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Volumn 7, Issue 7, 2015, Pages 3647-3674

Early events in chikungunya virus infection—from virus cell binding to membrane fusion

Author keywords

Alphavirus; Cell tropism; Chikungunya virus; Clathrin; Endocytosis; Entry; Entry inhibitors; Fusion; Neutralizing antibodies; Receptor

Indexed keywords

CHAPERONIN 60; GLYCOSAMINOGLYCAN; PHOSPHATIDYLSERINE; PROHIBITIN; PROTON TRANSPORTING ADENOSINE TRIPHOSPHATE SYNTHASE; VIRUS RECEPTOR;

EID: 84936947996     PISSN: None     EISSN: 19994915     Source Type: Journal    
DOI: 10.3390/v7072792     Document Type: Review
Times cited : (96)

References (188)
  • 2
    • 84907438885 scopus 로고    scopus 로고
    • Reemergence of Chikungunya Virus
    • Morrison, T.E. Reemergence of Chikungunya Virus. J. Virol. 2014, 88, 11644–11647.
    • (2014) J. Virol , vol.88 , pp. 11644-11647
    • Morrison, T.E.1
  • 3
    • 84859169887 scopus 로고    scopus 로고
    • Chikungunya Disease: Infection-Associated Markers from the Acute to the Chronic Phase of Arbovirus-Induced Arthralgia
    • Dupuis-Maguiraga, L.; Noret, M.; Brun, S.; Le Grand, R.; Gras, G.; Roques, P. Chikungunya Disease: Infection-Associated Markers from the Acute to the Chronic Phase of Arbovirus-Induced Arthralgia. PLoS Negl. Trop. Dis. 2012, 6, e1446.
    • (2012) Plos Negl. Trop. Dis , pp. 6
    • Dupuis-Maguiraga, L.1    Noret, M.2    Brun, S.3    Le Grand, R.4    Gras, G.5    Roques, P.6
  • 6
    • 70049086952 scopus 로고    scopus 로고
    • Chikungunya Fever: An Epidemiological Review of a Re-Emerging Infectious Disease
    • Staples, J.E.; Breiman, R.F.; Powers, A.M. Chikungunya Fever: An Epidemiological Review of a Re-Emerging Infectious Disease. Clin. Infect. Dis. 2009, 49, 942–948.
    • (2009) Clin. Infect.Dis , vol.49 , pp. 942-948
    • Staples, J.E.1    Breiman, R.F.2    Powers, A.M.3
  • 7
    • 84925400315 scopus 로고    scopus 로고
    • Chikungunya Virus and the Global Spread of a Mosquito-Borne Disease
    • Weaver, S.C.; Lecuit, M. Chikungunya Virus and the Global Spread of a Mosquito-Borne Disease. N. Engl. J. Med. 2015, 372, 1231–1239.
    • (2015) N. Engl. J. Med , vol.372 , pp. 1231-1239
    • Weaver, S.C.1    Lecuit, M.2
  • 9
    • 77953297262 scopus 로고    scopus 로고
    • Genome-Scale Phylogenetic Analyses of Chikungunya Virus Reveal Independent Emergences of Recent Epidemics and various Evolutionary Rates
    • Volk, S.M.; Chen, R.; Tsetsarkin, K.A.; Adams, A.P.; Garcia, T.I.; Sall, A.A.; Nasar, F.; Schuh, A.J.; Holmes, E.C.; Higgs, S.; et al. Genome-Scale Phylogenetic Analyses of Chikungunya Virus Reveal Independent Emergences of Recent Epidemics and various Evolutionary Rates. J. Virol. 2010, 84, 6497–6504.
    • (2010) . J. Virol , vol.84 , pp. 6497-6504
    • Volk, S.M.1    Chen, R.2    Tsetsarkin, K.A.3    Adams, A.P.4    Garcia, T.I.5    Sall, A.A.6    Nasar, F.7    Schuh, A.J.8    Holmes, E.C.9    Higgs, S.10
  • 10
    • 84930010146 scopus 로고    scopus 로고
    • Chikungunya: Evolutionary History and Recent Epidemic Spread
    • Weaver, S.C.; Forrester, N.L. Chikungunya: Evolutionary History and Recent Epidemic Spread. Antiviral Res. 2015, 120, 32–39.
    • (2015) Antiviral Res , vol.120 , pp. 32-39
    • Weaver, S.C.1    Forrester, N.L.2
  • 11
    • 84902436384 scopus 로고    scopus 로고
    • Multi-Peaked Adaptive Landscape for Chikungunya Virus Evolution Predicts Continued Fitness Optimization in Aedes Albopictus Mosquitoes. Nat
    • Tsetsarkin, K.A.; Chen, R.; Yun, R.; Rossi, S.L.; Plante, K.S.; Guerbois, M.; Forrester, N.; Perng, G.C.; Sreekumar, E.; Leal, G.; et al. Multi-Peaked Adaptive Landscape for Chikungunya Virus Evolution Predicts Continued Fitness Optimization in Aedes Albopictus Mosquitoes. Nat. Commun. 2014, 5, 4084.
    • (2014) Commun , vol.5 , pp. 4084
    • Tsetsarkin, K.A.1    Chen, R.2    Yun, R.3    Rossi, S.L.4    Plante, K.S.5    Guerbois, M.6    Forrester, N.7    Perng, G.C.8    Sreekumar, E.9    Leal, G.10
  • 12
    • 37849052513 scopus 로고    scopus 로고
    • A Single Mutation in Chikungunya Virus Affects Vector Specificity and Epidemic Potential
    • Tsetsarkin, K.A.; Vanlandingham, D.L.; McGee, C.E.; Higgs, S. A Single Mutation in Chikungunya Virus Affects Vector Specificity and Epidemic Potential. PLoS Pathog. 2007, 3, e201.
    • (2007) Plos Pathog , pp. 3
    • Tsetsarkin, K.A.1    Vanlandingham, D.L.2    McGee, C.E.3    Higgs, S.4
  • 13
    • 84899100887 scopus 로고    scopus 로고
    • Arrival of Chikungunya Virus in the New World: Prospects for Spread and Impact on Public Health. PLoS Negl Trop
    • Weaver, S.C. Arrival of Chikungunya Virus in the New World: Prospects for Spread and Impact on Public Health. PLoS Negl Trop. Dis. 2014, 8, e2921.
    • (2014) Dis , pp. 8
    • Weaver, S.C.1
  • 15
    • 70349199877 scopus 로고    scopus 로고
    • A Structural and Functional Perspective of Alphavirus Replication and Assembly
    • Jose, J.; Snyder, J.E.; Kuhn, R.J. A Structural and Functional Perspective of Alphavirus Replication and Assembly. Future Microbiol. 2009, 4, 837–856.
    • (2009) Future Microbiol , vol.4 , pp. 837-856
    • Jose, J.1    Snyder, J.E.2    Kuhn, R.J.3
  • 16
  • 17
    • 84882371677 scopus 로고    scopus 로고
    • Characterization of an Early-Stage Fusion Intermediate of Sindbis Virus using Cryoelectron Microscopy
    • Cao, S.; Zhang, W. Characterization of an Early-Stage Fusion Intermediate of Sindbis Virus using Cryoelectron Microscopy. Proc. Natl. Acad. Sci. USA 2013, 110, 13362–13367.
    • (2013) Proc. Natl. Acad. Sci. USA , vol.110 , pp. 13362-13367
    • Cao, S.1    Zhang, W.2
  • 18
    • 0024787006 scopus 로고
    • Membrane Phospholipid Asymmetry in Semliki Forest Virus Grown in BHK Cells
    • Allan, D.; Quinn, P. Membrane Phospholipid Asymmetry in Semliki Forest Virus Grown in BHK Cells. Biochim. Biophys. Acta Biomembr. 1989, 987, 199–204. 
    • (1989) Biochim. Biophys. Acta Biomembr , vol.987 , pp. 199-204
    • Allan, D.1    Quinn, P.2
  • 19
    • 0015147957 scopus 로고
    • The Lipid Class Composition of Semliki Forest Virus and Plasma Membranes of the Host Cells
    • Renkonen, O.; Kaarainen, L.; Simons, K.; Gahmberg, C.G. The Lipid Class Composition of Semliki Forest Virus and Plasma Membranes of the Host Cells. Virology 1971, 46, 318–326.
    • (1971) Virology , vol.46 , pp. 318-326
    • Renkonen, O.1    Kaarainen, L.2    Simons, K.3    Gahmberg, C.G.4
  • 20
    • 0019859745 scopus 로고
    • Phospholipid Asymmetry in Semliki Forest Virus Grown on Baby Hamster Kidney (BHK-21) Cells
    • Van Meer, G.; Simons, K.; Op den Kamp, J.A.; van Deenen, L.M. Phospholipid Asymmetry in Semliki Forest Virus Grown on Baby Hamster Kidney (BHK-21) Cells. Biochemistry 1981, 20, 1974–1981.
    • (1981) Biochemistry , vol.20 , pp. 1974-1981
    • Van Meer, G.1    Simons, K.2    Op Den Kamp, J.A.3    Van Deenen, L.M.4
  • 21
    • 67749139973 scopus 로고    scopus 로고
    • The Lipidomes of Vesicular Stomatitis Virus, Semliki Forest Virus, and the Host Plasma Membrane Analyzed by Quantitative Shotgun Mass Spectrometry
    • Kalvodova, L.; Sampaio, J.L.; Cordo, S.; Ejsing, C.S.; Shevchenko, A.; Simons, K. The Lipidomes of Vesicular Stomatitis Virus, Semliki Forest Virus, and the Host Plasma Membrane Analyzed by Quantitative Shotgun Mass Spectrometry. J. Virol. 2009, 83, 7996–8003.
