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Volumn 150, Issue 1, 2000, Pages 105-117

Close is not enough: SNARE-dependent membrane fusion requires an active mechanism that transduces force to membrane anchors

Author keywords

Isoprene; Lipid anchor; Lipid mixing; Liposome; Vesicular transport

Indexed keywords

LIPOSOME; SNARE PROTEIN;

EID: 0034631955     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.150.1.105     Document Type: Article
Times cited : (258)

References (64)
  • 1
    • 0024366008 scopus 로고
    • Synaptobrevin: An integral membrane protein of 18,000 daltons present in small synaptic vesicles of rat brain
    • Baumert, M., P.R. Maycox, F. Navone, P. De Camilli, and R. Jahn. 1989. Synaptobrevin: an integral membrane protein of 18,000 daltons present in small synaptic vesicles of rat brain. EMBO (Eur. Mol. Biol. Organ.) J. 8:379-384.
    • (1989) EMBO (Eur. Mol. Biol. Organ.) J. , vol.8 , pp. 379-384
    • Baumert, M.1    Maycox, P.R.2    Navone, F.3    De Camilli, P.4    Jahn, R.5
  • 2
    • 0026778460 scopus 로고
    • Syntaxin: A synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones
    • Bennett, M.K., N. Calakos, and R.H. Scheller. 1992. Syntaxin: a synaptic protein implicated in docking of synaptic vesicles at presynaptic active zones. Science, 257:255-259.
    • (1992) Science , vol.257 , pp. 255-259
    • Bennett, M.K.1    Calakos, N.2    Scheller, R.H.3
  • 3
    • 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
  • 4
    • 0028023726 scopus 로고
    • Structure of influenza haemagglutinin at the pH of membrane fusion
    • Bullough, P.A., F.M. Hughson, J.J. Skehel, and D.C. Wiley. 1994. Structure of influenza haemagglutinin 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
  • 5
    • 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
  • 6
    • 0033573955 scopus 로고    scopus 로고
    • Intracellular localisation of SNAP-23 to endosomal compartments
    • Chen, D., and S.W. Whiteheart. 1999. Intracellular localisation of SNAP-23 to endosomal compartments. Biochem. Biophys. Res. Commun. 255:340-346.
    • (1999) Biochem. Biophys. Res. Commun. , vol.255 , pp. 340-346
    • Chen, D.1    Whiteheart, S.W.2
  • 8
    • 0029144334 scopus 로고
    • Bending membranes to the task: Structural intermediates in bilayer fusion
    • Chernomordik, L.V., and J. Zimmerberg. 1995. Bending membranes to the task: structural intermediates in bilayer fusion. Curr. Opin. Struct. Biol. 5:541-547.
    • (1995) Curr. Opin. Struct. Biol. , vol.5 , pp. 541-547
    • Chernomordik, L.V.1    Zimmerberg, J.2
  • 9
    • 0029148061 scopus 로고
    • The hemifusion intermediate and its conversion to complete fusion: Regulation by membrane composition
    • Chernomordik, L., A. Chanturiya, J. Green, and J. Zimmerberg. 1995a. The hemifusion intermediate and its conversion to complete fusion: regulation by membrane composition. Biophys, J. 69:922-929.
    • (1995) Biophys, J. , vol.69 , pp. 922-929
    • Chernomordik, L.1    Chanturiya, A.2    Green, J.3    Zimmerberg, J.4
  • 11
    • 0032559801 scopus 로고    scopus 로고
    • The pathway of membrane fusion catalyzed by influenza hemagglutinin: Restriction of lipids, hemifusion, and lipidic fusion pore formation
    • Chernomordik, L.V., V.A. Frolov, E. Leikina, 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
    • Chernomordik, L.V.1    Frolov, V.A.2    Leikina, E.3    Bronk, P.4    Zimmerberg, J.5
  • 13
    • 0032584146 scopus 로고    scopus 로고
    • The transmembrane domain in viral fusion: Essential role for a conserved glycine residue in vesicular stomatitis virus G protein
    • Cleverley, D.Z., and J. Lenard. 1998. The transmembrane domain in viral fusion: essential role for a conserved glycine residue in vesicular stomatitis virus G protein. Proc. Natl. Acad. Sci. USA. 95:3425-3430.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 3425-3430
    • Cleverley, D.Z.1    Lenard, J.2
  • 15
    • 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
  • 16
    • 0030735370 scopus 로고    scopus 로고
    • Structural changes are associated with soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor complex formation
    • Fasshauer, D., H. Otto, W.K. Eliason, R. Jahn, and A.T. Brunger. 1997. Structural changes are associated with soluble N-ethylmaleimide-sensitive fusion protein attachment protein receptor complex formation. J. Biol. Chem. 272: 28036-28041.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28036-28041
    • Fasshauer, D.1    Otto, H.2    Eliason, W.K.3    Jahn, R.4    Brunger, A.T.5
  • 17
    • 0030002637 scopus 로고    scopus 로고
    • HIV-1 entry cofactor: Functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor
    • Feng, Y., C.C. Broder, P.E. Kennedy, and E.A. Berger. 1996. HIV-1 entry cofactor: functional cDNA cloning of a seven-transmembrane, G protein-coupled receptor. Science. 272:872-877.
