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Volumn 7, Issue 9, 2015, Pages 5145-5154

Tight junctions go viral!

Author keywords

Claudins; JAM A; Occludin; PDZ; Tight junctions; Virus; ZO 1

Indexed keywords

BINDING PROTEIN; CD81 ANTIGEN; CLAUDIN; COXSACKIE VIRUS AND ADENOVIRUS RECEPTOR; CYTOPLASM PROTEIN; DNA; IMMUNOGLOBULIN; ION; JUNCTIONAL ADHESION MOLECULE; JUNCTIONAL ADHESION MOLECULE A; JUNCTIONAL ADHESION MOLECULE B; JUNCTIONAL ADHESION MOLECULE C; MARVEL DOMAIN CONTAINING PROTEIN; MARVEL DOMAIN CONTAINING PROTEIN 3; MULTIPROTEIN COMPLEX; OCCLUDIN; PDZ PROTEIN; PDZ PROTEIN 1; PDZ PROTEIN 2; PDZ PROTEIN 3; PROTEIN KINASE C; RNA; SCAVENGER RECEPTOR BI; TIGHT JUNCTION PROTEIN; TRICELLULIN; UNCLASSIFIED DRUG; DNA VIRUS; VIRUS RECEPTOR;

EID: 84942421328     PISSN: None     EISSN: 19994915     Source Type: Journal    
DOI: 10.3390/v7092865     Document Type: Review
Times cited : (77)

References (72)
  • 1
    • 77249110786 scopus 로고    scopus 로고
    • Dynamics and functions of tight junctions
    • Steed, E.; Balda, M.S.; Matter, K. Dynamics and functions of tight junctions. Trends Cell Biol. 2010, 20, 142–149.
    • (2010) Trends Cell Biol , vol.20 , pp. 142-149
    • Steed, E.1    Balda, M.S.2    Matter, K.3
  • 2
    • 84862834603 scopus 로고    scopus 로고
    • Tight junctions on the move: Molecular mechanisms for epithelial barrier regulation
    • Shen, L. Tight junctions on the move: Molecular mechanisms for epithelial barrier regulation. Ann. N. Y. Acad. Sci. 2011, 1258, 9–18.
    • (2011) Ann. N. Y. Acad. Sci , vol.1258 , pp. 9-18
    • Shen, L.1
  • 3
    • 0022748005 scopus 로고
    • The function of tight junctions in maintaining differences in lipid composition between the apical and the basolateral cell surface domains of MDCK cells
    • Van Meer, G.; Simons, K. The function of tight junctions in maintaining differences in lipid composition between the apical and the basolateral cell surface domains of MDCK cells. EMBO J. 1986, 5, 1455–1464.
    • (1986) EMBO J , vol.5 , pp. 1455-1464
    • Van Meer, G.1    Simons, K.2
  • 6
    • 76349098227 scopus 로고    scopus 로고
    • Rho signaling and tight junction functions
    • Terry, S.; Nie, M.; Matter, K.; Balda, M.S. Rho signaling and tight junction functions. Physiology 2010, 25, 16–26.
    • (2010) Physiology , vol.25 , pp. 16-26
    • Terry, S.1    Nie, M.2    Matter, K.3    Balda, M.S.4
  • 7
    • 39849109700 scopus 로고    scopus 로고
    • Crosstalk of tight junction components with signaling pathways
    • González-Mariscal, L.; Tapia, R.; Chamorro, D. Crosstalk of tight junction components with signaling pathways. Biochim. Biophys. Acta 2008, 1778, 729–756.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 729-756
    • González-Mariscal, L.1    Tapia, R.2    Chamorro, D.3
  • 8
    • 84906057165 scopus 로고    scopus 로고
    • Signalling at tight junctions during epithelial differentiation and microbialpathogenesis
    • Zihni, C.; Balda, M.S.; Matter, K. Signalling at tight junctions during epithelial differentiation and microbialpathogenesis. J. Cell Sci. 2014, 15, 3401–3413.