    • (2009) J. Virol , vol.83 , pp. 7996-8003
    • Kalvodova, L.1    Sampaio, J.L.2    Cordo, S.3    Ejsing, C.S.4    Shevchenko, A.5    Simons, K.6
  • 22
    • 84879051627 scopus 로고    scopus 로고
    • Structural Analyses at Pseudo Atomic Resolution of Chikungunya Virus and Antibodies show Mechanisms of Neutralization
    • Sun, S.; Xiang, Y.; Akahata, W.; Holdaway, H.; Pal, P.; Zhang, X.; Diamond, M.S.; Nabel, G.J.; Rossmann, M.G. Structural Analyses at Pseudo Atomic Resolution of Chikungunya Virus and Antibodies show Mechanisms of Neutralization. eLife 2013, 2, e00435. 
    • (2013) Elife , vol.2
    • Sun, S.1    Xiang, Y.2    Akahata, W.3    Holdaway, H.4    Pal, P.5    Zhang, X.6    Diamond, M.S.7    Nabel, G.J.8    Rossmann, M.G.9
  • 24
    • 0035815282 scopus 로고    scopus 로고
    • The Fusion Glycoprotein Shell of Semliki Forest Virus: An Icosahedral Assembly Primed for Fusogenic Activation at Endosomal pH
    • Lescar, J.; Roussel, A.; Wien, M.W.; Navaza, J.; Fuller, S.D.; Wengler, G.; Wengler, G.; Rey, F.A. The Fusion Glycoprotein Shell of Semliki Forest Virus: An Icosahedral Assembly Primed for Fusogenic Activation at Endosomal pH. Cell 2001, 105, 137–148.
    • (2001) Cell , vol.105 , pp. 137-148
    • Lescar, J.1    Roussel, A.2    Wien, M.W.3    Navaza, J.4    Fuller, S.D.5    Wengler, G.6    Wengler, G.7    Rey, F.A.8
  • 25
    • 33644799064 scopus 로고    scopus 로고
    • Structure and Interactions at the Viral Surface of the Envelope Protein E1 of Semliki Forest Virus
    • Roussel, A.; Lescar, J.; Vaney, M.C.; Wengler, G.; Wengler, G.; Rey, F.A. Structure and Interactions at the Viral Surface of the Envelope Protein E1 of Semliki Forest Virus. Structure 2006, 14, 75–86.
    • (2006) Structure , vol.14 , pp. 75-86
    • Roussel, A.1    Lescar, J.2    Vaney, M.C.3    Wengler, G.4    Wengler, G.5    Rey, F.A.6
  • 27
    • 84857809812 scopus 로고    scopus 로고
    • Interactions of the Cytoplasmic Domain of Sindbis Virus E2 with Nucleocapsid Cores Promote Alphavirus Budding
    • 2nd
    • Jose, J.; Przybyla, L.; Edwards, T.J.; Perera, R.; Burgner, J.W., 2nd; Kuhn, R.J. Interactions of the Cytoplasmic Domain of Sindbis Virus E2 with Nucleocapsid Cores Promote Alphavirus Budding. J. Virol. 2012, 86, 2585–2599.
    • (2012) J. Virol , vol.86 , pp. 2585-2599
    • Jose, J.1    Przybyla, L.2    Edwards, T.J.3    Perera, R.4    Burgner, J.W.5    Kuhn, R.J.6
  • 29
    • 78649891889 scopus 로고    scopus 로고
    • Structural Changes of Envelope Proteins during Alphavirus Fusion
    • Li, L.; Jose, J.; Xiang, Y.; Kuhn, R.J.; Rossmann, M.G. Structural Changes of Envelope Proteins during Alphavirus Fusion. Nature 2010, 468, 705–708.
    • (2010) Nature , vol.468 , pp. 705-708
    • Li, L.1    Jose, J.2    Xiang, Y.3    Kuhn, R.J.4    Rossmann, M.G.5
  • 30
    • 0022539125 scopus 로고
    • Envelope Structure of Semliki Forest Virus Reconstructed from Cryo-Electron Micrographs
    • Vogel, R.H.; Provencher, S.W.; von Bonsdorff, C.H.; Adrian, M.; Dubochet, J. Envelope Structure of Semliki Forest Virus Reconstructed from Cryo-Electron Micrographs. Nature 1986, 320, 533–535.
    • (1986) Nature , vol.320 , pp. 533-535
    • Vogel, R.H.1    Provencher, S.W.2    Von Bonsdorff, C.H.3    Adrian, M.4    Dubochet, J.5
  • 37
    • 70350001140 scopus 로고    scopus 로고
    • Replication Cycle of Chikungunya: A Re-Emerging Arbovirus
    • Solignat, M.; Gay, B.; Higgs, S.; Briant, L.; Devaux, C. Replication Cycle of Chikungunya: A Re-Emerging Arbovirus. Virology 2009, 393, 183–197.
    • (2009) Virology , vol.393 , pp. 183-197
    • Solignat, M.1    Gay, B.2    Higgs, S.3    Briant, L.4    Devaux, C.5
  • 38
    • 84863012311 scopus 로고    scopus 로고
    • Chikungunya Virus Infection of Cell Lines: Analysis of the East, Central and South African Lineage
    • Wikan, N.; Sakoonwatanyoo, P.; Ubol, S.; Yoksan, S.; Smith, D.R. Chikungunya Virus Infection of Cell Lines: Analysis of the East, Central and South African Lineage. PLoS ONE 2012, 7, e31102.
    • (2012) Plos ONE , pp. 7
    • Wikan, N.1    Sakoonwatanyoo, P.2    Ubol, S.3    Yoksan, S.4    Smith, D.R.5
  • 39
    • 79851485115 scopus 로고    scopus 로고
    • Persistent Arthralgia Induced by Chikungunya Virus Infection is Associated with Interleukin-6 and Granulocyte Macrophage Colony-Stimulating Factor
    • Chow, A.; Her, Z.; Ong, E.K.; Chen, J.M.; Dimatatac, F.; Kwek, D.J.; Barkham, T.; Yang, H.; Renia, L.; Leo, Y.S.; et al. Persistent Arthralgia Induced by Chikungunya Virus Infection is Associated with Interleukin-6 and Granulocyte Macrophage Colony-Stimulating Factor. J. Infect. Dis. 2011, 203, 149–157.
    • (2011) . J. Infect. Dis , vol.203 , pp. 149-157
    • Chow, A.1    Her, Z.2    Ong, E.K.3    Chen, J.M.4    Dimatatac, F.5    Kwek, D.J.6    Barkham, T.7    Yang, H.8    Renia, L.9    Leo, Y.S.10
  • 40
    • 70349757159 scopus 로고    scopus 로고
    • Simultaneous Detection and Quantitation of Chikungunya, Dengue and West Nile Viruses by Multiplex RT-PCR Assays and Dengue Virus Typing using High Resolution Melting
    • Naze, F.; Le Roux, K.; Schuffenecker, I.; Zeller, H.; Staikowsky, F.; Grivard, P.; Michault, A.; Laurent, P. Simultaneous Detection and Quantitation of Chikungunya, Dengue and West Nile Viruses by Multiplex RT-PCR Assays and Dengue Virus Typing using High Resolution Melting. J. Virol. Methods 2009, 162, 1–7.
    • (2009) J. Virol. Methods , vol.162 , pp. 1-7
    • Naze, F.1    Le Roux, K.2    Schuffenecker, I.3    Zeller, H.4    Staikowsky, F.5    Grivard, P.6    Michault, A.7    Laurent, P.8
  • 43
    • 0021705779 scopus 로고
    • Mononuclear Cell Types in Chronic Synovial Effusions of Ross River Virus Disease. Aust
    • Fraser, J.R.; Becker, G.J. Mononuclear Cell Types in Chronic Synovial Effusions of Ross River Virus Disease. Aust. N. Z. J. Med. 1984, 14, 505–506.
    • (1984) N. Z. J. Med , vol.14 , pp. 505-506
    • Fraser, J.R.1    Becker, G.J.2
  • 44
    • 55249092120 scopus 로고    scopus 로고
    • Eastern and Venezuelan Equine Encephalitis Viruses Differ in their Ability to Infect Dendritic Cells and Macrophages: Impact of Altered Cell Tropism on Pathogenesis
    • Gardner, C.L.; Burke, C.W.; Tesfay, M.Z.; Glass, P.J.; Klimstra, W.B.; Ryman, K.D. Eastern and Venezuelan Equine Encephalitis Viruses Differ in their Ability to Infect Dendritic Cells and Macrophages: Impact of Altered Cell Tropism on Pathogenesis. J. Virol. 2008, 82, 10634–10646.
    • (2008) J. Virol , vol.82 , pp. 10634-10646
    • Gardner, C.L.1    Burke, C.W.2    Tesfay, M.Z.3    Glass, P.J.4    Klimstra, W.B.5    Ryman, K.D.6
  • 45
    • 23244439085 scopus 로고    scopus 로고
    • Alpha/Beta Interferon Production by Myeloid Dendritic Cells in Response to UV-Inactivated Virus Requires Viral Entry and Interferon Regulatory Factor 3 but Not MyD88
    • Hidmark, A.S.; McInerney, G.M.; Nordstrom, E.K.; Douagi, I.; Werner, K.M.; Liljestrom, P.; Karlsson Hedestam, G.B. Early Alpha/Beta Interferon Production by Myeloid Dendritic Cells in Response to UV-Inactivated Virus Requires Viral Entry and Interferon Regulatory Factor 3 but Not MyD88. J. Virol. 2005, 79, 10376–10385.