    • (1996) Science , vol.272 , pp. 872-877
    • Feng, Y.1    Broder, C.C.2    Kennedy, P.E.3    Berger, E.A.4
  • 18
    • 0033392946 scopus 로고    scopus 로고
    • Enzymology and biology of CaaX protein prenylation
    • Fu, H.W., and P.J. Casey. 1999. Enzymology and biology of CaaX protein prenylation. Recent Prog. Horm. Res. 54:315-342.
    • (1999) Recent Prog. Horm. Res. , vol.54 , pp. 315-342
    • Fu, H.W.1    Casey, P.J.2
  • 19
    • 0030846539 scopus 로고    scopus 로고
    • Neurotransmitter release: Four years of SNARE complexes
    • Hanson, P.I., J.E. Heuser, and R. Jahn. 1997a. Neurotransmitter release: four years of SNARE complexes. Curr. Opin. Neurobiol. 7:310-315.
    • (1997) Curr. Opin. Neurobiol. , vol.7 , pp. 310-315
    • Hanson, P.I.1    Heuser, J.E.2    Jahn, R.3
  • 20
    • 0030740252 scopus 로고    scopus 로고
    • Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy
    • Hanson, P.I., R. Roth, H. Morisaki, R. Jahn, and J.E. Heuser. 1997b. Structure and conformational changes in NSF and its membrane receptor complexes visualized by quick-freeze/deep-etch electron microscopy. Cell. 90:523-535.
    • (1997) Cell , vol.90 , pp. 523-535
    • Hanson, P.I.1    Roth, R.2    Morisaki, H.3    Jahn, R.4    Heuser, J.E.5
  • 22
    • 0026471991 scopus 로고
    • The 25 kDa synaptosomal-associated protein SNAP-25 is the major methionine-rich polypeptide in rapid axonal transport and a major substrate for palmitoylation in adult CNS
    • Hess, D.T., T.M. Slater, M.C. Wilson, and J.H. Skene. 1992. The 25 kDa synaptosomal-associated protein SNAP-25 is the major methionine-rich polypeptide in rapid axonal transport and a major substrate for palmitoylation in adult CNS. J. Neurosci. 12:4634-4641.
    • (1992) J. Neurosci. , vol.12 , pp. 4634-4641
    • Hess, D.T.1    Slater, T.M.2    Wilson, M.C.3    Skene, J.H.4
  • 23
    • 0032214690 scopus 로고    scopus 로고
    • Arrangement of subunits in 20 S particles consisting of NSF. SNAPs, and SNARE complexes
    • Hohl, T.M., F. Parlati, C. Wimmer, J.E. Rothman, T.H. Sollner, and H. Engelhardt. 1998. Arrangement of subunits in 20 S particles consisting of NSF. SNAPs, and SNARE complexes. Mol. Cell. 2:534-548.
    • (1998) Mol. Cell , vol.2 , pp. 534-548
    • Hohl, T.M.1    Parlati, F.2    Wimmer, C.3    Rothman, J.E.4    Sollner, T.H.5    Engelhardt, H.6
  • 24
    • 0033491695 scopus 로고    scopus 로고
    • Activity-dependent changes in partial VAMP complexes during neurotransmitter release
    • Hua, S.Y., and M.P. Charlton. 1999. Activity-dependent changes in partial VAMP complexes during neurotransmitter release. Nat. Neurosci. 2:1078-1083.