    • (2014) J. Cell Sci , vol.15 , pp. 3401-3413
    • Zihni, C.1    Balda, M.S.2    Matter, K.3
  • 9
    • 56749184887 scopus 로고    scopus 로고
    • Tight junction-based epithelial microenvironment and cell proliferation
    • Tsukita, S.; Yamazaki, Y.; Katsuno, T.; Tamura, A. Tight junction-based epithelial microenvironment and cell proliferation. Oncogene 2008, 27, 6930–6938.
    • (2008) Oncogene , vol.27 , pp. 6930-6938
    • Tsukita, S.1    Yamazaki, Y.2    Katsuno, T.3    Tamura, A.4
  • 10
    • 84942427976 scopus 로고    scopus 로고
    • Molecular basis of the core structure of tight junctions
    • Furuse, M. Molecular basis of the core structure of tight junctions. Cold Spring Harb. Perspect. Biol. 2010, 2.
    • (2010) Cold Spring Harb. Perspect. Biol
    • Furuse, M.1
  • 12
    • 70349316548 scopus 로고    scopus 로고
    • Structural determinants of Junctional Adhesion Molecule A (JAM-A) function and mechanisms of intracellular signaling
    • Severson, E.A.; Parkos, C.A. Structural determinants of Junctional Adhesion Molecule A (JAM-A) function and mechanisms of intracellular signaling. Curr. Opin. Cell Biol. 2009, 21, 701–707.
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 701-707
    • Severson, E.A.1    Parkos, C.A.2
  • 13
    • 84899432057 scopus 로고    scopus 로고
    • Tight junction dynamics: The role of junctional adhesion molecules (JAMs).
    • Garrido-Urbani, S.; Bradfield, P.F.; Imhof, B.A. Tight junction dynamics: The role of junctional adhesion molecules (JAMs). Cell Tissue Res. 2014, 355, 701–715.
    • (2014) Cell Tissue Res , vol.355 , pp. 701-715
    • Garrido-Urbani, S.1    Bradfield, P.F.2    Imhof, B.A.3
  • 14
    • 84925638126 scopus 로고    scopus 로고
    • Claudin clusters as determinants of epithelial barrier function
    • Markov, A.G.; Aschenbach, J.R.; Amasheh, S. Claudin clusters as determinants of epithelial barrier function. IUBMB Life 2015, 67, 29–35.
    • (2015) IUBMB Life , vol.67 , pp. 29-35
    • Markov, A.G.1    Aschenbach, J.R.2    Amasheh, S.3
  • 15
    • 84920861016 scopus 로고    scopus 로고
    • Model for the architecture of claudin-based paracellular ion channels through tight junctions
    • Suzuki, H.; Tani, K.; Tamura, A.; Tsukita, S.; Fujiyoshi, Y. Model for the architecture of claudin-based paracellular ion channels through tight junctions. J. Mol. Biol. 2015, 427, 291–297.
    • (2015) J. Mol. Biol , vol.427 , pp. 291-297
    • Suzuki, H.1    Tani, K.2    Tamura, A.3    Tsukita, S.4    Fujiyoshi, Y.5
  • 18
    • 39849102083 scopus 로고    scopus 로고
    • Stimulus-induced reorganization of tight junction structure: The role of membrane traffic
    • Yu, D.; Turner, J.R. Stimulus-induced reorganization of tight junction structure: the role of membrane traffic. Biochim. Biophys. Acta 2008, 1778, 709–716.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 709-716
    • Yu, D.1    Turner, J.R.2
  • 21
    • 77950663681 scopus 로고    scopus 로고
    • Tight junction-associated MARVEL proteins marveld3, tricellulin, and occludin have distinct but overlapping functions
    • Raleigh, D.R.; Marchiando, A.M.; Zhang, Y.; Shen, L.; Sasaki, H.; Wang, Y.; Long, M.; Turner, J.R. Tight junction-associated MARVEL proteins marveld3, tricellulin, and occludin have distinct but overlapping functions. Mol. Biol. Cell 2010, 21, 1200–1213.
