메뉴 건너뛰기




Volumn 359, Issue , 2012, Pages 59-78

Henipavirus receptor usage and tropism

Author keywords

[No Author keywords available]

Indexed keywords

EPHRIN B2; EPHRIN B3; VIRUS RECEPTOR;

EID: 84868310649     PISSN: 0070217X     EISSN: None     Source Type: Book Series    
DOI: 10.1007/82-2012-222     Document Type: Review
Times cited : (56)

References (118)
  • 1
    • 0033082959 scopus 로고    scopus 로고
    • Roles of ephrinB ligands and EphB receptors in cardiovascular development: Demarcation of arterial/venous domains, vascular morphogenesis, and sprouting angiogenesis
    • Adams RH, Wilkinson GA, Weiss C, Diella F, Gale NW et al (1999) Roles of ephrinb ligands and ephb receptors in cardiovascular development: demarcation of arterial/venous domains, vascular morphogenesis, and sprouting angiogenesis. Genes Dev 13:295-306 (Pubitemid 29095801)
    • (1999) Genes and Development , vol.13 , Issue.3 , pp. 295-306
    • Adams, R.H.1    Wilkinson, G.A.2    Weiss, C.3    Diella, F.4    Gale, N.W.5    Deutsch, U.6    Risau, W.7    Klein, R.8
  • 2
    • 79956089435 scopus 로고    scopus 로고
    • Emerging Paramyxoviruses: Molecular mechanisms and antiviral strategies
    • Aguilar HC, Lee B (2011) Emerging Paramyxoviruses: molecular mechanisms and antiviral strategies. Expert Rev Mol Med 13:e6
    • (2011) Expert Rev Mol Med , vol.13
    • Aguilar, H.C.1    Lee, B.2
  • 3
    • 0028941623 scopus 로고
    • Molecular cloning of a ligand for the eph-related receptor protein-tyrosine kinase htk
    • Bennett BD, Zeigler FC, Gu Q, Fendly B, Goddard AD et al (1995) Molecular cloning of a ligand for the eph-related receptor protein-tyrosine kinase htk. Proc Natl Acad Sci USA 92:1866-1870
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 1866-1870
    • Bennett, B.D.1    Zeigler, F.C.2    Gu, Q.3    Fendly, B.4    Goddard, A.D.5
  • 5
    • 0029099583 scopus 로고
    • Elf-2, a new member of the eph ligand family, is segmentally expressed in mouse embryos in the region of the hindbrain and newly forming somites
    • Bergemann AD, Cheng HJ, Brambilla R, Klein R, Flanagan JG (1995) Elf-2, a new member of the eph ligand family, is segmentally expressed in mouse embryos in the region of the hindbrain and newly forming somites. Mol Cell Biol 15:4921-4929
    • (1995) Mol Cell Biol , vol.15 , pp. 4921-4929
    • Bergemann, A.D.1    Cheng, H.J.2    Brambilla, R.3    Klein, R.4    Flanagan, J.G.5
  • 6
    • 0032576874 scopus 로고    scopus 로고
    • Ephrin-B3, a ligand for the receptor EphB3, expressed at the midline of the developing neural tube
    • Bergemann AD, Zhang L, Chiang MK, Brambilla R, Klein R et al (1998) Ephrin-B3, a ligand for the receptor EphB3, expressed at the midline of the developing neural tube. Oncogene 16:471-480 (Pubitemid 28062074)
    • (1998) Oncogene , vol.16 , Issue.4 , pp. 471-480
    • Bergemann, A.D.1    Zhang, L.2    Chiang, M.-K.3    Brambilla, R.4    Klein, R.5    Flanagan, J.G.6
  • 7
    • 55549116002 scopus 로고    scopus 로고
    • Residues in the stalk domain of the Hendra virus g glycoprotein modulate conformational changes associated with receptor binding
    • Bishop KA, Hickey AC, Khetawat D, Patch JR, Bossart KN et al (2008) Residues in the stalk domain of the Hendra virus g glycoprotein modulate conformational changes associated with receptor binding. J Virol 82:11398-11409
    • (2008) J Virol , vol.82 , pp. 11398-11409
    • Bishop, K.A.1    Hickey, A.C.2    Khetawat, D.3    Patch, J.R.4    Bossart, K.N.5
  • 10
    • 80054788706 scopus 로고    scopus 로고
    • A neutralizing human monoclonal antibody protects African green monkeys from Hendra virus challenge
    • Bossart KN, Geisbert TW, Feldmann H, Zhu Z, Feldmann F et al (2011) A neutralizing human monoclonal antibody protects African green monkeys from Hendra virus challenge. Sci Transl Med 3:105ra103
    • (2011) Sci Transl Med , vol.3
    • Bossart, K.N.1    Geisbert, T.W.2    Feldmann, H.3    Zhu, Z.4    Feldmann, F.5
  • 12
    • 0035841668 scopus 로고    scopus 로고
    • Functional expression and membrane fusion tropism of the envelope glycoproteins of Hendra virus
    • DOI 10.1006/viro.2001.1158
    • Bossart KN, Wang LF, Eaton BT, Broder CC (2001) Functional expression and membrane fusion tropism of the envelope glycoproteins of Hendra virus. Virology 290:121-135 (Pubitemid 33111883)
    • (2001) Virology , vol.290 , Issue.1 , pp. 121-135
    • Bossart, K.N.1    Wang, L.-F.2    Eaton, B.T.3    Broder, C.C.4
  • 13
    • 73849092511 scopus 로고    scopus 로고
    • A neutralizing human monoclonal antibody protects against lethal disease in a new ferret model of acute Nipah virus infection
    • Bossart KN, Zhu Z, Middleton D, Klippel J, Crameri G et al (2009) A neutralizing human monoclonal antibody protects against lethal disease in a new ferret model of acute Nipah virus infection. PLoS Pathog 5:e1000642
