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Volumn 446, Issue 1-2, 2013, Pages 303-313

The interaction between claudin-1 and dengue viral prM/M protein for its entry

Author keywords

Claudin 1; Dengue virus; Extracellular loops; PrM; Tight junction; Virus entry

Indexed keywords

CLAUDIN 1; ESSENTIAL AMINO ACID; SMALL INTERFERING RNA; UNCLASSIFIED DRUG; VIRAL MEMBRANE PROTEIN; VIRAL PRECURSOR MEMBRANE PROTEIN; VIRUS PROTEIN;

EID: 84884564516     PISSN: 00426822     EISSN: 10960341     Source Type: Journal    
DOI: 10.1016/j.virol.2013.08.009     Document Type: Article
Times cited : (50)

References (75)
  • 1
    • 79960725414 scopus 로고    scopus 로고
    • HIV-1-induced alterations of claudin-5 expression at the blood-brain barrier level
    • Andras I.E., Toborek M. HIV-1-induced alterations of claudin-5 expression at the blood-brain barrier level. Methods Mol. Biol. 2011, 762:355-370.
    • (2011) Methods Mol. Biol. , vol.762 , pp. 355-370
    • Andras, I.E.1    Toborek, M.2
  • 5
    • 0035055182 scopus 로고    scopus 로고
    • Dengue virus binding to human leukocyte cell lines: receptor usage differs between cell types and virus strains
    • Bielefeldt-Ohmann H., Meyer M., Fitzpatrick D.R., Mackenzie J.S. Dengue virus binding to human leukocyte cell lines: receptor usage differs between cell types and virus strains. Virus Res. 2001, 73:81-89.
    • (2001) Virus Res. , vol.73 , pp. 81-89
    • Bielefeldt-Ohmann, H.1    Meyer, M.2    Fitzpatrick, D.R.3    Mackenzie, J.S.4
  • 6
    • 74549219339 scopus 로고    scopus 로고
    • The development, optimization and validation of an assay for high throughput antiviral drug screening against Dengue virus
    • Che P., Wang L., Li Q. The development, optimization and validation of an assay for high throughput antiviral drug screening against Dengue virus. Int. J. Clin. Exp. Med. 2009, 2:363-373.
    • (2009) Int. J. Clin. Exp. Med. , vol.2 , pp. 363-373
    • Che, P.1    Wang, L.2    Li, Q.3
  • 7
    • 66149127009 scopus 로고    scopus 로고
    • Residues in a highly conserved claudin-1 motif are required for hepatitis C virus entry and mediate the formation of cell-cell contacts
    • Cukierman L., Meertens L., Bertaux C., Kajumo F., Dragic T. Residues in a highly conserved claudin-1 motif are required for hepatitis C virus entry and mediate the formation of cell-cell contacts. J. Virol. 2009, 83:5477-5484.
    • (2009) J. Virol. , vol.83 , pp. 5477-5484
    • Cukierman, L.1    Meertens, L.2    Bertaux, C.3    Kajumo, F.4    Dragic, T.5
  • 9
    • 0033881444 scopus 로고    scopus 로고
    • Infection of human cells by dengue virus is modulated by different cell types and viral strains
    • Diamond M.S., Edgil D., Roberts T.G., Lu B., Harris E. Infection of human cells by dengue virus is modulated by different cell types and viral strains. J. Virol. 2000, 74:7814-7823.
    • (2000) J. Virol. , vol.74 , pp. 7814-7823
    • Diamond, M.S.1    Edgil, D.2    Roberts, T.G.3    Lu, B.4    Harris, E.5
  • 11
    • 0026026342 scopus 로고
    • Is the hydrophobic effect stabilizing or destabilizing in proteins? The contribution of disulphide bonds to protein stability
    • Doig A.J., Williams D.H. Is the hydrophobic effect stabilizing or destabilizing in proteins? The contribution of disulphide bonds to protein stability. J. Mol. Biol. 1991, 217:389-398.
    • (1991) J. Mol. Biol. , vol.217 , pp. 389-398
    • Doig, A.J.1    Williams, D.H.2
  • 13
    • 28444489667 scopus 로고    scopus 로고
    • Helicobacter pylori activates myosin light-chain kinase to disrupt claudin-4 and claudin-5 and increase epithelial permeability
    • Fedwick J.P., Lapointe T.K., Meddings J.B., Sherman P.M., Buret A.G. Helicobacter pylori activates myosin light-chain kinase to disrupt claudin-4 and claudin-5 and increase epithelial permeability. Infect. Immun. 2005, 73:7844-7852.