    • (1999) Nat. Neurosci. , vol.2 , pp. 1078-1083
    • Hua, S.Y.1    Charlton, M.P.2
  • 25
    • 0026660586 scopus 로고
    • Cloning and sequence analysis of cDNA for a neuronal cell membrane antigen, HPC-1
    • Inoue, A., K. Obata, and K. Akagawa. 1992. Cloning and sequence analysis of cDNA for a neuronal cell membrane antigen, HPC-1. J. Biol. Chem. 267: 10613-10619.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10613-10619
    • Inoue, A.1    Obata, K.2    Akagawa, K.3
  • 26
    • 0032476605 scopus 로고    scopus 로고
    • Genetic and morphological analyses reveal a critical interaction between the C-termini of two SNARE proteins and a parallel four helical arrangement for the exocytic SNARE complex
    • Katz, L., P.I. Hanson, J.E. Heuser, and P. Brennwald. 1998. Genetic and morphological analyses reveal a critical interaction between the C-termini of two SNARE proteins and a parallel four helical arrangement for the exocytic SNARE complex. EMBO (Eur. Mol. Biol. Organ.) J. 17:6200-6209.
    • (1998) EMBO (Eur. Mol. Biol. Organ.) J. , vol.17 , pp. 6200-6209
    • Katz, L.1    Hanson, P.I.2    Heuser, J.E.3    Brennwald, P.4
  • 27
    • 0028179011 scopus 로고
    • Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion
    • Kemble, G.W., T. Danieli, and J.M. White. 1994. Lipid-anchored influenza hemagglutinin promotes hemifusion, not complete fusion. Cell. 76:383-391.
    • (1994) Cell , vol.76 , pp. 383-391
    • Kemble, G.W.1    Danieli, T.2    White, J.M.3
  • 29
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 30
    • 0032935886 scopus 로고    scopus 로고
    • The paramyxovirus fusion protein forms an extremely stable core trimer: Structural parallels to influenza virus haemagglutinin and HIV-1 gp41
    • Lamb, R.A., S.B. Joshi, and R.E. Dutch. 1999. The paramyxovirus fusion protein forms an extremely stable core trimer: structural parallels to influenza virus haemagglutinin and HIV-1 gp41. Mol. Membr. Biol. 16:11-14.
    • (1999) Mol. Membr. Biol. , vol.16 , pp. 11-14
    • Lamb, R.A.1    Joshi, S.B.2    Dutch, R.E.3
  • 31
    • 0028834461 scopus 로고
    • A trimeric structural domain of the HIV-1 transmembrane glycoprotein
    • Lu, M., S.C. Blacklow, and P.S. Kim. 1995. A trimeric structural domain of the HIV-1 transmembrane glycoprotein. Nat. Struct. Biol. 2:1075-1082.
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 1075-1082
    • Lu, M.1    Blacklow, S.C.2    Kim, P.S.3
  • 32
    • 0023028190 scopus 로고
    • The T4 gene encodes the AIDS virus receptor and is expressed in the immune system and the brain
    • Maddon, P.J., A.G. Dalgleish, J.S. McDougal, P.R. Clapham, R.A Weiss, and R. Axel. 1986. The T4 gene encodes the AIDS virus receptor and is expressed in the immune system and the brain. Cell. 47:333-348.
    • (1986) Cell , vol.47 , pp. 333-348
    • Maddon, P.J.1    Dalgleish, A.G.2    McDougal, J.S.3    Clapham, P.R.4    Weiss, R.A.5    Axel, R.6
  • 33
    • 0034037991 scopus 로고    scopus 로고
    • The lipid-anchored ectodomain of influenza virus hemagglutinin (GPI-HA) is capable of inducing nonenlarging fusion pores
    • Markosyan, R.M., F.S. Cohen, and G.B. Melikyan. 2000. The lipid-anchored ectodomain of influenza virus hemagglutinin (GPI-HA) is capable of inducing nonenlarging fusion pores. Mol. Biol. Cell. 11:1143-1152.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 1143-1152
    • Markosyan, R.M.1    Cohen, F.S.2    Melikyan, G.B.3
  • 35
    • 0033197735 scopus 로고    scopus 로고
    • The length of the flexible SNAREpin juxtamembrane region is a critical determinant of SNARE-dependent fusion
    • McNew, J.A., T. Weber, D.M. Engelman, T.H. Sollner, and J.E. Rothman. 1999. The length of the flexible SNAREpin juxtamembrane region is a critical determinant of SNARE-dependent fusion. Mol. Cell. 4:415-421.
