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Volumn 39, Issue 2, 2013, Pages 166-179

From endocytosis to membrane fusion: Emerging roles of dynamin in virus entry

Author keywords

Dynamin; Membrane fission; Membrane fusion; Virus entry

Indexed keywords

CLATHRIN; COAT PROTEIN; DYNAMIN; DYNAMIN I; DYNAMIN II; DYNAMIN III; PLECKSTRIN; PROTEIN;

EID: 84875923278     PISSN: 1040841X     EISSN: 15497828     Source Type: Journal    
DOI: 10.3109/1040841X.2012.694412     Document Type: Review
Times cited : (34)

References (127)
  • 1
    • 0032937051 scopus 로고    scopus 로고
    • Essential role of the dynamin pleckstrin homology domain in receptor-mediated endocytosis
    • Achiriloaie M, Barylko B, Albanesi JP. (1999). Essential role of the dynamin pleckstrin homology domain in receptor-mediated endocytosis. Mol Cell Biol, 19, 1410-1415.
    • (1999) Mol Cell Biol , vol.19 , pp. 1410-1415
    • Achiriloaie, M.1    Barylko, B.2    Albanesi, J.P.3
  • 2
    • 70350719853 scopus 로고    scopus 로고
    • Alternative infectious entry pathways for dengue virus serotypes into mammalian cells
    • Acosta EG, Castilla V, Damonte EB. (2009). Alternative infectious entry pathways for dengue virus serotypes into mammalian cells. Cell Microbiol, 11, 1533-1549.
    • (2009) Cell Microbiol , vol.11 , pp. 1533-1549
    • Acosta, E.G.1    Castilla, V.2    Damonte, E.B.3
  • 4
    • 76349086678 scopus 로고    scopus 로고
    • Localized topological changes of the plasma membrane upon exocytosis visualized by polarized TIRFM
    • Anantharam A, Onoa B, Edwards RH, Holz RW, Axelrod D. (2010). Localized topological changes of the plasma membrane upon exocytosis visualized by polarized TIRFM. J Cell Biol, 188, 415-428.
    • (2010) J Cell Biol , vol.188 , pp. 415-428
    • Anantharam, A.1    Onoa, B.2    Edwards, R.H.3    Holz, R.W.4    Axelrod, D.5
  • 5
    • 57649215874 scopus 로고    scopus 로고
    • GTPase cycle of dynamin is coupled to membrane squeeze and release, leading to spontaneous fssion
    • Bashkirov PV, Akimov SA, Evseev AI, Schmid SL, Zimmerberg J, Frolov VA. (2008). GTPase cycle of dynamin is coupled to membrane squeeze and release, leading to spontaneous fssion. Cell, 135, 1276-1286.
    • (2008) Cell , vol.135 , pp. 1276-1286
    • Bashkirov, P.V.1    Akimov, S.A.2    Evseev, A.I.3    Schmid, S.L.4    Zimmerberg, J.5    Frolov, V.A.6
  • 7
    • 38849103049 scopus 로고    scopus 로고
    • Equine infectious anemia virus entry occurs through clathrin-mediated endocytosis
    • Brindley MA, Maury W. (2008). Equine infectious anemia virus entry occurs through clathrin-mediated endocytosis. J Virol, 82, 1628-1637.
    • (2008) J Virol , vol.82 , pp. 1628-1637
    • Brindley, M.A.1    Maury, W.2
  • 8
    • 79951783943 scopus 로고    scopus 로고
    • A bacterial dynamin-like protein mediating nucleotide-independent membrane fusion
    • Bürmann F, Ebert N, van Baarle S, Bramkamp M. (2011). A bacterial dynamin-like protein mediating nucleotide-independent membrane fusion. Mol Microbiol, 79, 1294-1304.
    • (2011) Mol Microbiol , vol.79 , pp. 1294-1304
    • Bürmann, F.1    Ebert, N.2    Van Baarle, S.3    Bramkamp, M.4
  • 9
    • 0034094514 scopus 로고    scopus 로고
    • Disruption of Golgi structure and function in mammalian cells expressing a mutant dynamin
    • Cao H, Tompson HM, Krueger EW, McNiven MA. (2000). Disruption of Golgi structure and function in mammalian cells expressing a mutant dynamin. J Cell Sci, 113 (Pt 11), 1993-2002.
    • (2000) J Cell Sci , vol.113 , Issue.PART 11 , pp. 1993-2002
    • Cao, H.1    Tompson, H.M.2    Krueger, E.W.3    McNiven, M.A.4
  • 10
    • 77953023419 scopus 로고    scopus 로고
    • G domain dimerization controls dynamin's assembly-stimulated GTPase activity
    • Chappie JS, Acharya S, Leonard M, Schmid SL, Dyda F. (2010). G domain dimerization controls dynamin's assembly-stimulated GTPase activity. Nature, 465, 435-440.
    • (2010) Nature , vol.465 , pp. 435-440
    • Chappie, J.S.1    Acharya, S.2    Leonard, M.3    Schmid, S.L.4    Dyda, F.5
  • 13
    • 2542480756 scopus 로고    scopus 로고
    • The stalk region of dynamin drives the constriction of dynamin tubes
    • Chen YJ, Zhang P, Egelman EH, Hinshaw JE. (2004). The stalk region of dynamin drives the constriction of dynamin tubes. Nat Struct Mol Biol, 11, 574-575.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 574-575
    • Chen, Y.J.1    Zhang, P.2    Egelman, E.H.3    Hinshaw, J.E.4
  • 14
    • 33845601755 scopus 로고    scopus 로고
    • Cryo-electron tomography of clathrin-coated vesicles: Structural implications for coat assembly
    • Cheng Y, Boll W, Kirchhausen T, Harrison SC, Walz T. (2007). Cryo-electron tomography of clathrin-coated vesicles: structural implications for coat assembly. J Mol Biol, 365, 892-899.