    • (2005) Infect. Immun. , vol.73 , pp. 7844-7852
    • Fedwick, J.P.1    Lapointe, T.K.2    Meddings, J.B.3    Sherman, P.M.4    Buret, A.G.5
  • 14
    • 0034617463 scopus 로고    scopus 로고
    • Clostridium perfringens enterotoxin binds to the second extracellular loop of claudin-3, a tight junction integral membrane protein
    • Fujita K., Katahira J., Horiguchi Y., Sonoda N., Furuse M., Tsukita S. Clostridium perfringens enterotoxin binds to the second extracellular loop of claudin-3, a tight junction integral membrane protein. FEBS lett. 2000, 476:258-261.
    • (2000) FEBS lett. , vol.476 , pp. 258-261
    • Fujita, K.1    Katahira, J.2    Horiguchi, Y.3    Sonoda, N.4    Furuse, M.5    Tsukita, S.6
  • 15
    • 72949113004 scopus 로고    scopus 로고
    • Novel binding between pre-membrane protein and claudin-1 is required for efficient dengue virus entry
    • Gao F., Duan X., Lu X., Liu Y., Zheng L., Ding Z., Li J. Novel binding between pre-membrane protein and claudin-1 is required for efficient dengue virus entry. Biochem. Biophys. Res. Commun. 2010, 391:952-957.
    • (2010) Biochem. Biophys. Res. Commun. , vol.391 , pp. 952-957
    • Gao, F.1    Duan, X.2    Lu, X.3    Liu, Y.4    Zheng, L.5    Ding, Z.6    Li, J.7
  • 16
    • 84884544253 scopus 로고    scopus 로고
    • Tight Junctions, Current Frontiers and Perspectives in Cell Biology, Prof
    • ISBN: 978-953-51-0544-2, InTech.
    • Gonzalez-Mariscal, L., Quiros, M., Diaz-Coranguez, M., Bautista P., 2012. Tight Junctions, Current Frontiers and Perspectives in Cell Biology, Prof. Stevo Najman (Ed.), ISBN: 978-953-51-0544-2, InTech.
    • (2012) Stevo Najman (Ed.)
    • Gonzalez-Mariscal, L.1    Quiros, M.2    Diaz-Coranguez, M.3    Bautista, P.4
  • 18
    • 33750436249 scopus 로고    scopus 로고
    • Evidence that tight junctions are disrupted due to intimate bacterial contact and not inflammation during attaching and effacing pathogen infection in vivo
    • Guttman J.A., Samji F.N., Li Y., Vogl A.W., Finlay B.B. Evidence that tight junctions are disrupted due to intimate bacterial contact and not inflammation during attaching and effacing pathogen infection in vivo. Infect. Immun. 2006, 74:6075-6084.
    • (2006) Infect. Immun. , vol.74 , pp. 6075-6084
    • Guttman, J.A.1    Samji, F.N.2    Li, Y.3    Vogl, A.W.4    Finlay, B.B.5
  • 20
    • 0037136939 scopus 로고    scopus 로고
    • The future of dengue vaccines
    • Halstead S.B., Deen J. The future of dengue vaccines. Lancet 2002, 360:1243-1245.
    • (2002) Lancet , vol.360 , pp. 1243-1245
    • Halstead, S.B.1    Deen, J.2
  • 22
    • 34248559599 scopus 로고    scopus 로고
    • Gene splicing and mutagenesis by PCR-driven overlap extension
    • Heckman K.L., Pease L.R. Gene splicing and mutagenesis by PCR-driven overlap extension. Nat. Protocols 2007, 2:924-932.
    • (2007) Nat. Protocols , vol.2 , pp. 924-932
    • Heckman, K.L.1    Pease, L.R.2
  • 23
    • 1542466884 scopus 로고    scopus 로고
    • Flavivirus structure and membrane fusion
    • Heinz F.X., Allison S.L. Flavivirus structure and membrane fusion. Adv. Virus Res. 2003, 59:63-97.
    • (2003) Adv. Virus Res. , vol.59 , pp. 63-97
    • Heinz, F.X.1    Allison, S.L.2
  • 24
    • 77954723683 scopus 로고    scopus 로고
    • Resistance to dengue virus infection in mice is potentiated by CXCL10 and is independent of CXCL10-mediated leukocyte recruitment
    • Ip P.P., Liao F. Resistance to dengue virus infection in mice is potentiated by CXCL10 and is independent of CXCL10-mediated leukocyte recruitment. J. Immunol. 2010, 184:5705-5714.
