메뉴 건너뛰기




Volumn 23, Issue 2, 2013, Pages 90-101

Targeting membrane trafficking in infection prophylaxis: Dynamin inhibitors

Author keywords

Dynamin; Endocytosis; Neurotoxins; Pathogens; Prophylaxis; Trafficking

Indexed keywords

DYNAMIN; DYNAMIN INHIBITOR; ENZYME INHIBITOR; UNCLASSIFIED DRUG;

EID: 84872835489     PISSN: 09628924     EISSN: 18793088     Source Type: Journal    
DOI: 10.1016/j.tcb.2012.10.007     Document Type: Review
Times cited : (85)

References (118)
  • 1
    • 77955759831 scopus 로고    scopus 로고
    • Hijacking the endocytic machinery by microbial pathogens
    • Lin A.E., Guttman J.A. Hijacking the endocytic machinery by microbial pathogens. Protoplasma 2010, 244:75-90.
    • (2010) Protoplasma , vol.244 , pp. 75-90
    • Lin, A.E.1    Guttman, J.A.2
  • 3
    • 79960720320 scopus 로고    scopus 로고
    • Molecular mechanism and physiological functions of clathrin-mediated endocytosis
    • McMahon H.T., Boucrot E. Molecular mechanism and physiological functions of clathrin-mediated endocytosis. Nat. Rev. Mol. Cell Biol. 2011, 12:517-533.
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 517-533
    • McMahon, H.T.1    Boucrot, E.2
  • 4
    • 73949144556 scopus 로고    scopus 로고
    • Dynamin 2 orchestrates the global actomyosin cytoskeleton for epithelial maintenance and apical constriction
    • Chua J., et al. Dynamin 2 orchestrates the global actomyosin cytoskeleton for epithelial maintenance and apical constriction. Proc. Natl. Acad. Sci. U.S.A. 2009, 106:20770-20775.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 20770-20775
    • Chua, J.1
  • 5
    • 80053897195 scopus 로고    scopus 로고
    • Dynamin inhibition blocks botulinum neurotoxin type-A endocytosis in neurons and delays botulism
    • Harper C.B., et al. Dynamin inhibition blocks botulinum neurotoxin type-A endocytosis in neurons and delays botulism. J. Biol. Chem. 2011, 286:35966-35976.
    • (2011) J. Biol. Chem. , vol.286 , pp. 35966-35976
    • Harper, C.B.1
  • 6
    • 0017412506 scopus 로고
    • Depolarization-induced phosphorylation of specific proteins, mediated by calcium ion influx, in rat brain synaptosomes
    • Krueger B.K., et al. Depolarization-induced phosphorylation of specific proteins, mediated by calcium ion influx, in rat brain synaptosomes. J. Biol. Chem. 1977, 252:2764-2773.
    • (1977) J. Biol. Chem. , vol.252 , pp. 2764-2773
    • Krueger, B.K.1
  • 7
    • 0015875628 scopus 로고
    • Developmental properties of Shibire: a pleiotropic mutation affecting larval and adult locomotion and development
    • Poodry C.A., et al. Developmental properties of Shibire: a pleiotropic mutation affecting larval and adult locomotion and development. Dev. Biol. 1973, 32:373-386.
    • (1973) Dev. Biol. , vol.32 , pp. 373-386
    • Poodry, C.A.1
  • 8
    • 80052710376 scopus 로고    scopus 로고
    • Inhibition of dynamin by Dynole 34-2 induces cell death following cytokinesis failure in cancer cells
    • Chircop M., et al. Inhibition of dynamin by Dynole 34-2 induces cell death following cytokinesis failure in cancer cells. Mol. Cancer Ther. 2011, 10:1553-1562.
    • (2011) Mol. Cancer Ther. , vol.10 , pp. 1553-1562
    • Chircop, M.1
  • 9
    • 84868326542 scopus 로고    scopus 로고
    • Dynamin regulates specific membrane fusion events necessary for acrosomal exocytosis in mouse spermatozoa
    • Reid A.T., et al. Dynamin regulates specific membrane fusion events necessary for acrosomal exocytosis in mouse spermatozoa. J. Biol. Chem. 2012, 287:37659-37672.
    • (2012) J. Biol. Chem. , vol.287 , pp. 37659-37672
    • Reid, A.T.1
  • 10
    • 79957613290 scopus 로고    scopus 로고
    • A new role for the dynamin GTPase in the regulation of fusion pore expansion
    • Anantharam A., et al. A new role for the dynamin GTPase in the regulation of fusion pore expansion. Mol. Biol. Cell 2011, 22:1907-1908.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 1907-1908
    • Anantharam, A.1
  • 11
    • 33845188467 scopus 로고    scopus 로고
    • Inhibition of dynamin completely blocks compensatory synaptic vesicle endocytosis
    • Newton A.J., et al. Inhibition of dynamin completely blocks compensatory synaptic vesicle endocytosis. Proc. Natl. Acad. Sci. U.S.A. 2006, 103:17955-17960.
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 17955-17960
    • Newton, A.J.1
  • 12
    • 84861328690 scopus 로고    scopus 로고
    • Actin- and dynamin-dependent maturation of bulk endocytosis restores neurotransmission following synaptic depletion
    • Nguyen T.H., et al. Actin- and dynamin-dependent maturation of bulk endocytosis restores neurotransmission following synaptic depletion. PLoS ONE 2012, 7:e36913.
    • (2012) PLoS ONE , vol.7
    • Nguyen, T.H.1
  • 13
    • 67449143251 scopus 로고    scopus 로고
    • The phospho-dependent dynamin-syndapin interaction triggers activity-dependent bulk endocytosis of synaptic vesicles
    • Clayton E.L., et al. The phospho-dependent dynamin-syndapin interaction triggers activity-dependent bulk endocytosis of synaptic vesicles. J. Neurosci. 2009, 29:7706-7717.
    • (2009) J. Neurosci. , vol.29 , pp. 7706-7717
    • Clayton, E.L.1
  • 15
    • 0032489879 scopus 로고    scopus 로고
    • Dynamin-mediated internalization of caveolae
    • Henley J.R., et al. Dynamin-mediated internalization of caveolae. J. Cell Biol. 1998, 141:85-99.