    • (2010) Mol. Biol. Cell , vol.21 , pp. 1200-1213
    • Raleigh, D.R.1    Marchiando, A.M.2    Zhang, Y.3    Shen, L.4    Sasaki, H.5    Wang, Y.6    Long, M.7    Turner, J.R.8
  • 22
    • 67249084776 scopus 로고    scopus 로고
    • Zonula Occludens-1 and -2 are cytosolic scaffolds that regulate the assembly of cellular junctions
    • Fanning, A.S.; Anderson, J.M. Zonula Occludens-1 and -2 are cytosolic scaffolds that regulate the assembly of cellular junctions. Ann. N. Y. Acad. Sci. 2009, 1165, 113–120.
    • (2009) Ann. N. Y. Acad. Sci , vol.1165 , pp. 113-120
    • Fanning, A.S.1    Anderson, J.M.2
  • 23
    • 70349317350 scopus 로고    scopus 로고
    • ZO-1 stabilizes the tight junction solute barrier through coupling to the perijunctional cytoskeleton
    • Van Itallie, C.M.; Fanning, A.S.; Bridges, A.; Anderson, J.M. ZO-1 stabilizes the tight junction solute barrier through coupling to the perijunctional cytoskeleton. Mol. Biol. Cell 2009, 20, 3930–3940.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 3930-3940
    • Van Itallie, C.M.1    Fanning, A.S.2    Bridges, A.3    Anderson, J.M.4
  • 24
    • 0034253536 scopus 로고    scopus 로고
    • The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42
    • Joberty, G.; Petersen, C.; Gao, L.; Macara, I.G. The cell-polarity protein Par6 links Par3 and atypical protein kinase C to Cdc42. Nat. Cell Biol. 2000, 2, 531–539.
    • (2000) Nat. Cell Biol , vol.2 , pp. 531-539
    • Joberty, G.1    Petersen, C.2    Gao, L.3    Macara, I.G.4
  • 25
    • 0034623082 scopus 로고    scopus 로고
    • Junctional adhesion molecule interacts with the PDZ domain-containing proteins AF-6 and ZO-1
    • Ebnet, K.; Schulz, C.U.; Meyer Zu Brickwedde, M.K.; Pendl, G.G.; Vestweber, D. Junctional adhesion molecule interacts with the PDZ domain-containing proteins AF-6 and ZO-1. J. Biol. Chem. 2000, 275, 27979–27988.
    • (2000) J. Biol. Chem. , vol.275 , pp. 27979-27988
    • Ebnet, K.1    Schulz, C.U.2    Meyer Zu Brickwedde, M.K.3    Pendl, G.G.4    Vestweber, D.5
  • 26
    • 4744339309 scopus 로고    scopus 로고
    • Isoforms of the polarity protein par6 have distinct functions
    • Gao, L.; Macara, I.G. Isoforms of the polarity protein par6 have distinct functions. J. Biol. Chem. 2004, 279, 41557–41562.
    • (2004) J. Biol. Chem , vol.279 , pp. 41557-41562
    • Gao, L.1    Macara, I.G.2
  • 27
    • 0031440289 scopus 로고    scopus 로고
    • MAGI-1, a membrane-associated guanylate kinase with a unique arrangement of protein-protein interaction domains
    • Dobrosotskaya, I.; Guy, R.K.; James, G.L. MAGI-1, a membrane-associated guanylate kinase with a unique arrangement of protein-protein interaction domains. J. Biol. Chem. 1997, 272, 31589–31597.