    • (2010) J. Immunol. , vol.184 , pp. 5705-5714
    • Ip, P.P.1    Liao, F.2
  • 25
    • 9144259584 scopus 로고    scopus 로고
    • Virus overlay protein binding assay (VOPBA) reveals serotype specific heterogeneity of dengue virus binding proteins on HepG2 human liver cells
    • Jindadamrongwech S., Smith D.R. Virus overlay protein binding assay (VOPBA) reveals serotype specific heterogeneity of dengue virus binding proteins on HepG2 human liver cells. Intervirology 2004, 47:370-373.
    • (2004) Intervirology , vol.47 , pp. 370-373
    • Jindadamrongwech, S.1    Smith, D.R.2
  • 26
    • 0030996972 scopus 로고    scopus 로고
    • Construction of infectious cDNA clones for dengue 2 virus: strain 16681 and its attenuated vaccine derivative, strain PDK-53
    • Kinney R.M., Butrapet S., Chang G.J., Tsuchiya K.R., Roehrig J.T., Bhamarapravati N., Gubler D.J. Construction of infectious cDNA clones for dengue 2 virus: strain 16681 and its attenuated vaccine derivative, strain PDK-53. Virology 1997, 230:300-308.
    • (1997) Virology , vol.230 , pp. 300-308
    • Kinney, R.M.1    Butrapet, S.2    Chang, G.J.3    Tsuchiya, K.R.4    Roehrig, J.T.5    Bhamarapravati, N.6    Gubler, D.J.7
  • 28
    • 77956173389 scopus 로고    scopus 로고
    • Identification and characterization of prohibitin as a receptor protein mediating DENV-2 entry into insect cells
    • Kuadkitkan A., Wikan N., Fongsaran C., Smith D.R. Identification and characterization of prohibitin as a receptor protein mediating DENV-2 entry into insect cells. Virology 2010, 406:149-161.
    • (2010) Virology , vol.406 , pp. 149-161
    • Kuadkitkan, A.1    Wikan, N.2    Fongsaran, C.3    Smith, D.R.4
  • 30
    • 84880163557 scopus 로고    scopus 로고
    • Claudin-2 pore function requires an intramolecular disulfide bond between two conserved extracellular cysteines
    • Li J., Angelow S., Linge A., Zhuo M., Yu A.S. Claudin-2 pore function requires an intramolecular disulfide bond between two conserved extracellular cysteines. Am. J. Physiol.-Cell Physiol. 2013.
    • (2013) Am. J. Physiol.-Cell Physiol.
    • Li, J.1    Angelow, S.2    Linge, A.3    Zhuo, M.4    Yu, A.S.5
  • 31
    • 1542676405 scopus 로고    scopus 로고
    • Molecular biology of flaviviruses
    • Lindenbach B.D., Rice C.M. Molecular biology of flaviviruses. Adv. Virus Res. 2003, 59:23-61.
    • (2003) Adv. Virus Res. , vol.59 , pp. 23-61
    • Lindenbach, B.D.1    Rice, C.M.2
  • 33
    • 59649117842 scopus 로고    scopus 로고
    • Tight junction proteins claudin-1 and occludin control hepatitis C virus entry and are downregulated during infection to prevent superinfection
    • Liu S., Yang W., Shen L., Turner J.R., Coyne C.B., Wang T. Tight junction proteins claudin-1 and occludin control hepatitis C virus entry and are downregulated during infection to prevent superinfection. J. Virol. 2009, 83:2011-2014.
    • (2009) J. Virol. , vol.83 , pp. 2011-2014
    • Liu, S.1    Yang, W.2    Shen, L.3    Turner, J.R.4    Coyne, C.B.5    Wang, T.6
  • 35
    • 21244462832 scopus 로고    scopus 로고
    • Dendritic cell-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN)-mediated enhancement of dengue virus infection is independent of DC-SIGN internalization signals
    • Lozach P.Y., Burleigh L., Staropoli I., Navarro-Sanchez E., Harriague J., Virelizier J.L., Rey F.A., Despres P., Arenzana-Seisdedos F., Amara A. Dendritic cell-specific intercellular adhesion molecule 3-grabbing non-integrin (DC-SIGN)-mediated enhancement of dengue virus infection is independent of DC-SIGN internalization signals. J. Biol. Chem. 2005, 280:23698-23708.