    • (1998) J. Cell Biol. , vol.141 , pp. 85-99
    • Henley, J.R.1
  • 16
    • 80052942161 scopus 로고    scopus 로고
    • The Ebola virus glycoprotein mediates entry via a non-classical dynamin-dependent macropinocytic pathway
    • Mulherkar N., et al. The Ebola virus glycoprotein mediates entry via a non-classical dynamin-dependent macropinocytic pathway. Virology 2011, 419:72-83.
    • (2011) Virology , vol.419 , pp. 72-83
    • Mulherkar, N.1
  • 17
    • 78650267415 scopus 로고    scopus 로고
    • HIV-1 infects macrophages by exploiting an endocytic route dependent on dynamin, Rac1 and Pak1
    • Carter G.C., et al. HIV-1 infects macrophages by exploiting an endocytic route dependent on dynamin, Rac1 and Pak1. Virology 2011, 409:234-250.
    • (2011) Virology , vol.409 , pp. 234-250
    • Carter, G.C.1
  • 18
    • 38349014354 scopus 로고    scopus 로고
    • Dynamin 2 mediates fluid-phase micropinocytosis in epithelial cells
    • Cao H., et al. Dynamin 2 mediates fluid-phase micropinocytosis in epithelial cells. J. Cell Sci. 2007, 120:4167-4177.
    • (2007) J. Cell Sci. , vol.120 , pp. 4167-4177
    • Cao, H.1
  • 19
    • 0033385361 scopus 로고    scopus 로고
    • Dynamin 2 is required for phagocytosis in macrophages
    • Gold E.S., et al. Dynamin 2 is required for phagocytosis in macrophages. J. Exp. Med. 1999, 190:1849-1856.
    • (1999) J. Exp. Med. , vol.190 , pp. 1849-1856
    • Gold, E.S.1
  • 20
    • 57749173647 scopus 로고    scopus 로고
    • Dynamin 2 is required for actin assembly in phagocytosis in Sertoli cells
    • Otsuka A., et al. Dynamin 2 is required for actin assembly in phagocytosis in Sertoli cells. Biochem. Biophys. Res. Commun. 2009, 378:478-482.
    • (2009) Biochem. Biophys. Res. Commun. , vol.378 , pp. 478-482
    • Otsuka, A.1
  • 22
    • 0035265834 scopus 로고    scopus 로고
    • Interleukin 2 receptors and detergent-resistant membrane domains define a clathrin-independent endocytic pathway
    • Lamaze C., et al. Interleukin 2 receptors and detergent-resistant membrane domains define a clathrin-independent endocytic pathway. Mol. Cell 2001, 7:661-671.
    • (2001) Mol. Cell , vol.7 , pp. 661-671
    • Lamaze, C.1
  • 23
    • 78650271034 scopus 로고    scopus 로고
    • Endocytosis and toxicity of clostridial binary toxins depend on a clathrin-independent pathway regulated by Rho-GDI
    • Gibert M., et al. Endocytosis and toxicity of clostridial binary toxins depend on a clathrin-independent pathway regulated by Rho-GDI. Cell. Microbiol. 2011, 13:154-170.
    • (2011) Cell. Microbiol. , vol.13 , pp. 154-170
    • Gibert, M.1
  • 24
    • 0027203046 scopus 로고
    • Mutations in human dynamin block an intermediate stage in coated vesicle formation
    • van der Bliek A.M., et al. Mutations in human dynamin block an intermediate stage in coated vesicle formation. J. Cell Biol. 1993, 122:553-563.
    • (1993) J. Cell Biol. , vol.122 , pp. 553-563
    • van der Bliek, A.M.1
  • 25
    • 0034632034 scopus 로고    scopus 로고
    • Evidence that dynamin-2 functions as a signal-transducing GTPase
    • Fish K.N., et al. Evidence that dynamin-2 functions as a signal-transducing GTPase. J. Cell Biol. 2000, 150:145-154.
    • (2000) J. Cell Biol. , vol.150 , pp. 145-154
    • Fish, K.N.1
  • 26
    • 33745726868 scopus 로고    scopus 로고
    • Syndapin I is the phosphorylation-regulated dynamin I partner in synaptic vesicle endocytosis
    • Anggono V., et al. Syndapin I is the phosphorylation-regulated dynamin I partner in synaptic vesicle endocytosis. Nat. Neurosci. 2006, 9:752-760.
    • (2006) Nat. Neurosci. , vol.9 , pp. 752-760
    • Anggono, V.1
  • 27
    • 1842296915 scopus 로고    scopus 로고
    • Synaptic vesicle endocytosis impaired by disruption of dynamin-SH3 domain interactions
    • Shupliakov O., et al. Synaptic vesicle endocytosis impaired by disruption of dynamin-SH3 domain interactions. Science 1997, 276:259-263.
    • (1997) Science , vol.276 , pp. 259-263
    • Shupliakov, O.1
  • 28
    • 0032543766 scopus 로고    scopus 로고
    • Calcium triggers calcineurin-dependent synaptic vesicle recycling in mammalian nerve terminals
    • Marks B., McMahon H.T. Calcium triggers calcineurin-dependent synaptic vesicle recycling in mammalian nerve terminals. Curr. Biol. 1998, 8:740-749.
    • (1998) Curr. Biol. , vol.8 , pp. 740-749
    • Marks, B.1    McMahon, H.T.2
  • 29
    • 80053585085 scopus 로고    scopus 로고
    • Common membrane trafficking defects of disease-associated dynamin 2 mutations
    • Liu Y.W., et al. Common membrane trafficking defects of disease-associated dynamin 2 mutations. Traffic 2011, 12:1620-1633.
    • (2011) Traffic , vol.12 , pp. 1620-1633
    • Liu, Y.W.1
  • 30
    • 79951831654 scopus 로고    scopus 로고
    • Constitutive activated Cdc42-associated kinase (Ack) phosphorylation at arrested endocytic clathrin-coated pits of cells that lack dynamin
    • Shen H., et al. Constitutive activated Cdc42-associated kinase (Ack) phosphorylation at arrested endocytic clathrin-coated pits of cells that lack dynamin. Mol. Biol. Cell 2011, 22:493-502.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 493-502
    • Shen, H.1
  • 31
    • 79959316429 scopus 로고    scopus 로고
    • Overlapping role of dynamin isoforms in synaptic vesicle endocytosis
    • Raimondi A., et al. Overlapping role of dynamin isoforms in synaptic vesicle endocytosis. Neuron 2011, 70:1100-1114.
