메뉴 건너뛰기




Volumn , Issue , 2016, Pages 103-119

Rotavirus Attachment, Internalization, and Vesicular Traffic

Author keywords

Attachment and postattachment interactions; Endocytosis; ESCRT machinery; Glycans; Receptors and coreceptors; Vesicular traffic; Virus entry

Indexed keywords


EID: 84987778376     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1016/B978-0-12-802241-2.00006-7     Document Type: Chapter
Times cited : (7)

References (57)
  • 1
    • 84907587065 scopus 로고    scopus 로고
    • Structural correlates of rotavirus cell entry
    • Abdelhakim A.H., Salgado E.N., Fu X., et al. Structural correlates of rotavirus cell entry. PLoS Pathog. 2014, 10:e1004355.
    • (2014) PLoS Pathog. , vol.10 , pp. e1004355
    • Abdelhakim, A.H.1    Salgado, E.N.2    Fu, X.3
  • 2
    • 33847757520 scopus 로고    scopus 로고
    • Insight into host cell carbohydrate-recognition by human and porcine rotavirus from crystal structures of the virion spike associated carbohydrate-binding domain (VP8*)
    • Blanchard H., Yu X., Coulson B.S., von Itzstein M. Insight into host cell carbohydrate-recognition by human and porcine rotavirus from crystal structures of the virion spike associated carbohydrate-binding domain (VP8*). J. Mol. Biol. 2007, 367:1215-1226.
    • (2007) J. Mol. Biol. , vol.367 , pp. 1215-1226
    • Blanchard, H.1    Yu, X.2    Coulson, B.S.3    von Itzstein, M.4
  • 3
    • 84938313711 scopus 로고    scopus 로고
    • Revisiting the role of histo-blood group antigens in rotavirus host-cell invasion
    • Bohm R., Fleming F.E., Maggioni A., et al. Revisiting the role of histo-blood group antigens in rotavirus host-cell invasion. Nat. Commun. 2015, 6:5907.
    • (2015) Nat. Commun. , vol.6 , pp. 5907
    • Bohm, R.1    Fleming, F.E.2    Maggioni, A.3
  • 5
    • 19144365133 scopus 로고    scopus 로고
    • Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection
    • Chandran K., Sullivan N.J., Felbor U., Whelan S.P., Cunningham J.M. Endosomal proteolysis of the Ebola virus glycoprotein is necessary for infection. Science 2005, 308:1643-1645.
    • (2005) Science , vol.308 , pp. 1643-1645
    • Chandran, K.1    Sullivan, N.J.2    Felbor, U.3    Whelan, S.P.4    Cunningham, J.M.5
  • 6
    • 0035128179 scopus 로고    scopus 로고
    • Glycosphingolipid binding specificities of rotavirus: identification of a sialic acid-binding epitope
    • Delorme C., Brussow H., Sidoti J., et al. Glycosphingolipid binding specificities of rotavirus: identification of a sialic acid-binding epitope. J. Virol. 2001, 75:2276-2287.
    • (2001) J. Virol. , vol.75 , pp. 2276-2287
    • Delorme, C.1    Brussow, H.2    Sidoti, J.3
  • 7
    • 84873029314 scopus 로고    scopus 로고
    • The spike protein VP4 defines the endocytic pathway used by rotavirus to enter MA104 cells
    • Diaz-Salinas M.A., Romero P., Espinosa R., Hoshino Y., Lopez S., Arias C.F. The spike protein VP4 defines the endocytic pathway used by rotavirus to enter MA104 cells. J. Virol. 2013, 87:1658-1663.
    • (2013) J. Virol. , vol.87 , pp. 1658-1663
    • Diaz-Salinas, M.A.1    Romero, P.2    Espinosa, R.3    Hoshino, Y.4    Lopez, S.5    Arias, C.F.6
  • 8
    • 84897003474 scopus 로고    scopus 로고
    • Rotaviruses reach late endosomes and require the cation-dependent mannose-6-phosphate receptor and the activity of cathepsin proteases to enter the cell
    • Diaz-Salinas M.A., Silva-Ayala D., Lopez S., Arias C.F. Rotaviruses reach late endosomes and require the cation-dependent mannose-6-phosphate receptor and the activity of cathepsin proteases to enter the cell. J. Virol. 2014, 88:4389-4402.