    • (2005) J. Biol. Chem. , vol.280 , pp. 23698-23708
    • Lozach, P.Y.1    Burleigh, L.2    Staropoli, I.3    Navarro-Sanchez, E.4    Harriague, J.5    Virelizier, J.L.6    Rey, F.A.7    Despres, P.8    Arenzana-Seisdedos, F.9    Amara, A.10
  • 36
    • 0034767341 scopus 로고    scopus 로고
    • Assembly and maturation of the flavivirus Kunjin virus appear to occur in the rough endoplasmic reticulum and along the secretory pathway, respectively
    • Mackenzie J.M., Westaway E.G. Assembly and maturation of the flavivirus Kunjin virus appear to occur in the rough endoplasmic reticulum and along the secretory pathway, respectively. J. Virol. 2001, 75:10787-10799.
    • (2001) J. Virol. , vol.75 , pp. 10787-10799
    • Mackenzie, J.M.1    Westaway, E.G.2
  • 39
    • 48349093893 scopus 로고    scopus 로고
    • A dengue receptor as possible genetic marker of vector competence in Aedes aegypti
    • Mercado-Curiel R.F., Black W.C.T., Munoz Mde L. A dengue receptor as possible genetic marker of vector competence in Aedes aegypti. BMC Microbiol. 2008, 8:118.
    • (2008) BMC Microbiol. , vol.8 , pp. 118
    • Mercado-Curiel, R.F.1    Black, W.C.T.2    Munoz Mde, L.3
  • 42
    • 0027530821 scopus 로고
    • Processing of the dengue virus type 2 proteins prM and C-prM
    • Murray J.M., Aaskov J.G., Wright P.J. Processing of the dengue virus type 2 proteins prM and C-prM. J. Gen. Virol. 1993, 74(Pt 2):175-182.
    • (1993) J. Gen. Virol. , vol.74 , Issue.PART 2 , pp. 175-182
    • Murray, J.M.1    Aaskov, J.G.2    Wright, P.J.3
  • 43
    • 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
  • 44
    • 0041563793 scopus 로고    scopus 로고
    • Dendritic-cell-specific ICAM3-grabbing non-integrin is essential for the productive infection of human dendritic cells by mosquito-cell-derived dengue viruses
    • Navarro-Sanchez E., Altmeyer R., Amara A., Schwartz O., Fieschi F., Virelizier J.L., Arenzana-Seisdedos F., Despres P. Dendritic-cell-specific ICAM3-grabbing non-integrin is essential for the productive infection of human dendritic cells by mosquito-cell-derived dengue viruses. EMBO Rep. 2003, 4:723-728.
    • (2003) EMBO Rep. , vol.4 , pp. 723-728
    • Navarro-Sanchez, E.1    Altmeyer, R.2    Amara, A.3    Schwartz, O.4    Fieschi, F.5    Virelizier, J.L.6    Arenzana-Seisdedos, F.7    Despres, P.8
  • 45
    • 0034002422 scopus 로고    scopus 로고
    • Rotavirus-induced structural and functional alterations in tight junctions of polarized intestinal Caco-2 cell monolayers
    • Obert G., Peiffer I., Servin A.L. Rotavirus-induced structural and functional alterations in tight junctions of polarized intestinal Caco-2 cell monolayers. J. Virol. 2000, 74:4645-4651.
    • (2000) J. Virol. , vol.74 , pp. 4645-4651
    • Obert, G.1    Peiffer, I.2    Servin, A.L.3
  • 46
    • 48749123790 scopus 로고    scopus 로고
    • Structural proteomics of dengue virus
    • Perera R., Kuhn R.J. Structural proteomics of dengue virus. Curr. Opin. Microbiol. 2008, 11:369-377.
    • (2008) Curr. Opin. Microbiol. , vol.11 , pp. 369-377
    • Perera, R.1    Kuhn, R.J.2
  • 48
    • 60149090028 scopus 로고    scopus 로고
    • Human occludin is a hepatitis C virus entry factor required for infection of mouse cells
    • Ploss A., Evans M.J., Gaysinskaya V.A., Panis M., You H., de Jong Y.P., Rice C.M. Human occludin is a hepatitis C virus entry factor required for infection of mouse cells. Nature 2009, 457:882-886.