    • (2007) J Mol Biol , vol.365 , pp. 892-899
    • Cheng, Y.1    Boll, W.2    Kirchhausen, T.3    Harrison, S.C.4    Walz, T.5
  • 15
    • 0037123766 scopus 로고    scopus 로고
    • Molecular architecture and functional model of the endocytic AP2 complex
    • Collins BM, McCoy AJ, Kent HM, Evans PR, Owen DJ. (2002). Molecular architecture and functional model of the endocytic AP2 complex. Cell, 109, 523-535.
    • (2002) Cell , vol.109 , pp. 523-535
    • Collins, B.M.1    McCoy, A.J.2    Kent, H.M.3    Evans, P.R.4    Owen, D.J.5
  • 16
    • 0037422066 scopus 로고    scopus 로고
    • Regulated portals of entry into the cell
    • Conner SD, Schmid SL. (2003). Regulated portals of entry into the cell. Nature, 422, 37-44.
    • (2003) Nature , vol.422 , pp. 37-44
    • Conner, S.D.1    Schmid, S.L.2
  • 17
    • 79954617024 scopus 로고    scopus 로고
    • Fusing structure and function: A structural view of the herpesvirus entry machinery
    • Connolly SA, Jackson JO, Jardetzky TS, Longnecker R. (2011). Fusing structure and function: a structural view of the herpesvirus entry machinery. Nat Rev Microbiol, 9, 369-381.
    • (2011) Nat Rev Microbiol , vol.9 , pp. 369-381
    • Connolly, S.A.1    Jackson, J.O.2    Jardetzky, T.S.3    Longnecker, R.4
  • 18
    • 34548449917 scopus 로고    scopus 로고
    • Poliovirus entry into human brain microvascular cells requires receptor-induced activation of SHP-2
    • Coyne CB, Kim KS, Bergelson JM. (2007). Poliovirus entry into human brain microvascular cells requires receptor-induced activation of SHP-2. EMBO J, 26, 4016-4028.
    • (2007) EMBO J , vol.26 , pp. 4016-4028
    • Coyne, C.B.1    Kim, K.S.2    Bergelson, J.M.3
  • 19
    • 84861307148 scopus 로고    scopus 로고
    • Limited transferrin receptor clustering allows rapid difusion of canine parvovirus into clathrin endocytic structures
    • Cureton DK, Harbison CE, Cocucci E, Parrish CR, Kirchhausen T. (2012). Limited transferrin receptor clustering allows rapid difusion of canine parvovirus into clathrin endocytic structures. J Virol, 86, 5330-5340.
    • (2012) J Virol , vol.86 , pp. 5330-5340
    • Cureton, D.K.1    Harbison, C.E.2    Cocucci, E.3    Parrish, C.R.4    Kirchhausen, T.5
  • 20
    • 66349113767 scopus 로고    scopus 로고
    • Vesicular stomatitis virus enters cells through vesicles incompletely coated with clathrin that depend upon actin for internalization
    • Cureton DK, Massol RH, Safarian S, Kirchhausen TL, Whelan SP. (2009). Vesicular stomatitis virus enters cells through vesicles incompletely coated with clathrin that depend upon actin for internalization. PLoS Pathog, 5, e1000394.
    • (2009) PLoS Pathog , vol.5
    • Cureton, D.K.1    Massol, R.H.2    Safarian, S.3    Kirchhausen, T.L.4    Whelan, S.P.5
  • 21
    • 13744252968 scopus 로고    scopus 로고
    • Involvement of clathrin-mediated endocytosis in human immunodefciency virus type 1 entry
    • Daecke J, Fackler OT, Dittmar MT, Kräusslich HG. (2005). Involvement of clathrin-mediated endocytosis in human immunodefciency virus type 1 entry. J Virol, 79, 1581-1594.
    • (2005) J Virol , vol.79 , pp. 1581-1594
    • Daecke, J.1    Fackler, O.T.2    Dittmar, M.T.3    Kräusslich, H.G.4
  • 26
    • 0027945789 scopus 로고
    • Crystal structure at 2.2 A resolution of the pleckstrin homology domain from human dynamin
    • Ferguson KM, Lemmon MA, Schlessinger J, Sigler PB. (1994). Crystal structure at 2.2 A resolution of the pleckstrin homology domain from human dynamin. Cell, 79, 199-209.
    • (1994) Cell , vol.79 , pp. 199-209
    • Ferguson, K.M.1    Lemmon, M.A.2    Schlessinger, J.3    Sigler, P.B.4
  • 27
    • 80053376521 scopus 로고    scopus 로고
    • The crystal structure of dynamin
    • Ford MG, Jenni S, Nunnari J. (2011). The crystal structure of dynamin. Nature, 477, 561-566.
    • (2011) Nature , vol.477 , pp. 561-566
    • Ford, M.G.1    Jenni, S.2    Nunnari, J.3
  • 29
    • 56149117291 scopus 로고    scopus 로고
    • Infectious adenovirus type 2 transport through early but not late endosomes
    • Gastaldelli M, Imelli N, Boucke K, Amstutz B, Meier O, Greber UF. (2008). Infectious adenovirus type 2 transport through early but not late endosomes. Trafc, 9, 2265-2278.
    • (2008) Trafc , vol.9 , pp. 2265-2278
    • Gastaldelli, M.1    Imelli, N.2    Boucke, K.3    Amstutz, B.4    Meier, O.5    Greber, U.F.6
  • 30
    • 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, Jackson T, Monaghan P, Doyle N, Roberts LO. (2010). Murine norovirus-1 cell entry is mediated through a non-clathrin-, non-caveolae-, dynamin-and cholesterol-dependent pathway. J Gen Virol, 91, 1428-1438.