    • (2014) J. Virol. , vol.88 , pp. 4389-4402
    • Diaz-Salinas, M.A.1    Silva-Ayala, D.2    Lopez, S.3    Arias, C.F.4
  • 9
    • 84861309290 scopus 로고    scopus 로고
    • Activation of the Nipah virus fusion protein in MDCK cells is mediated by cathepsin B within the endosome-recycling compartment
    • Diederich S., Sauerhering L., Weis M., et al. Activation of the Nipah virus fusion protein in MDCK cells is mediated by cathepsin B within the endosome-recycling compartment. J. Virol. 2012, 86:3736-3745.
    • (2012) J. Virol. , vol.86 , pp. 3736-3745
    • Diederich, S.1    Sauerhering, L.2    Weis, M.3
  • 10
    • 0036500085 scopus 로고    scopus 로고
    • The rhesus rotavirus VP4 sialic acid binding domain has a galectin fold with a novel carbohydrate binding site
    • Dormitzer P.R., Sun Z.Y., Wagner G., Harrison S.C. The rhesus rotavirus VP4 sialic acid binding domain has a galectin fold with a novel carbohydrate binding site. Embo J. 2002, 21:885-897.
    • (2002) Embo J. , vol.21 , pp. 885-897
    • Dormitzer, P.R.1    Sun, Z.Y.2    Wagner, G.3    Harrison, S.C.4
  • 11
    • 0037025342 scopus 로고    scopus 로고
    • Cathepsin L and cathepsin B mediate reovirus disassembly in murine fibroblast cells
    • Ebert D.H., Deussing J., Peters C., Dermody T.S. Cathepsin L and cathepsin B mediate reovirus disassembly in murine fibroblast cells. J. Biol. Chem. 2002, 277:24609-24617.
    • (2002) J. Biol. Chem. , vol.277 , pp. 24609-24617
    • Ebert, D.H.1    Deussing, J.2    Peters, C.3    Dermody, T.S.4
  • 12
    • 79953227722 scopus 로고    scopus 로고
    • Determinants of the specificity of rotavirus interactions with the alpha2beta1 integrin
    • Fleming F.E., Graham K.L., Takada Y., Coulson B.S. Determinants of the specificity of rotavirus interactions with the alpha2beta1 integrin. J. Biol. Chem. 2011, 286:6165-6174.
    • (2011) J. Biol. Chem. , vol.286 , pp. 6165-6174
    • Fleming, F.E.1    Graham, K.L.2    Takada, Y.3    Coulson, B.S.4
  • 13
    • 0141458927 scopus 로고    scopus 로고
    • Integrin-using rotaviruses bind alpha2beta1 integrin alpha2 I domain via VP4 DGE sequence and recognize alphaXbeta2 and alphaVbeta3 by using VP7 during cell entry
    • Graham K.L., Halasz P., Tan Y., et al. Integrin-using rotaviruses bind alpha2beta1 integrin alpha2 I domain via VP4 DGE sequence and recognize alphaXbeta2 and alphaVbeta3 by using VP7 during cell entry. J. Virol. 2003, 77:9969-9978.
    • (2003) J. Virol. , vol.77 , pp. 9969-9978
    • Graham, K.L.1    Halasz, P.2    Tan, Y.3
  • 14
    • 0033809258 scopus 로고    scopus 로고
    • Biochemical characterization of rotavirus receptors in MA104 cells
    • Guerrero C.A., Zarate S., Corkidi G., Lopez S., Arias C.F. Biochemical characterization of rotavirus receptors in MA104 cells. J. Virol. 2000, 74:9362-9371.
    • (2000) J. Virol. , vol.74 , pp. 9362-9371
    • Guerrero, C.A.1    Zarate, S.2    Corkidi, G.3    Lopez, S.4    Arias, C.F.5
  • 15
    • 0036194651 scopus 로고    scopus 로고
    • Heat shock cognate protein 70 is involved in rotavirus cell entry
    • Guerrero C.A., Bouyssounade D., Zarate S., et al. Heat shock cognate protein 70 is involved in rotavirus cell entry. J. Virol. 2002, 76:4096-4102.