    • (2009) Nature , vol.457 , pp. 882-886
    • Ploss, A.1    Evans, M.J.2    Gaysinskaya, V.A.3    Panis, M.4    You, H.5    de Jong, Y.P.6    Rice, C.M.7
  • 49
    • 16244364801 scopus 로고    scopus 로고
    • Heat shock protein 90 and heat shock protein 70 are components of dengue virus receptor complex in human cells
    • Reyes-Del Valle J., Chavez-Salinas S., Medina F., Del Angel R.M. Heat shock protein 90 and heat shock protein 70 are components of dengue virus receptor complex in human cells. J. Virol. 2005, 79:4557-4567.
    • (2005) J. Virol. , vol.79 , pp. 4557-4567
    • Reyes-Del Valle, J.1    Chavez-Salinas, S.2    Medina, F.3    Del Angel, R.M.4
  • 50
    • 0346727181 scopus 로고    scopus 로고
    • Isolation of putative dengue virus receptor molecules by affinity chromatography using a recombinant E protein ligand
    • Reyes-del Valle J., Del Angel R.M. Isolation of putative dengue virus receptor molecules by affinity chromatography using a recombinant E protein ligand. J. Virol. Methods 2004, 116:95-102.
    • (2004) J. Virol. Methods , vol.116 , pp. 95-102
    • Reyes-del Valle, J.1    Del Angel, R.M.2
  • 53
    • 0036300466 scopus 로고    scopus 로고
    • Shigella flexneri regulates tight junction-associated proteins in human intestinal epithelial cells
    • Sakaguchi T., Kohler H., Gu X., McCormick B.A., Reinecker H.C. Shigella flexneri regulates tight junction-associated proteins in human intestinal epithelial cells. Cell. Microbiol. 2002, 4:367-381.
    • (2002) Cell. Microbiol. , vol.4 , pp. 367-381
    • Sakaguchi, T.1    Kohler, H.2    Gu, X.3    McCormick, B.A.4    Reinecker, H.C.5
  • 54
    • 34848906249 scopus 로고    scopus 로고
    • Evidence that the 45-kD glycoprotein, part of a putative dengue virus receptor complex in the mosquito cell line C6/36, is a heat-shock related protein
    • Salas-Benito J., Reyes-Del Valle J., Salas-Benito M., Ceballos-Olvera I., Mosso C., Del Angel R.M. Evidence that the 45-kD glycoprotein, part of a putative dengue virus receptor complex in the mosquito cell line C6/36, is a heat-shock related protein. Am. J. Trop. Med. Hyg. 2007, 77:283-290.
    • (2007) Am. J. Trop. Med. Hyg. , vol.77 , pp. 283-290
    • Salas-Benito, J.1    Reyes-Del Valle, J.2    Salas-Benito, M.3    Ceballos-Olvera, I.4    Mosso, C.5    Del Angel, R.M.6
  • 56
    • 0033523773 scopus 로고    scopus 로고
    • Clostridium perfringens enterotoxin fragment removes specific claudins from tight junction strands: evidence for direct involvement of claudins in tight junction barrier
    • Sonoda N., Furuse M., Sasaki H., Yonemura S., Katahira J., Horiguchi Y., Tsukita S. Clostridium perfringens enterotoxin fragment removes specific claudins from tight junction strands: evidence for direct involvement of claudins in tight junction barrier. J. Cell Biol. 1999, 147:195-204.
    • (1999) J. Cell Biol. , vol.147 , pp. 195-204
    • Sonoda, N.1    Furuse, M.2    Sasaki, H.3    Yonemura, S.4    Katahira, J.5    Horiguchi, Y.6    Tsukita, S.7
  • 59
    • 0025806533 scopus 로고
    • Evidence for intramolecular disulfide bond shuffling in the folding of mutant human lysozyme
    • Taniyama Y., Kuroki R., Omura F., Seko C., Kikuchi M. Evidence for intramolecular disulfide bond shuffling in the folding of mutant human lysozyme. J. Biol. Chem. 1991, 266:6456-6461.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6456-6461
    • Taniyama, Y.1    Kuroki, R.2    Omura, F.3    Seko, C.4    Kikuchi, M.5
  • 62
    • 33645963995 scopus 로고    scopus 로고
    • Claudins and epithelial paracellular transport
    • Van Itallie C.M., Anderson J.M. Claudins and epithelial paracellular transport. Annu. Rev. Physiol. 2006, 68:403-429.
