메뉴 건너뛰기




Volumn 116, Issue 36, 2019, Pages 18098-18108

Gangliosides interact with synaptotagmin to form the high-affinity receptor complex for botulinum neurotoxin B

Author keywords

Botulinum neurotoxin B receptor; Gangliosides; Synaptotagmin

Indexed keywords

BOTULINUM TOXIN B; CERAMIDE; GANGLIOSIDE GT 1B; OLIGOSACCHARIDE; SYNAPTOTAGMIN; TRYPTOPHAN; BOTULINUM TOXIN A; GANGLIOSIDE; SYNAPTOTAGMIN I; SYNAPTOTAGMIN II; SYT1 PROTEIN, RAT; SYT2 PROTEIN, RAT; TRISIALOGANGLIOSIDE GT1;

EID: 85071788842     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1908051116     Document Type: Article
Times cited : (35)

References (63)
  • 1
    • 85060010373 scopus 로고    scopus 로고
    • Why are botulinum neurotoxin-producing bacteria so diverse and botulinum neurotoxins so toxic?
    • B. Poulain, M. R. Popoff, Why are botulinum neurotoxin-producing bacteria so diverse and botulinum neurotoxins so toxic? Toxins (Basel) 11, E34 (2019).
    • (2019) Toxins (Basel) , vol.11 , pp. E34
    • Poulain, B.1    Popoff, M.R.2
  • 2
    • 84877619817 scopus 로고    scopus 로고
    • The life history of a botulinum toxin molecule
    • L. Simpson, The life history of a botulinum toxin molecule. Toxicon 68, 40-59 (2013).
    • (2013) Toxicon , vol.68 , pp. 40-59
    • Simpson, L.1
  • 3
    • 84877704954 scopus 로고    scopus 로고
    • Botulinum neurotoxins: Mechanism of action
    • A. P. Tighe, G. Schiavo, Botulinum neurotoxins: Mechanism of action. Toxicon 67, 87-93 (2013).
    • (2013) Toxicon , vol.67 , pp. 87-93
    • Tighe, A.P.1    Schiavo, G.2
  • 4
    • 84923190210 scopus 로고    scopus 로고
    • Botulinum neurotoxins: New questions arising from structural biology
    • R. A. Kammerer, R. M. Benoit, Botulinum neurotoxins: New questions arising from structural biology. Trends Biochem. Sci. 39, 517-526 (2014).
    • (2014) Trends Biochem. Sci. , vol.39 , pp. 517-526
    • Kammerer, R.A.1    Benoit, R.M.2
  • 5
    • 84890176367 scopus 로고    scopus 로고
    • The pre-synaptic motor nerve terminal as a site for antibody-mediated neurotoxicity in autoimmune neuropathies and synaptopathies
    • S. N. Fewou, J. J. Plomp, H. J. Willison, The pre-synaptic motor nerve terminal as a site for antibody-mediated neurotoxicity in autoimmune neuropathies and synaptopathies. J. Anat. 224, 36-44 (2014).
    • (2014) J. Anat. , vol.224 , pp. 36-44
    • Fewou, S.N.1    Plomp, J.J.2    Willison, H.J.3
  • 6
    • 77955597073 scopus 로고    scopus 로고
    • A hitchhiker's guide to the nervous system: The complex journey of viruses and toxins
    • S. Salinas, G. Schiavo, E. J. Kremer, A hitchhiker's guide to the nervous system: The complex journey of viruses and toxins. Nat. Rev. Microbiol. 8, 645-655 (2010).
    • (2010) Nat. Rev. Microbiol. , vol.8 , pp. 645-655
    • Salinas, S.1    Schiavo, G.2    Kremer, E.J.3
  • 8
    • 84982062283 scopus 로고    scopus 로고
    • Gangliosides of the vertebrate nervous system
    • R. L. Schnaar, Gangliosides of the vertebrate nervous system. J. Mol. Biol. 428, 3325-3336 (2016).