    • (2010) J Gen Virol , vol.91 , pp. 1428-1438
    • Gerondopoulos, A.1    Jackson, T.2    Monaghan, P.3    Doyle, N.4    Roberts, L.O.5
  • 32
    • 78650663541 scopus 로고    scopus 로고
    • {alpha}V{beta}3-integrin routes herpes simplex virus to an entry pathway dependent on cholesterol-rich lipid rafts and dynamin2
    • Gianni T, Gatta V, Campadelli-Fiume G. (2010). {alpha}V{beta}3-integrin routes herpes simplex virus to an entry pathway dependent on cholesterol-rich lipid rafts and dynamin2. Proc Natl Acad Sci USA, 107, 22260-22265.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 22260-22265
    • Gianni, T.1    Gatta, V.2    Campadelli-Fiume, G.3
  • 34
    • 33745207365 scopus 로고    scopus 로고
    • Domain interactions within Fzo1 oligomers are essential for mitochondrial fusion
    • Grifn EE, Chan DC. (2006a). Domain interactions within Fzo1 oligomers are essential for mitochondrial fusion. J Biol Chem, 281, 16599-16606.
    • (2006) J Biol Chem , vol.281 , pp. 16599-16606
    • Grifn, E.E.1    Chan, D.C.2
  • 35
    • 33745758647 scopus 로고    scopus 로고
    • Molecular mechanism of mitochondrial membrane fusion
    • Grifn EE, Detmer SA, Chan DC. (2006b). Molecular mechanism of mitochondrial membrane fusion. Biochim Biophys Acta, 1763, 482-489.
    • (2006) Biochim Biophys Acta , vol.1763 , pp. 482-489
    • Grifn, E.E.1    Detmer, S.A.2    Chan, D.C.3
  • 36
    • 67949124782 scopus 로고    scopus 로고
    • Viruses and endosome membrane dynamics
    • Gruenberg J. (2009). Viruses and endosome membrane dynamics. Curr Opin Cell Biol, 21, 582-588.
    • (2009) Curr Opin Cell Biol , vol.21 , pp. 582-588
    • Gruenberg, J.1
  • 37
    • 33745859044 scopus 로고    scopus 로고
    • Mechanisms of pathogen entry through the endosomal compartments
    • Gruenberg J, van der Goot FG. (2006). Mechanisms of pathogen entry through the endosomal compartments. Nat Rev Mol Cell Biol, 7, 495-504.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 495-504
    • Gruenberg, J.1    Van Der Goot, F.G.2
  • 39
    • 77956035360 scopus 로고    scopus 로고
    • Diferent rotavirus strains enter MA104 cells through diferent endocytic pathways: The role of clathrin-mediated endocytosis
    • Gutiérrez M, Isa P, Sánchez-San Martin C, Pérez-Vargas J, Espinosa R, Arias CF, López S. (2010). Diferent rotavirus strains enter MA104 cells through diferent endocytic pathways: the role of clathrin-mediated endocytosis. J Virol, 84, 9161-9169.
    • (2010) J Virol , vol.84 , pp. 9161-9169
    • Gutiérrez, M.1    Isa, P.2    Sánchez-San Martin, C.3    Pérez-Vargas, J.4    Espinosa, R.5    Arias, C.F.6    López, S.7
  • 40
    • 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
    • Heikkilä O, Susi P, Tevaluoto T, Härmä H, Marjomäki V, Hyypiä T, Kiljunen S. (2010). Internalization of coxsackievirus A9 is mediated by {beta}2-microglobulin, dynamin, and Arf6 but not by caveolin-1 or clathrin. J Virol, 84, 3666-3681.
    • (2010) J Virol , vol.84 , pp. 3666-3681
    • Heikkilä, O.1    Susi, P.2    Tevaluoto, T.3    Härmä, H.4    Marjomäki, V.5    Hyypiä, T.6    Kiljunen, S.7
  • 41
    • 75449110786 scopus 로고    scopus 로고
    • Dynamin-and clathrin-dependent endocytosis in African swine fever virus entry
    • Hernaez B, Alonso C. (2010). Dynamin-and clathrin-dependent endocytosis in African swine fever virus entry. J Virol, 84, 2100-2109.
    • (2010) J Virol , vol.84 , pp. 2100-2109
    • Hernaez, B.1    Alonso, C.2
  • 42
    • 0028898261 scopus 로고
    • Dynamin self-assembles into rings suggesting a mechanism for coated vesicle budding
    • Hinshaw JE, Schmid SL. (1995). Dynamin self-assembles into rings suggesting a mechanism for coated vesicle budding. Nature, 374, 190-192.
    • (1995) Nature , vol.374 , pp. 190-192
    • Hinshaw, J.E.1    Schmid, S.L.2
  • 43
    • 56349103980 scopus 로고    scopus 로고
    • The molecular mechanism of mitochondrial fusion
    • Hoppins S, Nunnari J. (2009). The molecular mechanism of mitochondrial fusion. Biochim Biophys Acta, 1793, 20-26.
    • (2009) Biochim Biophys Acta , vol.1793 , pp. 20-26
    • Hoppins, S.1    Nunnari, J.2
  • 44
    • 49149122454 scopus 로고    scopus 로고
    • A novel cellular protein, VPEF, facilitates vaccinia virus penetration into HeLa cells through fuid phase endocytosis
    • Huang CY, Lu TY, Bair CH, Chang YS, Jwo JK, Chang W. (2008). A novel cellular protein, VPEF, facilitates vaccinia virus penetration into HeLa cells through fuid phase endocytosis. J Virol, 82, 7988-7999.
    • (2008) J Virol , vol.82 , pp. 7988-7999
    • Huang, C.Y.1    Lu, T.Y.2    Bair, C.H.3    Chang, Y.S.4    Jwo, J.K.5    Chang, W.6
  • 45
    • 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 WR, Wang YC, Chi PI, Wang L, Wang CY, Lin CH, Liu HJ. (2011). 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, 286, 30780-30794.