    • (1997) J. Biol. Chem , vol.272 , pp. 31589-31597
    • Dobrosotskaya, I.1    Guy, R.K.2    James, G.L.3
  • 28
    • 84877944837 scopus 로고    scopus 로고
    • Epithelial barrier assembly requires coordinated activity of multiple domains of the tight junction protein ZO-1
    • Rodgers, L.S.; Beam, M.T.; Anderson, J.M.; Fanning, A.S. Epithelial barrier assembly requires coordinated activity of multiple domains of the tight junction protein ZO-1. J. Cell Sci. 2013, 126, 1565–1575.
    • (2013) J. Cell Sci , vol.126 , pp. 1565-1575
    • Rodgers, L.S.1    Beam, M.T.2    Anderson, J.M.3    Fanning, A.S.4
  • 30
    • 73149088602 scopus 로고    scopus 로고
    • Rotaviruses require basolateral molecules for efficient infection of polarized MDCKII cells
    • Realpe, M.; Espinosa, R.; López, S.; Arias, C.F. Rotaviruses require basolateral molecules for efficient infection of polarized MDCKII cells. Virus Res. 2010, 147, 231–241.
    • (2010) Virus Res , vol.147 , pp. 231-241
    • Realpe, M.1    Espinosa, R.2    López, S.3    Arias, C.F.4
  • 31
    • 42549140281 scopus 로고    scopus 로고
    • Reovirus preferentially infects the basolateral surface and is released from the apical surface of polarized human respiratory epithelial cells.
    • Excoffon, K.J.; Guglielmi, K.M.; Wetzel, J.D.; Gansemer, N.D.; Campbell, J.A.; Dermody, T.S.; Zabner, J. Reovirus preferentially infects the basolateral surface and is released from the apical surface of polarized human respiratory epithelial cells. J. Infect. Dis. 2008, 197, 1189–1197.
    • (2008) J. Infect. Dis. , vol.197 , pp. 1189-1197
    • Excoffon, K.J.1    Guglielmi, K.M.2    Wetzel, J.D.3    Gansemer, N.D.4    Campbell, J.A.5    Dermody, T.S.6    Zabner, J.7
  • 34
    • 0027166647 scopus 로고
    • Integrins α v β 3 and α v β 5 promote adenovirus internalization but not virus attachment
    • Wickham, T.J.; Mathias, P.; Cheresh, D.A.; Nemerow, G.R. Integrins α v β 3 and α v β 5 promote adenovirus internalization but not virus attachment. Cell 1993, 73, 309–319.
    • (1993) Cell , vol.73 , pp. 309-319
    • Wickham, T.J.1    Mathias, P.2    Cheresh, D.A.3    Nemerow, G.R.4
  • 35
    • 0030610717 scopus 로고    scopus 로고
    • Integrin alpha5beta1-mediated adenovirus infection is enhanced by the integrin-activating antibody TS2/16
    • Davison, E.; Diaz, R.M.; Hart, I.R.; Santis, G.; Marshall, J.F. Integrin alpha5beta1-mediated adenovirus infection is enhanced by the integrin-activating antibody TS2/16. J. Virol. 1997, 71, 6204–6207.
    • (1997) J. Virol , vol.71 , pp. 6204-6207
    • Davison, E.1    Diaz, R.M.2    Hart, I.R.3    Santis, G.4    Marshall, J.F.5
  • 39
    • 84964606786 scopus 로고    scopus 로고
    • 1. Alternative splicing of viral receptors: A review of the diverse morphologies and physiologies of adenoviral receptors
    • Excoffon, K.J.; Bowers, J.R.; Sharma, P. 1. Alternative splicing of viral receptors: A review of the diverse morphologies and physiologies of adenoviral receptors. Recent Res. Dev. Virol. 2014, 9, 1–24.
    • (2014) Recent Res. Dev. Virol , vol.9 , pp. 1-24
    • Excoffon, K.J.1    Bowers, J.R.2    Sharma, P.3
  • 40
    • 16844382964 scopus 로고    scopus 로고
    • CAR: A virus receptor within the tight junction
    • Coyne, C.B.; Bergelson, J.M. CAR: A virus receptor within the tight junction. Adv. Drug Deliv. Rev. 2005, 57, 869–882.