    • (2002) J. Virol. , vol.76 , pp. 4096-4102
    • Guerrero, C.A.1    Bouyssounade, D.2    Zarate, S.3
  • 16
    • 77956035360 scopus 로고    scopus 로고
    • Different rotavirus strains enter MA104 cells through different endocytic pathways: the role of clathrin-mediated endocytosis
    • Gutierrez M., Isa P., Sanchez-San Martin C., 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    Isa, P.2    Sanchez-San Martin, C.3
  • 17
    • 33845568286 scopus 로고    scopus 로고
    • STD NMR spectroscopy and molecular modeling investigation of the binding of N-acetylneuraminic acid derivatives to rhesus rotavirus VP8* core
    • Haselhorst T., Blanchard H., Frank M., et al. STD NMR spectroscopy and molecular modeling investigation of the binding of N-acetylneuraminic acid derivatives to rhesus rotavirus VP8* core. Glycobiology 2007, 17:68-81.
    • (2007) Glycobiology , vol.17 , pp. 68-81
    • Haselhorst, T.1    Blanchard, H.2    Frank, M.3
  • 18
    • 58249118009 scopus 로고    scopus 로고
    • Sialic acid dependence in rotavirus host cell invasion
    • Haselhorst T., Fleming F.E., Dyason J.C., et al. Sialic acid dependence in rotavirus host cell invasion. Nat. Chem. Biol. 2009, 5:91-93.
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 91-93
    • Haselhorst, T.1    Fleming, F.E.2    Dyason, J.C.3
  • 19
    • 84860786497 scopus 로고    scopus 로고
    • Cell attachment protein VP8* of a human rotavirus specifically interacts with A-type histo-blood group antigen
    • Hu L., Crawford S.E., Czako R., et al. Cell attachment protein VP8* of a human rotavirus specifically interacts with A-type histo-blood group antigen. Nature 2012, 485:256-259.
    • (2012) Nature , vol.485 , pp. 256-259
    • Hu, L.1    Crawford, S.E.2    Czako, R.3
  • 20
    • 84861309287 scopus 로고    scopus 로고
    • Spike protein VP8* of human rotavirus recognizes histo-blood group antigens in a type-specific manner
    • Huang P., Xia M., Tan M., et al. Spike protein VP8* of human rotavirus recognizes histo-blood group antigens in a type-specific manner. J. Virol. 2012, 86:4833-4843.
    • (2012) J. Virol. , vol.86 , pp. 4833-4843
    • Huang, P.1    Xia, M.2    Tan, M.3
  • 21
    • 80052233389 scopus 로고    scopus 로고
    • Endosome maturation
    • Huotari J., Helenius A. Endosome maturation. Embo J. 2011, 30:3481-3500.
    • (2011) Embo J. , vol.30 , pp. 3481-3500
    • Huotari, J.1    Helenius, A.2
  • 22
    • 1842291025 scopus 로고    scopus 로고
    • Functional and structural analysis of the sialic acid-binding domain of rotaviruses
    • Isa P., Lopez S., Segovia L., Arias C.F. Functional and structural analysis of the sialic acid-binding domain of rotaviruses. J. Virol. 1997, 71:6749-6756.
    • (1997) J. Virol. , vol.71 , pp. 6749-6756
    • Isa, P.1    Lopez, S.2    Segovia, L.3    Arias, C.F.4
  • 23
    • 1942489100 scopus 로고    scopus 로고
    • Rotavirus RRV associates with lipid membrane microdomains during cell entry
    • Isa P., Realpe M., Romero P., Lopez S., Arias C.F. Rotavirus RRV associates with lipid membrane microdomains during cell entry. Virology 2004, 322:370-381.
    • (2004) Virology , vol.322 , pp. 370-381
    • Isa, P.1    Realpe, M.2    Romero, P.3    Lopez, S.4    Arias, C.F.5
  • 24
    • 84866269118 scopus 로고    scopus 로고
    • Rotavirus VP8*: phylogeny, host range, and interaction with histo-blood group antigens
    • Liu Y., Huang P., Tan M., et al. Rotavirus VP8*: phylogeny, host range, and interaction with histo-blood group antigens. J. Virol. 2012, 86:9899-9910.
    • (2012) J. Virol. , vol.86 , pp. 9899-9910
    • Liu, Y.1    Huang, P.2    Tan, M.3
  • 25
    • 2542489194 scopus 로고    scopus 로고
    • Multistep entry of rotavirus into cells: a Versaillesque dance
    • Lopez S., Arias C.F. Multistep entry of rotavirus into cells: a Versaillesque dance. Trends Microbiol. 2004, 12(6):271-278.