    • (2011) J Biol Chem , vol.286 , pp. 30780-30794
    • Huang, W.R.1    Wang, Y.C.2    Chi, P.I.3    Wang, L.4    Wang, C.Y.5    Lin, C.H.6    Liu, H.J.7
  • 46
    • 34547743810 scopus 로고    scopus 로고
    • Clathrin-dependent entry of severe acute respiratory syndrome coronavirus into target cells expressing ACE2 with the cytoplasmic tail deleted
    • Inoue Y, Tanaka N, Tanaka Y, Inoue S, Morita K, Zhuang M, Hattori T, Sugamura K. (2007). Clathrin-dependent entry of severe acute respiratory syndrome coronavirus into target cells expressing ACE2 with the cytoplasmic tail deleted. J Virol, 81, 8722-8729.
    • (2007) J Virol , vol.81 , pp. 8722-8729
    • Inoue, Y.1    Tanaka, N.2    Tanaka, Y.3    Inoue, S.4    Morita, K.5    Zhuang, M.6    Hattori, T.7    Sugamura, K.8
  • 47
    • 0038222569 scopus 로고    scopus 로고
    • Clathrin-coated pits with long, dynamin-wrapped necks upon expression of a clathrin antisense RNA
    • Iversen TG, Skretting G, van Deurs B, Sandvig K. (2003). Clathrin-coated pits with long, dynamin-wrapped necks upon expression of a clathrin antisense RNA. Proc Natl Acad Sci USA, 100, 5175-5180.
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 5175-5180
    • Iversen, T.G.1    Skretting, G.2    Van Deurs, B.3    Sandvig, K.4
  • 48
    • 77953884976 scopus 로고    scopus 로고
    • A large-scale conformational change couples membrane recruitment to cargo binding in the AP2 clathrin adaptor complex
    • Jackson LP, Kelly BT, McCoy AJ, Gafry T, James LC, Collins BM, Höning S, Evans PR, Owen DJ. (2010). A large-scale conformational change couples membrane recruitment to cargo binding in the AP2 clathrin adaptor complex. Cell, 141, 1220-1229.
    • (2010) Cell , vol.141 , pp. 1220-1229
    • Jackson, L.P.1    Kelly, B.T.2    McCoy, A.J.3    Gafry, T.4    James, L.C.5    Collins, B.M.6    Höning, S.7    Evans, P.R.8    Owen, D.J.9
  • 50
    • 58149390171 scopus 로고    scopus 로고
    • Host cell factors and functions involved in vesicular stomatitis virus entry
    • Johannsdottir HK, Mancini R, Kartenbeck J, Amato L, Helenius A. (2009). Host cell factors and functions involved in vesicular stomatitis virus entry. J Virol, 83, 440-453.
    • (2009) J Virol , vol.83 , pp. 440-453
    • Johannsdottir, H.K.1    Mancini, R.2    Kartenbeck, J.3    Amato, L.4    Helenius, A.5
  • 52
    • 57749196168 scopus 로고    scopus 로고
    • A structural explanation for the binding of endocytic dileucine motifs by the AP2 complex
    • Kelly BT, McCoy AJ, Späte K, Miller SE, Evans PR, Höning S, Owen DJ. (2008). A structural explanation for the binding of endocytic dileucine motifs by the AP2 complex. Nature, 456, 976-979.
    • (2008) Nature , vol.456 , pp. 976-979
    • Kelly, B.T.1    McCoy, A.J.2    Späte, K.3    Miller, S.E.4    Evans, P.R.5    Höning, S.6    Owen, D.J.7
  • 53
    • 33644838018 scopus 로고    scopus 로고
    • Clathrin-independent endocytosis: New insights into caveolae and non-caveolar lipid raft carriers
    • Kirkham M, Parton RG. (2005). Clathrin-independent endocytosis: new insights into caveolae and non-caveolar lipid raft carriers. Biochim Biophys Acta, 1746, 349-363.
    • (2005) Biochim Biophys Acta , vol.1746 , pp. 349-363
    • Kirkham, M.1    Parton, R.G.2
  • 54
    • 0020603664 scopus 로고
    • Possible temperature-dependent blockage of synaptic vesicle recycling induced by a single gene mutation in Drosophila
    • Kosaka T, Ikeda K. (1983). Possible temperature-dependent blockage of synaptic vesicle recycling induced by a single gene mutation in Drosophila. J Neurobiol, 14, 207-225.
    • (1983) J Neurobiol , vol.14 , pp. 207-225
    • Kosaka, T.1    Ikeda, K.2
  • 57
    • 34548150618 scopus 로고    scopus 로고
    • Regulation of raft-dependent endocytosis
    • Lajoie P, Nabi IR. (2007). Regulation of raft-dependent endocytosis. J Cell Mol Med, 11, 644-653.
    • (2007) J Cell Mol Med , vol.11 , pp. 644-653
    • Lajoie, P.1    Nabi, I.R.2
  • 58
    • 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, Weisberg AS, Moss B. (2011). The membrane fusion step of vaccinia virus entry is cooperatively mediated by multiple viral proteins and host cell components. PLoS Pathog, 7, e1002446.
    • (2011) PLoS Pathog , vol.7
    • Laliberte, J.P.1    Weisberg, A.S.2    Moss, B.3
  • 59
    • 30544447100 scopus 로고    scopus 로고
    • Robust colorimetric assays for dynamin's basal and stimulated GTPase activities
    • Leonard M, Song BD, Ramachandran R, Schmid SL. (2005). Robust colorimetric assays for dynamin's basal and stimulated GTPase activities. Meth Enzymol, 404, 490-503.