    • (2009) PLoS Pathog , vol.5
    • Bossart, K.N.1    Zhu, Z.2    Middleton, D.3    Klippel, J.4    Crameri, G.5
  • 15
    • 56449121966 scopus 로고    scopus 로고
    • Crystal structure and carbohydrate analysis of Nipah virus attachment glycoprotein: A template for antiviral and vaccine design
    • Bowden TA, Crispin M, Harvey DJ, Aricescu AR, Grimes JM et al (2008b) Crystal structure and carbohydrate analysis of Nipah virus attachment glycoprotein: a template for antiviral and vaccine design. J Virol 82:11628-11636
    • (2008) J Virol , vol.82 , pp. 11628-11636
    • Bowden, T.A.1    Crispin, M.2    Harvey, D.J.3    Aricescu, A.R.4    Grimes, J.M.5
  • 16
    • 77952691868 scopus 로고    scopus 로고
    • Dimeric architecture of the Hendra virus attachment glycoprotein: Evidence for a conserved mode of assembly
    • Bowden TA, Crispin M, Harvey DJ, Jones EY, Stuart DI (2010a) Dimeric architecture of the Hendra virus attachment glycoprotein: evidence for a conserved mode of assembly. J Virol 84:6208-6217
    • (2010) J Virol , vol.84 , pp. 6208-6217
    • Bowden, T.A.1    Crispin, M.2    Harvey, D.J.3    Jones, E.Y.4    Stuart, D.I.5
  • 17
    • 77957287360 scopus 로고    scopus 로고
    • Shared paramyxoviral glycoprotein architecture is adapted for diverse attachment strategies
    • Bowden TA, Crispin M, Jones EY, Stuart DI (2010b) Shared paramyxoviral glycoprotein architecture is adapted for diverse attachment strategies. Biochem Soc Trans 38:1349-1355
    • (2010) Biochem Soc Trans , vol.38 , pp. 1349-1355
    • Bowden, T.A.1    Crispin, M.2    Jones, E.Y.3    Stuart, D.I.4
  • 20
    • 79952613929 scopus 로고    scopus 로고
    • Epidemiology, surveillance and control of Nipah virus infections in Malaysia
    • Chua KB (2010) Epidemiology, surveillance and control of Nipah virus infections in Malaysia. Malays J Pathol 32:69-73
    • (2010) Malays J Pathol , vol.32 , pp. 69-73
    • Chua, K.B.1
  • 22
    • 0035855819 scopus 로고    scopus 로고
    • The SH2/SH3 adaptor Grb4 transduces B-ephrin reverse signals
    • DOI 10.1038/35093123
    • Cowan CA, Henkemeyer M (2001) The sh2/sh3 adaptor grb4 transduces B-ephrin reverse signals. Nature 413:174-179 (Pubitemid 32867879)
    • (2001) Nature , vol.413 , Issue.6852 , pp. 174-179
    • Cowan, C.A.1    Henkemeyer, M.2
  • 24
    • 51449104971 scopus 로고    scopus 로고
    • Eph receptors and ephrin signaling pathways: A role in bone homeostasis
    • Edwards CM, Mundy GR (2008) Eph receptors and ephrin signaling pathways: a role in bone homeostasis. Int J Med Sci 5:263-272
    • (2008) Int J Med Sci , vol.5 , pp. 263-272
    • Edwards, C.M.1    Mundy, G.R.2
  • 25
    • 0031559401 scopus 로고    scopus 로고
    • Unified nomenclature for eph family receptors and their ligands, the ephrins. Eph nomenclature committee
    • Eph Nomenclature Committee
    • Eph Nomenclature Committee (1997) Unified nomenclature for eph family receptors and their ligands, the ephrins. Eph nomenclature committee. Cell 90:403-404
    • (1997) Cell , vol.90 , pp. 403-404
  • 26
    • 58149168980 scopus 로고    scopus 로고
    • Selective receptor expression restricts Nipah virus infection of endothelial cells
    • Erbar S, Diederich S, Maisner A (2008) Selective receptor expression restricts Nipah virus infection of endothelial cells. Virol. J 5:142
    • (2008) Virol. J , vol.5 , pp. 142
    • Erbar, S.1    Diederich, S.2    Maisner, A.3
  • 28
    • 0038497941 scopus 로고    scopus 로고
    • Forward EphB4 signaling in endothelial cells controls cellular repulsion and segregation from ephrinB2 positive cells
    • DOI 10.1242/jcs.00426
    • Füller T, Korff T, Kilian A, Dandekar G, Augustin HG (2003) Forward ephb4 signaling in endothelial cells controls cellular repulsion and segregation from ephrinB2 positive cells. J Cell Sci 116:2461-2470 (Pubitemid 36790128)
    • (2003) Journal of Cell Science , vol.116 , Issue.12 , pp. 2461-2470
    • Fuller, T.1    Korff, T.2    Kilian, A.3    Dandekar, G.4    Augustin, H.G.5
  • 29
    • 0035865227 scopus 로고    scopus 로고
    • Ephrin-B2 selectively marks arterial vessels and neovascularization sites in the adult, with expression in both endothelial and smooth-muscle cells
    • DOI 10.1006/dbio.2000.0112
    • Gale NW, Baluk P, Pan L, Kwan M, Holash J et al (2001) Ephrin-B2 selectively marks arterial vessels and neovascularization sites in the adult, with expression in both endothelial and smooth-muscle cells. Dev Biol 230:151-160 (Pubitemid 32171414)
    • (2001) Developmental Biology , vol.230 , Issue.2 , pp. 151-160
    • Gale, N.W.1    Baluk, P.2    Pan, L.3    Kwan, M.4    Holash, J.5    DeChiara, T.M.6    McDonald, D.M.7    Yancopoulos, G.D.8
  • 30
    • 77956283436 scopus 로고    scopus 로고