    • (2004) Trends Microbiol. , vol.12 , Issue.6 , pp. 271-278
    • Lopez, S.1    Arias, C.F.2
  • 27
    • 32944473016 scopus 로고    scopus 로고
    • Virus entry: open sesame
    • Marsh M., Helenius A. Virus entry: open sesame. Cell 2006, 124:729-740.
    • (2006) Cell , vol.124 , pp. 729-740
    • Marsh, M.1    Helenius, A.2
  • 28
    • 84872001253 scopus 로고    scopus 로고
    • Gangliosides have a functional role during rotavirus cell entry
    • Martinez M.A., Lopez S., Arias C.F., Isa P. Gangliosides have a functional role during rotavirus cell entry. J. Virol. 2013, 87:1115-1122.
    • (2013) J. Virol. , vol.87 , pp. 1115-1122
    • Martinez, M.A.1    Lopez, S.2    Arias, C.F.3    Isa, P.4
  • 30
    • 31144434884 scopus 로고    scopus 로고
    • High-resolution molecular and antigen structure of the VP8* core of a sialic acid-independent human rotavirus strain
    • Monnier N., Higo-Moriguchi K., Sun Z.Y., Prasad B.V., Taniguchi K., Dormitzer P.R. High-resolution molecular and antigen structure of the VP8* core of a sialic acid-independent human rotavirus strain. J. Virol. 2006, 80:1513-1523.
    • (2006) J. Virol. , vol.80 , pp. 1513-1523
    • Monnier, N.1    Higo-Moriguchi, K.2    Sun, Z.Y.3    Prasad, B.V.4    Taniguchi, K.5    Dormitzer, P.R.6
  • 31
    • 10944228240 scopus 로고    scopus 로고
    • The rotavirus surface protein VP8 modulates the gate and fence function of tight junctions in epithelial cells
    • Nava P., Lopez S., Arias C.F., Islas S., Gonzalez-Mariscal L. The rotavirus surface protein VP8 modulates the gate and fence function of tight junctions in epithelial cells. J. Cell Sci. 2004, 117:5509-5519.
    • (2004) J. Cell Sci. , vol.117 , pp. 5509-5519
    • Nava, P.1    Lopez, S.2    Arias, C.F.3    Islas, S.4    Gonzalez-Mariscal, L.5
  • 32
    • 84920721493 scopus 로고    scopus 로고
    • Both lewis and secretor status mediate susceptibility to rotavirus infections in a rotavirus genotype-dependent manner
    • Nordgren J., Sharma S., Bucardo F., et al. Both lewis and secretor status mediate susceptibility to rotavirus infections in a rotavirus genotype-dependent manner. Clin. Infect. Dis. 2014, 59:1567-1573.
    • (2014) Clin. Infect. Dis. , vol.59 , pp. 1567-1573
    • Nordgren, J.1    Sharma, S.2    Bucardo, F.3
  • 33
    • 33645212832 scopus 로고    scopus 로고
    • The peptide-binding and ATPase domains of recombinant hsc70 are required to interact with rotavirus and reduce its infectivity
    • Perez-Vargas J., Romero P., Lopez S., Arias C.F. The peptide-binding and ATPase domains of recombinant hsc70 are required to interact with rotavirus and reduce its infectivity. J. Virol. 2006, 80:3322-3331.
    • (2006) J. Virol. , vol.80 , pp. 3322-3331
    • Perez-Vargas, J.1    Romero, P.2    Lopez, S.3    Arias, C.F.4
  • 34
    • 0742288598 scopus 로고    scopus 로고
    • The dynamin superfamily: universal membrane tubulation and fission molecules?
    • Praefcke G.J., McMahon H.T. The dynamin superfamily: universal membrane tubulation and fission molecules?. Nat. Rev. Mol. Cell Biol. 2004, 5:133-147.
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 133-147
    • Praefcke, G.J.1    McMahon, H.T.2
  • 35
    • 84880350145 scopus 로고    scopus 로고
    • The VP8* domain of neonatal rotavirus strain G10P[11] binds to type II precursor glycans
    • Ramani S., Cortes-Penfield N.W., Hu L., et al. The VP8* domain of neonatal rotavirus strain G10P[11] binds to type II precursor glycans. J. Virol. 2013, 87:7255-7264.