    • (2006) Annu. Rev. Physiol. , vol.68 , pp. 403-429
    • Van Itallie, C.M.1    Anderson, J.M.2
  • 65
    • 0033053594 scopus 로고    scopus 로고
    • PrM- and cell-binding domains of the dengue virus E protein
    • Wang S., He R., Anderson R. PrM- and cell-binding domains of the dengue virus E protein. J. Virol. 1999, 73:2547-2551.
    • (1999) J. Virol. , vol.73 , pp. 2547-2551
    • Wang, S.1    He, R.2    Anderson, R.3
  • 66
    • 8644278061 scopus 로고    scopus 로고
    • Identification of cellular cofactors for human immunodeficiency virus replication via a ribozyme-based genomics approach
    • Waninger S., Kuhen K., Hu X., Chatterton J.E., Wong-Staal F., Tang H. Identification of cellular cofactors for human immunodeficiency virus replication via a ribozyme-based genomics approach. J. Virol. 2004, 78:12829-12837.
    • (2004) J. Virol. , vol.78 , pp. 12829-12837
    • Waninger, S.1    Kuhen, K.2    Hu, X.3    Chatterton, J.E.4    Wong-Staal, F.5    Tang, H.6
  • 67
    • 4544311402 scopus 로고    scopus 로고
    • Selective decrease in paracellular conductance of tight junctions: role of the first extracellular domain of claudin-5
    • Wen H., Watry D.D., Marcondes M.C., Fox H.S. Selective decrease in paracellular conductance of tight junctions: role of the first extracellular domain of claudin-5. Mol. Cell. Biol. 2004, 24:8408-8417.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 8408-8417
    • Wen, H.1    Watry, D.D.2    Marcondes, M.C.3    Fox, H.S.4
  • 68
    • 84884536328 scopus 로고    scopus 로고
    • WHO, Dengue and severe dengue fact sheet
    • WHO, 2012. Dengue and severe dengue fact sheet. The Journal of General Virology 87, pp. 1075-1084. http://www.who.int/.
    • (2012) The Journal of General Virology , vol.87 , pp. 1075-1084
  • 69
    • 70450208515 scopus 로고    scopus 로고
    • Association of the pr peptides with dengue virus at acidic pH blocks membrane fusion
    • Yu I.M., Holdaway H.A., Chipman P.R., Kuhn R.J., Rossmann M.G., Chen J. Association of the pr peptides with dengue virus at acidic pH blocks membrane fusion. J. Virol. 2009, 83:12101-12107.
    • (2009) J. Virol. , vol.83 , pp. 12101-12107
    • Yu, I.M.1    Holdaway, H.A.2    Chipman, P.R.3    Kuhn, R.J.4    Rossmann, M.G.5    Chen, J.6
  • 71
    • 0030775148 scopus 로고    scopus 로고
    • Enteropathogenic Escherichia coli-induced myosin light chain phosphorylation alters intestinal epithelial permeability
    • Yuhan R., Koutsouris A., Savkovic S.D., Hecht G. Enteropathogenic Escherichia coli-induced myosin light chain phosphorylation alters intestinal epithelial permeability. Gastroenterology 1997, 113:1873-1882.
    • (1997) Gastroenterology , vol.113 , pp. 1873-1882
    • Yuhan, R.1    Koutsouris, A.2    Savkovic, S.D.3    Hecht, G.4
  • 74
    • 36048954580 scopus 로고    scopus 로고
    • Claudin-6 and claudin-9 function as additional coreceptors for hepatitis C virus
    • Zheng A., Yuan F., Li Y., Zhu F., Hou P., Li J., Song X., Ding M., Deng H. Claudin-6 and claudin-9 function as additional coreceptors for hepatitis C virus. J. Virol. 2007, 81:12465-12471.
    • (2007) J. Virol. , vol.81 , pp. 12465-12471
    • Zheng, A.1    Yuan, F.2    Li, Y.3    Zhu, F.4    Hou, P.5    Li, J.6    Song, X.7    Ding, M.8    Deng, H.9
  • 75
    • 58149388463 scopus 로고    scopus 로고
    • Functional importance of dengue virus maturation: infectious properties of immature virions
    • Zybert I.A., van der Ende-Metselaar H., Wilschut J., Smit J.M. Functional importance of dengue virus maturation: infectious properties of immature virions. J. Gen. Virol. 2008, 89:3047-3051.
    • (2008) J. Gen. Virol. , vol.89 , pp. 3047-3051
    • Zybert, I.A.1    van der Ende-Metselaar, H.2    Wilschut, J.3    Smit, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.