    • (2005) Meth Enzymol , vol.404 , pp. 490-503
    • Leonard, M.1    Song, B.D.2    Ramachandran, R.3    Schmid, S.L.4
  • 62
    • 2542489194 scopus 로고    scopus 로고
    • Multistep entry of rotavirus into cells: A Versaillesque dance
    • López S, Arias CF. (2004). Multistep entry of rotavirus into cells: a Versaillesque dance. Trends Microbiol, 12, 271-278.
    • (2004) Trends Microbiol , vol.12 , pp. 271-278
    • López, S.1    Arias, C.F.2
  • 64
    • 62149144498 scopus 로고    scopus 로고
    • SNX9-A prelude to vesicle release
    • Lundmark R, Carlsson SR. (2009). SNX9-a prelude to vesicle release. J Cell Sci, 122, 5-11.
    • (2009) J Cell Sci , vol.122 , pp. 5-11
    • Lundmark, R.1    Carlsson, S.R.2
  • 68
  • 69
    • 32944473016 scopus 로고    scopus 로고
    • Virus entry: Open sesame
    • Marsh M, Helenius A. (2006). Virus entry: open sesame. Cell, 124, 729-740.
    • (2006) Cell , vol.124 , pp. 729-740
    • Marsh, M.1    Helenius, A.2
  • 70
    • 79960720320 scopus 로고    scopus 로고
    • Molecular mechanism and physiological functions of clathrin-mediated endocytosis
    • McMahon HT, Boucrot E. (2011). Molecular mechanism and physiological functions of clathrin-mediated endocytosis. Nat Rev Mol Cell Biol, 12, 517-533.
    • (2011) Nat Rev Mol Cell Biol , vol.12 , pp. 517-533
    • McMahon, H.T.1    Boucrot, E.2
  • 71
    • 35148862219 scopus 로고    scopus 로고
    • A corkscrew model for dynamin constriction
    • Mears JA, Ray P, Hinshaw JE. (2007). A corkscrew model for dynamin constriction. Structure, 15, 1190-1202.
    • (2007) Structure , vol.15 , pp. 1190-1202
    • Mears, J.A.1    Ray, P.2    Hinshaw, J.E.3
  • 72
    • 33751223214 scopus 로고    scopus 로고
    • Hepatitis C virus entry requires a critical postinternalization step and delivery to early endosomes via clathrin-coated vesicles
    • Meertens L, Bertaux C, Dragic T. (2006). Hepatitis C virus entry requires a critical postinternalization step and delivery to early endosomes via clathrin-coated vesicles. J Virol, 80, 11571-11578.
    • (2006) J Virol , vol.80 , pp. 11571-11578
    • Meertens, L.1    Bertaux, C.2    Dragic, T.3
  • 73
    • 42549153337 scopus 로고    scopus 로고
    • Vaccinia virus uses macropinocytosis and apoptotic mimicry to enter host cells
    • Mercer J, Helenius A. (2008). Vaccinia virus uses macropinocytosis and apoptotic mimicry to enter host cells. Science, 320, 531-535.
    • (2008) Science , vol.320 , pp. 531-535
    • Mercer, J.1    Helenius, A.2
  • 74
    • 65449120034 scopus 로고    scopus 로고
    • Virus entry by macropinocytosis
    • Mercer J, Helenius A. (2009). Virus entry by macropinocytosis. Nat Cell Biol, 11, 510-520.
    • (2009) Nat Cell Biol , vol.11 , pp. 510-520
    • Mercer, J.1    Helenius, A.2
  • 77
    • 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. (2009). HIV enters cells via endocytosis and dynamin-dependent fusion with endosomes. Cell, 137, 433-444.
    • (2009) Cell , vol.137 , pp. 433-444
    • Miyauchi, K.1    Kim, Y.2    Latinovic, O.3    Morozov, V.4    Melikyan, G.B.5
  • 78
    • 0030809132 scopus 로고    scopus 로고
    • Domain structure and intramolecular regulation of dynamin GTPase
    • Muhlberg AB, Warnock DE, Schmid SL. (1997). Domain structure and intramolecular regulation of dynamin GTPase. EMBO J, 16, 6676-6683.
    • (1997) EMBO J , vol.16 , pp. 6676-6683
    • Muhlberg, A.B.1    Warnock, D.E.2    Schmid, S.L.3
  • 79
    • 17644424000 scopus 로고    scopus 로고
    • An internal GAP domain negatively regulates presynaptic dynamin in vivo: A two-step model for dynamin function
    • Narayanan R, Leonard M, Song BD, Schmid SL, Ramaswami M. (2005). An internal GAP domain negatively regulates presynaptic dynamin in vivo: a two-step model for dynamin function. J Cell Biol, 169, 117-126.
    • (2005) J Cell Biol , vol.169 , pp. 117-126
    • Narayanan, R.1    Leonard, M.2    Song, B.D.3    Schmid, S.L.4    Ramaswami, M.5
  • 80
    • 0345706824 scopus 로고    scopus 로고
    • Caveosomes and endocytosis of lipid rafts
    • Nichols B. (2003). Caveosomes and endocytosis of lipid rafts. J Cell Sci, 116, 4707-4714.
    • (2003) J Cell Sci , vol.116 , pp. 4707-4714
    • Nichols, B.1
  • 81
    • 83655164541 scopus 로고    scopus 로고
    • Adeno-associated virus 2 infection requires endocytosis through the CLIC/GEEC pathway
    • Nonnenmacher M, Weber T. (2011). Adeno-associated virus 2 infection requires endocytosis through the CLIC/GEEC pathway. Cell Host Microbe, 10, 563-576.
    • (2011) Cell Host Microbe , vol.10 , pp. 563-576
    • Nonnenmacher, M.1    Weber, T.2
  • 82
    • 78650435425 scopus 로고    scopus 로고
    • Intersecting pathways in cell biology
    • O'Bryan JP. (2010). Intersecting pathways in cell biology. Sci Signal, 3, re10.