    • (2016) J. Mol. Biol. , vol.428 , pp. 3325-3336
    • Schnaar, R.L.1
  • 9
    • 33845885528 scopus 로고    scopus 로고
    • Structural basis of cell surface receptor recognition by botulinum neurotoxin B
    • Q. Chai et al., Structural basis of cell surface receptor recognition by botulinum neurotoxin B. Nature 444, 1096-1100 (2006).
    • (2006) Nature , vol.444 , pp. 1096-1100
    • Chai, Q.1
  • 10
    • 4644364793 scopus 로고    scopus 로고
    • Presynaptic receptor arrays for clostridial neurotoxins
    • C. Montecucco, O. Rossetto, G. Schiavo, Presynaptic receptor arrays for clostridial neurotoxins. Trends Microbiol. 12, 442-446 (2004).
    • (2004) Trends Microbiol. , vol.12 , pp. 442-446
    • Montecucco, C.1    Rossetto, O.2    Schiavo, G.3
  • 12
    • 0035826727 scopus 로고    scopus 로고
    • SNARE proteins are highly enriched in lipid rafts in PC12 cells: Implications for the spatial control of exocytosis
    • L. H. Chamberlain, R. D. Burgoyne, G. W. Gould, SNARE proteins are highly enriched in lipid rafts in PC12 cells: Implications for the spatial control of exocytosis. Proc. Natl. Acad. Sci. U.S.A. 98, 5619-5624 (2001).
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 5619-5624
    • Chamberlain, L.H.1    Burgoyne, R.D.2    Gould, G.W.3
  • 13
    • 84856284553 scopus 로고    scopus 로고
    • Uncoupling the roles of synaptotagmin i during endo-and exocytosis of synaptic vesicles
    • J. Yao, S. E. Kwon, J. D. Gaffaney, F. M. Dunning, E. R. Chapman, Uncoupling the roles of synaptotagmin I during endo-and exocytosis of synaptic vesicles. Nat. Neurosci. 15, 243-249 (2011).
    • (2011) Nat. Neurosci. , vol.15 , pp. 243-249
    • Yao, J.1    Kwon, S.E.2    Gaffaney, J.D.3    Dunning, F.M.4    Chapman, E.R.5
  • 14
    • 84867414968 scopus 로고    scopus 로고
    • Glycosylation is dispensable for sorting of synaptotagmin 1 but is critical for targeting of SV2 and synaptophysin to recycling synaptic vesicles
    • S. E. Kwon, E. R. Chapman, Glycosylation is dispensable for sorting of synaptotagmin 1 but is critical for targeting of SV2 and synaptophysin to recycling synaptic vesicles. J. Biol. Chem. 287, 35658-35668 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 35658-35668
    • Kwon, S.E.1    Chapman, E.R.2
  • 15
    • 85046130653 scopus 로고    scopus 로고
    • A Ca2+ sensor for exocytosis
    • E. R. Chapman, A Ca2+ sensor for exocytosis. Trends Neurosci. 41, 327-330 (2018).
    • (2018) Trends Neurosci. , vol.41 , pp. 327-330
    • Chapman, E.R.1
  • 16
    • 33845871995 scopus 로고    scopus 로고
    • Botulinum neurotoxin B recognizes its protein receptor with high affinity and specificity
    • R. Jin, A. Rummel, T. Binz, A. T. Brunger, Botulinum neurotoxin B recognizes its protein receptor with high affinity and specificity. Nature 444, 1092-1095 (2006).
    • (2006) Nature , vol.444 , pp. 1092-1095
    • Jin, R.1    Rummel, A.2    Binz, T.3    Brunger, A.T.4
  • 17
    • 84868382710 scopus 로고    scopus 로고
    • Botulinum neurotoxin D-C uses synaptotagmin i and II as receptors, and human synaptotagmin II is not an effective receptor for type B, D-C and G toxins
    • L. Peng et al., Botulinum neurotoxin D-C uses synaptotagmin I and II as receptors, and human synaptotagmin II is not an effective receptor for type B, D-C and G toxins. J. Cell Sci. 125, 3233-3242 (2012).