    • (2005) J. Virol , vol.79 , pp. 10376-10385
    • Hidmark, A.S.1    McInerney, G.M.2    Nordstrom, E.K.3    Douagi, I.4    Werner, K.M.5    Liljestrom, P.6    Hedestam, K.7    Early, G.B.8
  • 46
    • 33845800843 scopus 로고    scopus 로고
    • Differential Induction of Type I Interferon Responses in Myeloid Dendritic Cells by Mosquito and Mammalian-Cell-Derived Alphaviruses
    • Shabman, R.S.; Morrison, T.E.; Moore, C.; White, L.; Suthar, M.S.; Hueston, L.; Rulli, N.; Lidbury, B.; Ting, J.P.; Mahalingam, S.; et al. Differential Induction of Type I Interferon Responses in Myeloid Dendritic Cells by Mosquito and Mammalian-Cell-Derived Alphaviruses. J. Virol. 2007, 81, 237–247.
    • (2007) J. Virol , vol.81 , pp. 237-247
    • Shabman, R.S.1    Morrison, T.E.2    Moore, C.3    White, L.4    Suthar, M.S.5    Hueston, L.6    Rulli, N.7    Lidbury, B.8    Ting, J.P.9    Mahalingam, S.10
  • 50
    • 84903701032 scopus 로고    scopus 로고
    • Proteomic Profiling of Chikungunya Virus-Infected Human Muscle Cells: Reveal the Role of Cytoskeleton Network in CHIKV Replication
    • Issac, T.H.; Tan, E.L.; Chu, J.J. Proteomic Profiling of Chikungunya Virus-Infected Human Muscle Cells: Reveal the Role of Cytoskeleton Network in CHIKV Replication. J. Proteomics 2014, 108, 445–464.
    • (2014) J. Proteomics , vol.108 , pp. 445-464
    • Issac, T.H.1    Tan, E.L.2    Chu, J.J.3
  • 51
    • 71649101408 scopus 로고    scopus 로고
    • Focus on Chikungunya Pathophysiology in Human and Animal Models
    • Couderc, T.; Lecuit, M. Focus on Chikungunya Pathophysiology in Human and Animal Models. Microbes Infect. 2009, 11, 1197–1205.
    • (2009) Microbes Infect , vol.11 , pp. 1197-1205
    • Couderc, T.1    Lecuit, M.2
  • 56
    • 0021443017 scopus 로고
    • A Destructive Arthropathy Following Chikungunya Virus Arthritis—A Possible Association
    • Brighton, S.W.; Simson, I.W. A Destructive Arthropathy Following Chikungunya Virus Arthritis—A Possible Association. Clin. Rheumatol. 1984, 3, 253–258.
    • (1984) . Clin. Rheumatol , vol.3 , pp. 253-258
    • Brighton, S.W.1    Simson, I.W.2
  • 57
    • 84930790197 scopus 로고    scopus 로고
    • Chikungunya Infection: Self-Reported Rheumatic Morbidity and Impaired Quality of Life Persist 6 Years Later
    • Marimoutou, C.; Ferraro, J.; Javelle, E.; Deparis, X.; Simon, F. Chikungunya Infection: Self-Reported Rheumatic Morbidity and Impaired Quality of Life Persist 6 Years Later. Clin. Microbiol. Infect. 2015, 21, 688–693.
    • (2015) Clin. Microbiol. Infect , vol.21 , pp. 688-693
    • Marimoutou, C.1    Ferraro, J.2    Javelle, E.3    Deparis, X.4    Simon, F.5
  • 58
    • 81755178728 scopus 로고    scopus 로고
    • Trivandrum COPCORD Study Group. Rheumatic-Musculoskeletal Pain and Disorders in a Naive Group of Individuals 15 Months Following a Chikungunya Viral Epidemic in South India: A Population Based Observational Study
    • ;
    • Mathew, A.J.; Goyal, V.; George, E.; Thekkemuriyil, D.V.; Jayakumar, B.; Chopra, A.; Trivandrum COPCORD Study Group. Rheumatic-Musculoskeletal Pain and Disorders in a Naive Group of Individuals 15 Months Following a Chikungunya Viral Epidemic in South India: A Population Based Observational Study. Int. J. Clin. Pract. 2011, 65, 1306–1312.
    • (2011) Int. J. Clin. Pract , vol.65 , pp. 1306-1312
    • Mathew, A.J.1    Goyal, V.2    George, E.3    Thekkemuriyil, D.V.4    Jayakumar, B.5    Chopra, A.6
  • 59
    • 84923164540 scopus 로고    scopus 로고
    • Post-Chikungunya Rheumatoid Arthritis, Saint Martin. Emerg. Infect
    • Foissac, M.; Javelle, E.; Ray, S.; Guerin, B.; Simon, F. Post-Chikungunya Rheumatoid Arthritis, Saint Martin. Emerg. Infect. Dis. 2015, 21, 530–532.
    • (2015) Dis , vol.21 , pp. 530-532
    • Foissac, M.1    Javelle, E.2    Ray, S.3    Guerin, B.4    Simon, F.5
  • 61
    • 84865336359 scopus 로고    scopus 로고
    • The Cell Biology of Chikungunya Virus Infection
    • Tang, B.L. The Cell Biology of Chikungunya Virus Infection. Cell. Microbiol. 2012, 14, 1354–1363.
    • (2012) Cell. Microbiol , vol.14 , pp. 1354-1363
    • Tang, B.L.1
  • 70
    • 84884576982 scopus 로고    scopus 로고
    • Induction of Cytopathogenicity in Human Glioblastoma Cells by Chikungunya Virus
    • Abraham, R.; Mudaliar, P.; Padmanabhan, A.; Sreekumar, E. Induction of Cytopathogenicity in Human Glioblastoma Cells by Chikungunya Virus. PLoS ONE 2013, 8, e75854. 
    • (2013) Plos ONE , vol.8
    • Abraham, R.1    Mudaliar, P.2    Padmanabhan, A.3    Sreekumar, E.4
  • 71
    • 84895753004 scopus 로고    scopus 로고
    • A Polarized Cell Model for Chikungunya Virus Infection: Entry and Egress of Virus Occurs at the Apical Domain of Polarized Cells
    • Lim, P.J.; Chu, J.J. A Polarized Cell Model for Chikungunya Virus Infection: Entry and Egress of Virus Occurs at the Apical Domain of Polarized Cells. PLoS Negl. Trop. Dis. 2014, 8, e2661.
    • (2014) Plos Negl. Trop. Dis , vol.8
    • Lim, P.J.1    Chu, J.J.2
  • 72
    • 0028078572 scopus 로고
    • Virus Receptors: Binding, Adhesion Strengthening, and Changes in Viral Structure
    • Haywood, A.M. Virus Receptors: Binding, Adhesion Strengthening, and Changes in Viral Structure. J. Virol. 1994, 68, 1–5.
    • (1994) J. Virol , vol.68 , pp. 1-5
    • Haywood, A.M.1
  • 75
    • 84907965342 scopus 로고    scopus 로고
    • Residue 82 of the Chikungunya Virus E2 Attachment Protein Modulates Viral Dissemination and Arthritis in Mice
    • Ashbrook, A.W.; Burrack, K.S.; Silva, L.A.; Montgomery, S.A.; Heise, M.T.; Morrison, T.E.; Dermody, T.S. Residue 82 of the Chikungunya Virus E2 Attachment Protein Modulates Viral Dissemination and Arthritis in Mice. J. Virol. 2014, 88, 12180–12192.
    • (2014) J. Virol , vol.88 , pp. 12180-12192
    • Ashbrook, A.W.1    Burrack, K.S.2    Silva, L.A.3    Montgomery, S.A.4    Heise, M.T.5    Morrison, T.E.6    Dermody, T.S.7
  • 76
    • 84884542712 scopus 로고    scopus 로고
    • Identification of Structural Motifs in the E2 Glycoprotein of Chikungunya Involved in Virus-Host Interaction
    • 76.  Asnet Mary, J.; Paramasivan, R.; Tyagi, B.K.; Surender, M.; Shenbagarathai, R. Identification of Structural Motifs in the E2 Glycoprotein of Chikungunya Involved in Virus-Host Interaction. J. Biomol. Struct. Dyn. 2013, 31, 1077–1085.
    • (2013) J. Biomol. Struct. Dyn , vol.31 , pp. 1077-1085
    • Asnet Mary, J.1    Paramasivan, R.2    Tyagi, B.K.3    Surender, M.4    Shenbagarathai, R.5
  • 77
    • 84884245462 scopus 로고    scopus 로고
    • Structures and Target Recognition Modes of PDZ Domains: Recurring Themes and Emerging Pictures
    • Ye, F.; Zhang, M. Structures and Target Recognition Modes of PDZ Domains: Recurring Themes and Emerging Pictures. Biochem. J. 2013, 455, 1–14.
    • (2013) . Biochem. J , vol.455 , pp. 1-14
    • Ye, F.1    Zhang, M.2
  • 78
    • 34547407842 scopus 로고    scopus 로고
    • Extracellular Interaction between hCD98 and the PDZ Class II Domain of hCASK in Intestinal Epithelia
    • Yan, Y.; Vasudevan, S.; Nguyen, H.; Bork, U.; Sitaraman, S.; Merlin, D. Extracellular Interaction between hCD98 and the PDZ Class II Domain of hCASK in Intestinal Epithelia. J. Membr. Biol. 2007, 215, 15–26.
    • (2007) J. Membr. Biol , vol.215 , pp. 15-26
    • Yan, Y.1    Vasudevan, S.2    Nguyen, H.3    Bork, U.4    Sitaraman, S.5    Merlin, D.6
  • 79
    • 84880594815 scopus 로고    scopus 로고
    • Role of the Phosphatidylserine Receptor TIM-1 in Enveloped-Virus Entry
    • Moller-Tank, S.; Kondratowicz, A.S.; Davey, R.A.; Rennert, P.D.; Maury, W. Role of the Phosphatidylserine Receptor TIM-1 in Enveloped-Virus Entry. J. Virol. 2013, 87, 8327–8341.