    • (2013) J. Virol. , vol.87 , pp. 7255-7264
    • Ramani, S.1    Cortes-Penfield, N.W.2    Hu, L.3
  • 36
    • 84884288934 scopus 로고    scopus 로고
    • Double nicking by RNA-guided CRISPR Cas9 for enhanced genome editing specificity
    • Ran F.A., Hsu P.D., Lin C.Y., et al. Double nicking by RNA-guided CRISPR Cas9 for enhanced genome editing specificity. Cell 2013, 154:1380-1389.
    • (2013) Cell , vol.154 , pp. 1380-1389
    • Ran, F.A.1    Hsu, P.D.2    Lin, C.Y.3
  • 38
    • 33645788357 scopus 로고    scopus 로고
    • Role of endosomal cathepsins in entry mediated by the Ebola virus glycoprotein
    • Schornberg K., Matsuyama S., Kabsch K., Delos S., Bouton A., White J. Role of endosomal cathepsins in entry mediated by the Ebola virus glycoprotein. J. Virol. 2006, 80:4174-4178.
    • (2006) J. Virol. , vol.80 , pp. 4174-4178
    • Schornberg, K.1    Matsuyama, S.2    Kabsch, K.3    Delos, S.4    Bouton, A.5    White, J.6
  • 42
    • 79551686425 scopus 로고    scopus 로고
    • Directed differentiation of human pluripotent stem cells into intestinal tissue in vitro
    • Spence J.R., Mayhew C.N., Rankin S.A., et al. Directed differentiation of human pluripotent stem cells into intestinal tissue in vitro. Nature 2011, 470:105-109.
    • (2011) Nature , vol.470 , pp. 105-109
    • Spence, J.R.1    Mayhew, C.N.2    Rankin, S.A.3
  • 43
    • 68049105101 scopus 로고    scopus 로고
    • Rab GTPases as coordinators of vesicle traffic
    • Stenmark H. Rab GTPases as coordinators of vesicle traffic. Nat. Rev. Mol. Cell Biol. 2009, 10:513-525.
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 513-525
    • Stenmark, H.1
  • 44
    • 84874663620 scopus 로고    scopus 로고
    • Live cell imaging of viral entry
    • Sun E., He J., Zhuang X. Live cell imaging of viral entry. Curr. Opin. Virol. 2013, 3:34-43.
    • (2013) Curr. Opin. Virol. , vol.3 , pp. 34-43
    • Sun, E.1    He, J.2    Zhuang, X.3
  • 45
    • 84913553760 scopus 로고    scopus 로고
    • The tight junction protein JAM-A functions as coreceptor for rotavirus entry into MA104 cells
    • Torres-Flores J.M., Silva-Ayala D., Espinoza M.A., Lopez S., Arias C.F. The tight junction protein JAM-A functions as coreceptor for rotavirus entry into MA104 cells. Virology 2015, 475:172-178.
    • (2015) Virology , vol.475 , pp. 172-178
    • Torres-Flores, J.M.1    Silva-Ayala, D.2    Espinoza, M.A.3    Lopez, S.4    Arias, C.F.5
  • 46
    • 38449106713 scopus 로고    scopus 로고
    • Penetration of nonenveloped viruses into the cytoplasm
    • Tsai B. Penetration of nonenveloped viruses into the cytoplasm. Annu. Rev. Cell Dev. Biol. 2007, 23:23-43.
    • (2007) Annu. Rev. Cell Dev. Biol. , vol.23 , pp. 23-43
    • Tsai, B.1
  • 47
    • 82755161948 scopus 로고    scopus 로고
    • Cysteine cathepsins: from structure, function and regulation to new frontiers
    • Turk V., Stoka V., Vasiljeva O., et al. Cysteine cathepsins: from structure, function and regulation to new frontiers. Biochim. Biophys. Acta 2012, 1824:68-88.
    • (2012) Biochim. Biophys. Acta , vol.1824 , pp. 68-88
    • Turk, V.1    Stoka, V.2    Vasiljeva, O.3
  • 48
    • 84899560661 scopus 로고    scopus 로고
    • Association between norovirus and rotavirus infection and histo-blood group antigen types in Vietnamese children
    • Van Trang N., Vu H.T., Le N.T., Huang P., Jiang X., Anh D.D. Association between norovirus and rotavirus infection and histo-blood group antigen types in Vietnamese children. J. Clin. Microbiol. 2014, 52:1366-1374.