    • (2012) J. Cell Sci. , vol.125 , pp. 3233-3242
    • Peng, L.1
  • 18
    • 85060037659 scopus 로고    scopus 로고
    • Engineered botulinum neurotoxin B with improved binding to human receptors has enhanced efficacy in preclinical models
    • M. Elliott et al., Engineered botulinum neurotoxin B with improved binding to human receptors has enhanced efficacy in preclinical models. Sci. Adv. 5, eaau7196 (2019).
    • (2019) Sci. Adv. , vol.5 , pp. eaau7196
    • Elliott, M.1
  • 19
    • 84883167220 scopus 로고    scopus 로고
    • Structure of dual receptor binding to botulinum neurotoxin B
    • R. P. Berntsson, L. Peng, M. Dong, P. Stenmark, Structure of dual receptor binding to botulinum neurotoxin B. Nat. Commun. 4, 2058 (2013).
    • (2013) Nat. Commun. , vol.4 , pp. 2058
    • Berntsson, R.P.1    Peng, L.2    Dong, M.3    Stenmark, P.4
  • 20
    • 46149134882 scopus 로고
    • How do tetanus and botulinum toxins bind to neuronal membranes?
    • C. Montecucco, How do tetanus and botulinum toxins bind to neuronal membranes? Trends Biochem. Sci. 11, 314-317 (1986).
    • (1986) Trends Biochem. Sci. , vol.11 , pp. 314-317
    • Montecucco, C.1
  • 21
    • 33845889228 scopus 로고    scopus 로고
    • Structural biology: Dangerous liaisons on neurons
    • G. Schiavo, Structural biology: Dangerous liaisons on neurons. Nature 444, 1019-1020 (2006).
    • (2006) Nature , vol.444 , pp. 1019-1020
    • Schiavo, G.1
  • 22
    • 85048022116 scopus 로고    scopus 로고
    • A lipid-binding loop of botulinum neurotoxin serotypes B, DC and G is an essential feature to confer their exquisite potency
    • D. Stern et al., A lipid-binding loop of botulinum neurotoxin serotypes B, DC and G is an essential feature to confer their exquisite potency. PLoS Pathog. 14, e1007048 (2018).
    • (2018) PLoS Pathog. , vol.14 , pp. e1007048
    • Stern, D.1
  • 23
    • 85018175620 scopus 로고    scopus 로고
    • Affinity biosensors using recombinant native membrane proteins displayed on exosomes: Application to botulinum neurotoxin B receptor
    • R. Desplantes et al., Affinity biosensors using recombinant native membrane proteins displayed on exosomes: Application to botulinum neurotoxin B receptor. Sci. Rep. 7, 1032 (2017).
    • (2017) Sci. Rep. , vol.7 , pp. 1032
    • Desplantes, R.1
  • 24
    • 33748513877 scopus 로고    scopus 로고
    • Prediction of glycolipid-binding domains from the amino acid sequence of lipid raft-associated proteins: Application to HpaA, a protein involved in the adhesion of Helicobacter pylori to gastrointestinal cells
    • J. Fantini, N. Garmy, N. Yahi, Prediction of glycolipid-binding domains from the amino acid sequence of lipid raft-associated proteins: Application to HpaA, a protein involved in the adhesion of Helicobacter pylori to gastrointestinal cells. Biochemistry 45, 10957-10962 (2006).
    • (2006) Biochemistry , vol.45 , pp. 10957-10962
    • Fantini, J.1    Garmy, N.2    Yahi, N.3
  • 25
    • 79954534373 scopus 로고    scopus 로고
    • Molecular basis for the glycosphingolipid-binding specificity of α-synuclein: Key role of tyrosine 39 in membrane insertion
    • J. Fantini, N. Yahi, Molecular basis for the glycosphingolipid-binding specificity of α-synuclein: Key role of tyrosine 39 in membrane insertion. J. Mol. Biol. 408, 654-669 (2011).
