메뉴 건너뛰기




Volumn , Issue , 2015, Pages 1072-1094

Exploiting endocytic pathways to prevent bacterial toxin infection

Author keywords

Bacterial toxins; Clathrin mediated endocytosis (CME); Dynamin; Endocytosis; Membrane trafficking; Small molecule inhibitors

Indexed keywords


EID: 84955515930     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-800188-2.00037-9     Document Type: Chapter
Times cited : (4)

References (130)
  • 1
    • 33750684655 scopus 로고    scopus 로고
    • Bacterial protein toxins and lipids: pore formation or toxin entry into cells
    • Geny B, Popoff MR Bacterial protein toxins and lipids: pore formation or toxin entry into cells. Biol Cell 2006, 98(11):667-678.
    • (2006) Biol Cell , vol.98 , Issue.11 , pp. 667-678
    • Geny, B.1    Popoff, M.R.2
  • 5
    • 79961140522 scopus 로고    scopus 로고
    • Role of the clathrin terminal domain in regulating coated pit dynamics revealed by small molecule inhibition
    • von Kleist L, Stahlschmidt W, Bulut H, Gromova K, Puchkov D, Robertson MJ, et al. Role of the clathrin terminal domain in regulating coated pit dynamics revealed by small molecule inhibition. Cell 2011, 146(3):471-484.
    • (2011) Cell , vol.146 , Issue.3 , pp. 471-484
    • von Kleist, L.1    Stahlschmidt, W.2    Bulut, H.3    Gromova, K.4    Puchkov, D.5    Robertson, M.J.6
  • 6
    • 77950407292 scopus 로고    scopus 로고
    • Endocytosis of the anthrax toxin is mediated by clathrin, actin and unconventional adaptors
    • Abrami L, Bischofberger M, Kunz B, Groux R, van der Goot FG Endocytosis of the anthrax toxin is mediated by clathrin, actin and unconventional adaptors. PLoS Pathog 2010, 6(3):e1000792.
    • (2010) PLoS Pathog , vol.6 , Issue.3 , pp. e1000792
    • Abrami, L.1    Bischofberger, M.2    Kunz, B.3    Groux, R.4    van der Goot, F.G.5
  • 7
    • 84890278211 scopus 로고    scopus 로고
    • Selective inhibitor of endosomal trafficking pathways exploited by multiple toxins and viruses
    • Gillespie EJ, Ho CL, Balaji K, Clemens DL, Deng G, Wang YE, et al. Selective inhibitor of endosomal trafficking pathways exploited by multiple toxins and viruses. Proc Natl Acad Sci USA 2013, 110(50):E4904-E4912.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.50 , pp. E4904-E4912
    • Gillespie, E.J.1    Ho, C.L.2    Balaji, K.3    Clemens, D.L.4    Deng, G.5    Wang, Y.E.6
  • 8
    • 84876549670 scopus 로고    scopus 로고
    • Identification of novel host-targeted compounds that protect from anthrax lethal toxin-induced cell death
    • Slater LH, Hett EC, Mark K, Chumbler NM, Patel D, Lacy DB, et al. Identification of novel host-targeted compounds that protect from anthrax lethal toxin-induced cell death. ACS Chem Biol 2013, 8(4):812-822.
    • (2013) ACS Chem Biol , vol.8 , Issue.4 , pp. 812-822
    • Slater, L.H.1    Hett, E.C.2    Mark, K.3    Chumbler, N.M.4    Patel, D.5    Lacy, D.B.6
  • 9
    • 67650080312 scopus 로고    scopus 로고
    • Quantitative high-throughput screening identifies inhibitors of anthrax-induced cell death
    • Zhu PJ, Hobson JP, Southall N, Qiu C, Thomas CJ, Lu J, et al. Quantitative high-throughput screening identifies inhibitors of anthrax-induced cell death. Bioorg Med Chem 2009, 17(14):5139-5145.
    • (2009) Bioorg Med Chem , vol.17 , Issue.14 , pp. 5139-5145
    • Zhu, P.J.1    Hobson, J.P.2    Southall, N.3    Qiu, C.4    Thomas, C.J.5    Lu, J.6
  • 11
    • 79952032608 scopus 로고    scopus 로고
    • Bacillus sphaericus binary toxin elicits host cell autophagy as a response to intoxication
    • Opota O, Gauthier NC, Doye A, Berry C, Gounon P, Lemichez E, et al. Bacillus sphaericus binary toxin elicits host cell autophagy as a response to intoxication. PloS One 2011, 6(2):e14682.
    • (2011) PloS One , vol.6 , Issue.2 , pp. e14682
    • Opota, O.1    Gauthier, N.C.2    Doye, A.3    Berry, C.4    Gounon, P.5    Lemichez, E.6
  • 12
    • 33646248918 scopus 로고    scopus 로고
    • SV2 is the protein receptor for botulinum neurotoxin A
    • Dong M, Yeh F, Tepp WH, Dean C, Johnson EA, Janz R, et al. SV2 is the protein receptor for botulinum neurotoxin A. Science 2006, 312(5773):592-596.
    • (2006) Science , vol.312 , Issue.5773 , pp. 592-596
    • Dong, M.1    Yeh, F.2    Tepp, W.H.3    Dean, C.4    Johnson, E.A.5    Janz, R.6
  • 13
    • 80053897195 scopus 로고    scopus 로고
    • Dynamin inhibition blocks botulinum neurotoxin type A endocytosis in neurons and delays botulism
    • Harper CB, Martin S, Nguyen TH, Daniels SJ, Lavidis NA, Popoff MR, et al. Dynamin inhibition blocks botulinum neurotoxin type A endocytosis in neurons and delays botulism. J Biol Chem 2011, 286(41):35966-35976.
    • (2011) J Biol Chem , vol.286 , Issue.41 , pp. 35966-35976
    • Harper, C.B.1    Martin, S.2    Nguyen, T.H.3    Daniels, S.J.4    Lavidis, N.A.5    Popoff, M.R.6
  • 14
    • 78650271034 scopus 로고    scopus 로고
    • Endocytosis and toxicity of clostridial binary toxins depend on a clathrin-independent pathway regulated by Rho-GDI
    • Gibert M, Monier MN, Ruez R, Hale ML, Stiles BG, Benmerah A, et al. Endocytosis and toxicity of clostridial binary toxins depend on a clathrin-independent pathway regulated by Rho-GDI. Cell Microbiol 2011, 13(1):154-170.
    • (2011) Cell Microbiol , vol.13 , Issue.1 , pp. 154-170
    • Gibert, M.1    Monier, M.N.2    Ruez, R.3    Hale, M.L.4    Stiles, B.G.5    Benmerah, A.6
  • 15
    • 78449295494 scopus 로고    scopus 로고
    • Clostridium botulinum C2 toxin is internalized by clathrin- and Rho-dependent mechanisms
    • Pust S, Barth H, Sandvig K Clostridium botulinum C2 toxin is internalized by clathrin- and Rho-dependent mechanisms. Cell Microbiol 2010, 12(12):1809-1820.
    • (2010) Cell Microbiol , vol.12 , Issue.12 , pp. 1809-1820
    • Pust, S.1    Barth, H.2    Sandvig, K.3
  • 16
    • 84877139359 scopus 로고    scopus 로고
    • Mycoplasma pneumoniae CARDS toxin is internalized via clathrin-mediated endocytosis
    • Krishnan M, Kannan TR, Baseman JB Mycoplasma pneumoniae CARDS toxin is internalized via clathrin-mediated endocytosis. PloS One 2013, 8(5):e62706.
    • (2013) PloS One , vol.8 , Issue.5 , pp. e62706
    • Krishnan, M.1    Kannan, T.R.2    Baseman, J.B.3
  • 17
    • 0034762332 scopus 로고    scopus 로고
    • Internalization of cholera toxin by different endocytic mechanisms
    • Torgersen ML, Skretting G, van Deurs B, Sandvig K Internalization of cholera toxin by different endocytic mechanisms. J Cell Sci 2001, 114(Pt 20):3737-3747.
    • (2001) J Cell Sci , vol.114 , pp. 3737-3747
    • Torgersen, M.L.1    Skretting, G.2    van Deurs, B.3    Sandvig, K.4
  • 18
    • 3343011405 scopus 로고    scopus 로고
    • Cholera toxin toxicity does not require functional Arf6- and dynamin-dependent endocytic pathways
    • Massol RH, Larsen JE, Fujinaga Y, Lencer WI, Kirchhausen T Cholera toxin toxicity does not require functional Arf6- and dynamin-dependent endocytic pathways. Mol Biol Cell 2004, 15(8):3631-3641.