    • (2011) Neuron , vol.70 , pp. 1100-1114
    • Raimondi, A.1
  • 32
    • 2442614797 scopus 로고    scopus 로고
    • Long chain amines and long chain ammonium salts as novel inhibitors of dynamin GTPase activity
    • Hill T.A., et al. Long chain amines and long chain ammonium salts as novel inhibitors of dynamin GTPase activity. Bioorg. Med. Chem. Lett. 2004, 14:3275-3278.
    • (2004) Bioorg. Med. Chem. Lett. , vol.14 , pp. 3275-3278
    • Hill, T.A.1
  • 33
    • 79959585828 scopus 로고    scopus 로고
    • Dynamin inhibitors induce caspase-mediated apoptosis following cytokinesis failure in human cancer cells and this is blocked by Bcl-2 overexpression
    • Joshi S., et al. Dynamin inhibitors induce caspase-mediated apoptosis following cytokinesis failure in human cancer cells and this is blocked by Bcl-2 overexpression. Mol. Cancer 2011, 10:78.
    • (2011) Mol. Cancer , vol.10 , pp. 78
    • Joshi, S.1
  • 34
    • 28144443754 scopus 로고    scopus 로고
    • Small molecule inhibitors of dynamin I GTPase activity: development of dimeric tyrphostins
    • Hill T., et al. Small molecule inhibitors of dynamin I GTPase activity: development of dimeric tyrphostins. J. Med. Chem. 2005, 48:7781-7788.
    • (2005) J. Med. Chem. , vol.48 , pp. 7781-7788
    • Hill, T.1
  • 35
    • 37849039269 scopus 로고    scopus 로고
    • From Spanish fly to room-temperature ionic liquids (RTILs): synthesis, thermal stability and inhibition of dynamin 1 GTPase by a novel class of RTILs
    • Zhang J., et al. From Spanish fly to room-temperature ionic liquids (RTILs): synthesis, thermal stability and inhibition of dynamin 1 GTPase by a novel class of RTILs. New J. Chem. 2008, 32:28-36.
    • (2008) New J. Chem. , vol.32 , pp. 28-36
    • Zhang, J.1
  • 36
    • 33646892646 scopus 로고    scopus 로고
    • Dynasore, a cell-permeable inhibitor of dynamin
    • Macia E., et al. Dynasore, a cell-permeable inhibitor of dynamin. Dev. Cell 2006, 10:839-850.
    • (2006) Dev. Cell , vol.10 , pp. 839-850
    • Macia, E.1
  • 37
    • 84864463813 scopus 로고    scopus 로고
    • Analysis of synaptic vesicle endocytosis in synaptosomes by high-content screening
    • Daniel J.A., et al. Analysis of synaptic vesicle endocytosis in synaptosomes by high-content screening. Nat. Protoc. 2012, 7:1439-1455.
    • (2012) Nat. Protoc. , vol.7 , pp. 1439-1455
    • Daniel, J.A.1
  • 38
    • 77952705940 scopus 로고    scopus 로고
    • Iminochromene inhibitors of dynamins I and II GTPase activity and endocytosis
    • Hill T.A., et al. Iminochromene inhibitors of dynamins I and II GTPase activity and endocytosis. J. Med. Chem. 2010, 53:4094-4102.
    • (2010) J. Med. Chem. , vol.53 , pp. 4094-4102
    • Hill, T.A.1
  • 39
    • 77954701884 scopus 로고    scopus 로고
    • The pthaladyns: GTP competitive inhibitors of dynamin I and II GTPase derived from virtual screening
    • Odell L.R., et al. The pthaladyns: GTP competitive inhibitors of dynamin I and II GTPase derived from virtual screening. J. Med. Chem. 2010, 53:5267-5280.
    • (2010) J. Med. Chem. , vol.53 , pp. 5267-5280
    • Odell, L.R.1
  • 40
    • 67549119243 scopus 로고    scopus 로고
    • Inhibition of dynamin mediated endocytosis by the dynoles--synthesis and functional activity of a family of indoles
    • Hill T.A., et al. Inhibition of dynamin mediated endocytosis by the dynoles--synthesis and functional activity of a family of indoles. J. Med. Chem. 2009, 52:3762-3773.
    • (2009) J. Med. Chem. , vol.52 , pp. 3762-3773
    • Hill, T.A.1
  • 41
    • 84861083216 scopus 로고    scopus 로고
    • The Rhodadyns, a new class of small molecule inhibitors of dynamin GTPase activity
    • Robertson M.J., et al. The Rhodadyns, a new class of small molecule inhibitors of dynamin GTPase activity. ACS Med. Chem. Lett. 2012, 3:352-356.
    • (2012) ACS Med. Chem. Lett. , vol.3 , pp. 352-356
    • Robertson, M.J.1
  • 42
    • 0034789465 scopus 로고    scopus 로고
    • Elevated endosomal pH in HeLa cells overexpressing mutant dynamin can affect infection by pH-sensitive viruses
    • Huber M., et al. Elevated endosomal pH in HeLa cells overexpressing mutant dynamin can affect infection by pH-sensitive viruses. Traffic 2001, 2:727-736.
    • (2001) Traffic , vol.2 , pp. 727-736
    • Huber, M.1
  • 43
    • 84861215299 scopus 로고    scopus 로고
    • Preferential entry of botulinum neurotoxin A Hc domain through intestinal crypt cells and targeting to cholinergic neurons of the mouse intestine
    • Couesnon A., et al. Preferential entry of botulinum neurotoxin A Hc domain through intestinal crypt cells and targeting to cholinergic neurons of the mouse intestine. PLoS Pathog. 2012, 8:e1002583.
    • (2012) PLoS Pathog. , vol.8
    • Couesnon, A.1
  • 44
    • 77952676295 scopus 로고    scopus 로고
    • Murine norovirus-1 cell entry is mediated through a non-clathrin-, non-caveolae-, dynamin- and cholesterol-dependent pathway
    • Gerondopoulos A., et al. Murine norovirus-1 cell entry is mediated through a non-clathrin-, non-caveolae-, dynamin- and cholesterol-dependent pathway. J. Gen. Virol. 2010, 91:1428-1438.
    • (2010) J. Gen. Virol. , vol.91 , pp. 1428-1438
    • Gerondopoulos, A.1
  • 45
    • 79953273232 scopus 로고    scopus 로고
    • Dissection of the influenza A virus endocytic routes reveals macropinocytosis as an alternative entry pathway
    • de Vries E., et al. Dissection of the influenza A virus endocytic routes reveals macropinocytosis as an alternative entry pathway. PLoS Pathog. 2011, 7:e1001329.