    • Development of an acute and highly pathogenic nonhuman primate model of Nipah virus infection
    • Geisbert TW, Daddario-DiCaprio KM, Hickey AC, Smith MA, Chan Y et al (2010) Development of an acute and highly pathogenic nonhuman primate model of Nipah virus infection. PLoS ONE 5:e10690
    • (2010) PLoS ONE , vol.5
    • Geisbert, T.W.1    Daddario-DiCaprio, K.M.2    Hickey, A.C.3    Smith, M.A.4    Chan, Y.5
  • 31
    • 33645277094 scopus 로고    scopus 로고
    • Metalloproteinase/presenilin1 processing of ephrinb regulates ephb-induced src phosphorylation and signaling
    • Georgakopoulos A, Litterst C, Ghersi E, Baki L, Xu C et al (2006) Metalloproteinase/presenilin1 processing of ephrinb regulates ephb-induced src phosphorylation and signaling. EMBO J 25:1242-1252
    • (2006) EMBO J , vol.25 , pp. 1242-1252
    • Georgakopoulos, A.1    Litterst, C.2    Ghersi, E.3    Baki, L.4    Xu, C.5
  • 32
    • 80053931329 scopus 로고    scopus 로고
    • Presenilin1/gamma-secretase promotes the ephb2-induced phosphorylation of ephrinB2 by regulating phosphoprotein associated with glycosphingolipid- enriched microdomains/csk binding protein
    • Georgakopoulos A, Xu J, Xu C, Mauger G, Barthet G et al (2011) Presenilin1/gamma-secretase promotes the ephb2-induced phosphorylation of ephrinB2 by regulating phosphoprotein associated with glycosphingolipid-enriched microdomains/csk binding protein. FASEB J 25:3594-3604
    • (2011) FASEB J , vol.25 , pp. 3594-3604
    • Georgakopoulos, A.1    Xu, J.2    Xu, C.3    Mauger, G.4    Barthet, G.5
  • 33
    • 0036337787 scopus 로고    scopus 로고
    • Cardiovascular ephrinB2 function is essential for embryonic angiogenesis
    • Gerety SS, Anderson DJ (2002) Cardiovascular ephrinB2 function is essential for embryonic angiogenesis. Development 129:1397-1410 (Pubitemid 34874161)
    • (2002) Development , vol.129 , Issue.6 , pp. 1397-1410
    • Gerety, S.S.1    Anderson, D.J.2
  • 35
    • 33746214691 scopus 로고    scopus 로고
    • Evidence of a potential receptor-binding site on the Nipah virus G protein (NiV-G): Identification of globular head residues with a role in fusion promotion and their localization on an NiV-G structural model
    • DOI 10.1128/JVI.00190-06
    • Guillaume V, Aslan H, Ainouze M, Guerbois M, Wild TF et al (2006) Evidence of a potential receptor-binding site on the Nipah virus g protein (NiV-G): identification of globular head residues with a role in fusion promotion and their localization on an NiV-G structural model. J Virol 80:7546-7554 (Pubitemid 44092576)
    • (2006) Journal of Virology , vol.80 , Issue.15 , pp. 7546-7554
    • Guillaume, V.1    Aslan, H.2    Ainouze, M.3    Guerbois, M.4    Wild, T.F.5    Buckland, R.6    Langedijk, J.P.M.7
  • 36
    • 33748850801 scopus 로고    scopus 로고
    • Expression profile of Eph receptors and ephrin ligands in human skin and downregulation of EphA1 in nonmelanoma skin cancer
    • DOI 10.1038/modpathol.3800660, PII 3800660
    • Hafner C, Becker B, Landthaler M, Vogt T (2006) Expression profile of Eph receptors and ephrin ligands in human skin and downregulation of epha1 in nonmelanoma skin cancer. Mod Pathol 19:1369-1377 (Pubitemid 44423085)
    • (2006) Modern Pathology , vol.19 , Issue.10 , pp. 1369-1377
    • Hafner, C.1    Becker, B.2    Landthaler, M.3    Vogt, T.4
  • 37
    • 84857551831 scopus 로고    scopus 로고
    • Serologic evidence of Nipah virus infection in bats, Vietnam
    • Hasebe F, Thuy NTT, Inoue S, Yu F, Kaku Y et al (2012) Serologic evidence of Nipah virus infection in bats, Vietnam. Emerg Infect Dis 18:536-537
    • (2012) Emerg Infect Dis , vol.18 , pp. 536-537
    • Hasebe, F.1    Thuy, N.T.T.2    Inoue, S.3    Yu, F.4    Kaku, Y.5
  • 38
    • 84868140783 scopus 로고    scopus 로고
    • Measles virus hemagglutinin: Structural insights into cell entry and measles vaccine
    • Hashiguchi T, Maenaka K, Yanagi Y (2011a) Measles virus hemagglutinin: structural insights into cell entry and measles vaccine. Front Microbiol 2:247
    • (2011) Front Microbiol , vol.2 , pp. 247
    • Hashiguchi, T.1    Maenaka, K.2    Yanagi, Y.3
  • 39
    • 79551638780 scopus 로고    scopus 로고
    • Structure of the Measles virus hemagglutinin bound to its cellular receptor slam
    • Hashiguchi T, Ose T, Kubota M, Maita N, Kamishikiryo J et al (2011b) Structure of the Measles virus hemagglutinin bound to its cellular receptor slam. Nat Struct Mol Biol 18:135-141
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 135-141
    • Hashiguchi, T.1    Ose, T.2    Kubota, M.3    Maita, N.4    Kamishikiryo, J.5
  • 41
    • 80053070526 scopus 로고    scopus 로고
    • Antibodies to Henipavirus or Henipa-like viruses in domestic pigs in Ghana, West Africa
    • Hayman DTS, Wang L, Barr J, Baker KS, Suu-Ire R et al (2011) Antibodies to Henipavirus or Henipa-like viruses in domestic pigs in Ghana, West Africa. PLoS ONE 6:e25256