    • (2011) J. Mol. Biol. , vol.408 , pp. 654-669
    • Fantini, J.1    Yahi, N.2
  • 26
    • 77955033375 scopus 로고    scopus 로고
    • Greasing their way: Lipid modifications determine protein association with membrane rafts
    • I. Levental, M. Grzybek, K. Simons, Greasing their way: Lipid modifications determine protein association with membrane rafts. Biochemistry 49, 6305-6316 (2010).
    • (2010) Biochemistry , vol.49 , pp. 6305-6316
    • Levental, I.1    Grzybek, M.2    Simons, K.3
  • 27
    • 0037274881 scopus 로고    scopus 로고
    • Interaction of peptides with binary phospholipid membranes: Application of fluorescence methodologies
    • L. M. Loura, R. F. de Almeida, A. Coutinho, M. Prieto, Interaction of peptides with binary phospholipid membranes: Application of fluorescence methodologies. Chem. Phys. Lipids 122, 77-96 (2003).
    • (2003) Chem. Phys. Lipids , vol.122 , pp. 77-96
    • Loura, L.M.1    De Almeida, R.F.2    Coutinho, A.3    Prieto, M.4
  • 28
    • 15744370492 scopus 로고    scopus 로고
    • Ionization potentials of fluoroindoles and the origin of nonexponential tryptophan fluorescence decay in proteins
    • T. Liu et al., Ionization potentials of fluoroindoles and the origin of nonexponential tryptophan fluorescence decay in proteins. J. Am. Chem. Soc. 127, 4104-4113 (2005).
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 4104-4113
    • Liu, T.1
  • 29
    • 85021734647 scopus 로고    scopus 로고
    • Engineered botulinum neurotoxin B with improved efficacy for targeting human receptors
    • L. Tao et al., Engineered botulinum neurotoxin B with improved efficacy for targeting human receptors. Nat. Commun. 8, 53 (2017).
    • (2017) Nat. Commun. , vol.8 , pp. 53
    • Tao, L.1
  • 30
    • 67650104280 scopus 로고    scopus 로고
    • Electric dipole reorientation in the interaction of botulinum neurotoxins with neuronal membranes
    • F. Fogolari, S. C. Tosatto, L. Muraro, C. Montecucco, Electric dipole reorientation in the interaction of botulinum neurotoxins with neuronal membranes. FEBS Lett. 583, 2321-2325 (2009).
    • (2009) FEBS Lett. , vol.583 , pp. 2321-2325
    • Fogolari, F.1    Tosatto, S.C.2    Muraro, L.3    Montecucco, C.4
  • 31
    • 0141641129 scopus 로고    scopus 로고
    • Synaptotagmins i and II mediate entry of botulinum neurotoxin B into cells
    • M. Dong et al., Synaptotagmins I and II mediate entry of botulinum neurotoxin B into cells. J. Cell Biol. 162, 1293-1303 (2003).
    • (2003) J. Cell Biol. , vol.162 , pp. 1293-1303
    • Dong, M.1
  • 32
    • 84941695742 scopus 로고    scopus 로고
    • Botulinum neurotoxins can enter cultured neurons independent of synaptic vesicle recycling
    • S. Pellett, W. H. Tepp, J. M. Scherf, E. A. Johnson, Botulinum neurotoxins can enter cultured neurons independent of synaptic vesicle recycling. PLoS One 10, e0133737 (2015).
    • (2015) PLoS One , vol.10 , pp. e0133737
    • Pellett, S.1    Tepp, W.H.2    Scherf, J.M.3    Johnson, E.A.4
  • 33
    • 38049036925 scopus 로고    scopus 로고
    • Mechanism of botulinum neurotoxin B and G entry into hippocampal neurons
    • M. Dong, W. H. Tepp, H. Liu, E. A. Johnson, E. R. Chapman, Mechanism of botulinum neurotoxin B and G entry into hippocampal neurons. J. Cell Biol. 179, 1511-1522 (2007).