    • (2004) Mol Biol Cell , vol.15 , Issue.8 , pp. 3631-3641
    • Massol, R.H.1    Larsen, J.E.2    Fujinaga, Y.3    Lencer, W.I.4    Kirchhausen, T.5
  • 19
    • 77955902031 scopus 로고    scopus 로고
    • Clathrin-independent carriers form a high capacity endocytic sorting system at the leading edge of migrating cells
    • Howes MT, Kirkham M, Riches J, Cortese K, Walser PJ, Simpson F, et al. Clathrin-independent carriers form a high capacity endocytic sorting system at the leading edge of migrating cells. J Cell Biol 2010, 190(4):675-691.
    • (2010) J Cell Biol , vol.190 , Issue.4 , pp. 675-691
    • Howes, M.T.1    Kirkham, M.2    Riches, J.3    Cortese, K.4    Walser, P.J.5    Simpson, F.6
  • 20
    • 34548490308 scopus 로고    scopus 로고
    • Identification and characterization of small molecules that inhibit intracellular toxin transport
    • Saenz JB, Doggett TA, Haslam DB Identification and characterization of small molecules that inhibit intracellular toxin transport. Infect Immun 2007, 75(9):4552-4561.
    • (2007) Infect Immun , vol.75 , Issue.9 , pp. 4552-4561
    • Saenz, J.B.1    Doggett, T.A.2    Haslam, D.B.3
  • 21
    • 0034441256 scopus 로고    scopus 로고
    • Cellular internalization of cytolethal distending toxin from Haemophilus ducreyi
    • Cortes-Bratti X, Chaves-Olarte E, Lagergard T, Thelestam M Cellular internalization of cytolethal distending toxin from Haemophilus ducreyi. Infect Immun 2000, 68(12):6903-6911.
    • (2000) Infect Immun , vol.68 , Issue.12 , pp. 6903-6911
    • Cortes-Bratti, X.1    Chaves-Olarte, E.2    Lagergard, T.3    Thelestam, M.4
  • 22
    • 21344473248 scopus 로고    scopus 로고
    • Cellular internalization of cytolethal distending toxin: a new end to a known pathway
    • Guerra L, Teter K, Lilley BN, Stenerlow B, Holmes RK, Ploegh HL, et al. Cellular internalization of cytolethal distending toxin: a new end to a known pathway. Cell Microbiol 2005, 7(7):921-934.
    • (2005) Cell Microbiol , vol.7 , Issue.7 , pp. 921-934
    • Guerra, L.1    Teter, K.2    Lilley, B.N.3    Stenerlow, B.4    Holmes, R.K.5    Ploegh, H.L.6
  • 23
    • 84875187695 scopus 로고    scopus 로고
    • Cellular interactions of the cytolethal distending toxins from Escherichia coli and Haemophilus ducreyi
    • Gargi A, Tamilselvam B, Powers B, Prouty MG, Lincecum T, Eshraghi A, et al. Cellular interactions of the cytolethal distending toxins from Escherichia coli and Haemophilus ducreyi. J Biol Chem 2013, 288(11):7492-7505.
    • (2013) J Biol Chem , vol.288 , Issue.11 , pp. 7492-7505
    • Gargi, A.1    Tamilselvam, B.2    Powers, B.3    Prouty, M.G.4    Lincecum, T.5    Eshraghi, A.6
  • 24
    • 0034108090 scopus 로고    scopus 로고
    • The p21 Rho-activating toxin cytotoxic necrotizing factor 1 is endocytosed by a clathrin-independent mechanism and enters the cytosol by an acidic-dependent membrane translocation step
    • Contamin S, Galmiche A, Doye A, Flatau G, Benmerah A, Boquet P The p21 Rho-activating toxin cytotoxic necrotizing factor 1 is endocytosed by a clathrin-independent mechanism and enters the cytosol by an acidic-dependent membrane translocation step. Mol Biol Cell 2000, 11(5):1775-1787.
    • (2000) Mol Biol Cell , vol.11 , Issue.5 , pp. 1775-1787
    • Contamin, S.1    Galmiche, A.2    Doye, A.3    Flatau, G.4    Benmerah, A.5    Boquet, P.6
  • 25
    • 34548590305 scopus 로고    scopus 로고
    • Intracellular trafficking of Pseudomonas ExoS, a type III cytotoxin
    • Deng Q, Zhang Y, Barbieri JT Intracellular trafficking of Pseudomonas ExoS, a type III cytotoxin. Traffic 2007, 8(10):1331-1345.
    • (2007) Traffic , vol.8 , Issue.10 , pp. 1331-1345
    • Deng, Q.1    Zhang, Y.2    Barbieri, J.T.3
  • 26
    • 33644871336 scopus 로고    scopus 로고
    • Internalized pseudomonas exotoxin A can exploit multiple pathways to reach the endoplasmic reticulum
    • Smith DC, Spooner RA, Watson PD, Murray JL, Hodge TW, Amessou M, et al. Internalized pseudomonas exotoxin A can exploit multiple pathways to reach the endoplasmic reticulum. Traffic 2006, 7(4):379-393.
    • (2006) Traffic , vol.7 , Issue.4 , pp. 379-393
    • Smith, D.C.1    Spooner, R.A.2    Watson, P.D.3    Murray, J.L.4    Hodge, T.W.5    Amessou, M.6
  • 27
    • 34848849474 scopus 로고    scopus 로고
    • Mannheimia haemolytica leukotoxin binds to lipid rafts in bovine lymphoblastoid cells and is internalized in a dynamin-2- and clathrin-dependent manner
    • Atapattu DN, Czuprynski CJ Mannheimia haemolytica leukotoxin binds to lipid rafts in bovine lymphoblastoid cells and is internalized in a dynamin-2- and clathrin-dependent manner. Infect Immun 2007, 75(10):4719-4727.
    • (2007) Infect Immun , vol.75 , Issue.10 , pp. 4719-4727
    • Atapattu, D.N.1    Czuprynski, C.J.2
  • 28
    • 81555197168 scopus 로고    scopus 로고
    • The ins and outs of pertussis toxin
    • Locht C, Coutte L, Mielcarek N The ins and outs of pertussis toxin. FEBS J. 2011, 278(23):4668-4682.
    • (2011) FEBS J. , vol.278 , Issue.23 , pp. 4668-4682
    • Locht, C.1    Coutte, L.2    Mielcarek, N.3
  • 29
    • 34948824901 scopus 로고    scopus 로고
    • Intoxication of epithelial cells by plasmid-encoded toxin requires clathrin-mediated endocytosis
    • Navarro-Garcia F, Canizalez-Roman A, Vidal JE, Salazar MI Intoxication of epithelial cells by plasmid-encoded toxin requires clathrin-mediated endocytosis. Microbiology 2007, 153(Pt 9):2828-2838.
    • (2007) Microbiology , vol.153 , pp. 2828-2838
    • Navarro-Garcia, F.1    Canizalez-Roman, A.2    Vidal, J.E.3    Salazar, M.I.4
  • 30
    • 79953245323 scopus 로고    scopus 로고
    • Arf6-dependent intracellular trafficking of Pasteurella multocida toxin and pH-dependent translocation from late endosomes
    • Repella TL, Ho M, Chong TP, Bannai Y, Wilson BA Arf6-dependent intracellular trafficking of Pasteurella multocida toxin and pH-dependent translocation from late endosomes. Toxins 2011, 3(3):218-241.
    • (2011) Toxins , vol.3 , Issue.3 , pp. 218-241
    • Repella, T.L.1    Ho, M.2    Chong, T.P.3    Bannai, Y.4    Wilson, B.A.5
  • 31
    • 36749032244 scopus 로고    scopus 로고
    • Shiga toxin induces tubular membrane invaginations for its uptake into cells
    • Romer W, Berland L, Chambon V, Gaus K, Windschiegl B, Tenza D, et al. Shiga toxin induces tubular membrane invaginations for its uptake into cells. Nature 2007, 450(7170):670-675.
    • (2007) Nature , vol.450 , Issue.7170 , pp. 670-675
    • Romer, W.1    Berland, L.2    Chambon, V.3    Gaus, K.4    Windschiegl, B.5    Tenza, D.6
  • 32
    • 77049128273 scopus 로고    scopus 로고
    • Actin dynamics drive membrane reorganization and scission in clathrin-independent endocytosis
    • Romer W, Pontani LL, Sorre B, Rentero C, Berland L, Chambon V, et al. Actin dynamics drive membrane reorganization and scission in clathrin-independent endocytosis. Cell 2010, 140(4):540-553.