    • (2011) PLoS Pathog. , vol.7
    • de Vries, E.1
  • 46
    • 0033998692 scopus 로고    scopus 로고
    • Infectious entry pathway of adeno-associated virus and adeno-associated virus vectors
    • Bartlett J.S., et al. Infectious entry pathway of adeno-associated virus and adeno-associated virus vectors. J. Virol. 2000, 74:2777-2785.
    • (2000) J. Virol. , vol.74 , pp. 2777-2785
    • Bartlett, J.S.1
  • 47
    • 83655164541 scopus 로고    scopus 로고
    • Adeno-associated virus 2 infection requires endocytosis through the CLIC/GEEC pathway
    • Nonnenmacher M., Weber T. Adeno-associated virus 2 infection requires endocytosis through the CLIC/GEEC pathway. Cell Host Microbe 2011, 10:563-576.
    • (2011) Cell Host Microbe , vol.10 , pp. 563-576
    • Nonnenmacher, M.1    Weber, T.2
  • 48
    • 13744252968 scopus 로고    scopus 로고
    • Involvement of clathrin-mediated endocytosis in human immunodeficiency virus type 1 entry
    • Daecke J., et al. Involvement of clathrin-mediated endocytosis in human immunodeficiency virus type 1 entry. J. Virol. 2005, 79:1581-1594.
    • (2005) J. Virol. , vol.79 , pp. 1581-1594
    • Daecke, J.1
  • 49
    • 79961140522 scopus 로고    scopus 로고
    • Role of the clathrin terminal domain in regulating coated pit dynamics revealed by small molecule inhibition
    • von Kleist L., et al. Role of the clathrin terminal domain in regulating coated pit dynamics revealed by small molecule inhibition. Cell 2011, 146:471-484.
    • (2011) Cell , vol.146 , pp. 471-484
    • von Kleist, L.1
  • 50
    • 65249139458 scopus 로고    scopus 로고
    • HIV enters cells via endocytosis and dynamin-dependent fusion with endosomes
    • Miyauchi K., et al. HIV enters cells via endocytosis and dynamin-dependent fusion with endosomes. Cell 2009, 137:433-444.
    • (2009) Cell , vol.137 , pp. 433-444
    • Miyauchi, K.1
  • 51
    • 82655186589 scopus 로고    scopus 로고
    • Inhibition of HIV-1 endocytosis allows lipid mixing at the plasma membrane, but not complete fusion
    • de la Vega M., et al. Inhibition of HIV-1 endocytosis allows lipid mixing at the plasma membrane, but not complete fusion. Retrovirology 2011, 8:99.
    • (2011) Retrovirology , vol.8 , pp. 99
    • de la Vega, M.1
  • 52
    • 34848819775 scopus 로고    scopus 로고
    • Cellular internalization of green fluorescent protein fused with herpes simplex virus protein VP22 via a lipid raft-mediated endocytic pathway independent of caveolae and Rho family GTPases but dependent on dynamin and Arf6
    • Nishi K., Saigo K. Cellular internalization of green fluorescent protein fused with herpes simplex virus protein VP22 via a lipid raft-mediated endocytic pathway independent of caveolae and Rho family GTPases but dependent on dynamin and Arf6. J. Biol. Chem. 2007, 282:27503-27517.
    • (2007) J. Biol. Chem. , vol.282 , pp. 27503-27517
    • Nishi, K.1    Saigo, K.2
  • 53
    • 80054000888 scopus 로고    scopus 로고
    • Entry pathways of herpes simplex virus type 1 into human keratinocytes are dynamin- and cholesterol-dependent
    • Rahn E., et al. Entry pathways of herpes simplex virus type 1 into human keratinocytes are dynamin- and cholesterol-dependent. PLoS ONE 2011, 6:e25464.
    • (2011) PLoS ONE , vol.6
    • Rahn, E.1
  • 54
    • 78149301316 scopus 로고    scopus 로고
    • Cellular entry of ebola virus involves uptake by a macropinocytosis-like mechanism and subsequent trafficking through early and late endosomes
    • Saeed M.F., et al. Cellular entry of ebola virus involves uptake by a macropinocytosis-like mechanism and subsequent trafficking through early and late endosomes. PLoS Pathog. 2010, 6:e1001110.
    • (2010) PLoS Pathog. , vol.6
    • Saeed, M.F.1
  • 55
    • 0037405176 scopus 로고    scopus 로고
    • Human rhinovirus type 2 is internalized by clathrin-mediated endocytosis
    • Snyers L., et al. Human rhinovirus type 2 is internalized by clathrin-mediated endocytosis. J. Virol. 2003, 77:5360-5369.
    • (2003) J. Virol. , vol.77 , pp. 5360-5369
    • Snyers, L.1
  • 56
    • 79952535002 scopus 로고    scopus 로고
    • Entry of a heparan sulphate-binding HRV8 variant strictly depends on dynamin but not on clathrin, caveolin, and flotillin
    • Khan A.G., et al. Entry of a heparan sulphate-binding HRV8 variant strictly depends on dynamin but not on clathrin, caveolin, and flotillin. Virology 2011, 412:55-67.
    • (2011) Virology , vol.412 , pp. 55-67
    • Khan, A.G.1
  • 57
    • 84862989117 scopus 로고    scopus 로고
    • GM1 structure determines SV40-induced membrane invagination and infection
    • Ewers H., et al. GM1 structure determines SV40-induced membrane invagination and infection. Nat. Cell Biol. 2010, 12:11-18.
    • (2010) Nat. Cell Biol. , vol.12 , pp. 11-18
    • Ewers, H.1
  • 58
    • 0037134014 scopus 로고    scopus 로고
    • Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae
    • Pelkmans L., et al. Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae. Science 2002, 296:535-539.
    • (2002) Science , vol.296 , pp. 535-539
    • Pelkmans, L.1
  • 59
    • 77049128273 scopus 로고    scopus 로고
    • Actin dynamics drive membrane reorganization and scission in clathrin-independent endocytosis
    • Romer W., et al. Actin dynamics drive membrane reorganization and scission in clathrin-independent endocytosis. Cell 2010, 140:540-553.
    • (2010) Cell , vol.140 , pp. 540-553
    • Romer, W.1
  • 60
    • 77956035360 scopus 로고    scopus 로고
    • Different rotavirus strains enter MA104 cells through different endocytic pathways: the role of clathrin-mediated endocytosis
    • Gutierrez M., et al. Different rotavirus strains enter MA104 cells through different endocytic pathways: the role of clathrin-mediated endocytosis. J. Virol. 2010, 84:9161-9169.