    • (2011) PLoS ONE , vol.6
    • Hayman, D.T.S.1    Wang, L.2    Barr, J.3    Baker, K.S.4    Suu-Ire, R.5
  • 42
    • 35548948069 scopus 로고    scopus 로고
    • Cell-cell signaling via Eph receptors and ephrins
    • DOI 10.1016/j.ceb.2007.08.004, PII S0955067407001214, Cell to Cell Contact and Extracellular Matrix
    • Himanen J, Saha N, Nikolov DB (2007) Cell-cell signaling via Eph receptors and ephrins. Curr Opin Cell Biol 19:534-542 (Pubitemid 350016850)
    • (2007) Current Opinion in Cell Biology , vol.19 , Issue.5 , pp. 534-542
    • Himanen, J.-P.1    Saha, N.2    Nikolov, D.B.3
  • 43
    • 0036568740 scopus 로고    scopus 로고
    • Ephrins are not only unattractive
    • DOI 10.1016/S0166-2236(02)02149-5, PII S0166223602021495
    • Holmberg J, Frisén J (2002) Ephrins are not only unattractive. Trends Neurosci 25:239-243 (Pubitemid 34327797)
    • (2002) Trends in Neurosciences , vol.25 , Issue.5 , pp. 239-243
    • Holmberg, J.1    Frisen, J.2
  • 44
    • 77957294138 scopus 로고    scopus 로고
    • Nipah virus outbreak with person-to-person transmission in a district of Bangladesh, 2007
    • Homaira N, Rahman M, Hossain MJ, Epstein JH, Sultana R et al (2010) Nipah virus outbreak with person-to-person transmission in a district of Bangladesh, 2007. Epidemiol Infect 138:1630-1636
    • (2010) Epidemiol Infect , vol.138 , pp. 1630-1636
    • Homaira, N.1    Rahman, M.2    Hossain, M.J.3    Epstein, J.H.4    Sultana, R.5
  • 45
    • 0035028638 scopus 로고    scopus 로고
    • Comparative pathology of the diseases caused by Hendra and Nipah viruses
    • DOI 10.1016/S1286-4579(01)01385-5
    • Hooper P, Zaki S, Daniels P, Middleton D (2001) Comparative pathology of the diseases caused by Hendra and Nipah viruses. Microbes Infect 3:315-322 (Pubitemid 32385781)
    • (2001) Microbes and Infection , vol.3 , Issue.4 , pp. 315-322
    • Hooper, P.1    Zaki, S.2    Daniels, P.3    Middleton, D.4
  • 46
    • 0031179382 scopus 로고    scopus 로고
    • Lesions of experimental equine morbillivirus pneumonia in horses
    • Hooper PT, Ketterer PJ, Hyatt AD, Russell GM (1997a) Lesions of experimental equine Morbillivirus pneumonia in horses. Vet Pathol 34:312-322 (Pubitemid 127471113)
    • (1997) Veterinary Pathology , vol.34 , Issue.4 , pp. 312-322
    • Hooper, P.T.1    Ketterer, P.J.2    Hyatt, A.D.3    Russell, G.M.4
  • 47
    • 0031183813 scopus 로고    scopus 로고
    • Lesions of experimental equine morbillivirus disease in cats and guinea pigs
    • Hooper PT, Westbury HA, Russell GM (1997b) The lesions of experimental equine Morbillivirus disease in cats and guinea pigs. Vet Pathol 34:323-329 (Pubitemid 127471114)
    • (1997) Veterinary Pathology , vol.34 , Issue.4 , pp. 323-329
    • Hooper, P.T.1    Westbury, H.A.2    Russell, G.M.3
  • 52
    • 29144460894 scopus 로고    scopus 로고
    • Paramyxovirus membrane fusion: Lessons from the F and HN atomic structures
    • DOI 10.1016/j.virol.2005.09.007, PII S0042682205005684
    • Lamb RA, Paterson RG, Jardetzky TS (2006) Paramyxovirus membrane fusion: lessons from the F and HN atomic structures. Virology 344:30-37 (Pubitemid 41814447)
    • (2006) Virology , vol.344 , Issue.1 , pp. 30-37
    • Lamb, R.A.1    Paterson, R.G.2    Jardetzky, T.S.3
  • 53
    • 34250314942 scopus 로고    scopus 로고
    • Envelope-receptor interactions in Nipah virus pathobiology
    • DOI 10.1196/annals.1408.004, Biology of Emerging Viruses: SARS, Avian and Human Influenza, Metapneumovirus, Nipah, West Nile, and Ross River Virus
    • Lee B (2007) Envelope-receptor interactions in Nipah virus pathobiology. Ann NY Acad Sci 1102:51-65 (Pubitemid 47084909)
    • (2007) Annals of the New York Academy of Sciences , vol.1102 , pp. 51-65
    • Lee, B.1
  • 54
    • 79960918320 scopus 로고    scopus 로고
    • Modes of Paramyxovirus fusion: A Henipavirus perspective
    • Lee B, Ataman ZA (2011) Modes of Paramyxovirus fusion: a Henipavirus perspective. Trends Microbiol 19:389-399
    • (2011) Trends Microbiol , vol.19 , pp. 389-399
    • Lee, B.1    Ataman, Z.A.2
  • 55
    • 57049185810 scopus 로고    scopus 로고
    • Antibodies to nipah or nipah-like viruses in bats, China
    • Li Y, Wang J, Hickey AC, Zhang Y, Li Y et al (2008) Antibodies to nipah or nipah-like viruses in bats, China. Emerg Infect Dis 14:1974-1976
    • (2008) Emerg Infect Dis , vol.14 , pp. 1974-1976
    • Li, Y.1    Wang, J.2    Hickey, A.C.3    Zhang, Y.4    Li, Y.5
  • 56
    • 0037214226 scopus 로고    scopus 로고
    • MRNA expression of ephrins and Eph receptor tyrosine kinases in the neonatal and adult mouse central nervous system
    • DOI 10.1002/jnr.10457
    • Liebl DJ, Morris CJ, Henkemeyer M, Parada LF (2003) mRNA expression of ephrins and Eph receptor tyrosine kinases in the neonatal and adult mouse central nervous system. J Neurosci Res 71:7-22 (Pubitemid 36008398)