    • (2010) Cell , vol.140 , Issue.4 , pp. 540-553
    • Romer, W.1    Pontani, L.L.2    Sorre, B.3    Rentero, C.4    Berland, L.5    Chambon, V.6
  • 33
    • 75749125021 scopus 로고    scopus 로고
    • Shiga toxins--from cell biology to biomedical applications
    • Johannes L, Romer W Shiga toxins--from cell biology to biomedical applications. Nat Rev Microbiol 2010, 8(2):105-116.
    • (2010) Nat Rev Microbiol , vol.8 , Issue.2 , pp. 105-116
    • Johannes, L.1    Romer, W.2
  • 34
    • 77951735286 scopus 로고    scopus 로고
    • Inhibition of retrograde transport protects mice from lethal ricin challenge
    • Stechmann B, Bai SK, Gobbo E, Lopez R, Merer G, Pinchard S, et al. Inhibition of retrograde transport protects mice from lethal ricin challenge. Cell 2010, 141(2):231-242.
    • (2010) Cell , vol.141 , Issue.2 , pp. 231-242
    • Stechmann, B.1    Bai, S.K.2    Gobbo, E.3    Lopez, R.4    Merer, G.5    Pinchard, S.6
  • 35
    • 84856074275 scopus 로고    scopus 로고
    • Manganese blocks intracellular trafficking of Shiga toxin and protects against Shiga toxicosis
    • Mukhopadhyay S, Linstedt AD Manganese blocks intracellular trafficking of Shiga toxin and protects against Shiga toxicosis. Science 2012, 335(6066):332-335.
    • (2012) Science , vol.335 , Issue.6066 , pp. 332-335
    • Mukhopadhyay, S.1    Linstedt, A.D.2
  • 36
    • 84881044294 scopus 로고    scopus 로고
    • Shiga toxin-binding site for host cell receptor GPP130 reveals unexpected divergence in toxin-trafficking mechanisms
    • Mukhopadhyay S, Redler B, Linstedt AD Shiga toxin-binding site for host cell receptor GPP130 reveals unexpected divergence in toxin-trafficking mechanisms. Mol Biol Cell 2013, 24(15):2311-2318.
    • (2013) Mol Biol Cell , vol.24 , Issue.15 , pp. 2311-2318
    • Mukhopadhyay, S.1    Redler, B.2    Linstedt, A.D.3
  • 37
    • 33746618384 scopus 로고    scopus 로고
    • Tetanus toxin is internalized by a sequential clathrin-dependent mechanism initiated within lipid microdomains and independent of epsin1
    • Deinhardt K, Berninghausen O, Willison HJ, Hopkins CR, Schiavo G Tetanus toxin is internalized by a sequential clathrin-dependent mechanism initiated within lipid microdomains and independent of epsin1. J Cell Biol 2006, 174(3):459-471.
    • (2006) J Cell Biol , vol.174 , Issue.3 , pp. 459-471
    • Deinhardt, K.1    Berninghausen, O.2    Willison, H.J.3    Hopkins, C.R.4    Schiavo, G.5
  • 38
    • 84861169060 scopus 로고    scopus 로고
    • Tetanus toxin and botulinum toxin a utilize unique mechanisms to enter neurons of the central nervous system
    • Blum FC, Chen C, Kroken AR, Barbieri JT Tetanus toxin and botulinum toxin a utilize unique mechanisms to enter neurons of the central nervous system. Infect Immun 2012, 80(5):1662-1669.
    • (2012) Infect Immun , vol.80 , Issue.5 , pp. 1662-1669
    • Blum, F.C.1    Chen, C.2    Kroken, A.R.3    Barbieri, J.T.4
  • 39
    • 79251482759 scopus 로고    scopus 로고
    • SV2 mediates entry of tetanus neurotoxin into central neurons
    • Yeh FL, Dong M, Yao J, Tepp WH, Lin G, Johnson EA, et al. SV2 mediates entry of tetanus neurotoxin into central neurons. PLoS Pathog 2010, 6(11):e1001207.
    • (2010) PLoS Pathog , vol.6 , Issue.11 , pp. e1001207
    • Yeh, F.L.1    Dong, M.2    Yao, J.3    Tepp, W.H.4    Lin, G.5    Johnson, E.A.6
  • 40
    • 26244459823 scopus 로고    scopus 로고
    • Helicobacter pylori VacA cytotoxin: a probe for a clathrin-independent and Cdc42-dependent pinocytic pathway routed to late endosomes
    • Gauthier NC, Monzo P, Kaddai V, Doye A, Ricci V, Boquet P Helicobacter pylori VacA cytotoxin: a probe for a clathrin-independent and Cdc42-dependent pinocytic pathway routed to late endosomes. Mol Biol Cell 2005, 16(10):4852-4866.
    • (2005) Mol Biol Cell , vol.16 , Issue.10 , pp. 4852-4866
    • Gauthier, N.C.1    Monzo, P.2    Kaddai, V.3    Doye, A.4    Ricci, V.5    Boquet, P.6
  • 42
    • 0031031848 scopus 로고    scopus 로고
    • Membrane translocation of diphtheria toxin fragment A exploits early to late endosome trafficking machinery
    • Lemichez E, Bomsel M, Devilliers G, vanderSpek J, Murphy JR, Lukianov EV, et al. Membrane translocation of diphtheria toxin fragment A exploits early to late endosome trafficking machinery. Mol Microbiol 1997, 23(3):445-457.
    • (1997) Mol Microbiol , vol.23 , Issue.3 , pp. 445-457
    • Lemichez, E.1    Bomsel, M.2    Devilliers, G.3    vanderSpek, J.4    Murphy, J.R.5    Lukianov, E.V.6
  • 43
    • 0037415611 scopus 로고    scopus 로고
    • Anthrax toxin triggers endocytosis of its receptor via a lipid raft-mediated clathrin-dependent process
    • Abrami L, Liu S, Cosson P, Leppla SH, van der Goot FG Anthrax toxin triggers endocytosis of its receptor via a lipid raft-mediated clathrin-dependent process. J Cell Biol 2003, 160(3):321-328.
    • (2003) J Cell Biol , vol.160 , Issue.3 , pp. 321-328
    • Abrami, L.1    Liu, S.2    Cosson, P.3    Leppla, S.H.4    van der Goot, F.G.5
  • 44
    • 4744354687 scopus 로고    scopus 로고
    • Effects of dynamin inactivation on pathways of anthrax toxin uptake
    • Boll W, Ehrlich M, Collier RJ, Kirchhausen T Effects of dynamin inactivation on pathways of anthrax toxin uptake. Eur J Cell Biol 2004, 83(6):281-288.
    • (2004) Eur J Cell Biol , vol.83 , Issue.6 , pp. 281-288
    • Boll, W.1    Ehrlich, M.2    Collier, R.J.3    Kirchhausen, T.4
  • 45
    • 76549104967 scopus 로고    scopus 로고
    • Anthrax toxin triggers the activation of src-like kinases to mediate its own uptake
    • Abrami L, Kunz B, van der Goot FG Anthrax toxin triggers the activation of src-like kinases to mediate its own uptake. Proc Natl Acad Sci USA 2010, 107(4):1420-1424.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.4 , pp. 1420-1424
    • Abrami, L.1    Kunz, B.2    van der Goot, F.G.3
  • 46
    • 0034789465 scopus 로고    scopus 로고
    • Elevated endosomal pH in HeLa cells overexpressing mutant dynamin can affect infection by pH-sensitive viruses
    • Huber M, Brabec M, Bayer N, Blaas D, Fuchs R Elevated endosomal pH in HeLa cells overexpressing mutant dynamin can affect infection by pH-sensitive viruses. Traffic 2001, 2(10):727-736.
    • (2001) Traffic , vol.2 , Issue.10 , pp. 727-736
    • Huber, M.1    Brabec, M.2    Bayer, N.3    Blaas, D.4    Fuchs, R.5
  • 47
    • 0028057494 scopus 로고
    • Ultrastructural localization of gangliosides; GM1 is concentrated in caveolae
    • Parton RG Ultrastructural localization of gangliosides; GM1 is concentrated in caveolae. J Histochem Cytochem 1994, 42(2):155-166.
    • (1994) J Histochem Cytochem , vol.42 , Issue.2 , pp. 155-166
    • Parton, R.G.1
  • 48
    • 0023449563 scopus 로고
    • Ligands internalized through coated or noncoated invaginations follow a common intracellular pathway
    • Tran D, Carpentier JL, Sawano F, Gorden P, Orci L Ligands internalized through coated or noncoated invaginations follow a common intracellular pathway. Proc Natl Acad Sci USA 1987, 84(22):7957-7961.