    • (2007) J. Cell Biol. , vol.179 , pp. 1511-1522
    • Dong, M.1    Tepp, W.H.2    Liu, H.3    Johnson, E.A.4    Chapman, E.R.5
  • 34
    • 0031663156 scopus 로고    scopus 로고
    • Ganglioside GT1b as a complementary receptor component for Clostridium botulinum neurotoxins
    • S. Kozaki, Y. Kamata, S. Watarai, T. Nishiki, S. Mochida, Ganglioside GT1b as a complementary receptor component for Clostridium botulinum neurotoxins. Microb. Pathog. 25, 91-99 (1998).
    • (1998) Microb. Pathog. , vol.25 , pp. 91-99
    • Kozaki, S.1    Kamata, Y.2    Watarai, S.3    Nishiki, T.4    Mochida, S.5
  • 35
    • 80052994116 scopus 로고    scopus 로고
    • Receptor binding enables botulinum neurotoxin B to sense low pH for translocation channel assembly
    • S. Sun et al., Receptor binding enables botulinum neurotoxin B to sense low pH for translocation channel assembly. Cell Host Microbe 10, 237-247 (2011).
    • (2011) Cell Host Microbe , vol.10 , pp. 237-247
    • Sun, S.1
  • 36
    • 0021953447 scopus 로고
    • Tetanus toxin interaction with human erythrocytes I. Properties of polysialoganglioside association with the cell surface
    • P. Lazarovici, E. Yavin, Tetanus toxin interaction with human erythrocytes. I. Properties of polysialoganglioside association with the cell surface. Biochim. Biophys. Acta 812, 523-531 (1985).
    • (1985) Biochim. Biophys. Acta , vol.812 , pp. 523-531
    • Lazarovici, P.1    Yavin, E.2
  • 37
    • 70350371732 scopus 로고    scopus 로고
    • Gangliosides as high affinity receptors for tetanus neurotoxin
    • C. Chen, Z. Fu, J. J. Kim, J. T. Barbieri, M. R. Baldwin, Gangliosides as high affinity receptors for tetanus neurotoxin. J. Biol. Chem. 284, 26569-26577 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 26569-26577
    • Chen, C.1    Fu, Z.2    Kim, J.J.3    Barbieri, J.T.4    Baldwin, M.R.5
  • 38
    • 0020004058 scopus 로고
    • Localization of sites for 125I-labelled botulinum neurotoxin at murine neuromuscular junction and its binding to rat brain synaptosomes
    • J. O. Dolly et al., Localization of sites for 125I-labelled botulinum neurotoxin at murine neuromuscular junction and its binding to rat brain synaptosomes. Toxicon 20, 141-148 (1982).
    • (1982) Toxicon , vol.20 , pp. 141-148
    • Dolly, J.O.1
  • 39
    • 84900450139 scopus 로고    scopus 로고
    • Sialic acids in the brain: Gangliosides and polysialic acid in nervous system development, stability, disease, and regeneration
    • R. L. Schnaar, R. Gerardy-Schahn, H. Hildebrandt, Sialic acids in the brain: Gangliosides and polysialic acid in nervous system development, stability, disease, and regeneration. Physiol. Rev. 94, 461-518 (2014).
    • (2014) Physiol. Rev. , vol.94 , pp. 461-518
    • Schnaar, R.L.1    Gerardy-Schahn, R.2    Hildebrandt, H.3
  • 40
    • 17744390877 scopus 로고    scopus 로고
    • Action-at-A-distance interactions enhance protein binding affinity
    • B. A. Joughin, D. F. Green, B. Tidor, Action-at-A-distance interactions enhance protein binding affinity. Protein Sci. 14, 1363-1369 (2005).