    • (2010) J. Virol. , vol.84 , pp. 9161-9169
    • Gutierrez, M.1
  • 61
    • 70350719853 scopus 로고    scopus 로고
    • Alternative infectious entry pathways for dengue virus serotypes into mammalian cells
    • Acosta E.G., et al. Alternative infectious entry pathways for dengue virus serotypes into mammalian cells. Cell. Microbiol. 2009, 11:1533-1549.
    • (2009) Cell. Microbiol. , vol.11 , pp. 1533-1549
    • Acosta, E.G.1
  • 62
    • 80052163065 scopus 로고    scopus 로고
    • Infectious dengue-1 virus entry into mosquito C6/36 cells
    • Acosta E.G., et al. Infectious dengue-1 virus entry into mosquito C6/36 cells. Virus Res. 2011, 160:173-179.
    • (2011) Virus Res. , vol.160 , pp. 173-179
    • Acosta, E.G.1
  • 63
    • 70349309767 scopus 로고    scopus 로고
    • Modulation of membrane traffic between endoplasmic reticulum, ERGIC and Golgi to generate compartments for the replication of bacteria and viruses
    • Pierini R., et al. Modulation of membrane traffic between endoplasmic reticulum, ERGIC and Golgi to generate compartments for the replication of bacteria and viruses. Semin. Cell Dev. Biol. 2009, 20:828-833.
    • (2009) Semin. Cell Dev. Biol. , vol.20 , pp. 828-833
    • Pierini, R.1
  • 64
    • 0037230596 scopus 로고    scopus 로고
    • The large GTPase dynamin is required for hepatitis B virus protein secretion from hepatocytes
    • Abdulkarim A.S., et al. The large GTPase dynamin is required for hepatitis B virus protein secretion from hepatocytes. J. Hepatol. 2003, 38:76-83.
    • (2003) J. Hepatol. , vol.38 , pp. 76-83
    • Abdulkarim, A.S.1
  • 65
    • 77950531323 scopus 로고    scopus 로고
    • Src kinase regulates the integrity and function of the Golgi apparatus via activation of dynamin 2
    • Weller S.G., et al. Src kinase regulates the integrity and function of the Golgi apparatus via activation of dynamin 2. Proc. Natl. Acad. Sci. U.S.A. 2010, 107:5863-5868.
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 5863-5868
    • Weller, S.G.1
  • 66
    • 51649111041 scopus 로고    scopus 로고
    • HPV16 and BPV1 infection can be blocked by the dynamin inhibitor dynasore
    • Abban C.Y., et al. HPV16 and BPV1 infection can be blocked by the dynamin inhibitor dynasore. Am. J. Ther. 2008, 15:304-311.
    • (2008) Am. J. Ther. , vol.15 , pp. 304-311
    • Abban, C.Y.1
  • 67
    • 84861207605 scopus 로고    scopus 로고
    • Entry of human papillomavirus type 16 by actin-dependent, clathrin- and lipid raft-independent endocytosis
    • Schelhaas M., et al. Entry of human papillomavirus type 16 by actin-dependent, clathrin- and lipid raft-independent endocytosis. PLoS Pathog. 2012, 8:e1002657.
    • (2012) PLoS Pathog. , vol.8
    • Schelhaas, M.1
  • 68
    • 77953642001 scopus 로고    scopus 로고
    • Botulinum neurotoxin: a marvel of protein design
    • Montal M. Botulinum neurotoxin: a marvel of protein design. Annu. Rev. Biochem. 2010, 79:591-617.
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 591-617
    • Montal, M.1
  • 69
    • 58349103136 scopus 로고    scopus 로고
    • Differential entry of botulinum neurotoxin A into neuronal and intestinal cells
    • Couesnon A., et al. Differential entry of botulinum neurotoxin A into neuronal and intestinal cells. Cell. Microbiol. 2009, 11:289-308.
    • (2009) Cell. Microbiol. , vol.11 , pp. 289-308
    • Couesnon, A.1
  • 70
    • 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., et al. Tetanus toxin is internalized by a sequential clathrin-dependent mechanism initiated within lipid microdomains and independent of epsin1. J. Cell Biol. 2006, 174:459-471.
    • (2006) J. Cell Biol. , vol.174 , pp. 459-471
    • Deinhardt, K.1
  • 71
    • 79251482759 scopus 로고    scopus 로고
    • SV2 mediates entry of tetanus neurotoxin into central neurons
    • Yeh F.L., et al. SV2 mediates entry of tetanus neurotoxin into central neurons. PLoS Pathog. 2010, 6:e1001207.
    • (2010) PLoS Pathog. , vol.6
    • Yeh, F.L.1
  • 72
    • 77956461530 scopus 로고    scopus 로고
    • Clostridial glucosylating toxins enter cells via clathrin-mediated endocytosis
    • Papatheodorou P., et al. Clostridial glucosylating toxins enter cells via clathrin-mediated endocytosis. PLoS ONE 2010, 5:e10673.
    • (2010) PLoS ONE , vol.5
    • Papatheodorou, P.1
  • 73
    • 0037415611 scopus 로고    scopus 로고
    • Anthrax toxin triggers endocytosis of its receptor via a lipid raft-mediated clathrin-dependent process
    • Abrami L., et al. Anthrax toxin triggers endocytosis of its receptor via a lipid raft-mediated clathrin-dependent process. J. Cell Biol. 2003, 160:321-328.
    • (2003) J. Cell Biol. , vol.160 , pp. 321-328
    • Abrami, L.1
  • 74
    • 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 D.N., Czuprynski C.J. 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, 75:4719-4727.
    • (2007) Infect. Immun. , vol.75 , pp. 4719-4727
    • Atapattu, D.N.1    Czuprynski, C.J.2
  • 75
    • 78449295494 scopus 로고    scopus 로고
    • Clostridium botulinum C2 toxin is internalized by clathrin- and Rho-dependent mechanisms
    • Pust S., et al. Clostridium botulinum C2 toxin is internalized by clathrin- and Rho-dependent mechanisms. Cell. Microbiol. 2010, 12:1809-1820.