    • (1987) Proc Natl Acad Sci USA , vol.84 , Issue.22 , pp. 7957-7961
    • Tran, D.1    Carpentier, J.L.2    Sawano, F.3    Gorden, P.4    Orci, L.5
  • 49
    • 0031750101 scopus 로고    scopus 로고
    • Filipin-dependent inhibition of cholera toxin: evidence for toxin internalization and activation through caveolae-like domains
    • Orlandi PA, Fishman PH Filipin-dependent inhibition of cholera toxin: evidence for toxin internalization and activation through caveolae-like domains. J Cell Biol 1998, 141(4):905-915.
    • (1998) J Cell Biol , vol.141 , Issue.4 , pp. 905-915
    • Orlandi, P.A.1    Fishman, P.H.2
  • 50
    • 0037013269 scopus 로고    scopus 로고
    • Uncoupling of the cholera toxin-G(M1) ganglioside receptor complex from endocytosis, retrograde Golgi trafficking, and downstream signal transduction by depletion of membrane cholesterol
    • Wolf AA, Fujinaga Y, Lencer WI Uncoupling of the cholera toxin-G(M1) ganglioside receptor complex from endocytosis, retrograde Golgi trafficking, and downstream signal transduction by depletion of membrane cholesterol. J Biol Chem 2002, 277(18):16249-16256.
    • (2002) J Biol Chem , vol.277 , Issue.18 , pp. 16249-16256
    • Wolf, A.A.1    Fujinaga, Y.2    Lencer, W.I.3
  • 51
    • 38149080449 scopus 로고    scopus 로고
    • Distinct role of clathrin-mediated endocytosis in the functional uptake of cholera toxin
    • Broeck DV, Lagrou AR, De Wolf MJ Distinct role of clathrin-mediated endocytosis in the functional uptake of cholera toxin. Acta Biochim Pol 2007, 54(4):757-767.
    • (2007) Acta Biochim Pol , vol.54 , Issue.4 , pp. 757-767
    • Broeck, D.V.1    Lagrou, A.R.2    De Wolf, M.J.3
  • 52
    • 0035937752 scopus 로고    scopus 로고
    • Cholera toxin is found in detergent-insoluble rafts/domains at the cell surface of hippocampal neurons but is internalized via a raft-independent mechanism
    • Shogomori H, Futerman AH Cholera toxin is found in detergent-insoluble rafts/domains at the cell surface of hippocampal neurons but is internalized via a raft-independent mechanism. J Biol Chem 2001, 276(12):9182-9188.
    • (2001) J Biol Chem , vol.276 , Issue.12 , pp. 9182-9188
    • Shogomori, H.1    Futerman, A.H.2
  • 53
    • 84859264679 scopus 로고    scopus 로고
    • Intoxication strategy of Helicobacter pylori VacA toxin
    • Boquet P, Ricci V Intoxication strategy of Helicobacter pylori VacA toxin. Trends Microbiol 2012, 20(4):165-174.
    • (2012) Trends Microbiol , vol.20 , Issue.4 , pp. 165-174
    • Boquet, P.1    Ricci, V.2
  • 55
    • 58549094719 scopus 로고    scopus 로고
    • Glycosylated SV2A and SV2B mediate the entry of botulinum neurotoxin E into neurons
    • Dong M, Liu H, Tepp WH, Johnson EA, Janz R, Chapman ER Glycosylated SV2A and SV2B mediate the entry of botulinum neurotoxin E into neurons. Mol Biol Cell 2008, 19(12):5226-5237.
    • (2008) Mol Biol Cell , vol.19 , Issue.12 , pp. 5226-5237
    • Dong, M.1    Liu, H.2    Tepp, W.H.3    Johnson, E.A.4    Janz, R.5    Chapman, E.R.6
  • 56
    • 69949182315 scopus 로고    scopus 로고
    • Botulinum neurotoxins C, E and F bind gangliosides via a conserved binding site prior to stimulation-dependent uptake with botulinum neurotoxin F utilising the three isoforms of SV2 as second receptor
    • Rummel A, Hafner K, Mahrhold S, Darashchonak N, Holt M, Jahn R, et al. Botulinum neurotoxins C, E and F bind gangliosides via a conserved binding site prior to stimulation-dependent uptake with botulinum neurotoxin F utilising the three isoforms of SV2 as second receptor. J Neurochem 2009, 110(6):1942-1954.
    • (2009) J Neurochem , vol.110 , Issue.6 , pp. 1942-1954
    • Rummel, A.1    Hafner, K.2    Mahrhold, S.3    Darashchonak, N.4    Holt, M.5    Jahn, R.6
  • 57
    • 67649210455 scopus 로고    scopus 로고
    • Glycosylated SV2 and gangliosides as dual receptors for botulinum neurotoxin serotype F
    • Fu Z, Chen C, Barbieri JT, Kim JJ, Baldwin MR Glycosylated SV2 and gangliosides as dual receptors for botulinum neurotoxin serotype F. Biochemistry 2009, 48(24):5631-5641.
    • (2009) Biochemistry , vol.48 , Issue.24 , pp. 5631-5641
    • Fu, Z.1    Chen, C.2    Barbieri, J.T.3    Kim, J.J.4    Baldwin, M.R.5
  • 58
    • 79953289881 scopus 로고    scopus 로고
    • Botulinum neurotoxin D uses synaptic vesicle protein SV2 and gangliosides as receptors
    • Peng L, Tepp WH, Johnson EA, Dong M Botulinum neurotoxin D uses synaptic vesicle protein SV2 and gangliosides as receptors. PLoS Pathog 2011, 7(3):e1002008.
    • (2011) PLoS Pathog , vol.7 , Issue.3 , pp. e1002008
    • Peng, L.1    Tepp, W.H.2    Johnson, E.A.3    Dong, M.4
  • 59
    • 0028341442 scopus 로고
    • Identification of protein receptor for Clostridium botulinum type B neurotoxin in rat brain synaptosomes
    • Nishiki T, Kamata Y, Nemoto Y, Omori A, Ito T, Takahashi M, et al. Identification of protein receptor for Clostridium botulinum type B neurotoxin in rat brain synaptosomes. J Biol Chem 1994, 269(14):10498-10503.
    • (1994) J Biol Chem , vol.269 , Issue.14 , pp. 10498-10503
    • Nishiki, T.1    Kamata, Y.2    Nemoto, Y.3    Omori, A.4    Ito, T.5    Takahashi, M.6
  • 60
    • 0030064241 scopus 로고    scopus 로고
    • The high-affinity binding of Clostridium botulinum type B neurotoxin to synaptotagmin II associated with gangliosides GT1b/GD1a
    • Nishiki T, Tokuyama Y, Kamata Y, Nemoto Y, Yoshida A, Sato K, et al. The high-affinity binding of Clostridium botulinum type B neurotoxin to synaptotagmin II associated with gangliosides GT1b/GD1a. FEBS Lett 1996, 378(3):253-257.
    • (1996) FEBS Lett , vol.378 , Issue.3 , pp. 253-257
    • Nishiki, T.1    Tokuyama, Y.2    Kamata, Y.3    Nemoto, Y.4    Yoshida, A.5    Sato, K.6
  • 62
    • 3142735021 scopus 로고    scopus 로고
    • Synaptotagmins I and II act as nerve cell receptors for botulinum neurotoxin G
    • Rummel A, Karnath T, Henke T, Bigalke H, Binz T Synaptotagmins I and II act as nerve cell receptors for botulinum neurotoxin G. J Biol Chem 2004, 279(29):30865-30870.
    • (2004) J Biol Chem , vol.279 , Issue.29 , pp. 30865-30870
    • Rummel, A.1    Karnath, T.2    Henke, T.3    Bigalke, H.4    Binz, T.5
  • 63
    • 38049036925 scopus 로고    scopus 로고
    • Mechanism of botulinum neurotoxin B and G entry into hippocampal neurons
    • Dong M, Tepp WH, Liu H, Johnson EA, Chapman ER Mechanism of botulinum neurotoxin B and G entry into hippocampal neurons. J Cell Biol 2007, 179(7):1511-1522.
    • (2007) J Cell Biol , vol.179 , Issue.7 , pp. 1511-1522
    • Dong, M.1    Tepp, W.H.2    Liu, H.3    Johnson, E.A.4    Chapman, E.R.5
  • 64
    • 84875809331 scopus 로고    scopus 로고
    • Double receptor anchorage of botulinum neurotoxins accounts for their exquisite neurospecificity
    • Rummel A Double receptor anchorage of botulinum neurotoxins accounts for their exquisite neurospecificity. Curr Top Microbiol Immunol 2013, 364:61-90.