    • (2005) Protein Sci. , vol.14 , pp. 1363-1369
    • Joughin, B.A.1    Green, D.F.2    Tidor, B.3
  • 41
    • 70350029187 scopus 로고    scopus 로고
    • Specific membrane binding of neurotoxin II can facilitate its delivery to acetylcholine receptor
    • D. M. Lesovoy et al., Specific membrane binding of neurotoxin II can facilitate its delivery to acetylcholine receptor. Biophys. J. 97, 2089-2097 (2009).
    • (2009) Biophys. J. , vol.97 , pp. 2089-2097
    • Lesovoy, D.M.1
  • 42
    • 0030064241 scopus 로고    scopus 로고
    • The high-affinity binding of Clostridium botulinum type B neurotoxin to synaptotagmin II associated with gangliosides GT1b/GD1a
    • T. Nishiki et al., The high-affinity binding of Clostridium botulinum type B neurotoxin to synaptotagmin II associated with gangliosides GT1b/GD1a. FEBS Lett. 378, 253-257 (1996).
    • (1996) FEBS Lett. , vol.378 , pp. 253-257
    • Nishiki, T.1
  • 43
    • 13844272574 scopus 로고    scopus 로고
    • Synaptic proteins and SNARE complexes are localized in lipid rafts from rat brain synaptosomes
    • C. Gil, A. Soler-Jover, J. Blasi, J. Aguilera, Synaptic proteins and SNARE complexes are localized in lipid rafts from rat brain synaptosomes. Biochem. Biophys. Res. Commun. 329, 117-124 (2005).
    • (2005) Biochem. Biophys. Res. Commun. , vol.329 , pp. 117-124
    • Gil, C.1    Soler-Jover, A.2    Blasi, J.3    Aguilera, J.4
  • 44
    • 0036196917 scopus 로고    scopus 로고
    • Lipid microdomains are involved in neurospecific binding and internalisation of clostridial neurotoxins
    • J. Herreros, G. Schiavo, Lipid microdomains are involved in neurospecific binding and internalisation of clostridial neurotoxins. Int. J. Med. Microbiol. 291, 447-453 (2002).
    • (2002) Int. J. Med. Microbiol. , vol.291 , pp. 447-453
    • Herreros, J.1    Schiavo, G.2
  • 45
    • 59649101806 scopus 로고    scopus 로고
    • The N-terminal half of the receptor domain of botulinum neurotoxin A binds to microdomains of the plasma membrane
    • L. Muraro, S. Tosatto, L. Motterlini, O. Rossetto, C. Montecucco, The N-terminal half of the receptor domain of botulinum neurotoxin A binds to microdomains of the plasma membrane. Biochem. Biophys. Res. Commun. 380, 76-80 (2009).
    • (2009) Biochem. Biophys. Res. Commun. , vol.380 , pp. 76-80
    • Muraro, L.1    Tosatto, S.2    Motterlini, L.3    Rossetto, O.4    Montecucco, C.5
  • 46
    • 81255144013 scopus 로고    scopus 로고
    • Post-translational modifications and lipid binding profile of insect cellexpressed full-length mammalian synaptotagmin 1
    • M. Vrljic et al., Post-translational modifications and lipid binding profile of insect cellexpressed full-length mammalian synaptotagmin 1. Biochemistry 50, 9998-10012 (2011).
    • (2011) Biochemistry , vol.50 , pp. 9998-10012
    • Vrljic, M.1
  • 47
    • 0027980589 scopus 로고
    • Binding of GM1 ganglioside to a synthetic peptide derived from the lysosomal sphingolipid activator protein saposin B
    • M. J. Champagne, S. Lamontagne, M. Potier, Binding of GM1 ganglioside to a synthetic peptide derived from the lysosomal sphingolipid activator protein saposin B. FEBS Lett. 349, 439-441 (1994).