    • (2010) Cell. Microbiol. , vol.12 , pp. 1809-1820
    • Pust, S.1
  • 76
    • 77955902031 scopus 로고    scopus 로고
    • Clathrin-independent carriers form a high capacity endocytic sorting system at the leading edge of migrating cells
    • Howes M.T., et al. Clathrin-independent carriers form a high capacity endocytic sorting system at the leading edge of migrating cells. J. Cell Biol. 2010, 190:675-691.
    • (2010) J. Cell Biol. , vol.190 , pp. 675-691
    • Howes, M.T.1
  • 77
    • 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, 20:165-174.
    • (2012) Trends Microbiol. , vol.20 , pp. 165-174
    • Boquet, P.1    Ricci, V.2
  • 78
    • 3042639390 scopus 로고    scopus 로고
    • Efficient endosome-to-Golgi transport of Shiga toxin is dependent on dynamin and clathrin
    • Lauvrak S.U., et al. Efficient endosome-to-Golgi transport of Shiga toxin is dependent on dynamin and clathrin. J. Cell Sci. 2004, 117:2321-2331.
    • (2004) J. Cell Sci. , vol.117 , pp. 2321-2331
    • Lauvrak, S.U.1
  • 79
    • 35848959730 scopus 로고    scopus 로고
    • Invasive and adherent bacterial pathogens co-Opt host clathrin for infection
    • Veiga E., et al. Invasive and adherent bacterial pathogens co-Opt host clathrin for infection. Cell Host Microbe 2007, 2:340-351.
    • (2007) Cell Host Microbe , vol.2 , pp. 340-351
    • Veiga, E.1
  • 80
    • 79955082658 scopus 로고    scopus 로고
    • Streptolysin O inhibits clathrin-dependent internalization of group A Streptococcus
    • e00332-10
    • Logsdon L.K., et al. Streptolysin O inhibits clathrin-dependent internalization of group A Streptococcus. MBio 2011, 2. e00332-10.
    • (2011) MBio , vol.2
    • Logsdon, L.K.1
  • 81
    • 83755183062 scopus 로고    scopus 로고
    • Clathrin phosphorylation is required for actin recruitment at sites of bacterial adhesion and internalization
    • Bonazzi M., et al. Clathrin phosphorylation is required for actin recruitment at sites of bacterial adhesion and internalization. J. Cell Biol. 2011, 195:525-536.
    • (2011) J. Cell Biol. , vol.195 , pp. 525-536
    • Bonazzi, M.1
  • 82
    • 55749095583 scopus 로고    scopus 로고
    • Clathrin, AP-2, and the NPXY-binding subset of alternate endocytic adaptors facilitate FimH-mediated bacterial invasion of host cells
    • Eto D.S., et al. Clathrin, AP-2, and the NPXY-binding subset of alternate endocytic adaptors facilitate FimH-mediated bacterial invasion of host cells. Cell. Microbiol. 2008, 10:2553-2567.
    • (2008) Cell. Microbiol. , vol.10 , pp. 2553-2567
    • Eto, D.S.1
  • 83
    • 67650135490 scopus 로고    scopus 로고
    • Candida albicans internalization by host cells is mediated by a clathrin-dependent mechanism
    • Moreno-Ruiz E., et al. Candida albicans internalization by host cells is mediated by a clathrin-dependent mechanism. Cell. Microbiol. 2009, 11:1179-1189.
    • (2009) Cell. Microbiol. , vol.11 , pp. 1179-1189
    • Moreno-Ruiz, E.1
  • 84
    • 81755183022 scopus 로고    scopus 로고
    • The pore-forming toxin listeriolysin O mediates a novel entry pathway of L. monocytogenes into human hepatocytes
    • Vadia S., et al. The pore-forming toxin listeriolysin O mediates a novel entry pathway of L. monocytogenes into human hepatocytes. PLoS Pathog. 2011, 7:e1002356.
    • (2011) PLoS Pathog. , vol.7
    • Vadia, S.1
  • 85
    • 79955675275 scopus 로고    scopus 로고
    • Recent advances in Chlamydia subversion of host cytoskeletal and membrane trafficking pathways
    • Scidmore M.A. Recent advances in Chlamydia subversion of host cytoskeletal and membrane trafficking pathways. Microbes Infect. 2011, 13:527-535.
    • (2011) Microbes Infect. , vol.13 , pp. 527-535
    • Scidmore, M.A.1
  • 86
    • 34547621080 scopus 로고    scopus 로고
    • Mechanisms of Chlamydia trachomatis entry into nonphagocytic cells
    • Hybiske K., Stephens R.S. Mechanisms of Chlamydia trachomatis entry into nonphagocytic cells. Infect. Immun. 2007, 75:3925-3934.
    • (2007) Infect. Immun. , vol.75 , pp. 3925-3934
    • Hybiske, K.1    Stephens, R.S.2
  • 87
    • 0032977966 scopus 로고    scopus 로고
    • Chlamydia infection of epithelial cells expressing dynamin and Eps15 mutants: clathrin-independent entry into cells and dynamin-dependent productive growth
    • Boleti H., et al. Chlamydia infection of epithelial cells expressing dynamin and Eps15 mutants: clathrin-independent entry into cells and dynamin-dependent productive growth. J. Cell Sci. 1999, 112:1487-1496.
    • (1999) J. Cell Sci. , vol.112 , pp. 1487-1496
    • Boleti, H.1
  • 88
    • 77649278899 scopus 로고    scopus 로고
    • Dynasore, a dynamin inhibitor, inhibits Trypanosoma cruzi entry into peritoneal macrophages
    • Barrias E.S., et al. Dynasore, a dynamin inhibitor, inhibits Trypanosoma cruzi entry into peritoneal macrophages. PLoS ONE 2010, 5:e7764.
    • (2010) PLoS ONE , vol.5
    • Barrias, E.S.1
  • 89
    • 69049085270 scopus 로고    scopus 로고
    • Inhibitors of clathrin-dependent endocytosis enhance TGFbeta signaling and responses
    • Chen C.L., et al. Inhibitors of clathrin-dependent endocytosis enhance TGFbeta signaling and responses. J. Cell Sci. 2009, 122:1863-1871.
    • (2009) J. Cell Sci. , vol.122 , pp. 1863-1871
    • Chen, C.L.1
  • 90
    • 74549131774 scopus 로고    scopus 로고
    • Identification of dynamin-2-mediated endocytosis as a new target of osteoporosis drugs, bisphosphonates
    • Masaike Y., et al. Identification of dynamin-2-mediated endocytosis as a new target of osteoporosis drugs, bisphosphonates. Mol. Pharmacol. 2010, 77:262-269.