    • (2013) Curr Top Microbiol Immunol , vol.364 , pp. 61-90
    • Rummel, A.1
  • 65
    • 79959549721 scopus 로고    scopus 로고
    • The biological activity of botulinum neurotoxin type C is dependent upon novel types of ganglioside binding sites
    • Strotmeier J, Gu S, Jutzi S, Mahrhold S, Zhou J, Pich A, et al. The biological activity of botulinum neurotoxin type C is dependent upon novel types of ganglioside binding sites. Mol Microbiol 2011, 81(1):143-156.
    • (2011) Mol Microbiol , vol.81 , Issue.1 , pp. 143-156
    • Strotmeier, J.1    Gu, S.2    Jutzi, S.3    Mahrhold, S.4    Zhou, J.5    Pich, A.6
  • 66
    • 84870028543 scopus 로고    scopus 로고
    • Botulinum neurotoxin serotype C associates with dual ganglioside receptors to facilitate cell entry
    • Karalewitz AP, Fu Z, Baldwin MR, Kim JJ, Barbieri JT Botulinum neurotoxin serotype C associates with dual ganglioside receptors to facilitate cell entry. J Biol Chem 2012, 287(48):40806-40816.
    • (2012) J Biol Chem , vol.287 , Issue.48 , pp. 40806-40816
    • Karalewitz, A.P.1    Fu, Z.2    Baldwin, M.R.3    Kim, J.J.4    Barbieri, J.T.5
  • 67
    • 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
    • Peng L, Berntsson RP, Tepp WH, Pitkin RM, Johnson EA, Stenmark P, 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 2012, 125(Pt 13):3233-3242.
    • (2012) J Cell Sci , vol.125 , pp. 3233-3242
    • Peng, L.1    Berntsson, R.P.2    Tepp, W.H.3    Pitkin, R.M.4    Johnson, E.A.5    Stenmark, P.6
  • 68
    • 84904510042 scopus 로고    scopus 로고
    • Botulinum neurotoxins: genetic, structural and mechanistic insights
    • Rossetto O, Pirazzini M, Montecucco C Botulinum neurotoxins: genetic, structural and mechanistic insights. Nat Rev Microbiol 2014, 12(8):535-549.
    • (2014) Nat Rev Microbiol , vol.12 , Issue.8 , pp. 535-549
    • Rossetto, O.1    Pirazzini, M.2    Montecucco, C.3
  • 69
    • 85054456557 scopus 로고    scopus 로고
    • Thioredoxin and its reductase are present on synaptic vesicles, and their inhibition prevents the paralysis induced by botulinum neurotoxins
    • press
    • Pirazzini M, Tehran DA, Zanetti G,Megighian A, Scorzeto M, Fillo S, et al. Thioredoxin and its reductase are present on synaptic vesicles, and their inhibition prevents the paralysis induced by botulinum neurotoxins. Cell Rep. in press.
    • Cell Rep.
    • Pirazzini, M.1    Tehran, D.A.2    Zanetti, G.3    Megighian, A.4    Scorzeto, M.5    Fillo, S.6
  • 70
    • 34848840291 scopus 로고    scopus 로고
    • Botulinum neurotoxin heavy chain belt as an intramolecular chaperone for the light chain
    • Brunger AT, Breidenbach MA, Jin R, Fischer A, Santos JS, Montal M Botulinum neurotoxin heavy chain belt as an intramolecular chaperone for the light chain. PLoS Pathog 2007, 3(9):1191-1194.
    • (2007) PLoS Pathog , vol.3 , Issue.9 , pp. 1191-1194
    • Brunger, A.T.1    Breidenbach, M.A.2    Jin, R.3    Fischer, A.4    Santos, J.S.5    Montal, M.6
  • 71
    • 0037222077 scopus 로고    scopus 로고
    • Translocation of botulinum neurotoxin light chain protease through the heavy chain channel
    • Koriazova LK, Montal M Translocation of botulinum neurotoxin light chain protease through the heavy chain channel. Nat Struct Biol 2003, 10(1):13-18.
    • (2003) Nat Struct Biol , vol.10 , Issue.1 , pp. 13-18
    • Koriazova, L.K.1    Montal, M.2
  • 72
    • 84891554851 scopus 로고    scopus 로고
    • Molecular characterization of a novel botulinum neurotoxin type H gene
    • Dover N, Barash JR, Hill KK, Xie G, Arnon SS Molecular characterization of a novel botulinum neurotoxin type H gene. J Infect Dis 2014, 209(2):192-202.
    • (2014) J Infect Dis , vol.209 , Issue.2 , pp. 192-202
    • Dover, N.1    Barash, J.R.2    Hill, K.K.3    Xie, G.4    Arnon, S.S.5
  • 73
    • 84891543590 scopus 로고    scopus 로고
    • A novel strain of Clostridium botulinum that produces type B and type H botulinum toxins
    • Barash JR, Arnon SS A novel strain of Clostridium botulinum that produces type B and type H botulinum toxins. J Infect Dis 2014, 209(2):183-191.
    • (2014) J Infect Dis , vol.209 , Issue.2 , pp. 183-191
    • Barash, J.R.1    Arnon, S.S.2
  • 74
    • 33845188467 scopus 로고    scopus 로고
    • Inhibition of dynamin completely blocks compensatory synaptic vesicle endocytosis
    • Newton AJ, Kirchhausen T, Murthy VN Inhibition of dynamin completely blocks compensatory synaptic vesicle endocytosis. Proc Natl Acad Sci USA 2006, 103(47):17955-17960.
    • (2006) Proc Natl Acad Sci USA , vol.103 , Issue.47 , pp. 17955-17960
    • Newton, A.J.1    Kirchhausen, T.2    Murthy, V.N.3
  • 75
    • 79959316429 scopus 로고    scopus 로고
    • Overlapping role of dynamin isoforms in synaptic vesicle endocytosis
    • Raimondi A, Ferguson SM, Lou X, Armbruster M, Paradise S, Giovedi S, et al. Overlapping role of dynamin isoforms in synaptic vesicle endocytosis. Neuron 2011, 70(6):1100-1114.
    • (2011) Neuron , vol.70 , Issue.6 , pp. 1100-1114
    • Raimondi, A.1    Ferguson, S.M.2    Lou, X.3    Armbruster, M.4    Paradise, S.5    Giovedi, S.6
  • 76
    • 0029847230 scopus 로고    scopus 로고
    • Synaptic vesicle endocytosis mediates the entry of tetanus neurotoxin into hippocampal neurons
    • Matteoli M, Verderio C, Rossetto O, Iezzi N, Coco S, Schiavo G, et al. Synaptic vesicle endocytosis mediates the entry of tetanus neurotoxin into hippocampal neurons. Proc Natl Acad Sci USA 1996, 93(23):13310-13315.
    • (1996) Proc Natl Acad Sci USA , vol.93 , Issue.23 , pp. 13310-13315
    • Matteoli, M.1    Verderio, C.2    Rossetto, O.3    Iezzi, N.4    Coco, S.5    Schiavo, G.6
  • 77
    • 29644438627 scopus 로고    scopus 로고
    • Tetanus toxin is transported in a novel neuronal compartment characterized by a specialized pH regulation
    • Bohnert S, Schiavo G Tetanus toxin is transported in a novel neuronal compartment characterized by a specialized pH regulation. J Biol Chem. 2005, 280(51):42336-42344.
    • (2005) J Biol Chem. , vol.280 , Issue.51 , pp. 42336-42344
    • Bohnert, S.1    Schiavo, G.2
  • 78
    • 84864309597 scopus 로고    scopus 로고
    • Listeriolysin O: the Swiss army knife of Listeria
    • Hamon MA, Ribet D, Stavru F, Cossart P Listeriolysin O: the Swiss army knife of Listeria. Trend Microbiol 2012, 20(8):360-368.
    • (2012) Trend Microbiol , vol.20 , Issue.8 , pp. 360-368
    • Hamon, M.A.1    Ribet, D.2    Stavru, F.3    Cossart, P.4
  • 79
    • 84875620662 scopus 로고    scopus 로고
    • A syringe-like injection mechanism in Photorhabdus luminescens toxins
    • Gatsogiannis C, Lang AE, Meusch D, Pfaumann V, Hofnagel O, Benz R, et al. A syringe-like injection mechanism in Photorhabdus luminescens toxins. Nature 2013, 495(7442):520-523.