    • (2010) Sci Signal , vol.3
    • O'Bryan, J.P.1
  • 83
    • 0032489880 scopus 로고    scopus 로고
    • Dynamin at the neck of caveolae mediates their budding to form transport vesicles by GTP-driven fssion from the plasma membrane of endothelium
    • Oh P, McIntosh DP, Schnitzer JE. (1998). Dynamin at the neck of caveolae mediates their budding to form transport vesicles by GTP-driven fssion from the plasma membrane of endothelium. J Cell Biol, 141, 101-114.
    • (1998) J Cell Biol , vol.141 , pp. 101-114
    • Oh, P.1    McIntosh, D.P.2    Schnitzer, J.E.3
  • 85
    • 44949131548 scopus 로고    scopus 로고
    • Recombinant protein of heptad-repeat HR212, a stable fusion inhibitor with potent anti-HIV action in vitro
    • Pang W, Wang RR, Yang LM, Liu CM, Tien P, Zheng YT. (2008). Recombinant protein of heptad-repeat HR212, a stable fusion inhibitor with potent anti-HIV action in vitro. Virology, 377, 80-87.
    • (2008) Virology , vol.377 , pp. 80-87
    • Pang, W.1    Wang, R.R.2    Yang, L.M.3    Liu, C.M.4    Tien, P.5    Zheng, Y.T.6
  • 87
    • 0035017308 scopus 로고    scopus 로고
    • Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER
    • Pelkmans L, Kartenbeck J, Helenius A. (2001). Caveolar endocytosis of simian virus 40 reveals a new two-step vesicular-transport pathway to the ER. Nat Cell Biol, 3, 473-483.
    • (2001) Nat Cell Biol , vol.3 , pp. 473-483
    • Pelkmans, L.1    Kartenbeck, J.2    Helenius, A.3
  • 88
    • 0037134014 scopus 로고    scopus 로고
    • Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae
    • Pelkmans L, Püntener D, Helenius A. (2002). Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae. Science, 296, 535-539.
    • (2002) Science , vol.296 , pp. 535-539
    • Pelkmans, L.1    Püntener, D.2    Helenius, A.3
  • 90
    • 77952693635 scopus 로고    scopus 로고
    • Endocytosis of murine norovirus 1 into murine macrophages is dependent on dynamin II and cholesterol
    • Perry JW, Wobus CE. (2010). Endocytosis of murine norovirus 1 into murine macrophages is dependent on dynamin II and cholesterol. J Virol, 84, 6163-6176.
    • (2010) J Virol , vol.84 , pp. 6163-6176
    • Perry, J.W.1    Wobus, C.E.2
  • 92
    • 6344275643 scopus 로고    scopus 로고
    • Echovirus 1 endocytosis into caveosomes requires lipid rafts, dynamin II, and signaling events
    • Pietiäinen V, Marjomäki V, Upla P, Pelkmans L, Helenius A, Hyypiä T. (2004). Echovirus 1 endocytosis into caveosomes requires lipid rafts, dynamin II, and signaling events. Mol Biol Cell, 15, 4911-4925.
    • (2004) Mol Biol Cell , vol.15 , pp. 4911-4925
    • Pietiäinen, V.1    Marjomäki, V.2    Upla, P.3    Pelkmans, L.4    Helenius, A.5    Hyypiä, T.6
  • 93
    • 67650809304 scopus 로고    scopus 로고
    • Cell biology: Ahead of the curve
    • Powell K. (2009). Cell biology: ahead of the curve. Nature, 460, 318-320.
    • (2009) Nature , vol.460 , pp. 318-320
    • Powell, K.1
  • 94
    • 0742288598 scopus 로고    scopus 로고
    • The dynamin superfamily: Universal membrane tubulation and fssion molecules?
    • Praefcke GJ, McMahon HT. (2004). The dynamin superfamily: universal membrane tubulation and fssion molecules? Nat Rev Mol Cell Biol, 5, 133-147.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , pp. 133-147
    • Praefcke, G.J.1    McMahon, H.T.2
  • 95
    • 57649238675 scopus 로고    scopus 로고
    • Real-time visualization of dynamin-catalyzed membrane fssion and vesicle release
    • Pucadyil TJ, Schmid SL. (2008). Real-time visualization of dynamin-catalyzed membrane fssion and vesicle release. Cell, 135, 1263-1275.
    • (2008) Cell , vol.135 , pp. 1263-1275
    • Pucadyil, T.J.1    Schmid, S.L.2
  • 96
    • 69949183624 scopus 로고    scopus 로고
    • Conserved functions of membrane active GTPases in coated vesicle formation
    • Pucadyil TJ, Schmid SL. (2009). Conserved functions of membrane active GTPases in coated vesicle formation. Science, 325, 1217-1220.
    • (2009) Science , vol.325 , pp. 1217-1220
    • Pucadyil, T.J.1    Schmid, S.L.2
  • 98
    • 80054000888 scopus 로고    scopus 로고
    • Entry pathways of herpes simplex virus type 1 into human keratinocytes are dynamin-and cholesterol-dependent
    • Rahn E, Petermann P, Hsu MJ, Rixon FJ, Knebel-Mörsdorf D. (2011). Entry pathways of herpes simplex virus type 1 into human keratinocytes are dynamin-and cholesterol-dependent. PLoS ONE, 6, e25464.
    • (2011) PLoS ONE , vol.6
    • Rahn, E.1    Petermann, P.2    Hsu, M.J.3    Rixon, F.J.4    Knebel-Mörsdorf, D.5
  • 100
    • 47749148446 scopus 로고    scopus 로고
    • Diferent mechanisms of cell entry by human-pathogenic Old World and New World arenaviruses
    • Rojek JM, Sanchez AB, Nguyen NT, de la Torre JC, Kunz S. (2008). Diferent mechanisms of cell entry by human-pathogenic Old World and New World arenaviruses. J Virol, 82, 7677-7687.