    • (2003) Journal of Neuroscience Research , vol.71 , Issue.1 , pp. 7-22
    • Liebl, D.J.1    Morris, C.J.2    Henkemeyer, M.3    Parada, L.F.4
  • 57
    • 0033129780 scopus 로고    scopus 로고
    • Meningoencephalitis caused by a novel Paramyxovirus: An advanced MRI case report in an emerging disease
    • Lim CC, Sitoh YY, Lee KE, Kurup A, Hui F (1999) Meningoencephalitis caused by a novel Paramyxovirus: an advanced MRI case report in an emerging disease. Singap Med J 40:356-358
    • (1999) Singap Med J , vol.40 , pp. 356-358
    • Lim, C.C.1    Sitoh, Y.Y.2    Lee, K.E.3    Kurup, A.4    Hui, F.5
  • 59
    • 72849124628 scopus 로고    scopus 로고
    • Transmission of human infection with Nipah virus
    • Luby SP, Gurley ES, Hossain MJ (2009) Transmission of human infection with Nipah virus. Clin Infect Dis 49:1743-1748
    • (2009) Clin Infect Dis , vol.49 , pp. 1743-1748
    • Luby, S.P.1    Gurley, E.S.2    Hossain, M.J.3
  • 63
    • 84863995623 scopus 로고    scopus 로고
    • Cysteines in the stalk of the Nipah virus G glycoprotein are located in a distinct subdomain critical for fusion activation
    • (in press)
    • Maar D, Harmon B, Chu D et al (2012) Cysteines in the stalk of the Nipah virus G glycoprotein are located in a distinct subdomain critical for fusion activation. J Virol (in press)
    • (2012) J Virol
    • Maar, D.1    Harmon, B.2    Chu, D.3
  • 64
    • 0141839882 scopus 로고    scopus 로고
    • Rac-dependent trans-endocytosis of ephrinBs regulates Eph-ephrin contact repulsion
    • DOI 10.1038/ncb1044
    • Marston DJ, Dickinson S, Nobes CD (2003) Rac-dependent trans-endocytosis of ephrinbs regulates Eph-ephrin contact repulsion. Nat Cell Biol 5:879-888 (Pubitemid 37220693)
    • (2003) Nature Cell Biology , vol.5 , Issue.10 , pp. 879-888
    • Marston, D.J.1    Dickinson, S.2    Nobes, C.D.3
  • 65
    • 4143051366 scopus 로고    scopus 로고
    • Measles virus (MV) hemagglutinin: Evidence that attachment sites for MV receptors SLAM and CD46 overlap on the globular head
    • DOI 10.1128/JVI.78.17.9051-9063.2004
    • Massé N, Ainouze M, Néel B, Wild TF, Buckland R et al (2004) Measles virus (mv) hemagglutinin: evidence that attachment sites for mv receptors slam and CD46 overlap on the globular head. J Virol 78:9051-9063 (Pubitemid 39096516)
    • (2004) Journal of Virology , vol.78 , Issue.17 , pp. 9051-9063
    • Masse, N.1    Ainouze, M.2    Neel, B.3    Wild, T.F.4    Buckland, R.5    Langedijk, J.P.M.6
  • 66
    • 79960427717 scopus 로고    scopus 로고
    • Nipah virus uses leukocytes for efficient dissemination within a host
    • Mathieu C, Pohl C, Szecsi J, Trajkovic-Bodennec S, Devergnas S et al (2011) Nipah virus uses leukocytes for efficient dissemination within a host. J Virol 85:7863-7871
    • (2011) J Virol , vol.85 , pp. 7863-7871
    • Mathieu, C.1    Pohl, C.2    Szecsi, J.3    Trajkovic-Bodennec, S.4    Devergnas, S.5
  • 67
    • 82455167216 scopus 로고    scopus 로고
    • Investigation of the climatic and environmental context of Hendra virus spillover events 1994-2010
    • McFarlane R, Becker N, Field H (2011) Investigation of the climatic and environmental context of Hendra virus spillover events 1994-2010. PLoS ONE 6:e28374
    • (2011) PLoS ONE , vol.6
    • McFarlane, R.1    Becker, N.2    Field, H.3
  • 68
    • 42549153337 scopus 로고    scopus 로고
    • Vaccinia virus uses macropinocytosis and apoptotic mimicry to enter host cells
    • DOI 10.1126/science.1155164
    • Mercer J, Helenius A (2008) Vaccinia virus uses macropinocytosis and apoptotic mimicry to enter host cells. Science 320:531-535 (Pubitemid 351590666)
    • (2008) Science , vol.320 , Issue.5875 , pp. 531-535
    • Mercer, J.1    Helenius, A.2
  • 69
    • 33644639107 scopus 로고    scopus 로고
    • Ephrin-B2 overexpression enhances integrin-mediated ECM-attachment and migration of B16 melanoma cells
    • Meyer S, Hafner C, Guba M, Flegel S, Geissler EK et al (2005) Ephrin-B2 overexpression enhances integrin-mediated ECM-attachment and migration of B16 melanoma cells. Int J Oncol 27:1197-1206
    • (2005) Int J Oncol , vol.27 , pp. 1197-1206
    • Meyer, S.1    Hafner, C.2    Guba, M.3    Flegel, S.4    Geissler, E.K.5
  • 71
    • 84355161614 scopus 로고    scopus 로고
    • Adherens junction protein nectin-4 is the epithelial receptor for Measles virus
    • Mühlebach MD, Mateo M, Sinn PL, Prüfer S, Uhlig KM et al (2011) Adherens junction protein nectin-4 is the epithelial receptor for Measles virus. Nature 480:530-533
    • (2011) Nature , vol.480 , pp. 530-533
    • Mühlebach, M.D.1    Mateo, M.2    Sinn, P.L.3    Prüfer, S.4    Uhlig, K.M.5
  • 74
    • 79954434311 scopus 로고    scopus 로고
    • Date palm sap collection: Exploring opportunities to prevent nipah transmission