    • (2013) Nature , vol.495 , Issue.7442 , pp. 520-523
    • Gatsogiannis, C.1    Lang, A.E.2    Meusch, D.3    Pfaumann, V.4    Hofnagel, O.5    Benz, R.6
  • 81
    • 79951510199 scopus 로고    scopus 로고
    • Cell type-dependent internalization of the Escherichia coli STb enterotoxin
    • Albert MA, Kojic LD, Nabi IR, Dubreuil JD Cell type-dependent internalization of the Escherichia coli STb enterotoxin. FEMS Immunol Med Microbiol 2011, 61(2):205-217.
    • (2011) FEMS Immunol Med Microbiol , vol.61 , Issue.2 , pp. 205-217
    • Albert, M.A.1    Kojic, L.D.2    Nabi, I.R.3    Dubreuil, J.D.4
  • 82
    • 84867033127 scopus 로고    scopus 로고
    • Oligomerization of Clostridium perfringens epsilon toxin is dependent upon caveolins 1 and 2
    • Fennessey CM, Sheng J, Rubin DH, McClain MS Oligomerization of Clostridium perfringens epsilon toxin is dependent upon caveolins 1 and 2. PloS One 2012, 7(10):e46866.
    • (2012) PloS One , vol.7 , Issue.10 , pp. e46866
    • Fennessey, C.M.1    Sheng, J.2    Rubin, D.H.3    McClain, M.S.4
  • 83
    • 84888183395 scopus 로고    scopus 로고
    • Clostridium perfringens epsilon toxin: a malevolent molecule for animals and man?
    • Stiles BG, Barth G, Barth H, Popoff MR Clostridium perfringens epsilon toxin: a malevolent molecule for animals and man?. Toxins (Basel) 2013, 5(11):2138-2160.
    • (2013) Toxins (Basel) , vol.5 , Issue.11 , pp. 2138-2160
    • Stiles, B.G.1    Barth, G.2    Barth, H.3    Popoff, M.R.4
  • 84
    • 2442614797 scopus 로고    scopus 로고
    • Long chain amines and long chain ammonium salts as novel inhibitors of dynamin GTPase activity
    • Hill TA, Odell LR, Quan A, Abagyan R, Ferguson G, Robinson PJ, et al. Long chain amines and long chain ammonium salts as novel inhibitors of dynamin GTPase activity. Bioorg Med Chem Lett 2004, 14(12):3275-3278.
    • (2004) Bioorg Med Chem Lett , vol.14 , Issue.12 , pp. 3275-3278
    • Hill, T.A.1    Odell, L.R.2    Quan, A.3    Abagyan, R.4    Ferguson, G.5    Robinson, P.J.6
  • 85
    • 28144443754 scopus 로고    scopus 로고
    • Small molecule inhibitors of dynamin I GTPase activity: development of dimeric tyrphostins
    • Hill T, Odell LR, Edwards JK, Graham ME, McGeachie AB, Rusak J, et al. Small molecule inhibitors of dynamin I GTPase activity: development of dimeric tyrphostins. J Med Chem 2005, 48(24):7781-7788.
    • (2005) J Med Chem , vol.48 , Issue.24 , pp. 7781-7788
    • Hill, T.1    Odell, L.R.2    Edwards, J.K.3    Graham, M.E.4    McGeachie, A.B.5    Rusak, J.6
  • 87
    • 36348985073 scopus 로고    scopus 로고
    • Myristyl trimethyl ammonium bromide and octadecyl trimethyl ammonium bromide are surface-active small molecule dynamin inhibitors that block endocytosis mediated by dynamin I or dynamin II
    • Quan A, McGeachie AB, Keating DJ, van Dam EM, Rusak J, Chau N, et al. Myristyl trimethyl ammonium bromide and octadecyl trimethyl ammonium bromide are surface-active small molecule dynamin inhibitors that block endocytosis mediated by dynamin I or dynamin II. Mol Pharmacol 2007, 72(6):1425-1439.
    • (2007) Mol Pharmacol , vol.72 , Issue.6 , pp. 1425-1439
    • Quan, A.1    McGeachie, A.B.2    Keating, D.J.3    van Dam, E.M.4    Rusak, J.5    Chau, N.6
  • 88
    • 67549119243 scopus 로고    scopus 로고
    • Inhibition of dynamin mediated endocytosis by the dynoles--synthesis and functional activity of a family of indoles
    • Hill TA, Gordon CP, McGeachie AB, Venn-Brown B, Odell LR, Chau N, et al. Inhibition of dynamin mediated endocytosis by the dynoles--synthesis and functional activity of a family of indoles. J Med Chem 2009, 52(12):3762-3773.
    • (2009) J Med Chem , vol.52 , Issue.12 , pp. 3762-3773
    • Hill, T.A.1    Gordon, C.P.2    McGeachie, A.B.3    Venn-Brown, B.4    Odell, L.R.5    Chau, N.6
  • 90
    • 77954578662 scopus 로고    scopus 로고
    • The dynamin inhibitors MiTMAB and OcTMAB induce cytokinesis failure and inhibit cell proliferation in human cancer cells
    • Joshi S, Perera S, Gilbert J, Smith CM, Mariana A, Gordon CP, et al. The dynamin inhibitors MiTMAB and OcTMAB induce cytokinesis failure and inhibit cell proliferation in human cancer cells. Mol Cancer Ther 2010, 9(7):1995-2006.
    • (2010) Mol Cancer Ther , vol.9 , Issue.7 , pp. 1995-2006
    • Joshi, S.1    Perera, S.2    Gilbert, J.3    Smith, C.M.4    Mariana, A.5    Gordon, C.P.6
  • 91
    • 77954701884 scopus 로고    scopus 로고
    • The pthaladyns: GTP competitive inhibitors of dynamin I and II GTPase derived from virtual screening
    • Odell LR, Howan D, Gordon CP, Robertson MJ, Chau N, Mariana A, et al. The pthaladyns: GTP competitive inhibitors of dynamin I and II GTPase derived from virtual screening. J Med Chem 2010, 53(14):5267-5280.
    • (2010) J Med Chem , vol.53 , Issue.14 , pp. 5267-5280
    • Odell, L.R.1    Howan, D.2    Gordon, C.P.3    Robertson, M.J.4    Chau, N.5    Mariana, A.6
  • 92
    • 80052710376 scopus 로고    scopus 로고
    • Inhibition of dynamin by dynole 34-2 induces cell death following cytokinesis failure in cancer cells
    • Chircop M, Perera S, Mariana A, Lau H, Ma MP, Gilbert J, et al. Inhibition of dynamin by dynole 34-2 induces cell death following cytokinesis failure in cancer cells. Mol Cancer Ther 2011, 10(9):1553-1562.
    • (2011) Mol Cancer Ther , vol.10 , Issue.9 , pp. 1553-1562
    • Chircop, M.1    Perera, S.2    Mariana, A.3    Lau, H.4    Ma, M.P.5    Gilbert, J.6
  • 93
    • 84864463813 scopus 로고    scopus 로고
    • Analysis of synaptic vesicle endocytosis in synaptosomes by high-content screening
    • Daniel JA, Malladi CS, Kettle E, McCluskey A, Robinson PJ Analysis of synaptic vesicle endocytosis in synaptosomes by high-content screening. Nat Protoc 2012, 7(8):1439-1455.
    • (2012) Nat Protoc , vol.7 , Issue.8 , pp. 1439-1455
    • Daniel, J.A.1    Malladi, C.S.2    Kettle, E.3    McCluskey, A.4    Robinson, P.J.5
  • 94
    • 84861083216 scopus 로고    scopus 로고
    • The Rhodadyns, a New Class of Small Molecule Inhibitors of Dynamin GTPase Activity
    • Robertson MJ, Hadzic G, Ambrus J, Pome DY, Hyde E, Whiting A, et al. The Rhodadyns, a New Class of Small Molecule Inhibitors of Dynamin GTPase Activity. ACS Med Chem Lett 2012, 3(5):352-356.
    • (2012) ACS Med Chem Lett , vol.3 , Issue.5 , pp. 352-356
    • Robertson, M.J.1    Hadzic, G.2    Ambrus, J.3    Pome, D.Y.4    Hyde, E.5    Whiting, A.6
  • 95
    • 84887610283 scopus 로고    scopus 로고
    • Building a better dynasore: the dyngo compounds potently inhibit dynamin and endocytosis
    • McCluskey A, Daniel JA, Hadzic G, Chau N, Clayton EL, Mariana A, et al. Building a better dynasore: the dyngo compounds potently inhibit dynamin and endocytosis. Traffic 2013, 14(12):1272-1289.