    • (1999) Mol. Cell , vol.4 , pp. 415-421
    • McNew, J.A.1    Weber, T.2    Engelman, D.M.3    Sollner, T.H.4    Rothman, J.E.5
  • 36
    • 0028865392 scopus 로고
    • GP1-anchored influenza hemagglutinin induces hemifusion to both red blood cell and planar bilayer membranes
    • Melikyan, G.B., J.M. White, and F.S. Cohen. 1995. GP1-anchored influenza hemagglutinin induces hemifusion to both red blood cell and planar bilayer membranes. J. Cell Biol. 131:679-691.
    • (1995) J. Cell Biol. , vol.131 , pp. 679-691
    • Melikyan, G.B.1    White, J.M.2    Cohen, F.S.3
  • 37
    • 0033017030 scopus 로고    scopus 로고
    • Amino acid sequence requirements of the transmembrane and cytoplasmic domains of influenza virus hemagglutinin for viable membrane fusion
    • Melikyan, G.B., S. Lin, M.G. Roth, and F.S. Cohen. 1999. Amino acid sequence requirements of the transmembrane and cytoplasmic domains of influenza virus hemagglutinin for viable membrane fusion. Mol. Biol. Cell. 10:1821-1836.
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1821-1836
    • Melikyan, G.B.1    Lin, S.2    Roth, M.G.3    Cohen, F.S.4
  • 38
    • 0027096398 scopus 로고
    • The exocylotic fusion pore
    • Monck, J.R., and J.M. Fernandez. 1992. The exocylotic fusion pore. J. Cell Biol. 119:1395-1404.
    • (1992) J. Cell Biol. , vol.119 , pp. 1395-1404
    • Monck, J.R.1    Fernandez, J.M.2
  • 39
    • 0028353472 scopus 로고
    • The exocytotic fusion pore and neurotransmitter release
    • Monck, J.R., and J.M. Fernandez. 1994. The exocytotic fusion pore and neurotransmitter release. Neuron. 12:707-716.
    • (1994) Neuron , vol.12 , pp. 707-716
    • Monck, J.R.1    Fernandez, J.M.2
  • 40
    • 0030222281 scopus 로고    scopus 로고
    • The fusion pore and mechanisms of biological membrane fusion
    • Monck, J.R., and J.M. Fernandez. 1996. The fusion pore and mechanisms of biological membrane fusion. Curr. Opin. Cell Biol. 8:524-533.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 524-533
    • Monck, J.R.1    Fernandez, J.M.2
  • 41
    • 0029205480 scopus 로고
    • The exocytotic fusion pore interface: A model of the site of neurotransmitter release
    • Monck, J.R., A.F. Oberhauser, and J.M. Fernandez. 1995. The exocytotic fusion pore interface: a model of the site of neurotransmitter release. Mol. Memb. Biol. 12:151-156.
    • (1995) Mol. Memb. Biol. , vol.12 , pp. 151-156
    • Monck, J.R.1    Oberhauser, A.F.2    Fernandez, J.M.3
  • 43
    • 0033607182 scopus 로고    scopus 로고
    • Content mixing and membrane integrity during membrane fusion driven by pairing of isolated v-SNAREs and t-SNAREs
    • Nickel, W., T. Weber, J.A. McNew, F. Parlati, T.H. Sollner, and J.E. Rothman. 1999. Content mixing and membrane integrity during membrane fusion driven by pairing of isolated v-SNAREs and t-SNAREs. Proc. Natl. Acad. Sci. USA. 96: 12571-12576.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12571-12576
    • Nickel, W.1    Weber, T.2    McNew, J.A.3    Parlati, F.4    Sollner, T.H.5    Rothman, J.E.6
  • 44
    • 0028012576 scopus 로고
    • Mutations in the membrane-spanning domain of the human immunodeficiency virus envelope glycoprotien that affect fusion activity
    • Owens, R.J., C. Burke, and J.K. Rose. 1994. Mutations in the membrane-spanning domain of the human immunodeficiency virus envelope glycoprotien that affect fusion activity. J. Virol. 68:570-574.