    • (1994) FEBS Lett. , vol.349 , pp. 439-441
    • Champagne, M.J.1    Lamontagne, S.2    Potier, M.3
  • 48
    • 0033525077 scopus 로고    scopus 로고
    • Role of lipid modifications in targeting proteins to detergent-resistant membrane rafts Many raft proteins are acylated, while few are prenylated
    • K. A. Melkonian, A. G. Ostermeyer, J. Z. Chen, M. G. Roth, D. A. Brown, Role of lipid modifications in targeting proteins to detergent-resistant membrane rafts. Many raft proteins are acylated, while few are prenylated. J. Biol. Chem. 274, 3910-3917 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 3910-3917
    • Melkonian, K.A.1    Ostermeyer, A.G.2    Chen, J.Z.3    Roth, M.G.4    Brown, D.A.5
  • 49
    • 35348926769 scopus 로고    scopus 로고
    • Dissociation of the insulin receptor and caveolin-1 complex by ganglioside GM3 in the state of insulin resistance
    • K. Kabayama et al., Dissociation of the insulin receptor and caveolin-1 complex by ganglioside GM3 in the state of insulin resistance. Proc. Natl. Acad. Sci. U.S.A. 104, 13678-13683 (2007).
    • (2007) Proc. Natl. Acad. Sci. U.S.A. , vol.104 , pp. 13678-13683
    • Kabayama, K.1
  • 50
    • 33847022701 scopus 로고    scopus 로고
    • GM1 specifically interacts with alpha-synuclein and inhibits fibrillation
    • Z. Martinez, M. Zhu, S. Han, A. L. Fink, GM1 specifically interacts with alpha-synuclein and inhibits fibrillation. Biochemistry 46, 1868-1877 (2007).
    • (2007) Biochemistry , vol.46 , pp. 1868-1877
    • Martinez, Z.1    Zhu, M.2    Han, S.3    Fink, A.L.4
  • 51
    • 0032548943 scopus 로고    scopus 로고
    • Structural transitions associated with the interaction of Alzheimer beta-amyloid peptides with gangliosides
    • J. McLaurin, T. Franklin, P. E. Fraser, A. Chakrabartty, Structural transitions associated with the interaction of Alzheimer beta-amyloid peptides with gangliosides. J. Biol. Chem. 273, 4506-4515 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 4506-4515
    • McLaurin, J.1    Franklin, T.2    Fraser, P.E.3    Chakrabartty, A.4
  • 52
    • 84906239240 scopus 로고    scopus 로고
    • How do membranes initiate Alzheimer's disease? Formation of toxic amyloid fibrils by the amyloid β-protein on ganglioside clusters
    • K. Matsuzaki, How do membranes initiate Alzheimer's disease? Formation of toxic amyloid fibrils by the amyloid β-protein on ganglioside clusters. Acc. Chem. Res. 47, 2397-2404 (2014).
    • (2014) Acc. Chem. Res. , vol.47 , pp. 2397-2404
    • Matsuzaki, K.1
  • 53
    • 79959677155 scopus 로고    scopus 로고
    • A readily retrievable pool of synaptic vesicles
    • Y. Hua et al., A readily retrievable pool of synaptic vesicles. Nat. Neurosci. 14, 833-839 (2011).
    • (2011) Nat. Neurosci. , vol.14 , pp. 833-839
    • Hua, Y.1
  • 54
    • 33745901961 scopus 로고    scopus 로고
    • Synaptic vesicles interchange their membrane proteins with a large surface reservoir during recycling
    • T. Fernández-Alfonso, R. Kwan, T. A. Ryan, Synaptic vesicles interchange their membrane proteins with a large surface reservoir during recycling. Neuron 51, 179-186 (2006).
    • (2006) Neuron , vol.51 , pp. 179-186
    • Fernández-Alfonso, T.1    Kwan, R.2    Ryan, T.A.3
  • 55
    • 33645839858 scopus 로고    scopus 로고
    • STED microscopy reveals that synaptotagmin remains clustered after synaptic vesicle exocytosis
    • K. I. Willig, S. O. Rizzoli, V. Westphal, R. Jahn, S. W. Hell, STED microscopy reveals that synaptotagmin remains clustered after synaptic vesicle exocytosis. Nature 440, 935-939 (2006).