    • (2008) J Virol , vol.82 , pp. 7677-7687
    • Rojek, J.M.1    Sanchez, A.B.2    Nguyen, N.T.3    De La Torre, J.C.4    Kunz, S.5
  • 101
    • 33745026786 scopus 로고    scopus 로고
    • GTP-dependent twisting of dynamin implicates constriction and tension in membrane fssion
    • Roux A, Uyhazi K, Frost A, De Camilli P. (2006). GTP-dependent twisting of dynamin implicates constriction and tension in membrane fssion. Nature, 441, 528-531.
    • (2006) Nature , vol.441 , pp. 528-531
    • Roux, A.1    Uyhazi, K.2    Frost, A.3    De Camilli, P.4
  • 102
    • 2542452779 scopus 로고    scopus 로고
    • Assembly of endocytic machinery around individual infuenza viruses during viral entry
    • Rust MJ, Lakadamyali M, Zhang F, Zhuang X. (2004). Assembly of endocytic machinery around individual infuenza viruses during viral entry. Nat Struct Mol Biol, 11, 567-573.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 567-573
    • Rust, M.J.1    Lakadamyali, M.2    Zhang, F.3    Zhuang, X.4
  • 103
    • 78249252059 scopus 로고    scopus 로고
    • Come in and take your coat of-how host cells provide endocytosis for virus entry
    • Schelhaas M. (2010). Come in and take your coat of-how host cells provide endocytosis for virus entry. Cell Microbiol, 12, 1378-1388.
    • (2010) Cell Microbiol , vol.12 , pp. 1378-1388
    • Schelhaas, M.1
  • 105
    • 34548176765 scopus 로고    scopus 로고
    • Integrating molecular and network biology to decode endocytosis
    • Schmid EM, McMahon HT. (2007). Integrating molecular and network biology to decode endocytosis. Nature, 448, 883-888.
    • (2007) Nature , vol.448 , pp. 883-888
    • Schmid, E.M.1    McMahon, H.T.2
  • 106
    • 80052248915 scopus 로고    scopus 로고
    • Dynamin: Functional design of a membrane fssion catalyst
    • Schmid SL, Frolov VA. (2011). Dynamin: functional design of a membrane fssion catalyst. Annu Rev Cell Dev Biol, 27, 79-105.
    • (2011) Annu Rev Cell Dev Biol , vol.27 , pp. 79-105
    • Schmid, S.L.1    Frolov, V.A.2
  • 108
    • 0030001553 scopus 로고    scopus 로고
    • Role of GTP hydrolysis in fssion of caveolae directly from plasma membranes (vol 274, pg 239, 1996)
    • Schnitzer JE. (1996). Role of GTP hydrolysis in fssion of caveolae directly from plasma membranes (vol 274, pg 239, 1996). Science, 274, 1069.
    • (1996) Science , vol.274 , pp. 1069
    • Schnitzer, J.E.1
  • 109
    • 0034605101 scopus 로고    scopus 로고
    • Dynamin:GTP controls the formation of constricted coated pits, the rate limiting step in clathrin-mediated endocytosis
    • Sever S, Damke H, Schmid SL. (2000). Dynamin:GTP controls the formation of constricted coated pits, the rate limiting step in clathrin-mediated endocytosis. J Cell Biol, 150, 1137-1148.
    • (2000) J Cell Biol , vol.150 , pp. 1137-1148
    • Sever, S.1    Damke, H.2    Schmid, S.L.3
  • 110
    • 0033535593 scopus 로고    scopus 로고
    • Impairment of dynamin's GAP domain stimulates receptor-mediated endocytosis
    • Sever S, Muhlberg AB, Schmid SL. (1999). Impairment of dynamin's GAP domain stimulates receptor-mediated endocytosis. Nature, 398, 481-486.
    • (1999) Nature , vol.398 , pp. 481-486
    • Sever, S.1    Muhlberg, A.B.2    Schmid, S.L.3
  • 111
    • 0024342278 scopus 로고
    • Identifcation of dynamin, a novel mechanochemical enzyme that mediates interactions between microtubules
    • Shpetner HS, Vallee RB. (1989). Identifcation of dynamin, a novel mechanochemical enzyme that mediates interactions between microtubules. Cell, 59, 421-432.
    • (1989) Cell , vol.59 , pp. 421-432
    • Shpetner, H.S.1    Vallee, R.B.2
  • 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 JL, Campos SK, Ozbun MA. (2007). Human papillomavirus type 31 uses a caveolin 1-and dynamin 2-mediated entry pathway for infection of human keratinocytes. J Virol, 81, 9922-9931.
    • (2007) J Virol , vol.81 , pp. 9922-9931
    • Smith, J.L.1    Campos, S.K.2    Ozbun, M.A.3
  • 113
    • 0037452537 scopus 로고    scopus 로고
    • A molecular motor or a regulator? Dynamin's in a class of its own
    • Song BD, Schmid SL. (2003). A molecular motor or a regulator? Dynamin's in a class of its own. Biochemistry, 42, 1369-1376.
    • (2003) Biochemistry , vol.42 , pp. 1369-1376
    • Song, B.D.1    Schmid, S.L.2
  • 114
    • 0033128097 scopus 로고    scopus 로고
    • Nucleotide-dependent conformational changes in dynamin: Evidence for a mechanochemical molecular spring
    • Stowell MH, Marks B, Wigge P, McMahon HT. (1999). Nucleotide-dependent conformational changes in dynamin: evidence for a mechanochemical molecular spring. Nat Cell Biol, 1, 27-32.
    • (1999) Nat Cell Biol , vol.1 , pp. 27-32
    • Stowell, M.H.1    Marks, B.2    Wigge, P.3    McMahon, H.T.4
  • 115
    • 0032511190 scopus 로고    scopus 로고
    • Dynamin undergoes a GTP-dependent conformational change causing vesiculation
    • Sweitzer SM, Hinshaw JE. (1998). Dynamin undergoes a GTP-dependent conformational change causing vesiculation. Cell, 93, 1021-1029.