    • (2013) J. Virol , vol.87 , pp. 8327-8341
    • Moller-Tank, S.1    Kondratowicz, A.S.2    Davey, R.A.3    Rennert, P.D.4    Maury, W.5
  • 80
    • 84894187925 scopus 로고    scopus 로고
    • Single-Amino-Acid Polymorphism in Chikungunya Virus E2 Glycoprotein Influences Glycosaminoglycan Utilization
    • Silva, L.A.; Khomandiak, S.; Ashbrook, A.W.; Weller, R.; Heise, M.T.; Morrison, T.E.; Dermody, T.S. A Single-Amino-Acid Polymorphism in Chikungunya Virus E2 Glycoprotein Influences Glycosaminoglycan Utilization. J. Virol. 2014, 88, 2385–2397.
    • (2014) J. Virol , vol.88 , pp. 2385-2397
    • Silva, L.A.1    Khomandiak, S.2    Ashbrook, A.W.3    Weller, R.4    Heise, M.T.5    Morrison, T.E.6    Dermody, T.7
  • 82
    • 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
  • 83
    • 70349398032 scopus 로고    scopus 로고
    • Characterization of Chikungunya Pseudotyped Viruses: Identification of Refractory Cell Lines and Demonstration of Cellular Tropism Differences Mediated by Mutations in E1 Glycoprotein
    • Salvador, B.; Zhou, Y.; Michault, A.; Muench, M.O.; Simmons, G. Characterization of Chikungunya Pseudotyped Viruses: Identification of Refractory Cell Lines and Demonstration of Cellular Tropism Differences Mediated by Mutations in E1 Glycoprotein. Virology 2009, 393, 33–41.
    • (2009) Virology , vol.393 , pp. 33-41
    • Salvador, B.1    Zhou, Y.2    Michault, A.3    Muench, M.O.4    Simmons, G.5
  • 84
    • 84899070398 scopus 로고    scopus 로고
    • Prohibitins Role in Cellular Survival through Ras-Raf-MEK-ERK Pathway
    • Chowdhury, I.; Thompson, W.E.; Thomas, K. Prohibitins Role in Cellular Survival through Ras-Raf-MEK-ERK Pathway. J. Cell. Physiol. 2014, 229, 998–1004.
    • (2014) J. Cell. Physiol , vol.229 , pp. 998-1004
    • Chowdhury, I.1    Thompson, W.E.2    Thomas, K.3
  • 85
    • 84866552156 scopus 로고    scopus 로고
    • Vascular-Targeted Nanotherapy for Obesity: Unexpected Passive Targeting Mechanism to Obese Fat for the Enhancement of Active Drug Delivery
    • Hossen, M.N.; Kajimoto, K.; Akita, H.; Hyodo, M.; Harashima, H. Vascular-Targeted Nanotherapy for Obesity: Unexpected Passive Targeting Mechanism to Obese Fat for the Enhancement of Active Drug Delivery. J. Control. Release 2012, 163, 101–110.
    • (2012) J. Control. Release , vol.163 , pp. 101-110
    • Hossen, M.N.1    Kajimoto, K.2    Akita, H.3    Hyodo, M.4    Harashima, H.5
  • 86
    • 2942703809 scopus 로고    scopus 로고
    • Reversal of Obesity by Targeted Ablation of Adipose Tissue
    • Kolonin, M.G.; Saha, P.K.; Chan, L.; Pasqualini, R.; Arap, W. Reversal of Obesity by Targeted Ablation of Adipose Tissue. Nat. Med. 2004, 10, 625–632.
    • (2004) Nat. Med , vol.10 , pp. 625-632
    • Kolonin, M.G.1    Saha, P.K.2    Chan, L.3    Pasqualini, R.4    Arap, W.5
  • 87
    • 56349102165 scopus 로고    scopus 로고
    • Prohibitin Function within Mitochondria: Essential Roles for Cell Proliferation and Cristae Morphogenesis
    • Merkwirth, C.; Langer, T. Prohibitin Function within Mitochondria: Essential Roles for Cell Proliferation and Cristae Morphogenesis. Biochim. Biophys. Acta 2009, 1793, 27–32.
    • (2009) Biochim. Biophys.Acta , vol.1793 , pp. 27-32
    • Merkwirth, C.1    Langer, T.2
  • 93
    • 84901363457 scopus 로고    scopus 로고
    • Characterizing Functional Domains for TIM-Mediated Enveloped Virus Entry
    • Moller-Tank, S.; Albritton, L.M.; Rennert, P.D.; Maury, W. Characterizing Functional Domains for TIM-Mediated Enveloped Virus Entry. J. Virol. 2014, 88, 6702–6713.
    • (2014) J. Virol , vol.88 , pp. 6702-6713
    • Moller-Tank, S.1    Albritton, L.M.2    Rennert, P.D.3    Maury, W.4
  • 94
    • 56649100319 scopus 로고    scopus 로고
    • The Structure of Glycosaminoglycans and their Interactions with Proteins
    • Gandhi, N.S.; Mancera, R.L. The Structure of Glycosaminoglycans and their Interactions with Proteins. Chem. Biol. Drug Des. 2008, 72, 455–482.
    • (2008) Chem. Biol. Drug Des , vol.72 , pp. 455-482
    • Gandhi, N.S.1    Mancera, R.L.2
  • 95
    • 0031869503 scopus 로고    scopus 로고
    • Adaptation of Sindbis Virus to BHK Cells Selects for use of Heparan Sulfate as an Attachment Receptor
    • Klimstra, W.B.; Ryman, K.D.; Johnston, R.E. Adaptation of Sindbis Virus to BHK Cells Selects for use of Heparan Sulfate as an Attachment Receptor. J. Virol. 1998, 72, 7357–7366.
    • (1998) J. Virol , vol.72 , pp. 7357-7366
    • Klimstra, W.B.1    Ryman, K.D.2    Johnston, R.E.3
  • 96
    • 0034633834 scopus 로고    scopus 로고
    • Mutations in the E2 Glycoprotein of Venezuelan Equine Encephalitis Virus Confer Heparan Sulfate Interaction, Low Morbidity, and Rapid Clearance from Blood of Mice
    • Bernard, K.A.; Klimstra, W.B.; Johnston, R.E. Mutations in the E2 Glycoprotein of Venezuelan Equine Encephalitis Virus Confer Heparan Sulfate Interaction, Low Morbidity, and Rapid Clearance from Blood of Mice. Virology 2000, 276, 93–103.
    • (2000) Virology , vol.276 , pp. 93-103
    • Bernard, K.A.1    Klimstra, W.B.2    Johnston, R.E.3
  • 97
    • 84880624223 scopus 로고    scopus 로고
    • Natural Variation in the Heparan Sulfate Binding Domain of the Eastern Equine Encephalitis Virus E2 Glycoprotein Alters Interactions with Cell Surfaces and Virulence in Mice
    • Gardner, C.L.; Choi-Nurvitadhi, J.; Sun, C.; Bayer, A.; Hritz, J.; Ryman, K.D.; Klimstra, W.B. Natural Variation in the Heparan Sulfate Binding Domain of the Eastern Equine Encephalitis Virus E2 Glycoprotein Alters Interactions with Cell Surfaces and Virulence in Mice. J. Virol. 2013, 87, 8582–8590.
    • (2013) . J. Virol , vol.87 , pp. 8582-8590
    • Gardner, C.L.1    Choi-Nurvitadhi, J.2    Sun, C.3    Bayer, A.4    Hritz, J.5    Ryman, K.D.6    Klimstra, W.B.7
  • 98
    • 0036784563 scopus 로고    scopus 로고
    • Adaptation of Alphaviruses to Heparan Sulfate: Interaction of Sindbis and Semliki Forest Viruses with Liposomes Containing Lipid-Conjugated Heparin
    • Smit, J.M.; Waarts, B.L.; Kimata, K.; Klimstra, W.B.; Bittman, R.; Wilschut, J. Adaptation of Alphaviruses to Heparan Sulfate: Interaction of Sindbis and Semliki Forest Viruses with Liposomes Containing Lipid-Conjugated Heparin. J. Virol. 2002, 76, 10128–10137.
    • (2002) J. Virol , vol.76 , pp. 10128-10137
    • Smit, J.M.1    Waarts, B.L.2    Kimata, K.3    Klimstra, W.B.4    Bittman, R.5    Wilschut, J.6
  • 99
    • 33645031982 scopus 로고    scopus 로고
    • Heparin-Binding and Patterns of Virulence for Two Recombinant Strains of Sindbis Virus
    • Bear, J.S.; Byrnes, A.P.; Griffin, D.E. Heparin-Binding and Patterns of Virulence for Two Recombinant Strains of Sindbis Virus. Virology 2006, 347, 183–190.
    • (2006) Virology , vol.347 , pp. 183-190
    • Bear, J.S.1    Byrnes, A.P.2    Griffin, D.E.3
  • 100
    • 0037229326 scopus 로고    scopus 로고
    • Glycosaminoglycan Binding Properties of Natural Venezuelan Equine Encephalitis Virus Isolates
    • Wang, E.; Brault, A.C.; Powers, A.M.; Kang, W.; Weaver, S.C. Glycosaminoglycan Binding Properties of Natural Venezuelan Equine Encephalitis Virus Isolates. J. Virol. 2003, 77, 1204–1210.
    • (2003) J. Virol , vol.77 , pp. 1204-1210
    • Wang, E.1    Brault, A.C.2    Powers, A.M.3    Kang, W.4    Weaver, S.C.5
  • 101
    • 0034984146 scopus 로고    scopus 로고
    • An Amino Acid Substitution in the Coding Region of the E2 Glycoprotein Adapts Ross River Virus to Utilize Heparan Sulfate as an Attachment Moiety
    • Heil, M.L.; Albee, A.; Strauss, J.H.; Kuhn, R.J. An Amino Acid Substitution in the Coding Region of the E2 Glycoprotein Adapts Ross River Virus to Utilize Heparan Sulfate as an Attachment Moiety. J. Virol. 2001, 75, 6303–6309.