    • (2006) Nature , vol.440 , pp. 935-939
    • Willig, K.I.1    Rizzoli, S.O.2    Westphal, V.3    Jahn, R.4    Hell, S.W.5
  • 56
    • 85034639606 scopus 로고    scopus 로고
    • Structural basis for the unique ganglioside and cell membrane recognition mechanism of botulinum neurotoxin DC
    • S. Zhang et al., Structural basis for the unique ganglioside and cell membrane recognition mechanism of botulinum neurotoxin DC. Nat. Commun. 8, 1637 (2017).
    • (2017) Nat. Commun. , vol.8 , pp. 1637
    • Zhang, S.1
  • 57
    • 84904700172 scopus 로고    scopus 로고
    • Interaction of Alzheimer's β-amyloid peptides with cholesterol: Mechanistic insights into amyloid pore formation
    • C. Di Scala, H. Chahinian, N. Yahi, N. Garmy, J. Fantini, Interaction of Alzheimer's β-amyloid peptides with cholesterol: Mechanistic insights into amyloid pore formation. Biochemistry 53, 4489-4502 (2014).
    • (2014) Biochemistry , vol.53 , pp. 4489-4502
    • Di Scala, C.1    Chahinian, H.2    Yahi, N.3    Garmy, N.4    Fantini, J.5
  • 58
    • 3242877618 scopus 로고    scopus 로고
    • DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • L. Whitmore, B. A. Wallace, DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Res. 32, W668-W673 (2004).
    • (2004) Nucleic Acids Res. , vol.32 , pp. W668-W673
    • Whitmore, L.1    Wallace, B.A.2
  • 59
    • 0036168995 scopus 로고    scopus 로고
    • DICHROWEB: An interactive website for the analysis of protein secondary structure from circular dichroism spectra
    • A. Lobley, L. Whitmore, B. A. Wallace, DICHROWEB: An interactive website for the analysis of protein secondary structure from circular dichroism spectra. Bioinformatics 18, 211-212 (2002).
    • (2002) Bioinformatics , vol.18 , pp. 211-212
    • Lobley, A.1    Whitmore, L.2    Wallace, B.A.3
  • 60
    • 85013071814 scopus 로고    scopus 로고
    • Hybrid in silico/in vitro approaches for the identification of functional cholesterol-binding domains in membrane proteins
    • C. Di Scala, J. Fantini, Hybrid in silico/in vitro approaches for the identification of functional cholesterol-binding domains in membrane proteins. Methods Mol. Biol. 1583, 7-19 (2017).
    • (2017) Methods Mol. Biol. , vol.1583 , pp. 7-19
    • Di Scala, C.1    Fantini, J.2
  • 61
    • 85059702092 scopus 로고    scopus 로고
    • CHARMM-GUI membrane builder for complex biological membrane simulations with glycolipids and lipoglycans
    • J. Lee et al., CHARMM-GUI membrane builder for complex biological membrane simulations with glycolipids and lipoglycans. J. Chem. Theory Comput. 15, 775-786 (2019).
    • (2019) J. Chem. Theory Comput. , vol.15 , pp. 775-786
    • Lee, J.1
  • 62
    • 84903945355 scopus 로고    scopus 로고
    • CHARMM all-atom additive force field for sphingomyelin: Elucidation of hydrogen bonding and of positive curvature
    • R. M. Venable et al., CHARMM all-atom additive force field for sphingomyelin: Elucidation of hydrogen bonding and of positive curvature. Biophys. J. 107, 134-145 (2014).
    • (2014) Biophys. J. , vol.107 , pp. 134-145
    • Venable, R.M.1
  • 63
    • 55349124614 scopus 로고    scopus 로고
    • Additive empirical force field for hexopyranose monosaccharides
    • O. Guvench et al., Additive empirical force field for hexopyranose monosaccharides. J. Comput. Chem. 29, 2543-2564 (2008).
    • (2008) J. Comput. Chem. , vol.29 , pp. 2543-2564
    • Guvench, O.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.