    • (2013) Traffic , vol.14 , Issue.12 , pp. 1272-1289
    • McCluskey, A.1    Daniel, J.A.2    Hadzic, G.3    Chau, N.4    Clayton, E.L.5    Mariana, A.6
  • 96
    • 84880557627 scopus 로고    scopus 로고
    • Pyrimidyn compounds: dual-action small molecule pyrimidine-based dynamin inhibitors
    • McGeachie AB, Odell LR, Quan A, Daniel JA, Chau N, Hill TA, et al. Pyrimidyn compounds: dual-action small molecule pyrimidine-based dynamin inhibitors. ACS Chem Biol 2013, 8(7):1507-1518.
    • (2013) ACS Chem Biol , vol.8 , Issue.7 , pp. 1507-1518
    • McGeachie, A.B.1    Odell, L.R.2    Quan, A.3    Daniel, J.A.4    Chau, N.5    Hill, T.A.6
  • 97
    • 84897136241 scopus 로고    scopus 로고
    • Synthesis of Dynole 34-2, Dynole 2-24 and Dyngo 4a for investigating dynamin GTPase
    • Robertson MJ, Deane FM, Robinson PJ, McCluskey A Synthesis of Dynole 34-2, Dynole 2-24 and Dyngo 4a for investigating dynamin GTPase. Nat Protoc 2014, 9(4):851-870.
    • (2014) Nat Protoc , vol.9 , Issue.4 , pp. 851-870
    • Robertson, M.J.1    Deane, F.M.2    Robinson, P.J.3    McCluskey, A.4
  • 99
    • 78650267415 scopus 로고    scopus 로고
    • HIV-1 infects macrophages by exploiting an endocytic route dependent on dynamin, Rac1 and Pak1
    • Carter GC, Bernstone L, Baskaran D, James W HIV-1 infects macrophages by exploiting an endocytic route dependent on dynamin, Rac1 and Pak1. Virology 2011, 409(2):234-250.
    • (2011) Virology , vol.409 , Issue.2 , pp. 234-250
    • Carter, G.C.1    Bernstone, L.2    Baskaran, D.3    James, W.4
  • 100
    • 65249139458 scopus 로고    scopus 로고
    • HIV enters cells via endocytosis and dynamin-dependent fusion with endosomes
    • Miyauchi K, Kim Y, Latinovic O, Morozov V, Melikyan GB HIV enters cells via endocytosis and dynamin-dependent fusion with endosomes. Cell 2009, 137(3):433-444.
    • (2009) Cell , vol.137 , Issue.3 , pp. 433-444
    • Miyauchi, K.1    Kim, Y.2    Latinovic, O.3    Morozov, V.4    Melikyan, G.B.5
  • 101
    • 84888112438 scopus 로고    scopus 로고
    • Dynamin triple knockout cells reveal off target effects of commonly used dynamin inhibitors
    • Park RJ, Shen H, Liu L, Liu X, Ferguson SM, De Camilli P Dynamin triple knockout cells reveal off target effects of commonly used dynamin inhibitors. J Cell Sci 2013, 126(Pt 22):5305-5312.
    • (2013) J Cell Sci , vol.126 , pp. 5305-5312
    • Park, R.J.1    Shen, H.2    Liu, L.3    Liu, X.4    Ferguson, S.M.5    De Camilli, P.6
  • 102
    • 84872268808 scopus 로고    scopus 로고
    • Inhibition of clathrin by pitstop 2 activates the spindle assembly checkpoint and induces cell death in dividing HeLa cancer cells
    • Smith CM, Haucke V, McCluskey A, Robinson PJ, Chircop M Inhibition of clathrin by pitstop 2 activates the spindle assembly checkpoint and induces cell death in dividing HeLa cancer cells. Mol Cancer 2013, 12:4.
    • (2013) Mol Cancer , vol.12 , pp. 4
    • Smith, C.M.1    Haucke, V.2    McCluskey, A.3    Robinson, P.J.4    Chircop, M.5
  • 105
    • 84866705891 scopus 로고    scopus 로고
    • Pitstop 2 is a potent inhibitor of clathrin-independent endocytosis
    • Dutta D, Williamson CD, Cole NB, Donaldson JG Pitstop 2 is a potent inhibitor of clathrin-independent endocytosis. PloS One 2012, 7(9):e45799.
    • (2012) PloS One , vol.7 , Issue.9 , pp. e45799
    • Dutta, D.1    Williamson, C.D.2    Cole, N.B.3    Donaldson, J.G.4
  • 106
    • 84979587738 scopus 로고    scopus 로고
    • Non-specificity of Pitstop 2 in clathrin-mediated endocytosis
    • Willox AK, Sahraoui YM, Royle SJ Non-specificity of Pitstop 2 in clathrin-mediated endocytosis. Biol Open 2014, 3(5):326-331.
    • (2014) Biol Open , vol.3 , Issue.5 , pp. 326-331
    • Willox, A.K.1    Sahraoui, Y.M.2    Royle, S.J.3
  • 107
    • 84896704835 scopus 로고    scopus 로고
    • Clathrin terminal domain-ligand interactions regulate sorting of mannose 6-phosphate receptors mediated by AP-1 and GGA adaptors
    • Stahlschmidt W, Robertson MJ, Robinson PJ, McCluskey A, Haucke V Clathrin terminal domain-ligand interactions regulate sorting of mannose 6-phosphate receptors mediated by AP-1 and GGA adaptors. J Biol Chem 2014, 289(8):4906-4918.
    • (2014) J Biol Chem , vol.289 , Issue.8 , pp. 4906-4918
    • Stahlschmidt, W.1    Robertson, M.J.2    Robinson, P.J.3    McCluskey, A.4    Haucke, V.5
  • 108
    • 84901425609 scopus 로고    scopus 로고
    • In silico docking, molecular dynamics and binding energy insights into the bolinaquinone-clathrin terminal domain binding site
    • Abdel-Hamid MK, McCluskey A In silico docking, molecular dynamics and binding energy insights into the bolinaquinone-clathrin terminal domain binding site. Molecules 2014, 19(5):6609-6622.
    • (2014) Molecules , vol.19 , Issue.5 , pp. 6609-6622
    • Abdel-Hamid, M.K.1    McCluskey, A.2
  • 110
    • 84866498531 scopus 로고    scopus 로고
    • Interactions of high-affinity cationic blockers with the translocation pores of B. anthracis, C. botulinum, and C. perfringens binary toxins
    • Bezrukov SM, Liu X, Karginov VA, Wein AN, Leppla SH, Popoff MR, et al. Interactions of high-affinity cationic blockers with the translocation pores of B. anthracis, C. botulinum, and C. perfringens binary toxins. Biophys J 2012, 103(6):1208-1217.
    • (2012) Biophys J , vol.103 , Issue.6 , pp. 1208-1217
    • Bezrukov, S.M.1    Liu, X.2    Karginov, V.A.3    Wein, A.N.4    Leppla, S.H.5    Popoff, M.R.6
  • 111
    • 84892532262 scopus 로고    scopus 로고
    • Inhibitions of the translocation pore of Clostridium botulinum C2 toxin by tailored azolopyridinium salts protects human cells from intoxication
    • Bronnhuber A, Maier E, Riedl Z, Hajos G, Benz R, Barth H Inhibitions of the translocation pore of Clostridium botulinum C2 toxin by tailored azolopyridinium salts protects human cells from intoxication. Toxicology 2014, 316:25-33.
    • (2014) Toxicology , vol.316 , pp. 25-33
    • Bronnhuber, A.1    Maier, E.2    Riedl, Z.3    Hajos, G.4    Benz, R.5    Barth, H.6
  • 112
    • 84879271159 scopus 로고    scopus 로고
    • Designed azolopyridinium salts block protective antigen pores in vitro and protect cells from anthrax toxin
    • Beitzinger C, Bronnhuber A, Duscha K, Riedl Z, Huber-Lang M, Benz R, et al. Designed azolopyridinium salts block protective antigen pores in vitro and protect cells from anthrax toxin. PloS One 2013, 8(6):e66099.
    • (2013) PloS One , vol.8 , Issue.6 , pp. e66099
    • Beitzinger, C.1    Bronnhuber, A.2    Duscha, K.3    Riedl, Z.4    Huber-Lang, M.5    Benz, R.6
  • 114
    • 27244439667 scopus 로고    scopus 로고
    • Blocking anthrax lethal toxin at the protective antigen channel by using structure-inspired drug design
    • Karginov VA, Nestorovich EM, Moayeri M, Leppla SH, Bezrukov SM Blocking anthrax lethal toxin at the protective antigen channel by using structure-inspired drug design. Proc Natl Acad Sci USA 2005, 102(42):15075-15080.