    • Nahar N, Sultana R, Gurley ES, Hossain MJ, Luby SP (2010) Date palm sap collection: exploring opportunities to prevent nipah transmission. Ecohealth 7:196-203
    • (2010) Ecohealth , vol.7 , pp. 196-203
    • Nahar, N.1    Sultana, R.2    Gurley, E.S.3    Hossain, M.J.4    Luby, S.P.5
  • 75
    • 34648830167 scopus 로고    scopus 로고
    • Single amino acid changes in the Nipah and Hendra virus attachment glycoproteins distinguish ephrinb2 from ephrinb3 usage
    • DOI 10.1128/JVI.00999-07
    • Negrete OA, Chu D, Aguilar HC, Lee B (2007) Single amino acid changes in the nipah and Hendra virus attachment glycoproteins distinguish ephrinB2 from ephrinB3 usage. J Virol 81:10804-10814 (Pubitemid 47463353)
    • (2007) Journal of Virology , vol.81 , Issue.19 , pp. 10804-10814
    • Negrete, O.A.1    Chu, D.2    Aguilar, H.C.3    Lee, B.4
  • 77
    • 33645764477 scopus 로고    scopus 로고
    • Two key residues in ephrinB3 are critical for its use as an alternative receptor for Nipah virus
    • Negrete OA, Wolf MC, Aguilar HC, Enterlein S, Wang W et al (2006) Two key residues in ephrinB3 are critical for its use as an alternative receptor for Nipah virus. PLoS Pathog 2:e7
    • (2006) PLoS Pathog , vol.2
    • Negrete, O.A.1    Wolf, M.C.2    Aguilar, H.C.3    Enterlein, S.4    Wang, W.5
  • 80
    • 1642422313 scopus 로고    scopus 로고
    • Intramembrane cleavage of ephrinB3 by the human rhomboid family protease, RHBDL2
    • DOI 10.1016/j.bbrc.2004.03.039, PII S0006291X04005339
    • Pascall JC, Brown KD (2004) Intramembrane cleavage of ephrinB3 by the human rhomboid family protease, RHBDl2. Biochem Biophys Res Commun 317:244-252 (Pubitemid 38401991)
    • (2004) Biochemical and Biophysical Research Communications , vol.317 , Issue.1 , pp. 244-252
    • Pascall, J.C.1    Brown, K.D.2
  • 81
    • 41149084179 scopus 로고    scopus 로고
    • Eph-ephrin bidirectional signaling in physiology and disease
    • DOI 10.1016/j.cell.2008.03.011, PII S0092867408003863
    • Pasquale EB (2008) Eph-ephrin bidirectional signaling in physiology and disease. Cell 133:38-52 (Pubitemid 351442996)
    • (2008) Cell , vol.133 , Issue.1 , pp. 38-52
    • Pasquale, E.B.1
  • 83
    • 59549088691 scopus 로고    scopus 로고
    • Involvement of endothelial ephrin-B2 in adhesion and transmigration of EphB-receptor-expressing monocytes
    • Pfaff D, Héroult M, Riedel M, Reiss Y, Kirmse R et al (2008) Involvement of endothelial ephrin-B2 in adhesion and transmigration of EphB-receptor-expressing monocytes. J Cell Sci 121:3842-3850
    • (2008) J Cell Sci , vol.121 , pp. 3842-3850
    • Pfaff, D.1    Héroult, M.2    Riedel, M.3    Reiss, Y.4    Kirmse, R.5
  • 84
    • 78349252732 scopus 로고    scopus 로고
    • Eph/ephrin molecules - A hub for signaling and endocytosis
    • Pitulescu ME, Adams RH (2010) Eph/ephrin molecules - a hub for signaling and endocytosis. Genes Dev 24:2480-2492
    • (2010) Genes Dev , vol.24 , pp. 2480-2492
    • Pitulescu, M.E.1    Adams, R.H.2
  • 86
    • 0032900498 scopus 로고    scopus 로고
    • ARF6 requirement for Rac ruffling suggests a role for membrane trafficking in cortical actin rearrangements
    • Radhakrishna H, Al-Awar O, Khachikian Z, Donaldson JG (1999) ARF6 requirement for Rac ruffling suggests a role for membrane trafficking in cortical actin rearrangements. J Cell Sci 112(Pt 6):855-866 (Pubitemid 29179318)
    • (1999) Journal of Cell Science , vol.112 , Issue.6 , pp. 855-866
    • Radhakrishna, H.1    Al-Awar, O.2    Khachikian, Z.3    Donaldson, J.G.4
  • 88
    • 77956865767 scopus 로고    scopus 로고
    • A novel model of lethal Hendra virus infection in African green monkeys and the effectiveness of ribavirin treatment
    • Rockx B, Bossart KN, Feldmann F, Geisbert JB, Hickey AC et al (2010) A novel model of lethal Hendra virus infection in African green monkeys and the effectiveness of ribavirin treatment. J Virol 84:9831-9839
    • (2010) J Virol , vol.84 , pp. 9831-9839
    • Rockx, B.1    Bossart, K.N.2    Feldmann, F.3    Geisbert, J.B.4    Hickey, A.C.5
  • 89
    • 78149301316 scopus 로고    scopus 로고
    • Cellular entry of Ebola virus involves uptake by a macropinocytosis-like mechanism and subsequent trafficking through early and late endosomes
    • Saeed MF, Kolokoltsov AA, Albrecht T, Davey RA (2010) Cellular entry of Ebola virus involves uptake by a macropinocytosis-like mechanism and subsequent trafficking through early and late endosomes. PLoS Pathog 6:e1001110
    • (2010) PLoS Pathog , vol.6
    • Saeed, M.F.1    Kolokoltsov, A.A.2    Albrecht, T.3    Davey, R.A.4
  • 91
    • 2342471342 scopus 로고    scopus 로고
    • Single phosphorylation of Tyr304 in the cytoplasmic tail of ephrin B2 confers high-affinity and bifunctional binding to both the SH2 domain of Grb4 and the PDZ domain of the PDZ-RGS3 protein
