    • 0034108437 scopus 로고    scopus 로고
    • Dynamics of fusion pores connecting membranes of different tensions
    • Chizmadzhev YA, Kuzmin PI, Kumenko DA, Zimmerberg J, Cohen FS. 2000. Dynamics of fusion pores connecting membranes of different tensions. Biophys J 78:2241-2256. http://dx.doi.org/10.1016/S0006-3495(00)76771-3.
    • (2000) Biophys J , vol.78 , pp. 2241-2256
    • Chizmadzhev, Y.A.1    Kuzmin, P.I.2    Kumenko, D.A.3    Zimmerberg, J.4    Cohen, F.S.5
  • 61
    • 0141865601 scopus 로고    scopus 로고
    • Dynamic tension spectroscopy and strength of biomembranes
    • Evans E, Heinrich V, Ludwig F, Rawicz W. 2003. Dynamic tension spectroscopy and strength of biomembranes. Biophys J 85:2342-2350. http://dx.doi.org/10.1016/S0006-3495(03)74658-X.
    • (2003) Biophys J , vol.85 , pp. 2342-2350
    • Evans, E.1    Heinrich, V.2    Ludwig, F.3    Rawicz, W.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.