    • (2001) J. Virol , vol.75 , pp. 6303-6309
    • Heil, M.L.1    Albee, A.2    Strauss, J.H.3    Kuhn, R.J.4
  • 102
    • 84857034750 scopus 로고    scopus 로고
    • Interferon-Alpha/Beta Deficiency Greatly Exacerbates Arthritogenic Disease in Mice Infected with Wild-Type Chikungunya Virus but Not with the Cell Culture-Adapted Live-Attenuated 181/25 Vaccine Candidate
    • Gardner, C.L.; Burke, C.W.; Higgs, S.T.; Klimstra, W.B.; Ryman, K.D. Interferon-Alpha/Beta Deficiency Greatly Exacerbates Arthritogenic Disease in Mice Infected with Wild-Type Chikungunya Virus but Not with the Cell Culture-Adapted Live-Attenuated 181/25 Vaccine Candidate. Virology 2012, 425, 103–112. 
    • (2012) Virology , vol.425 , pp. 103-112
    • Gardner, C.L.1    Burke, C.W.2    Higgs, S.T.3    Klimstra, W.B.4    Ryman, K.D.5
  • 103
    • 0022967762 scopus 로고
    • Development of an Attenuated Strain of Chikungunya Virus for use in Vaccine Production
    • Levitt, N.H.; Ramsburg, H.H.; Hasty, S.E.; Repik, P.M.; Cole, F.E., Jr.; Lupton, H.W. Development of an Attenuated Strain of Chikungunya Virus for use in Vaccine Production. Vaccine 1986, 4, 157–162.
    • (1986) Vaccine , vol.4 , pp. 157-162
    • Levitt, N.H.1    Ramsburg, H.H.2    Hasty, S.E.3    Repik, P.M.4    Cole, F.E.5    Lupton, H.W.6
  • 104
    • 84895727739 scopus 로고    scopus 로고
    • Deliberate Attenuation of Chikungunya Virus by Adaptation to Heparan Sulfate-Dependent Infectivity: A Model for Rational Arboviral Vaccine Design. PLoS Negl. Trop
    • Gardner, C.L.; Hritz, J.; Sun, C.; Vanlandingham, D.L.; Song, T.Y.; Ghedin, E.; Higgs, S.; Klimstra, W.B.; Ryman, K.D. Deliberate Attenuation of Chikungunya Virus by Adaptation to Heparan Sulfate-Dependent Infectivity: A Model for Rational Arboviral Vaccine Design. PLoS Negl. Trop. Dis. 2014, 8, e2719.
    • (2014) Dis , pp. 8
    • Gardner, C.L.1    Hritz, J.2    Sun, C.3    Vanlandingham, D.L.4    Song, T.Y.5    Ghedin, E.6    Higgs, S.7    Klimstra, W.B.8    Ryman, K.D.9
  • 105
    • 84863613754 scopus 로고    scopus 로고
    • Attenuation of Chikungunya Virus Vaccine Strain 181/Clone 25 is Determined by Two Amino Acid Substitutions in the E2 Envelope Glycoprotein
    • Gorchakov, R.; Wang, E.; Leal, G.; Forrester, N.L.; Plante, K.; Rossi, S.L.; Partidos, C.D.; Adams, A.P.; Seymour, R.L.; Weger, J.; et al. Attenuation of Chikungunya Virus Vaccine Strain 181/Clone 25 is Determined by Two Amino Acid Substitutions in the E2 Envelope Glycoprotein. J. Virol. 2012, 86, 6084–6096.
    • (2012) J. Virol , vol.86 , pp. 6084-6096
    • Gorchakov, R.1    Wang, E.2    Leal, G.3    Forrester, N.L.4    Plante, K.5    Rossi, S.L.6    Partidos, C.D.7    Adams, A.P.8    Seymour, R.L.9    Weger, J.10
  • 107
    • 79952071002 scopus 로고    scopus 로고
    • A Novel Mechanism of Gamma/Delta T-Lymphocyte and Endothelial Activation by Shear Stress: The Role of Ecto-ATP Synthase Beta Chain
    • Fu, Y.; Hou, Y.; Fu, C.; Gu, M.; Li, C.; Kong, W.; Wang, X.; Shyy, J.Y.; Zhu, Y. A Novel Mechanism of Gamma/Delta T-Lymphocyte and Endothelial Activation by Shear Stress: The Role of Ecto-ATP Synthase Beta Chain. Circ. Res. 2011, 108, 410–417.
    • (2011) . Circ. Res , vol.108 , pp. 410-417
    • Fu, Y.1    Hou, Y.2    Fu, C.3    Gu, M.4    Li, C.5    Kong, W.6    Wang, X.7    Shyy, J.Y.8    Zhu, Y.9
  • 110
    • 84897482488 scopus 로고    scopus 로고
    • Kinetic Analysis of Mouse Brain Proteome Alterations Following Chikungunya Virus Infection before and After Appearance of Clinical Symptoms
    • Fraisier, C.; Koraka, P.; Belghazi, M.; Bakli, M.; Granjeaud, S.; Pophillat, M.; Lim, S.M.; Osterhaus, A.; Martina, B.; Camoin, L.; et al. Kinetic Analysis of Mouse Brain Proteome Alterations Following Chikungunya Virus Infection before and After Appearance of Clinical Symptoms. PLoS ONE 2014, 9, e91397.
    • (2014) Plos ONE , pp. 9
    • Fraisier, C.1    Koraka, P.2    Belghazi, M.3    Bakli, M.4    Granjeaud, S.5    Pophillat, M.6    Lim, S.M.7    Osterhaus, A.8    Martina, B.9    Camoin, L.10
  • 111
    • 0028086074 scopus 로고
    • Multiple Adenovirus Serotypes use Alpha V Integrins for Infection
    • Mathias, P.; Wickham, T.; Moore, M.; Nemerow, G. Multiple Adenovirus Serotypes use Alpha V Integrins for Infection. J. Virol. 1994, 68, 6811–6814.
    • (1994) J. Virol , vol.68 , pp. 6811-6814
    • Mathias, P.1    Wickham, T.2    Moore, M.3    Nemerow, G.4
  • 113
  • 116
    • 0031147756 scopus 로고    scopus 로고
    • Cell Surface Localization of the 60 kDa Heat Shock Chaperonin Protein (Hsp60) in Mammalian Cells
    • Soltys, B.J.; Gupta, R.S. Cell Surface Localization of the 60 kDa Heat Shock Chaperonin Protein (hsp60) in Mammalian Cells. Cell Biol. Int. 1997, 21, 315–320.
    • (1997) Cell Biol.Int , vol.21 , pp. 315-320
    • Soltys, B.J.1    Gupta, R.S.2
  • 117
    • 0032765705 scopus 로고    scopus 로고
    • Plasma Membrane Expression of Heat Shock Protein 60 in vivo in Response to Infection
    • Belles, C.; Kuhl, A.; Nosheny, R.; Carding, S.R. Plasma Membrane Expression of Heat Shock Protein 60 in vivo in Response to Infection. Infect. Immun. 1999, 67, 4191–4200.
    • (1999) Infect. Immun , vol.67 , pp. 4191-4200
    • Belles, C.1    Kuhl, A.2    Nosheny, R.3    Carding, S.R.4
  • 118
    • 84903775961 scopus 로고    scopus 로고
    • Serratia Odorifera Mediated Enhancement in Susceptibility of Aedes Aegypti for Chikungunya Virus. Indian
    • Apte-Deshpande, A.D.; Paingankar, M.S.; Gokhale, M.D.; Deobagkar, D.N. Serratia Odorifera Mediated Enhancement in Susceptibility of Aedes Aegypti for Chikungunya Virus. Indian J. Med. Res. 2014, 139, 762–768.
    • (2014) J. Med. Res , vol.139 , pp. 762-768
    • Apte-Deshpande, A.D.1    Paingankar, M.S.2    Gokhale, M.D.3    Deobagkar, D.N.4
  • 119
    • 64649101521 scopus 로고    scopus 로고
    • RNA Interference Mediated Silencing of Hsp60 Gene in Human Monocytic Myeloma Cell Line U937 Revealed Decreased Dengue Virus Multiplication
    • Padwad, Y.S.; Mishra, K.P.; Jain, M.; Chanda, S.; Karan, D.; Ganju, L. RNA Interference Mediated Silencing of Hsp60 Gene in Human Monocytic Myeloma Cell Line U937 Revealed Decreased Dengue Virus Multiplication. Immunobiology 2009, 214, 422–429.
    • (2009) Immunobiology , vol.214 , pp. 422-429
    • Padwad, Y.S.1    Mishra, K.P.2    Jain, M.3    Chanda, S.4    Karan, D.5    Ganju, L.6
  • 120
    • 84875780190 scopus 로고    scopus 로고
    • Alphavirus Genome Delivery Occurs Directly at the Plasma Membrane in a Time- and Temperature-Dependent Process
    • Vancini, R.; Wang, G.; Ferreira, D.; Hernandez, R.; Brown, D.T. Alphavirus Genome Delivery Occurs Directly at the Plasma Membrane in a Time- and Temperature-Dependent Process. J. Virol. 2013, 87, 4352–4359.
    • (2013) J. Virol , vol.87 , pp. 4352-4359
    • Vancini, R.1    Wang, G.2    Ferreira, D.3    Hernandez, R.4    Brown, D.T.5
  • 121
    • 2942733550 scopus 로고    scopus 로고
    • Conformational Changes in Sindbis Virions Resulting from Exposure to Low pH and Interactions with Cells Suggest that Cell Penetration may Occur at the Cell Surface in the Absence of Membrane Fusion
    • Paredes, A.M.; Ferreira, D.; Horton, M.; Saad, A.; Tsuruta, H.; Johnston, R.; Klimstra, W.; Ryman, K.; Hernandez, R.; Chiu, W.; et al. Conformational Changes in Sindbis Virions Resulting from Exposure to Low pH and Interactions with Cells Suggest that Cell Penetration may Occur at the Cell Surface in the Absence of Membrane Fusion. Virology 2004, 324, 373–386.