    • DOI 10.1111/j.1432-1033.2004.04078.x
    • Su Z, Xu P, Ni F (2004) Single phosphorylation of TYR304 in the cytoplasmic tail of ephrin B2 confers high-affinity and bifunctional binding to both the SH2 domain of GRB4 and the PDZ domain of the PDZ-RGS3 protein. Eur J Biochem 271:1725-1736 (Pubitemid 38586304)
    • (2004) European Journal of Biochemistry , vol.271 , Issue.9 , pp. 1725-1736
    • Su, Z.1    Xu, P.2    Ni, F.3
  • 92
    • 63449089372 scopus 로고    scopus 로고
    • Characterization of Dengue virus entry into HEPG2 cells
    • Suksanpaisan L, Susantad T, Smith DR (2009) Characterization of Dengue virus entry into HEPG2 cells. J Biomed Sci 16:17
    • (2009) J Biomed Sci , vol.16 , pp. 17
    • Suksanpaisan, L.1    Susantad, T.2    Smith, D.R.3
  • 93
    • 0037423280 scopus 로고    scopus 로고
    • Small GTPase Rah/Rab34 is associated with membrane ruffles and macropinosomes and promotes macropinosome formation
    • DOI 10.1074/jbc.M208699200
    • Sun P, Yamamoto H, Suetsugu S, Miki H, Takenawa T et al (2003) Small GTPase Rah/Rab34 is associated with membrane ruffles and macropinosomes and promotes macropinosome formation. J Biol Chem 278:4063-4071 (Pubitemid 36801141)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.6 , pp. 4063-4071
    • Sun, P.1    Yamamoto, H.2    Suetsugu, S.3    Miki, H.4    Takenawa, T.5    Endo, T.6
  • 94
    • 56349167202 scopus 로고    scopus 로고
    • Nipah virus encephalitis
    • Tan C, Chua K (2008) Nipah virus encephalitis. Curr Infect Dis Rep 10:315-320
    • (2008) Curr Infect Dis Rep , vol.10 , pp. 315-320
    • Tan, C.1    Chua, K.2
  • 95
    • 33748846578 scopus 로고    scopus 로고
    • Distribution of viral antigens and development of lesions in chicken embryos inoculated with nipah virus
    • DOI 10.1016/j.jcpa.2006.05.001, PII S0021997506000454
    • Tanimura N, Imada T, Kashiwazaki Y, Sharifah SH (2006) Distribution of viral antigens and development of lesions in chicken embryos inoculated with Nipah virus. J Comp Pathol 135:74-82 (Pubitemid 44417992)
    • (2006) Journal of Comparative Pathology , vol.135 , Issue.2-3 , pp. 74-82
    • Tanimura, N.1    Imada, T.2    Kashiwazaki, Y.3    Sharifah, S.H.4
  • 96
    • 0034710650 scopus 로고    scopus 로고
    • Slam (CDw150) is a cellular receptor for measles virus
    • DOI 10.1038/35022579
    • Tatsuo H, Ono N, Tanaka K, Yanagi Y (2000) Slam (CDW150) is a cellular receptor for Measles virus. Nature 406:893-897 (Pubitemid 30664265)
    • (2000) Nature , vol.406 , Issue.6798 , pp. 893-897
    • Tatsuo, H.1    Ono, N.2    Tanaka, K.3    Yanagi, Y.4
  • 98
    • 79958274058 scopus 로고    scopus 로고
    • Hendra and nipah infection: Pathology, models and potential therapies
    • Vigant F, Lee B (2011) Hendra and nipah infection: pathology, models and potential therapies. Infect Disord Drug Targets 11:315-336
    • (2011) Infect Disord Drug Targets , vol.11 , pp. 315-336
    • Vigant, F.1    Lee, B.2
  • 99
    • 77950581527 scopus 로고    scopus 로고
    • A longitudinal study of the prevalence of Nipah virus in Pteropus lylei bats in Thailand: Evidence for seasonal preference in disease transmission
    • Wacharapluesadee S, Boongird K, Wanghongsa S, Ratanasetyuth N, Supavonwong P et al (2010) A longitudinal study of the prevalence of Nipah virus in Pteropus lylei bats in Thailand: evidence for seasonal preference in disease transmission. Vector Borne Zoonotic Dis 10:183-190
    • (2010) Vector Borne Zoonotic Dis , vol.10 , pp. 183-190
    • Wacharapluesadee, S.1    Boongird, K.2    Wanghongsa, S.3    Ratanasetyuth, N.4    Supavonwong, P.5
  • 100
    • 0032577446 scopus 로고    scopus 로고
    • Molecular distinction and angiogenic interaction between embryonic arteries and veins revealed by ephrin-B2 and its receptor Eph-B4
    • DOI 10.1016/S0092-8674(00)81436-1
    • Wang HU, Chen ZF, Anderson DJ (1998) Molecular distinction and angiogenic interaction between embryonic arteries and veins revealed by ephrin-B2 and its receptor Eph-B4. Cell 93:741-753 (Pubitemid 28257581)
    • (1998) Cell , vol.93 , Issue.5 , pp. 741-753
    • Wang, H.U.1    Chen, Z.-F.2    Anderson, D.J.3
  • 101
    • 77954478665 scopus 로고    scopus 로고
    • Tyrosine residues in the cytoplasmic domains affect sorting and fusion activity of the Nipah virus glycoproteins in polarized epithelial cells
    • Weise C, Erbar S, Lamp B, Vogt C, Diederich S et al (2010) Tyrosine residues in the cytoplasmic domains affect sorting and fusion activity of the Nipah virus glycoproteins in polarized epithelial cells. J Virol 84:7634-7641
    • (2010) J Virol , vol.84 , pp. 7634-7641
    • Weise, C.1    Erbar, S.2    Lamp, B.3    Vogt, C.4    Diederich, S.5
  • 102
    • 0141617343 scopus 로고    scopus 로고
    • How attraction turns to repulsion