    • (2005) Adv. Drug Deliv. Rev , vol.57 , pp. 869-882
    • Coyne, C.B.1    Bergelson, J.M.2
  • 41
    • 10644287588 scopus 로고    scopus 로고
    • Interaction with coxsackievirus and adenovirus receptor, but not with decay-accelerating factor (DAF), induces A-particle formation in a DAF-binding coxsackievirus B3 isolate
    • Milstone, A.M.; Petrella, J.; Sanchez, M.D.; Mahmud, M.; Whitbeck, J.C.; Bergelson, J.M. Interaction with coxsackievirus and adenovirus receptor, but not with decay-accelerating factor (DAF), induces A-particle formation in a DAF-binding coxsackievirus B3 isolate. J. Virol. 2005, 79, 655–660.
    • (2005) J. Virol , vol.79 , pp. 655-660
    • Milstone, A.M.1    Petrella, J.2    Sanchez, M.D.3    Mahmud, M.4    Whitbeck, J.C.5    Bergelson, J.M.6
  • 42
    • 0036720838 scopus 로고    scopus 로고
    • Interaction with decay-accelerating factor facilitates coxsackievirus B infection of polarized epithelial cells
    • Shieh, J.T.C.; Bergelson, J.M. Interaction with decay-accelerating factor facilitates coxsackievirus B infection of polarized epithelial cells. J. Virol. 2002, 76, 9474–9480.
    • (2002) J. Virol , vol.76 , pp. 9474-9480
    • Shieh, J.T.C.1    Bergelson, J.M.2
  • 43
    • 30344475861 scopus 로고    scopus 로고
    • Virus-induced Abl and Fyn kinase signals permit coxsackievirus entry through epithelial tight junctions
    • Coyne, C.B.; Bergelson, J.M. Virus-induced Abl and Fyn kinase signals permit coxsackievirus entry through epithelial tight junctions. Cell 2006, 124, 119–131.
    • (2006) Cell , vol.124 , pp. 119-131
    • Coyne, C.B.1    Bergelson, J.M.2
  • 44
    • 34548433948 scopus 로고    scopus 로고
    • Coxsackievirus entry from epithelial tight junctions requires occludin and the small GTPases Rab34 and Rab5
    • Coyne, C.B.; Shen, L.; Turner, J.R.; Bergelson, J.M. Coxsackievirus entry from epithelial tight junctions requires occludin and the small GTPases Rab34 and Rab5. Cell Host Microbe 2007, 2, 181–192.
    • (2007) Cell Host Microbe , vol.2 , pp. 181-192
    • Coyne, C.B.1    Shen, L.2    Turner, J.R.3    Bergelson, J.M.4
  • 45
    • 81255123312 scopus 로고    scopus 로고
    • Decay-accelerating factor binding determines the entry route of echovirus 11 in polarized epithelial cells
    • Sobo, K.; Rubbia-Brandt, L.; Brown, T.D.K.; Stuart, A.D.; McKee, T.A. Decay-accelerating factor binding determines the entry route of echovirus 11 in polarized epithelial cells. J. Virol. 2011, 85, 12376–12386.
    • (2011) J. Virol , vol.85 , pp. 12376-12386
    • Sobo, K.1    Rubbia-Brandt, L.2    Brown, T.D.K.3    Stuart, A.D.4    McKee, T.A.5
  • 46
    • 79952430951 scopus 로고    scopus 로고
    • Tupaia CD81, SR-BI, claudin-1, and occluding support hepatitis C virus infection
    • Tong, Y.; Zhu, Y.; Xia, X.; Liu, Y.; Feng, Y.; Hua, X.; Qi, Z.T. Tupaia CD81, SR-BI, claudin-1, and occluding support hepatitis C virus infection. J. Virol. 2011, 85, 2793–2802.