    • (2004) Virology , vol.324 , pp. 373-386
    • Paredes, A.M.1    Ferreira, D.2    Horton, M.3    Saad, A.4    Tsuruta, H.5    Johnston, R.6    Klimstra, W.7    Ryman, K.8    Hernandez, R.9    Chiu, W.10
  • 122
    • 34447524004 scopus 로고    scopus 로고
    • Clathrin-Coated Pits: Vive La Difference?
    • Benmerah, A.; Lamaze, C. Clathrin-Coated Pits: Vive La Difference? Traffic 2007, 8, 970–982.
    • (2007) Traffic , vol.8 , pp. 970-982
    • Benmerah, A.1    Lamaze, C.2
  • 123
    • 84899704909 scopus 로고    scopus 로고
    • Molecular Structure, Function, and Dynamics of Clathrin-Mediated Membrane Traffic. Cold Spring Harb
    • Kirchhausen, T.; Owen, D.; Harrison, S.C. Molecular Structure, Function, and Dynamics of Clathrin-Mediated Membrane Traffic. Cold Spring Harb. Perspect. Biol. 2014, 6.
    • (2014) Perspect. Biol , pp. 6
    • Kirchhausen, T.1    Owen, D.2    Harrison, S.C.3
  • 124
    • 35648935496 scopus 로고    scopus 로고
    • Venezuelan Equine Encephalitis Virus Infection of Mosquito Cells Requires Acidification as Well as Mosquito Homologs of the Endocytic Proteins Rab5 and Rab7
    • Colpitts, T.M.; Moore, A.C.; Kolokoltsov, A.A.; Davey, R.A. Venezuelan Equine Encephalitis Virus Infection of Mosquito Cells Requires Acidification as Well as Mosquito Homologs of the Endocytic Proteins Rab5 and Rab7. Virology 2007, 369, 78–91.
    • (2007) Virology , vol.369 , pp. 78-91
    • Colpitts, T.M.1    Moore, A.C.2    Kolokoltsov, A.A.3    Davey, R.A.4
  • 125
    • 0020724144 scopus 로고
    • Penetration of Semliki Forest Virus from Acidic Prelysosomal Vacuoles
    • Marsh, M.; Bolzau, E.; Helenius, A. Penetration of Semliki Forest Virus from Acidic Prelysosomal Vacuoles. Cell 1983, 32, 931–940.
    • (1983) Cell , vol.32 , pp. 931-940
    • Marsh, M.1    Bolzau, E.2    Helenius, A.3
  • 126
    • 33646059520 scopus 로고    scopus 로고
    • Venezuelan Equine Encephalitis Virus Entry Mechanism Requires Late Endosome Formation and Resists Cell Membrane Cholesterol Depletion
    • Kolokoltsov, A.A.; Fleming, E.H.; Davey, R.A. Venezuelan Equine Encephalitis Virus Entry Mechanism Requires Late Endosome Formation and Resists Cell Membrane Cholesterol Depletion. Virology 2006, 347, 333–342.
    • (2006) Virology , vol.347 , pp. 333-342
    • Kolokoltsov, A.A.1    Fleming, E.H.2    Davey, R.A.3
  • 127
    • 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
  • 129
    • 77955347331 scopus 로고    scopus 로고
    • Endocytosis of Chikungunya Virus into Mammalian Cells: Role of Clathrin and Early Endosomal Compartments
    • Bernard, E.; Solignat, M.; Gay, B.; Chazal, N.; Higgs, S.; Devaux, C.; Briant, L. Endocytosis of Chikungunya Virus into Mammalian Cells: Role of Clathrin and Early Endosomal Compartments. PLoS ONE 2010, 5, e11479.
    • (2010) Plos ONE , pp. 5
    • Bernard, E.1    Solignat, M.2    Gay, B.3    Chazal, N.4    Higgs, S.5    Devaux, C.6    Briant, L.7
  • 131
    • 84892844477 scopus 로고    scopus 로고
    • Genome-Wide RNAi Screen Identifies Novel Host Proteins Required for Alphavirus Entry
    • Ooi, Y.S.; Stiles, K.M.; Liu, C.Y.; Taylor, G.M.; Kielian, M. Genome-Wide RNAi Screen Identifies Novel Host Proteins Required for Alphavirus Entry. PLoS Pathog. 2013, 9, e1003835.
    • (2013) Plos Pathog , pp. 9
    • Ooi, Y.S.1    Stiles, K.M.2    Liu, C.Y.3    Taylor, G.M.4    Kielian, M.5
  • 134
    • 84936964928 scopus 로고    scopus 로고
    • or http://www. webcita-tion.org/6YFhQFTB1(accessed on 3 May 2015)
    • The Murphy Lab. Differences in Early Endosomal pH between Cell Types, Available online: http://murphylab.web.cmu.edu/projects/endosomal-pH-references.html or http://www. webcita-tion.org/6YFhQFTB1. (accessed on 3 May 2015).
    • The Murphy Lab. Differences in Early Endosomal Ph between Cell Types
  • 135
    • 84936964929 scopus 로고    scopus 로고
    • Chikungunya Virus Fusion Properties Elucidated by Single-Particle and Bulk Approaches
    • Van Duijl-Richter, M.; Blijleven, J.; van Oijen, A.; Smit, J. Chikungunya Virus Fusion Properties Elucidated by Single-Particle and Bulk Approaches. J. Gen. Virol. 2015.
    • (2015) J. Gen. Virol
    • Van Duijl-Richter, M.1    Blijleven, J.2    Van Oijen, A.3    Smit, J.4
  • 136
    • 84923197392 scopus 로고    scopus 로고
    • 3rd. Residue-Level Resolution of Alphavirus Envelope Protein Interactions in pH-Dependent Fusion
    • Zeng, X.; Mukhopadhyay, S.; Brooks, C.L., 3rd. Residue-Level Resolution of Alphavirus Envelope Protein Interactions in pH-Dependent Fusion. Proc. Natl. Acad. Sci. USA 2015, 112, 2034–2039.
    • (2015) Proc. Natl. Acad. Sci.Usa , vol.112 , pp. 2034-2039
    • Zeng, X.1    Mukhopadhyay, S.2    Brooks, C.L.3
  • 137
    • 0001696895 scopus 로고
    • PH-Dependent Fusion between the Semliki Forest Virus Membrane and Liposomes
    • White, J.; Helenius, A. pH-Dependent Fusion between the Semliki Forest Virus Membrane and Liposomes. Proc. Natl. Acad. Sci. USA 1980, 77, 3273–3277.
    • (1980) . Proc. Natl. Acad. Sci. USA , vol.77 , pp. 3273-3277
    • White, J.1    Helenius, A.2
  • 138
    • 0027509351 scopus 로고
    • Membrane Fusion of Semliki Forest Virus in a Model System: Correlation between Fusion Kinetics and Structural Changes in the Envelope Glycoprotein
    • Bron, R.; Wahlberg, J.M.; Garoff, H.; Wilschut, J. Membrane Fusion of Semliki Forest Virus in a Model System: Correlation between Fusion Kinetics and Structural Changes in the Envelope Glycoprotein. EMBO J. 1993, 12, 693–701.
    • (1993) EMBO J , vol.12 , pp. 693-701
    • Bron, R.1    Wahlberg, J.M.2    Garoff, H.3    Wilschut, J.4
  • 139
    • 0032874859 scopus 로고    scopus 로고
    • Low-pH-Dependent Fusion of Sindbis Virus with Receptor-Free Cholesterol- and Sphingolipid-Containing Liposomes
    • Smit, J.M.; Bittman, R.; Wilschut, J. Low-pH-Dependent Fusion of Sindbis Virus with Receptor-Free Cholesterol- and Sphingolipid-Containing Liposomes. J. Virol. 1999, 73, 8476–8484.
    • (1999) . J. Virol , vol.73 , pp. 8476-8484
    • Smit, J.M.1    Bittman, R.2    Wilschut, J.3
  • 140
    • 0024455501 scopus 로고
    • The Heterodimeric Association between the Membrane Proteins of Semliki Forest Virus Changes its Sensitivity to Low pH during Virus Maturation
    • Wahlberg, J.M.; Boere, W.A.; Garoff, H. The Heterodimeric Association between the Membrane Proteins of Semliki Forest Virus Changes its Sensitivity to Low pH during Virus Maturation. J. Virol. 1989, 63, 4991–4997.
    • (1989) J. Virol , vol.63 , pp. 4991-4997
    • Wahlberg, J.M.1    Boere, W.A.2    Garoff, H.3
  • 141
    • 33749266195 scopus 로고    scopus 로고
    • The Role of Histidine Residues in Low-pH-Mediated Viral Membrane Fusion
    • Kampmann, T.; Mueller, D.S.; Mark, A.E.; Young, P.R.; Kobe, B. The Role of Histidine Residues in Low-pH-Mediated Viral Membrane Fusion. Structure 2006, 14, 1481–1487.
    • (2006) Structure , vol.14 , pp. 1481-1487
    • Kampmann, T.1    Mueller, D.S.2    Mark, A.E.3    Young, P.R.4    Kobe, B.5
  • 142
    • 84875486890 scopus 로고    scopus 로고
    • Key Interaction between the Alphavirus Envelope Proteins Responsible for Initial Dimer Dissociation during Fusion
    • Fields, W.; Kielian, M. A Key Interaction between the Alphavirus Envelope Proteins Responsible for Initial Dimer Dissociation during Fusion. J. Virol. 2013, 87, 3774–3781.