    • (1994) J. Virol. , vol.68 , pp. 570-574
    • Owens, R.J.1    Burke, C.2    Rose, J.K.3
  • 45
    • 0024828306 scopus 로고
    • The identification of a novel synaptosomal-associated protein. SNAP-25, differentially expressed by neuronal subpopulations
    • Oyler, G.A., G.A. Higgins, R.A. Hart, F. Battenberg, M. Billingsley. F.E. Bloom, and M.C. Wilson. 1989. The identification of a novel synaptosomal-associated protein. SNAP-25, differentially expressed by neuronal subpopulations. J. Cell Biol. 109:3039-3052.
    • (1989) J. Cell Biol. , vol.109 , pp. 3039-3052
    • Oyler, G.A.1    Higgins, G.A.2    Hart, R.A.3    Battenberg, F.4    Billingsley, M.5    Bloom, F.E.6    Wilson, M.C.7
  • 46
    • 0033607279 scopus 로고    scopus 로고
    • Rapid and efficient fusion of phospholipid vesicles by the alpha-helical core of a SNARE complex in the absence of an N-terminal regulatory domain
    • Parlati, F., T. Weber, J.A. McNew, B. Westermann, T.H. Sollner, and J.E. Rothman. 1999. Rapid and efficient fusion of phospholipid vesicles by the alpha-helical core of a SNARE complex in the absence of an N-terminal regulatory domain. New. Natl. Acad. Sci. USA. 96:12565-12570.
    • (1999) New. Natl. Acad. Sci. USA , vol.96 , pp. 12565-12570
    • Parlati, F.1    Weber, T.2    McNew, J.A.3    Westermann, B.4    Sollner, T.H.5    Rothman, J.E.6
  • 47
    • 0037926157 scopus 로고    scopus 로고
    • Peptides and membrane fusion: Towards an understanding of the molecular mechanism of protein-induced fusion
    • Pecheur, E.I., J. Sainte-Marie, A. Bienvene, and D. Hockstra. 1999. Peptides and membrane fusion: towards an understanding of the molecular mechanism of protein-induced fusion. J. Membr. Biol. 167:1-17.
    • (1999) J. Membr. Biol. , vol.167 , pp. 1-17
    • Pecheur, E.I.1    Sainte-Marie, J.2    Bienvene, A.3    Hockstra, D.4
  • 48
    • 0033591307 scopus 로고    scopus 로고
    • Are the fusion processes involved in birth, life and death of the cell depending on tilted insertion of peptides into membranes?
    • Peuvot, J., A. Schanck, L. Lins, and R. Brasseur. 1999. Are the fusion processes involved in birth, life and death of the cell depending on tilted insertion of peptides into membranes?. J. Theor. Biol. 198:173-181.
    • (1999) J. Theor. Biol. , vol.198 , pp. 173-181
    • Peuvot, J.1    Schanck, A.2    Lins, L.3    Brasseur, R.4
  • 50
    • 0021301852 scopus 로고
    • Lipopolymers, isoprenoids, and the assembly of the gram-positive cell wall
    • Reuseh, V.M., Jr. 1984. Lipopolymers, isoprenoids, and the assembly of the gram-positive cell wall. Crit. Rev. Microbiol. 11:129-155.
    • (1984) Crit. Rev. Microbiol. , vol.11 , pp. 129-155
    • Reuseh V.M., Jr.1
  • 51
    • 0015716692 scopus 로고
    • A rapid, sensitive, and specific method for the determination of protein in dilute solution
    • Schaffner, W., and C. Weissmann. 1973. A rapid, sensitive, and specific method for the determination of protein in dilute solution. Anal. Biochem. 56:502-514.
    • (1973) Anal. Biochem. , vol.56 , pp. 502-514
    • Schaffner, W.1    Weissmann, C.2
  • 52
    • 0032431055 scopus 로고    scopus 로고
    • Coiled coils in both intracellular vesicle and viral membrane fusion
    • Skehel, J.J., and D.C. Wiley. 1998. Coiled coils in both intracellular vesicle and viral membrane fusion. Cell. 95:871-874.