    • (2011) J. Virol , vol.85 , pp. 2793-2802
    • Tong, Y.1    Zhu, Y.2    Xia, X.3    Liu, Y.4    Feng, Y.5    Hua, X.6    Qi, Z.T.7
  • 48
    • 42949118005 scopus 로고    scopus 로고
    • Hepatitis C virus entry
    • Von Hahn, T.; Rice, C.M. Hepatitis C virus entry. J. Biol. Chem. 2008, 283, 3689–3693.
    • (2008) J. Biol. Chem , vol.283 , pp. 3689-3693
    • Von Hahn, T.1    Rice, C.M.2
  • 49
    • 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
  • 50
    • 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
  • 51
    • 84884564516 scopus 로고    scopus 로고
    • The interaction between claudin-1 and dengue viral prM/M protein for its entry
    • Che, P.; Tang, H.; Li, Q. The interaction between claudin-1 and dengue viral prM/M protein for its entry. Virology 2013, 446, 303–313.
    • (2013) Virology , vol.446 , pp. 303-313
    • Che, P.1    Tang, H.2    Li, Q.3
  • 52
    • 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.; López, 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    López, S.4    Arias, C.F.5
  • 53
    • 33646184221 scopus 로고    scopus 로고
    • Junctional adhesion molecule 1 is a functional receptor for feline calicivirus
    • Makino, A.; Shimojima, M.; Miyazawa, T.; Kato, K.; Tohya, Y.; Akashi, H. Junctional adhesion molecule 1 is a functional receptor for feline calicivirus. J. Virol. 2006, 80, 4482–4490.
    • (2006) J. Virol , vol.80 , pp. 4482-4490
    • Makino, A.1    Shimojima, M.2    Miyazawa, T.3    Kato, K.4    Tohya, Y.5    Akashi, H.6
  • 55
    • 58149263468 scopus 로고    scopus 로고
    • Structure of reovirus sigma1 in complex with its receptor junctional adhesion molecule-A
    • Kirchner, E.; Guglielmi, K.M.; Strauss, H.M.; Dermody, T.S.; Stehle, T. Structure of reovirus sigma1 in complex with its receptor junctional adhesion molecule-A. PLoS Pathog. 2008, 4, e1000235.
    • (2008) Plos Pathog , vol.4
    • Kirchner, E.1    Guglielmi, K.M.2    Strauss, H.M.3    Dermody, T.S.4    Stehle, T.5
  • 57
    • 84879564567 scopus 로고    scopus 로고
    • Mechanisms of reovirus bloodstream dissemination
    • Boehme, K.W.; Lai, C.M.; Dermody, T.S. Mechanisms of reovirus bloodstream dissemination. Adv. Virus Res. 2013, 87, 1–35.
    • (2013) Adv. Virus Res , vol.87 , pp. 1-35
    • Boehme, K.W.1    Lai, C.M.2    Dermody, T.S.3
  • 60
    • 84861126381 scopus 로고    scopus 로고
    • West Nile virus-induced disruption of the blood-brain barrier in mice is characterized by the degradation of the junctional complex proteins and increase in multiple matrix metalloproteinases.
    • Roe, K.; Kumar, M.; Lum, S.; Orillo, B.; Nerurkar, V.R.; Verma, S. West Nile virus-induced disruption of the blood-brain barrier in mice is characterized by the degradation of the junctional complex proteins and increase in multiple matrix metalloproteinases. J. Gen. Virol. 2012, 93, 1193–1203.