    • (1998) Cell , vol.93 , pp. 1021-1029
    • Sweitzer, S.M.1    Hinshaw, J.E.2
  • 117
    • 0028923349 scopus 로고
    • Tubular membrane invaginations coated by dynamin rings are induced by GTP-gamma S in nerve terminals
    • Takei K, McPherson PS, Schmid SL, De Camilli P. (1995). Tubular membrane invaginations coated by dynamin rings are induced by GTP-gamma S in nerve terminals. Nature, 374, 186-190.
    • (1995) Nature , vol.374 , pp. 186-190
    • Takei, K.1    McPherson, P.S.2    Schmid, S.L.3    De Camilli, P.4
  • 119
    • 52649098867 scopus 로고    scopus 로고
    • Clathrin-and caveolae-independent entry of feline infectious peritonitis virus in monocytes depends on dynamin
    • Van Hamme E, Dewerchin HL, Cornelissen E, Verhasselt B, Nauwynck HJ. (2008). Clathrin-and caveolae-independent entry of feline infectious peritonitis virus in monocytes depends on dynamin. J Gen Virol, 89, 2147-2156.
    • (2008) J Gen Virol , vol.89 , pp. 2147-2156
    • Van Hamme, E.1    Dewerchin, H.L.2    Cornelissen, E.3    Verhasselt, B.4    Nauwynck, H.J.5
  • 120
    • 45849110264 scopus 로고    scopus 로고
    • Pichindé virus is trafcked through a dynamin 2 endocytic pathway that is dependent on cellular Rab5-and Rab7-mediated endosomes
    • Vela EM, Colpitts TM, Zhang L, Davey RA, Aronson J F. (2008). Pichindé virus is trafcked through a dynamin 2 endocytic pathway that is dependent on cellular Rab5-and Rab7-mediated endosomes. Arch Virol, 153, 1391-1396.
    • (2008) Arch Virol , vol.153 , pp. 1391-1396
    • Vela, E.M.1    Colpitts, T.M.2    Zhang, L.3    Davey, R.A.4    Aronson, J.F.5
  • 121
    • 22744447453 scopus 로고    scopus 로고
    • Rab7 associates with early endosomes to mediate sorting and transport of Semliki forest virus to late endosomes
    • Vonderheit A, Helenius A. (2005). Rab7 associates with early endosomes to mediate sorting and transport of Semliki forest virus to late endosomes. PLoS Biol, 3, e233.
    • (2005) PLoS Biol , vol.3
    • Vonderheit, A.1    Helenius, A.2
  • 122
    • 53049089051 scopus 로고    scopus 로고
    • Structure and plasticity of Endophilin and Sorting Nexin 9
    • Wang Q, Kaan HY, Hooda RN, Goh SL, Sondermann H. (2008). Structure and plasticity of Endophilin and Sorting Nexin 9. Structure, 16, 1574-1587.
    • (2008) Structure , vol.16 , pp. 1574-1587
    • Wang, Q.1    Kaan, H.Y.2    Hooda, R.N.3    Goh, S.L.4    Sondermann, H.5
  • 124
    • 3142663245 scopus 로고    scopus 로고
    • Structural basis for coronavirus-mediated membrane fusion. Crystal structure of mouse hepatitis virus spike protein fusion core
    • Xu Y, Liu Y, Lou Z, Qin L, Li X, Bai Z, Pang H, Tien P, Gao G F, Rao Z. (2004). Structural basis for coronavirus-mediated membrane fusion. Crystal structure of mouse hepatitis virus spike protein fusion core. J Biol Chem, 279, 30514-30522.
    • (2004) J Biol Chem , vol.279 , pp. 30514-30522
    • Xu, Y.1    Liu, Y.2    Lou, Z.3    Qin, L.4    Li, X.5    Bai, Z.6    Pang, H.7    Tien, P.8    Gao, G.F.9    Rao, Z.10
  • 125
    • 2442691605 scopus 로고    scopus 로고
    • PH-dependent entry of severe acute respiratory syndrome coronavirus is mediated by the spike glycoprotein and enhanced by dendritic cell transfer through DC-SIGN
    • Yang ZY, Huang Y, Ganesh L, Leung K, Kong WP, Schwartz O, Subbarao K, Nabel GJ. (2004). pH-dependent entry of severe acute respiratory syndrome coronavirus is mediated by the spike glycoprotein and enhanced by dendritic cell transfer through DC-SIGN. J Virol, 78, 5642-5650.
    • (2004) J Virol , vol.78 , pp. 5642-5650
    • Yang, Z.Y.1    Huang, Y.2    Ganesh, L.3    Leung, K.4    Kong, W.P.5    Schwartz, O.6    Subbarao, K.7    Nabel, G.J.8
  • 126
    • 0034784987 scopus 로고    scopus 로고
    • Tree-dimensional reconstruction of dynamin in the constricted state
    • Zhang P, Hinshaw JE. (2001). Tree-dimensional reconstruction of dynamin in the constricted state. Nat Cell Biol, 3, 922-926.
    • (2001) Nat Cell Biol , vol.3 , pp. 922-926
    • Zhang, P.1    Hinshaw, J.E.2
  • 127
    • 27744533984 scopus 로고    scopus 로고
    • Design and characterization of viral polypeptide inhibitors targeting Newcastle disease virus fusion
    • Zhu J, Jiang X, Liu Y, Tien P, Gao GF. (2005). Design and characterization of viral polypeptide inhibitors targeting Newcastle disease virus fusion. J Mol Biol, 354, 601-613.
    • (2005) J Mol Biol , vol.354 , pp. 601-613
    • Zhu, J.1    Jiang, X.2    Liu, Y.3    Tien, P.4    Gao, G.F.5


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