    • DOI 10.1038/ncb1003-851
    • Wilkinson DG (2003) How attraction turns to repulsion. Nat Cell Biol 5:851-853 (Pubitemid 37220684)
    • (2003) Nature Cell Biology , vol.5 , Issue.10 , pp. 851-853
    • Wilkinson, D.G.1
  • 103
  • 105
    • 78649236517 scopus 로고    scopus 로고
    • Henipavirus: A review of laboratory animal pathology
    • Williamson MM, Torres-Velez FJ (2010) Henipavirus: a review of laboratory animal pathology. Vet Pathol 47:871-880
    • (2010) Vet Pathol , vol.47 , pp. 871-880
    • Williamson, M.M.1    Torres-Velez, F.J.2
  • 108
    • 48249113696 scopus 로고    scopus 로고
    • Host cell recognition by the Henipaviruses: Crystal structures of the nipah g attachment glycoprotein and its complex with ephrin-B3
    • Xu K, Rajashankar KR, Chan Y, Himanen JP, Broder CC et al (2008) Host cell recognition by the Henipaviruses: crystal structures of the nipah g attachment glycoprotein and its complex with ephrin-B3. Proc Natl Acad Sci USA 105:9953-9958
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 9953-9958
    • Xu, K.1    Rajashankar, K.R.2    Chan, Y.3    Himanen, J.P.4    Broder, C.C.5
  • 111
    • 80051725061 scopus 로고    scopus 로고
    • Mutations in the G-H loopregion of ephrin-B2 can enhance Nipah virus binding and infection
    • Yuan J, Marsh G, Khetawat D, Broder CC, Wang L et al (2011a) Mutations in the G-H loopregion of ephrin-B2 can enhance Nipah virus binding and infection. J Gen Virol 92:2142-2152
    • (2011) J Gen Virol , vol.92 , pp. 2142-2152
    • Yuan, J.1    Marsh, G.2    Khetawat, D.3    Broder, C.C.4    Wang, L.5
  • 112
    • 3843070948 scopus 로고    scopus 로고
    • Syndecan-1 up-regulated by ephrinB2/EphB4 plays dual roles in inflammatory angiogenesis
    • DOI 10.1182/blood-2003-09-3334
    • Yuan K, Hong T, Chen JJW, Tsai WH, Lin MT (2004) Syndecan-1 up-regulated by ephrinB2/EphB4 plays dual roles in inflammatory angiogenesis. Blood 104:1025-1033 (Pubitemid 39038022)
    • (2004) Blood , vol.104 , Issue.4 , pp. 1025-1033
    • Yuan, K.1    Hong, T.-M.2    Chen, J.J.W.3    Tsai, W.H.4    Lin, M.T.5
  • 113
    • 0034198659 scopus 로고    scopus 로고
    • Expression of tie-2, angiopoietin-1, angiopoietin-2, ephrinb2 and ephb4 in pyogenic granuloma of human gingiva implicates their roles in inflammatory angiogenesis
    • Yuan K, Jin YT, Lin MT (2000) Expression of tie-2, angiopoietin-1, angiopoietin-2, ephrinb2 and ephb4 in pyogenic granuloma of human gingiva implicates their roles in inflammatory angiogenesis. J Periodont Res 35:165-171
    • (2000) J Periodont Res , vol.35 , pp. 165-171
    • Yuan, K.1    Jin, Y.T.2    Lin, M.T.3
  • 114
    • 49049109230 scopus 로고    scopus 로고
    • Domain architecture and oligomerization properties of the Paramyxovirus PIV 5 hemagglutinin-neuraminidase (HN) protein
    • Yuan P, Leser GP, Demeler B, Lamb RA, Jardetzky TS (2008) Domain architecture and oligomerization properties of the Paramyxovirus PIV 5 hemagglutinin-neuraminidase (HN) protein. Virology 378:282-291
    • (2008) Virology , vol.378 , pp. 282-291
    • Yuan, P.1    Leser, G.P.2    Demeler, B.3    Lamb, R.A.4    Jardetzky, T.S.5
  • 115
    • 80052564183 scopus 로고    scopus 로고
    • Structure of the newcastle disease virus hemagglutinin-neuraminidase (HN) ectodomain reveals a four-helix bundle stalk
    • Yuan P, Swanson KA, Leser GP, Paterson RG, Lamb RA et al (2011b) Structure of the newcastle disease virus hemagglutinin-neuraminidase (HN) ectodomain reveals a four-helix bundle stalk. Proc Natl Acad Sci USA 108:14920-14925
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 14920-14925
    • Yuan, P.1    Swanson, K.A.2    Leser, G.P.3    Paterson, R.G.4    Lamb, R.A.5
  • 116
    • 70849088745 scopus 로고    scopus 로고
    • Rac1 and CDC42 GTPases cross-talk regulates formation of filopodia required for Dengue virus type-2 entry into HMEC-1 cells
    • Epub 2009 Aug 26
    • Zamudio-Meza H, Castillo AM, González-Bonilla C et al (2009) Rac1 and CDC42 GTPases cross-talk regulates formation of filopodia required for Dengue virus type-2 entry into HMEC-1 cells. J Gen Virol 90(pt 12):2902-2911. Epub 2009 Aug 26
    • (2009) J Gen Virol , vol.90 , Issue.PART 12 , pp. 2902-2911
    • Zamudio-Meza, H.1    Castillo, A.M.2    González-Bonilla, C.3
  • 118
    • 0141839883 scopus 로고    scopus 로고
    • EphB-ephrinB bi-directional endocytosis terminates adhesion allowing contact mediated repulsion
    • DOI 10.1038/ncb1045
    • Zimmer M, Palmer A, Köhler J, Klein R (2003) EphB-ephrinB bi-directional endocytosis terminates adhesion allowing contact mediated repulsion. Nat Cell Biol 5:869-878 (Pubitemid 37220692)
    • (2003) Nature Cell Biology , vol.5 , Issue.10 , pp. 869-878
    • Zimmer, M.1    Palmer, A.2    Kohler, J.3    Klein, R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.