    • (2014) J. Clin. Microbiol. , vol.52 , pp. 1366-1374
    • Van Trang, N.1    Vu, H.T.2    Le, N.T.3    Huang, P.4    Jiang, X.5    Anh, D.D.6
  • 49
    • 84905169995 scopus 로고    scopus 로고
    • Structural basis of glycan interaction in gastroenteric viral pathogens
    • Venkataram Prasad B.V., Shanker S., Hu L., et al. Structural basis of glycan interaction in gastroenteric viral pathogens. Curr. Opin. Virol. 2014, 7:119-127.
    • (2014) Curr. Opin. Virol. , vol.7 , pp. 119-127
    • Venkataram Prasad, B.V.1    Shanker, S.2    Hu, L.3
  • 50
    • 84930178369 scopus 로고    scopus 로고
    • High-performance probes for light and electron microscopy
    • Viswanathan S., Williams M.E., Bloss E.B., et al. High-performance probes for light and electron microscopy. Nat. Methods 2015, 12:568-576.
    • (2015) Nat. Methods , vol.12 , pp. 568-576
    • Viswanathan, S.1    Williams, M.E.2    Bloss, E.B.3
  • 51
    • 79952409054 scopus 로고    scopus 로고
    • Rhesus rotavirus entry into a polarized epithelium is endocytosis dependent and involves sequential VP4 conformational changes
    • Wolf M., Vo P.T., Greenberg H.B. Rhesus rotavirus entry into a polarized epithelium is endocytosis dependent and involves sequential VP4 conformational changes. J. Virol. 2011, 85:2492-2503.
    • (2011) J. Virol. , vol.85 , pp. 2492-2503
    • Wolf, M.1    Vo, P.T.2    Greenberg, H.B.3
  • 52
    • 84861303407 scopus 로고    scopus 로고
    • Rhesus rotavirus trafficking during entry into MA104 cells is restricted to the early endosome compartment
    • Wolf M., Deal E.M., Greenberg H.B. Rhesus rotavirus trafficking during entry into MA104 cells is restricted to the early endosome compartment. J. Virol. 2012, 86:4009-4013.
    • (2012) J. Virol. , vol.86 , pp. 4009-4013
    • Wolf, M.1    Deal, E.M.2    Greenberg, H.B.3
  • 53
    • 84877898099 scopus 로고    scopus 로고
    • Virus entry at a glance
    • Yamauchi Y., Helenius A. Virus entry at a glance. J. Cell Sci. 2013, 126:1289-1295.
    • (2013) J. Cell Sci. , vol.126 , pp. 1289-1295
    • Yamauchi, Y.1    Helenius, A.2
  • 54
    • 33645750724 scopus 로고    scopus 로고
    • Alternative intermolecular contacts underlie the rotavirus VP5* two- to three-fold rearrangement
    • Yoder J.D., Dormitzer P.R. Alternative intermolecular contacts underlie the rotavirus VP5* two- to three-fold rearrangement. Embo J 2006, 25:1559-1568.
    • (2006) Embo J , vol.25 , pp. 1559-1568
    • Yoder, J.D.1    Dormitzer, P.R.2
  • 56
    • 0038001658 scopus 로고    scopus 로고
    • Interaction of rotaviruses with Hsc70 during cell entry is mediated by VP5
    • Zarate S., Cuadras M.A., Espinosa R., et al. Interaction of rotaviruses with Hsc70 during cell entry is mediated by VP5. J. Virol. 2003, 77:7254-7260.
    • (2003) J. Virol. , vol.77 , pp. 7254-7260
    • Zarate, S.1    Cuadras, M.A.2    Espinosa, R.3
  • 57
    • 4644249737 scopus 로고    scopus 로고
    • VP7 mediates the interaction of rotaviruses with integrin alphavbeta3 through a novel integrin-binding site
    • Zarate S., Romero P., Espinosa R., Arias C.F., Lopez S. VP7 mediates the interaction of rotaviruses with integrin alphavbeta3 through a novel integrin-binding site. J. Virol. 2004, 78:10839-10847.
    • (2004) J. Virol. , vol.78 , pp. 10839-10847
    • Zarate, S.1    Romero, P.2    Espinosa, R.3    Arias, C.F.4    Lopez, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.