    • (2012) J. Gen. Virol. , vol.93 , pp. 1193-1203
    • Roe, K.1    Kumar, M.2    Lum, S.3    Orillo, B.4    Nerurkar, V.R.5    Verma, S.6
  • 61
    • 66749140932 scopus 로고    scopus 로고
    • Alterations in actin cytoskeletal assembly and junctional protein complexes in human endothelial cells induced by dengue virus infection and mimicry of leukocyte transendothelial migration
    • Kanlaya, R.; Pattanakitsakul, S.N.; Sinchaikul, S.; Chen, S.T.; Thongboonkerd, V. Alterations in actin cytoskeletal assembly and junctional protein complexes in human endothelial cells induced by dengue virus infection and mimicry of leukocyte transendothelial migration. J. Proteome Res. 2009, 8, 2551–2562.
    • (2009) J. Proteome Res , vol.8 , pp. 2551-2562
    • Kanlaya, R.1    Pattanakitsakul, S.N.2    Sinchaikul, S.3    Chen, S.T.4    Thongboonkerd, V.5
  • 62
    • 34848917967 scopus 로고    scopus 로고
    • Human blood-brain barrier disruption by retroviral-infected lymphocytes: Role of myosin light chain kinase in endothelial tight-junction disorganization
    • Afonso, P.V.; Ozden, S.; Prevost, M.C.; Schmitt, C.; Seilhean, D.; Weksler, B.; Couraud, P.O.; Gessain, A.; Romero, I.A.; Ceccaldi, P.E. Human blood-brain barrier disruption by retroviral-infected lymphocytes: Role of myosin light chain kinase in endothelial tight-junction disorganization. J. Immunol. 2007, 179, 2576–2583.
    • (2007) J. Immunol , vol.179 , pp. 2576-2583
    • Afonso, P.V.1    Ozden, S.2    Prevost, M.C.3    Schmitt, C.4    Seilhean, D.5    Weksler, B.6    Couraud, P.O.7    Gessain, A.8    Romero, I.A.9    Ceccaldi, P.E.10
  • 63
    • 33845764425 scopus 로고    scopus 로고
    • HIV-1 gp120 compromises blood-brain barrier integrity and enhances monocyte migration across blood-brain barrier: Implication for viral neuropathogenesis
    • Kanmogne, G.D.; Schall, K.; Leibhart, J.; Knipe, B.; Gendelman, H.E.; Persidsky, Y. HIV-1 gp120 compromises blood-brain barrier integrity and enhances monocyte migration across blood-brain barrier: Implication for viral neuropathogenesis. J. Cereb. Blood Flow Metab. 2007, 27, 123–134.
    • (2007) J. Cereb. Blood Flow Metab , vol.27 , pp. 123-134
    • Kanmogne, G.D.1    Schall, K.2    Leibhart, J.3    Knipe, B.4    Gendelman, H.E.5    Persidsky, Y.6
  • 64
    • 77952705907 scopus 로고    scopus 로고
    • PDZ domains and their binding partners: Structure, specificity, and modification
    • Lee, H.J.; Zheng, J.J. PDZ domains and their binding partners: Structure, specificity, and modification. Cell Commun. Signal. 2010, 8.
    • (2010) Cell Commun. Signal
    • Lee, H.J.1    Zheng, J.J.2
  • 65
    • 0034597533 scopus 로고    scopus 로고
    • Interactions of the PDZ-protein MAGI-1 with adenovirus E4-ORF1 and high-risk papillomavirus E6 oncoproteins
    • Glaunsinger, B.A.; Lee, S.S.; Thomas, M.; Banks, L.; Javier, R. Interactions of the PDZ-protein MAGI-1 with adenovirus E4-ORF1 and high-risk papillomavirus E6 oncoproteins. Oncogene 2000, 19, 5270–5280.
    • (2000) Oncogene , vol.19 , pp. 5270-5280
    • Glaunsinger, B.A.1    Lee, S.S.2    Thomas, M.3    Banks, L.4    Javier, R.5
  • 66
    • 0035887255 scopus 로고    scopus 로고
    • Link of the unique oncogenic properties of adenovirus type 9 E4-ORF1 to a select interaction with the candidate tumor suppressor protein ZO-2
    • Glaunsinger, B.A.; Weiss, R.S.; Lee, S.S.; Javier, R. Link of the unique oncogenic properties of adenovirus type 9 E4-ORF1 to a select interaction with the candidate tumor suppressor protein ZO-2. EMBO J. 2001, 20, 5578–5586.