    • (2013) J. Virol , vol.87 , pp. 3774-3781
    • Fields, W.1    Kielian, M.A.2
  • 143
    • 0037470148 scopus 로고    scopus 로고
    • Prefusion Rearrangements Resulting in Fusion Peptide Exposure in Semliki Forest Virus
    • Hammar, L.; Markarian, S.; Haag, L.; Lankinen, H.; Salmi, A.; Cheng, R.H. Prefusion Rearrangements Resulting in Fusion Peptide Exposure in Semliki Forest Virus. J. Biol. Chem. 2003, 278, 7189–7198.
    • (2003) J. Biol. Chem , vol.278 , pp. 7189-7198
    • Hammar, L.1    Markarian, S.2    Haag, L.3    Lankinen, H.4    Salmi, A.5    Cheng, R.H.6
  • 144
    • 1842457801 scopus 로고    scopus 로고
    • Multistep Regulation of Membrane Insertion of the Fusion Peptide of Semliki Forest Virus
    • Gibbons, D.L.; Ahn, A.; Liao, M.; Hammar, L.; Cheng, R.H.; Kielian, M. Multistep Regulation of Membrane Insertion of the Fusion Peptide of Semliki Forest Virus. J. Virol. 2004, 78, 3312–3318.
    • (2004) J. Virol , vol.78 , pp. 3312-3318
    • Gibbons, D.L.1    Ahn, A.2    Liao, M.3    Hammar, L.4    Cheng, R.H.5    Kielian, M.6
  • 145
    • 31344432402 scopus 로고    scopus 로고
    • Virus Membrane-Fusion Proteins: More than One Way to make a Hairpin. Nat
    • Kielian, M.; Rey, F.A. Virus Membrane-Fusion Proteins: More than One Way to make a Hairpin. Nat. Rev. Microbiol. 2006, 4, 67–76.
    • (2006) Rev. Microbiol , vol.4 , pp. 67-76
    • Kielian, M.1    Rey, F.A.2
  • 146
    • 0036118329 scopus 로고    scopus 로고
    • The Fusion Peptide of Semliki Forest Virus Associates with Sterol-Rich Membrane Domains
    • Ahn, A.; Gibbons, D.L.; Kielian, M. The Fusion Peptide of Semliki Forest Virus Associates with Sterol-Rich Membrane Domains. J. Virol. 2002, 76, 3267–3275.
    • (2002) J. Virol , vol.76 , pp. 3267-3275
    • Ahn, A.1    Gibbons, D.L.2    Kielian, M.3
  • 147
    • 0028152964 scopus 로고
    • Klimjack, M.R.; Jeffrey, S.; Kielian, M. Membrane and Protein Interactions of a Soluble Form of the Semliki Forest Virus Fusion Protein. J. Virol. 1994, 68, 6940–6946.
    • (1994) J. Virol , vol.68 , pp. 6940-6946
    • Klimjack, M.R.1    Jeffrey, S.2    Kielian, M.M.3
  • 148
    • 0028199032 scopus 로고
    • Membrane Fusion of Semliki Forest Virus Requires Sphingolipids in the Target Membrane
    • Nieva, J.L.; Bron, R.; Corver, J.; Wilschut, J. Membrane Fusion of Semliki Forest Virus Requires Sphingolipids in the Target Membrane. EMBO J. 1994, 13, 2797–2804.
    • (1994) EMBO J , vol.13 , pp. 2797-2804
    • Nieva, J.L.1    Bron, R.2    Corver, J.3    Wilschut, J.4
  • 149
    • 0031919431 scopus 로고    scopus 로고
    • A Single Point Mutation Controls the Cholesterol Dependence of Semliki Forest Virus Entry and Exit
    • Vashishtha, M.; Phalen, T.; Marquardt, M.T.; Ryu, J.S.; Ng, A.C.; Kielian, M. A Single Point Mutation Controls the Cholesterol Dependence of Semliki Forest Virus Entry and Exit. J. Cell Biol. 1998, 140, 91–99.
    • (1998) J. Cell Biol , vol.140 , pp. 91-99
    • Vashishtha, M.1    Phalen, T.2    Marquardt, M.T.3    Ryu, J.S.4    Ng, A.C.5    Kielian, M.6
  • 150
    • 0033918941 scopus 로고    scopus 로고
    • Biochemical Consequences of a Mutation that Controls the Cholesterol Dependence of Semliki Forest Virus Fusion
    • Chatterjee, P.K.; Vashishtha, M.; Kielian, M. Biochemical Consequences of a Mutation that Controls the Cholesterol Dependence of Semliki Forest Virus Fusion. J. Virol. 2000, 74, 1623–1631.
    • (2000) J. Virol , vol.74 , pp. 1623-1631
    • Chatterjee, P.K.1    Vashishtha, M.2    Kielian, M.3
  • 151
    • 0032930413 scopus 로고    scopus 로고
    • The Cholesterol Requirement for Sindbis Virus Entry and Exit and Characterization of a Spike Protein Region Involved in Cholesterol Dependence
    • Lu, Y.E.; Cassese, T.; Kielian, M. The Cholesterol Requirement for Sindbis Virus Entry and Exit and Characterization of a Spike Protein Region Involved in Cholesterol Dependence. J. Virol. 1999, 73, 4272–4278.
    • (1999) J. Virol , vol.73 , pp. 4272-4278
    • Lu, Y.E.1    Cassese, T.2    Kielian, M.3
  • 153
    • 84855289560 scopus 로고    scopus 로고
    • Sequential Adaptive Mutations Enhance Efficient Vector Switching by Chikungunya Virus and its Epidemic Emergence
    • Tsetsarkin, K.A.; Weaver, S.C. Sequential Adaptive Mutations Enhance Efficient Vector Switching by Chikungunya Virus and its Epidemic Emergence. PLoS Pathog. 2011, 7, e1002412.
    • (2011) Plos Pathog , pp. 7
    • Tsetsarkin, K.A.1    Weaver, S.C.2
  • 155
    • 0036891862 scopus 로고    scopus 로고
    • Novel Mutations that Control the Sphingolipid and Cholesterol Dependence of the Semliki Forest Virus Fusion Protein
    • Chatterjee, P.K.; Eng, C.H.; Kielian, M. Novel Mutations that Control the Sphingolipid and Cholesterol Dependence of the Semliki Forest Virus Fusion Protein. J. Virol. 2002, 76, 12712–12722.
    • (2002) J. Virol , vol.76 , pp. 12712-12722
    • Chatterjee, P.K.1    Eng, C.H.2    Kielian, M.3
  • 156
    • 35748931458 scopus 로고    scopus 로고
    • Lipids as Modulators of Membrane Fusion Mediated by Viral Fusion Proteins
    • Teissier, E.; Pecheur, E.I. Lipids as Modulators of Membrane Fusion Mediated by Viral Fusion Proteins. Eur. Biophys. J. 2007, 36, 887–899.
    • (2007) Eur. Biophys. J , vol.36 , pp. 887-899
    • Teissier, E.1    Pecheur, E.I.2
  • 157
    • 0026495818 scopus 로고
    • Membrane Fusion of Semliki Forest Virus Involves Homotrimers of the Fusion Protein
    • Wahlberg, J.M.; Bron, R.; Wilschut, J.; Garoff, H. Membrane Fusion of Semliki Forest Virus Involves Homotrimers of the Fusion Protein. J. Virol. 1992, 66, 7309–7318.
    • (1992) J. Virol , vol.66 , pp. 7309-7318
    • Wahlberg, J.M.1    Bron, R.2    Wilschut, J.3    Garoff, H.4
  • 158
    • 80052056371 scopus 로고    scopus 로고
    • The Domain I-Domain III Linker Plays an Important Role in the Fusogenic Conformational Change of the Alphavirus Membrane Fusion Protein
    • Zheng, Y.; Sanchez-San Martin, C.; Qin, Z.L.; Kielian, M. The Domain I-Domain III Linker Plays an Important Role in the Fusogenic Conformational Change of the Alphavirus Membrane Fusion Protein. J. Virol. 2011, 85, 6334–6342.
    • (2011) J. Virol , vol.85 , pp. 6334-6342
    • Zheng, Y.1    Sanchez-San Martin, C.2    Qin, Z.L.3    Kielian, M.4
  • 159
    • 66149140928 scopus 로고    scopus 로고
    • Role of Conserved Histidine Residues in the Low-pH Dependence of the Semliki Forest Virus Fusion Protein
    • Qin, Z.L.; Zheng, Y.; Kielian, M. Role of Conserved Histidine Residues in the Low-pH Dependence of the Semliki Forest Virus Fusion Protein. J. Virol. 2009, 83, 4670–4677.
    • (2009) J. Virol , vol.83 , pp. 4670-4677
    • Qin, Z.L.1    Zheng, Y.2    Kielian, M.3
  • 160
    • 1642540249 scopus 로고    scopus 로고
    • Conformational Change and Protein-Protein Interactions of the Fusion Protein of Semliki Forest Virus
    • Gibbons, D.L.; Vaney, M.C.; Roussel, A.; Vigouroux, A.; Reilly, B.; Lepault, J.; Kielian, M.; Rey, F.A. Conformational Change and Protein-Protein Interactions of the Fusion Protein of Semliki Forest Virus. Nature 2004, 427, 320–325.
    • (2004) Nature , vol.427 , pp. 320-325
    • Gibbons, D.L.1    Vaney, M.C.2    Roussel, A.3    Vigouroux, A.4    Reilly, B.5    Lepault, J.6    Kielian, M.7    Rey, F.A.8
  • 161
    • 57049101667 scopus 로고    scopus 로고
    • A Stable Prefusion Intermediate of the Alphavirus Fusion Protein Reveals Critical Features of Class II Membrane Fusion
    • Sanchez-San Martin, C.; Sosa, H.; Kielian, M. A Stable Prefusion Intermediate of the Alphavirus Fusion Protein Reveals Critical Features of Class II Membrane Fusion. Cell Host Microbe 2008, 4, 600–608.