    • (2010) Mol. Pharmacol. , vol.77 , pp. 262-269
    • Masaike, Y.1
  • 91
    • 48849085276 scopus 로고    scopus 로고
    • Some selective serotonin reuptake inhibitors inhibit dynamin I guanosine triphosphatase (GTPase)
    • Otomo M., et al. Some selective serotonin reuptake inhibitors inhibit dynamin I guanosine triphosphatase (GTPase). Biol. Pharm. Bull. 2008, 31:1489-1495.
    • (2008) Biol. Pharm. Bull. , vol.31 , pp. 1489-1495
    • Otomo, M.1
  • 92
    • 34247583278 scopus 로고    scopus 로고
    • A selective activity-dependent requirement for dynamin 1 in synaptic vesicle endocytosis
    • Ferguson S.M., et al. A selective activity-dependent requirement for dynamin 1 in synaptic vesicle endocytosis. Science 2007, 316:570-574.
    • (2007) Science , vol.316 , pp. 570-574
    • Ferguson, S.M.1
  • 93
    • 80051789504 scopus 로고    scopus 로고
    • Phosphorylation of dynamin II at serine-764 is associated with cytokinesis
    • Chircop M., et al. Phosphorylation of dynamin II at serine-764 is associated with cytokinesis. Biochim. Biophys. Acta 2011, 1813:1689-1699.
    • (2011) Biochim. Biophys. Acta , vol.1813 , pp. 1689-1699
    • Chircop, M.1
  • 94
    • 84856074275 scopus 로고    scopus 로고
    • Manganese blocks intracellular trafficking of Shiga toxin and protects against Shiga toxicosis
    • Mukhopadhyay S., Linstedt A.D. Manganese blocks intracellular trafficking of Shiga toxin and protects against Shiga toxicosis. Science 2012, 335:332-335.
    • (2012) Science , vol.335 , pp. 332-335
    • Mukhopadhyay, S.1    Linstedt, A.D.2
  • 95
    • 77951735286 scopus 로고    scopus 로고
    • Inhibition of retrograde transport protects mice from lethal ricin challenge
    • Stechmann B., et al. Inhibition of retrograde transport protects mice from lethal ricin challenge. Cell 2010, 141:231-242.
    • (2010) Cell , vol.141 , pp. 231-242
    • Stechmann, B.1
  • 96
    • 77951460389 scopus 로고    scopus 로고
    • Inhibition of the PtdIns(5) kinase PIKfyve disrupts intracellular replication of Salmonella
    • Kerr M.C., et al. Inhibition of the PtdIns(5) kinase PIKfyve disrupts intracellular replication of Salmonella. EMBO J. 2010, 29:1331-1347.
    • (2010) EMBO J. , vol.29 , pp. 1331-1347
    • Kerr, M.C.1
  • 97
    • 60849107288 scopus 로고    scopus 로고
    • Bimodal modulation of the botulinum neurotoxin protein-conducting channel
    • Fischer A., et al. Bimodal modulation of the botulinum neurotoxin protein-conducting channel. Proc Natl Acad Sci USA 2009, 3:1330-1335.
    • (2009) Proc Natl Acad Sci USA , vol.3 , pp. 1330-1335
    • Fischer, A.1
  • 98
    • 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., 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, 72:1425-1439.
    • (2007) Mol. Pharmacol. , vol.72 , pp. 1425-1439
    • Quan, A.1
  • 99
    • 0037119944 scopus 로고    scopus 로고
    • Adenovirus triggers macropinocytosis and endosomal leakage together with its clathrin-mediated uptake
    • Meier O., et al. Adenovirus triggers macropinocytosis and endosomal leakage together with its clathrin-mediated uptake. J. Cell Biol. 2002, 158:1119-1131.
    • (2002) J. Cell Biol. , vol.158 , pp. 1119-1131
    • Meier, O.1
  • 100
    • 75449110786 scopus 로고    scopus 로고
    • Dynamin- and clathrin-dependent endocytosis in African swine fever virus entry
    • Hernaez B., Alonso C. Dynamin- and clathrin-dependent endocytosis in African swine fever virus entry. J. Virol. 2010, 84:2100-2109.
    • (2010) J. Virol. , vol.84 , pp. 2100-2109
    • Hernaez, B.1    Alonso, C.2
  • 101
    • 80052249258 scopus 로고    scopus 로고
    • Cell entry of avian reovirus follows a caveolin-1-mediated and dynamin-2-dependent endocytic pathway that requires activation of p38 mitogen-activated protein kinase (MAPK) and Src signaling pathways as well as microtubules and small GTPase Rab5 protein
    • Huang W.R., et al. Cell entry of avian reovirus follows a caveolin-1-mediated and dynamin-2-dependent endocytic pathway that requires activation of p38 mitogen-activated protein kinase (MAPK) and Src signaling pathways as well as microtubules and small GTPase Rab5 protein. J. Biol. Chem. 2011, 286:30780-30794.
    • (2011) J. Biol. Chem. , vol.286 , pp. 30780-30794
    • Huang, W.R.1
  • 102
    • 77956196470 scopus 로고    scopus 로고
    • A clathrin independent macropinocytosis-like entry mechanism used by bluetongue virus-1 during infection of BHK cells
    • Gold S., et al. A clathrin independent macropinocytosis-like entry mechanism used by bluetongue virus-1 during infection of BHK cells. PLoS ONE 2010, 5:e11360.
    • (2010) PLoS ONE , vol.5
    • Gold, S.1
  • 103
    • 77949343121 scopus 로고    scopus 로고
    • Internalization of coxsackievirus A9 is mediated by {beta}2-microglobulin, dynamin, and Arf6 but not by caveolin-1 or clathrin
    • Heikkila O., et al. Internalization of coxsackievirus A9 is mediated by {beta}2-microglobulin, dynamin, and Arf6 but not by caveolin-1 or clathrin. J. Virol. 2010, 84:3666-3681.
    • (2010) J. Virol. , vol.84 , pp. 3666-3681
    • Heikkila, O.1
  • 104
    • 70350277393 scopus 로고    scopus 로고
    • Dynamin- and lipid raft-dependent entry of decay-accelerating factor (DAF)-binding and non-DAF-binding coxsackieviruses into nonpolarized cells
    • Patel K.P., et al. Dynamin- and lipid raft-dependent entry of decay-accelerating factor (DAF)-binding and non-DAF-binding coxsackieviruses into nonpolarized cells. J. Virol. 2009, 83:11064-11077.