    • (2005) Proc Natl Acad Sci USA , vol.102 , Issue.42 , pp. 15075-15080
    • Karginov, V.A.1    Nestorovich, E.M.2    Moayeri, M.3    Leppla, S.H.4    Bezrukov, S.M.5
  • 115
    • 34250745336 scopus 로고    scopus 로고
    • Inhibition of S. aureus alpha-hemolysin and B. anthracis lethal toxin by beta-cyclodextrin derivatives
    • Karginov VA, Nestorovich EM, Schmidtmann F, Robinson TM, Yohannes A, Fahmi NE, et al. Inhibition of S. aureus alpha-hemolysin and B. anthracis lethal toxin by beta-cyclodextrin derivatives. Bioorg Med Chem 2007, 15(16):5424-5431.
    • (2007) Bioorg Med Chem , vol.15 , Issue.16 , pp. 5424-5431
    • Karginov, V.A.1    Nestorovich, E.M.2    Schmidtmann, F.3    Robinson, T.M.4    Yohannes, A.5    Fahmi, N.E.6
  • 118
    • 44449142853 scopus 로고    scopus 로고
    • In vivo efficacy of beta-cyclodextrin derivatives against anthrax lethal toxin
    • Moayeri M, Robinson TM, Leppla SH, Karginov VA In vivo efficacy of beta-cyclodextrin derivatives against anthrax lethal toxin. Antimicrob Agents Chemother 2008, 52(6):2239-2241.
    • (2008) Antimicrob Agents Chemother , vol.52 , Issue.6 , pp. 2239-2241
    • Moayeri, M.1    Robinson, T.M.2    Leppla, S.H.3    Karginov, V.A.4
  • 119
    • 77954345106 scopus 로고    scopus 로고
    • Blockage of anthrax PA63 pore by a multicharged high-affinity toxin inhibitor
    • Nestorovich EM, Karginov VA, Berezhkovskii AM, Bezrukov SM Blockage of anthrax PA63 pore by a multicharged high-affinity toxin inhibitor. Biophys J 2010, 99(1):134-143.
    • (2010) Biophys J , vol.99 , Issue.1 , pp. 134-143
    • Nestorovich, E.M.1    Karginov, V.A.2    Berezhkovskii, A.M.3    Bezrukov, S.M.4
  • 120
    • 80051937100 scopus 로고    scopus 로고
    • Tailored ss-cyclodextrin blocks the translocation pores of binary exotoxins from C. botulinum and C. perfringens and protects cells from intoxication
    • Nestorovich EM, Karginov VA, Popoff MR, Bezrukov SM, Barth H Tailored ss-cyclodextrin blocks the translocation pores of binary exotoxins from C. botulinum and C. perfringens and protects cells from intoxication. PloS One 2011, 6(8):e23927.
    • (2011) PloS One , vol.6 , Issue.8 , pp. e23927
    • Nestorovich, E.M.1    Karginov, V.A.2    Popoff, M.R.3    Bezrukov, S.M.4    Barth, H.5
  • 121
    • 84888003275 scopus 로고    scopus 로고
    • Neutralisation of specific surface carboxylates speeds up translocation of botulinum neurotoxin type B enzymatic domain
    • Pirazzini M, Henke T, Rossetto O, Mahrhold S, Krez N, Rummel A, et al. Neutralisation of specific surface carboxylates speeds up translocation of botulinum neurotoxin type B enzymatic domain. FEBS Lett 2013, 587(23):3831-3836.
    • (2013) FEBS Lett , vol.587 , Issue.23 , pp. 3831-3836
    • Pirazzini, M.1    Henke, T.2    Rossetto, O.3    Mahrhold, S.4    Krez, N.5    Rummel, A.6
  • 122
    • 84892603497 scopus 로고    scopus 로고
    • (S)-N-Methyldihydroquinazolinones are the Active Enantiomers of Retro-2 Derived Compounds against Toxins
    • Gupta N, Pons V, Noel R, Buisson DA, Michau A, Johannes L, et al. (S)-N-Methyldihydroquinazolinones are the Active Enantiomers of Retro-2 Derived Compounds against Toxins. ACS Med Chem Lett 2014, 5(1):94-97.
    • (2014) ACS Med Chem Lett , vol.5 , Issue.1 , pp. 94-97
    • Gupta, N.1    Pons, V.2    Noel, R.3    Buisson, D.A.4    Michau, A.5    Johannes, L.6
  • 123
    • 84876864878 scopus 로고    scopus 로고
    • N-methyldihydroquinazolinone derivatives of Retro-2 with enhanced efficacy against Shiga toxin
    • Noel R, Gupta N, Pons V, Goudet A, Garcia-Castillo MD, Michau A, et al. N-methyldihydroquinazolinone derivatives of Retro-2 with enhanced efficacy against Shiga toxin. J Med Chem 2013, 56(8):3404-3413.
    • (2013) J Med Chem , vol.56 , Issue.8 , pp. 3404-3413
    • Noel, R.1    Gupta, N.2    Pons, V.3    Goudet, A.4    Garcia-Castillo, M.D.5    Michau, A.6
  • 124
    • 77952541863 scopus 로고    scopus 로고
    • Resveratrol, a natural polyphenolic compound, inhibits cholera toxin-induced cyclic AMP accumulation in Vero cells
    • Morinaga N, Yahiro K, Noda M Resveratrol, a natural polyphenolic compound, inhibits cholera toxin-induced cyclic AMP accumulation in Vero cells. Toxicon 2010, 56(1):29-35.
    • (2010) Toxicon , vol.56 , Issue.1 , pp. 29-35
    • Morinaga, N.1    Yahiro, K.2    Noda, M.3
  • 125
    • 20744459427 scopus 로고    scopus 로고
    • Differential activities of plant polyphenols on the binding and internalization of cholera toxin in vero cells
    • Morinaga N, Iwamaru Y, Yahiro K, Tagashira M, Moss J, Noda M Differential activities of plant polyphenols on the binding and internalization of cholera toxin in vero cells. J Biol Chem 2005, 280(24):23303-23309.
    • (2005) J Biol Chem , vol.280 , Issue.24 , pp. 23303-23309
    • Morinaga, N.1    Iwamaru, Y.2    Yahiro, K.3    Tagashira, M.4    Moss, J.5    Noda, M.6
  • 126
    • 20044396942 scopus 로고    scopus 로고
    • Inhibitory effects of polyphenols on gastric injury by Helicobacter pylori VacA toxin
    • Yahiro K, Shirasaka D, Tagashira M, Wada A, Morinaga N, Kuroda F, et al. Inhibitory effects of polyphenols on gastric injury by Helicobacter pylori VacA toxin. Helicobacter 2005, 10(3):231-239.
    • (2005) Helicobacter , vol.10 , Issue.3 , pp. 231-239
    • Yahiro, K.1    Shirasaka, D.2    Tagashira, M.3    Wada, A.4    Morinaga, N.5    Kuroda, F.6
  • 127
  • 128
    • 84899829096 scopus 로고    scopus 로고
    • Antibody-mediated inhibition of ricin toxin retrograde transport
    • Yermakova A, Klokk TI, Cole R, Sandvig K, Mantis NJ Antibody-mediated inhibition of ricin toxin retrograde transport. MBio 2014, 5(2):e00995.
    • (2014) MBio , vol.5 , Issue.2 , pp. e00995
    • Yermakova, A.1    Klokk, T.I.2    Cole, R.3    Sandvig, K.4    Mantis, N.J.5
  • 129
    • 74549131774 scopus 로고    scopus 로고
    • Identification of dynamin-2-mediated endocytosis as a new target of osteoporosis drugs, bisphosphonates
    • Masaike Y, Takagi T, Hirota M, Yamada J, Ishihara S, Yung TM, et al. Identification of dynamin-2-mediated endocytosis as a new target of osteoporosis drugs, bisphosphonates. Mol Pharmacol 2010, 77(2):262-269.
    • (2010) Mol Pharmacol , vol.77 , Issue.2 , pp. 262-269
    • Masaike, Y.1    Takagi, T.2    Hirota, M.3    Yamada, J.4    Ishihara, S.5    Yung, T.M.6
  • 130
    • 48849085276 scopus 로고    scopus 로고
    • Some selective serotonin reuptake inhibitors inhibit dynamin I guanosine triphosphatase (GTPase)
    • Otomo M, Takahashi K, Miyoshi H, Osada K, Nakashima H, Yamaguchi N Some selective serotonin reuptake inhibitors inhibit dynamin I guanosine triphosphatase (GTPase). Biol Pharm Bull 2008, 31(8):1489-1495.
    • (2008) Biol Pharm Bull , vol.31 , Issue.8 , pp. 1489-1495
    • Otomo, M.1    Takahashi, K.2    Miyoshi, H.3    Osada, K.4    Nakashima, H.5    Yamaguchi, N.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.