    • (2001) EMBO J , vol.20 , pp. 5578-5586
    • Glaunsinger, B.A.1    Weiss, R.S.2    Lee, S.S.3    Javier, R.4
  • 67
    • 0033815457 scopus 로고    scopus 로고
    • Multi-PDZ domain protein MUPP1 is a cellular target for both adenovirus E4-ORF1 and high-risk papillomavirus type 18 E6 oncoproteins
    • Lee, S.S.; Glaunsinger, B.; Mantovani, F.; Banks, L.; Javier, R.T. Multi-PDZ domain protein MUPP1 is a cellular target for both adenovirus E4-ORF1 and high-risk papillomavirus type 18 E6 oncoproteins. J. Virol. 2000, 74, 9680–9693.
    • (2000) J. Virol , vol.74 , pp. 9680-9693
    • Lee, S.S.1    Glaunsinger, B.2    Mantovani, F.3    Banks, L.4    Javier, R.T.5
  • 68
    • 27144466422 scopus 로고    scopus 로고
    • Viral oncoprotein-induced mislocalization of select PDZ proteins disrupts tight junctions and causes polarity defects in epithelial cells
    • Latorre, I.J.; Roh, M.H.; Frese, K.K.; Weiss, R.S.; Margolis, B.; Javier, R.T. Viral oncoprotein-induced mislocalization of select PDZ proteins disrupts tight junctions and causes polarity defects in epithelial cells. J. Cell Sci. 2005, 118, 4283–4293.
    • (2005) J. Cell Sci , vol.118 , pp. 4283-4293
    • Latorre, I.J.1    Roh, M.H.2    Frese, K.K.3    Weiss, R.S.4    Margolis, B.5    Javier, R.T.6
  • 69
    • 80054997526 scopus 로고    scopus 로고
    • The avian influenza virus NS1 ESEV PDZ binding motif associates with Dlg1 and Scribble to disrupt cellular tight junctions
    • Golebiewski, L.; Liu, H.; Javier, R.T.; Rice, A.P. The avian influenza virus NS1 ESEV PDZ binding motif associates with Dlg1 and Scribble to disrupt cellular tight junctions. J. Virol. 2011, 85, 10639–10648.
    • (2011) J. Virol , vol.85 , pp. 10639-10648
    • Golebiewski, L.1    Liu, H.2    Javier, R.T.3    Rice, A.P.4
  • 70
  • 71
    • 84896777815 scopus 로고    scopus 로고
    • HIV-associated disruption of tight and adherens junctions of oral epithelial cells facilitates HSV-1 infection and spread
    • Sufiawati, I.; Tugizov, S.M. HIV-associated disruption of tight and adherens junctions of oral epithelial cells facilitates HSV-1 infection and spread. PLoS ONE 2014, 9, e88803.
    • (2014) Plos ONE , vol.9
    • Sufiawati, I.1    Tugizov, S.M.2
  • 72
    • 0037145045 scopus 로고    scopus 로고
    • Adenovirus fiber disrupts CAR-mediated intercellular adhesion allowing virus escape
    • Walters, R.W.; Freimuth, P.; Moninger, T.O.; Ganske, I.; Zabner, J.; Welsh, M.J. Adenovirus fiber disrupts CAR-mediated intercellular adhesion allowing virus escape. Cell 2002, 110, 789–799.
    • (2002) Cell , vol.110 , pp. 789-799
    • Walters, R.W.1    Freimuth, P.2    Moninger, T.O.3    Ganske, I.4    Zabner, J.5    Welsh, M.J.6


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