    • (1998) Cell , vol.95 , pp. 871-874
    • Skehel, J.J.1    Wiley, D.C.2
  • 54
    • 0026484172 scopus 로고
    • Structures of archaebacterial membrane lipids
    • Sprott, G.D. 1992. Structures of archaebacterial membrane lipids. J. Bioenerg. Biomembr. 24:555-566.
    • (1992) J. Bioenerg. Biomembr. , vol.24 , pp. 555-566
    • Sprott, G.D.1
  • 55
    • 0019874707 scopus 로고
    • Use of resonance energy transfer to monitor membrane fusion
    • Struck, D.K., D. Hoekstra, and R.E. Pagano. 1981. Use of resonance energy transfer to monitor membrane fusion. Biochemistry. 20:4093-4099.
    • (1981) Biochemistry , vol.20 , pp. 4093-4099
    • Struck, D.K.1    Hoekstra, D.2    Pagano, R.E.3
  • 56
    • 3543096759 scopus 로고    scopus 로고
    • Crystal structure of a SNARE complex involved in synaptic cxocytosis at 2.4 A resolution
    • Sutton, R.B., D. Fasshauer, R. Jahn, and A.T. Brunger. 1998. Crystal structure of a SNARE complex involved in synaptic cxocytosis at 2.4 A resolution. Nature. 395:347-353.
    • (1998) Nature , vol.395 , pp. 347-353
    • Sutton, R.B.1    Fasshauer, D.2    Jahn, R.3    Brunger, A.T.4
  • 57
    • 0006602702 scopus 로고
    • VAMP-1: A synaptic vesicle-associated integral membrane protein
    • Trimble, W.S., D.M. Cowan, and R.H. Scheller. 1988. VAMP-1: a synaptic vesicle-associated integral membrane protein. Proc. Natl Acad. Sci. USA. 85: 4538-4542.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 4538-4542
    • Trimble, W.S.1    Cowan, D.M.2    Scheller, R.H.3
  • 58
    • 0018369107 scopus 로고
    • The chemistry and biosynthesis of selected bacterial capsular polymers
    • Troy, F.A. 2d. 1979. The chemistry and biosynthesis of selected bacterial capsular polymers. Annu. Rev. Microbiol. 33:519-560.
    • (1979) Annu. Rev. Microbiol. , vol.33 , pp. 519-560
    • Troy F.A. II1
  • 59
    • 0032506543 scopus 로고    scopus 로고
    • Defining the functions of trans-SNARE pairs
    • Ungermann, C., K. Sato, and W. Wickner. 1998. Defining the functions of trans-SNARE pairs. Nature. 396:543-548.
    • (1998) Nature , vol.396 , pp. 543-548
    • Ungermann, C.1    Sato, K.2    Wickner, W.3
  • 60
    • 18244432240 scopus 로고    scopus 로고
    • Multiple palmitoylation of synaptotagmin and the t-SNARE SNAP-25
    • Veit, M., T.H. Sollner, and J.E. Rothman. 1996. Multiple palmitoylation of synaptotagmin and the t-SNARE SNAP-25. FEBS Lett. 385:119-123.
    • (1996) FEBS Lett. , vol.385 , pp. 119-123
    • Veit, M.1    Sollner, T.H.2    Rothman, J.E.3
  • 63
    • 0019890491 scopus 로고
    • Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution
    • Wilson, I.A., J.J. Skehel, and D.C. Wiley. 1981. Structure of the haemagglutinin membrane glycoprotein of influenza virus at 3 A resolution. Nature. 289: 366-373.
    • (1981) Nature , vol.289 , pp. 366-373
    • Wilson, I.A.1    Skehel, J.J.2    Wiley, D.C.3
  • 64
    • 0033598965 scopus 로고    scopus 로고
    • Inhibition of SNARE complex assembly differentially affects kinetic components of exocytosis
    • Xu, T., B. Rammner, M. Margittai, A.R. Artalejo, H. Neher, and R. Jahn. 1999. Inhibition of SNARE complex assembly differentially affects kinetic components of exocytosis. Cell. 99:713-722.
    • (1999) Cell , vol.99 , pp. 713-722
    • Xu, T.1    Rammner, B.2    Margittai, M.3    Artalejo, A.R.4    Neher, H.5    Jahn, R.6


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