    • (2009) J. Virol. , vol.83 , pp. 11064-11077
    • Patel, K.P.1
  • 105
    • 6344275643 scopus 로고    scopus 로고
    • Echovirus 1 endocytosis into caveosomes requires lipid rafts, dynamin II, and signaling events
    • Pietiainen V., et al. Echovirus 1 endocytosis into caveosomes requires lipid rafts, dynamin II, and signaling events. Mol. Biol. Cell 2004, 15:4911-4925.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 4911-4925
    • Pietiainen, V.1
  • 106
    • 38849103049 scopus 로고    scopus 로고
    • Equine infectious anemia virus entry occurs through clathrin-mediated endocytosis
    • Brindley M.A., Maury W. Equine infectious anemia virus entry occurs through clathrin-mediated endocytosis. J. Virol. 2008, 82:1628-1637.
    • (2008) J. Virol. , vol.82 , pp. 1628-1637
    • Brindley, M.A.1    Maury, W.2
  • 107
    • 0036061569 scopus 로고    scopus 로고
    • Hantaan virus enters cells by clathrin-dependent receptor-mediated endocytosis
    • Jin M., et al. Hantaan virus enters cells by clathrin-dependent receptor-mediated endocytosis. Virology 2002, 294:60-69.
    • (2002) Virology , vol.294 , pp. 60-69
    • Jin, M.1
  • 108
    • 72849144468 scopus 로고    scopus 로고
    • Hepatitis B virus requires intact caveolin-1 function for productive infection in HepaRG cells
    • Macovei A., et al. Hepatitis B virus requires intact caveolin-1 function for productive infection in HepaRG cells. J. Virol. 2010, 84:243-253.
    • (2010) J. Virol. , vol.84 , pp. 243-253
    • Macovei, A.1
  • 109
    • 77956934197 scopus 로고    scopus 로고
    • The second extracellular loop dictates Occludin-mediated HCV entry
    • Liu S., et al. The second extracellular loop dictates Occludin-mediated HCV entry. Virology 2010, 407:160-170.
    • (2010) Virology , vol.407 , pp. 160-170
    • Liu, S.1
  • 110
    • 80051622108 scopus 로고    scopus 로고
    • The 2009 pandemic A/Wenshan/01/2009 H1N1 induces apoptotic cell death in human airway epithelial cells
    • Yang N., et al. The 2009 pandemic A/Wenshan/01/2009 H1N1 induces apoptotic cell death in human airway epithelial cells. J. Mol. Cell Biol. 2011, 3:221-229.
    • (2011) J. Mol. Cell Biol. , vol.3 , pp. 221-229
    • Yang, N.1
  • 111
    • 68049085465 scopus 로고    scopus 로고
    • Involvement of cellular proteins in Junin arenavirus entry
    • Martinez M.G., et al. Involvement of cellular proteins in Junin arenavirus entry. Biotechnol. J. 2009, 4:866-870.
    • (2009) Biotechnol. J. , vol.4 , pp. 866-870
    • Martinez, M.G.1
  • 112
    • 35348849085 scopus 로고    scopus 로고
    • Human papillomavirus type 31 uses a caveolin 1- and dynamin 2-mediated entry pathway for infection of human keratinocytes
    • Smith J.L., et al. Human papillomavirus type 31 uses a caveolin 1- and dynamin 2-mediated entry pathway for infection of human keratinocytes. J. Virol. 2007, 81:9922-9931.
    • (2007) J. Virol. , vol.81 , pp. 9922-9931
    • Smith, J.L.1
  • 113
    • 0033937284 scopus 로고    scopus 로고
    • Cellular uptake and infection by canine parvovirus involves rapid dynamin-regulated clathrin-mediated endocytosis, followed by slower intracellular trafficking
    • Parker J.S., Parrish C.R. Cellular uptake and infection by canine parvovirus involves rapid dynamin-regulated clathrin-mediated endocytosis, followed by slower intracellular trafficking. J. Virol. 2000, 74:1919-1930.
    • (2000) J. Virol. , vol.74 , pp. 1919-1930
    • Parker, J.S.1    Parrish, C.R.2
  • 114
    • 34548449917 scopus 로고    scopus 로고
    • Poliovirus entry into human brain microvascular cells requires receptor-induced activation of SHP-2
    • Coyne C.B., et al. Poliovirus entry into human brain microvascular cells requires receptor-induced activation of SHP-2. EMBO J. 2007, 26:4016-4028.
    • (2007) EMBO J. , vol.26 , pp. 4016-4028
    • Coyne, C.B.1
  • 115
    • 0032541402 scopus 로고    scopus 로고
    • The clathrin endocytic pathway in viral infection
    • DeTulleo L., Kirchhausen T. The clathrin endocytic pathway in viral infection. EMBO J. 1998, 17:4585-4593.
    • (1998) EMBO J. , vol.17 , pp. 4585-4593
    • DeTulleo, L.1    Kirchhausen, T.2
  • 116
    • 80052064799 scopus 로고    scopus 로고
    • Entry of tiger frog virus (an Iridovirus) into HepG2 cells via a pH-dependent, atypical, caveola-mediated endocytosis pathway
    • Guo C.J., et al. Entry of tiger frog virus (an Iridovirus) into HepG2 cells via a pH-dependent, atypical, caveola-mediated endocytosis pathway. J. Virol. 2011, 85:6416-6426.
    • (2011) J. Virol. , vol.85 , pp. 6416-6426
    • Guo, C.J.1
  • 117
    • 84855274274 scopus 로고    scopus 로고
    • The membrane fusion step of vaccinia virus entry is cooperatively mediated by multiple viral proteins and host cell components
    • Laliberte J.P., et al. The membrane fusion step of vaccinia virus entry is cooperatively mediated by multiple viral proteins and host cell components. PLoS Pathog. 2011, 7:e1002446.
    • (2011) PLoS Pathog. , vol.7
    • Laliberte, J.P.1
  • 118
    • 66349113767 scopus 로고    scopus 로고
    • Vesicular stomatitis virus enters cells through vesicles incompletely coated with clathrin that depend upon actin for internalization
    • Cureton D.K., et al. Vesicular stomatitis virus enters cells through vesicles incompletely coated with clathrin that depend upon actin for internalization. PLoS Pathog. 2009, 5:e1000394.
    • (2009) PLoS Pathog. , vol.5
    • Cureton, D.K.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.