    • (2008) Cell Host Microbe , vol.4 , pp. 600-608
    • Sanchez-San Martin, C.1    Sosa, H.2    Kielian, M.3
  • 162
    • 84880343667 scopus 로고    scopus 로고
    • Cross-Inhibition of Chikungunya Virus Fusion and Infection by Alphavirus E1 Domain III Proteins
    • Sanchez-San Martin, C.; Nanda, S.; Zheng, Y.; Fields, W.; Kielian, M. Cross-Inhibition of Chikungunya Virus Fusion and Infection by Alphavirus E1 Domain III Proteins. J. Virol. 2013, 87, 7680–7687.
    • (2013) J. Virol , vol.87 , pp. 7680-7687
    • Sanchez-San Martin, C.1    Nanda, S.2    Zheng, Y.3    Fields, W.4    Kielian, M.5
  • 163
    • 2942674829 scopus 로고    scopus 로고
    • During Entry of Alphaviruses, the E1 Glycoprotein Molecules Probably Form Two Separate Populations that Generate either a Fusion Pore Or Ion-Permeable Pores
    • Wengler, G.; Koschinski, A.; Wengler, G.; Repp, H. During Entry of Alphaviruses, the E1 Glycoprotein Molecules Probably Form Two Separate Populations that Generate either a Fusion Pore Or Ion-Permeable Pores. J. Gen. Virol. 2004, 85, 1695–1701.
    • (2004) J. Gen. Virol , vol.85 , pp. 1695-1701
    • Wengler, G.1    Koschinski, A.2    Wengler, G.3    Repp, H.4
  • 164
    • 84884591270 scopus 로고    scopus 로고
    • Chikungunya Virus: An Update on Antiviral Development and Challenges. Drug Discov
    • Kaur, P.; Chu, J.J. Chikungunya Virus: An Update on Antiviral Development and Challenges. Drug Discov. Today 2013, 18, 969–983.
    • (2013) Today , vol.18 , pp. 969-983
    • Kaur, P.1    Chu, J.J.2
  • 165
    • 84911895337 scopus 로고    scopus 로고
    • The Green Tea Catechin, Epigallocatechin Gallate Inhibits Chikungunya Virus Infection
    • Weber, C.; Sliva, K.; von Rhein, C.; Kummerer, B.M.; Schnierle, B.S. The Green Tea Catechin, Epigallocatechin Gallate Inhibits Chikungunya Virus Infection. Antiviral Res. 2015, 113, 1–3.
    • (2015) Antiviral Res , vol.113 , pp. 1-3
    • Weber, C.1    Sliva, K.2    Von Rhein, C.3    Kummerer, B.M.4    Schnierle, B.S.5
  • 166
    • 84904608511 scopus 로고    scopus 로고
    • A Small Molecule Inhibits Virion Attachment to Heparan Sulfate- or Sialic Acid-Containing Glycans
    • Colpitts, C.C.; Schang, L.M. A Small Molecule Inhibits Virion Attachment to Heparan Sulfate- or Sialic Acid-Containing Glycans. J. Virol. 2014, 88, 7806–7817.
    • (2014) J. Virol , vol.88 , pp. 7806-7817
    • Colpitts, C.C.1    Schang, L.M.2
  • 168
    • 84871745796 scopus 로고    scopus 로고
    • Use of Human Monoclonal Antibodies to Treat Chikungunya Virus Infection
    • Fric, J.; Bertin-Maghit, S.; Wang, C.I.; Nardin, A.; Warter, L. Use of Human Monoclonal Antibodies to Treat Chikungunya Virus Infection. J. Infect. Dis. 2013, 207, 319–322.
    • (2013) J. Infect. Dis , vol.207 , pp. 319-322
    • Fric, J.1    Bertin-Maghit, S.2    Wang, C.I.3    Nardin, A.4    Warter, L.5
  • 169
    • 84911475829 scopus 로고    scopus 로고
    • Mabila, M.; et al. Exposure of Epitope Residues on the Outer Face of the Chikungunya Virus Envelope Trimer Determines Antibody Neutralizing Efficacy
    • Fong, R.H.; Banik, S.S.; Mattia, K.; Barnes, T.; Tucker, D.; Liss, N.; Lu, K.; Selvarajah, S.; Srinivasan, S.; Mabila, M.; et al. Exposure of Epitope Residues on the Outer Face of the Chikungunya Virus Envelope Trimer Determines Antibody Neutralizing Efficacy. J. Virol. 2014, 88, 14364–14379.
    • (2014) J. Virol , vol.88 , pp. 14364-14379
    • Fong, R.H.1    Banik, S.S.2    Mattia, K.3    Barnes, T.4    Tucker, D.5    Liss, N.6    Lu, K.7    Selvarajah, S.8    Srinivasan, S.9
  • 170
    • 83655212354 scopus 로고    scopus 로고
    • Inhibitors of Alphavirus Entry and Replication Identified with a Stable Chikungunya Replicon Cell Line and Virus-Based Assays
    • Pohjala, L.; Utt, A.; Varjak, M.; Lulla, A.; Merits, A.; Ahola, T.; Tammela, P. Inhibitors of Alphavirus Entry and Replication Identified with a Stable Chikungunya Replicon Cell Line and Virus-Based Assays. PLoS ONE 2011, 6, e28923.
    • (2011) Plos ONE , pp. 6
    • Pohjala, L.1    Utt, A.2    Varjak, M.3    Lulla, A.4    Merits, A.5    Ahola, T.6    Tammela, P.7
  • 171
    • 76249126162 scopus 로고    scopus 로고
    • Unbiased Probing of the Entire Hepatitis C Virus Life Cycle Identifies Clinical Compounds that Target Multiple Aspects of the Infection
    • Gastaminza, P.; Whitten-Bauer, C.; Chisari, F.V. Unbiased Probing of the Entire Hepatitis C Virus Life Cycle Identifies Clinical Compounds that Target Multiple Aspects of the Infection. Proc. Natl. Acad. Sci. USA 2010, 107, 291–296.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 291-296
    • Gastaminza, P.1    Whitten-Bauer, C.2    Chisari, F.V.3
  • 173
    • 77950997597 scopus 로고    scopus 로고
    • Assessment of in vitro Prophylactic and Therapeutic Efficacy of Chloroquine Against Chikungunya Virus in Vero Cells
    • Khan, M.; Santhosh, S.R.; Tiwari, M.; Lakshmana Rao, P.V.; Parida, M. Assessment of in vitro Prophylactic and Therapeutic Efficacy of Chloroquine Against Chikungunya Virus in Vero Cells. J. Med. Virol. 2010, 82, 817–824.
    • (2010) . J. Med. Virol , vol.82 , pp. 817-824
    • Khan, M.1    Santhosh, S.R.2    Tiwari, M.3    Lakshmana Rao, P.V.4    Parida, M.5
  • 174
    • 79954609525 scopus 로고    scopus 로고
    • Chikungunya Disease and Chloroquine Treatment
    • Delogu, I.; de Lamballerie, X. Chikungunya Disease and Chloroquine Treatment. J. Med. Virol. 2011, 83, 1058–1059.
    • (2011) J. Med. Virol , vol.83 , pp. 1058-1059
    • Delogu, I.1    Lamballerie, D.X.2
  • 176
    • 26444506252 scopus 로고    scopus 로고
    • Domain III from Class II Fusion Proteins Functions as a Dominant-Negative Inhibitor of Virus Membrane Fusion
    • Liao, M.; Kielian, M. Domain III from Class II Fusion Proteins Functions as a Dominant-Negative Inhibitor of Virus Membrane Fusion. J. Cell Biol. 2005, 171, 111–120.
    • (2005) J. Cell Biol , vol.171 , pp. 111-120
    • Liao, M.1    Kielian, M.2
  • 177
    • 79953805715 scopus 로고    scopus 로고
    • In vitro Antiviral Activity of Arbidol Against Chikungunya Virus and Characteristics of a Selected Resistant Mutant
    • Delogu, I.; Pastorino, B.; Baronti, C.; Nougairede, A.; Bonnet, E.; de Lamballerie, X. In vitro Antiviral Activity of Arbidol Against Chikungunya Virus and Characteristics of a Selected Resistant Mutant. Antiviral Res. 2011, 90, 99–107.
    • (2011) Antiviral Res , vol.90 , pp. 99-107
    • Delogu, I.1    Pastorino, B.2    Baronti, C.3    Nougairede, A.4    Bonnet, E.5    De Lamballerie, X.6
  • 179
    • 77953993735 scopus 로고    scopus 로고
    • Membranotropic Effects of Arbidol, a Broad Anti-Viral Molecule, on Phospholipid Model Membranes
    • Villalain, J. Membranotropic Effects of Arbidol, a Broad Anti-Viral Molecule, on Phospholipid Model Membranes. J. Phys. Chem. B 2010, 114, 8544–8554.
    • (2010) J. Phys. Chem. B , vol.114 , pp. 8544-8554
    • Villalain, J.1
  • 180
    • 44349125733 scopus 로고    scopus 로고
    • Arbidol: A Broad-Spectrum Antiviral Compound that Blocks Viral Fusion
    • Boriskin, Y.S.; Leneva, I.A.; Pecheur, E.I.; Polyak, S.J. Arbidol: A Broad-Spectrum Antiviral Compound that Blocks Viral Fusion. Curr. Med. Chem. 2008, 15, 997–1005.
    • (2008) Curr. Med. Chem , vol.15 , pp. 997-1005
    • Boriskin, Y.S.1    Leneva, I.A.2    Pecheur, E.I.3    Polyak, S.J.4
  • 184
    • 0030071668 scopus 로고    scopus 로고
    • Antibody-Dependent Enhancement and Persistence in Macrophages of an Arbovirus Associated with Arthritis
    • Linn, M.L.; Aaskov, J.G.; Suhrbier, A. Antibody-Dependent Enhancement and Persistence in Macrophages of an Arbovirus Associated with Arthritis. J. Gen. Virol. 1996, 77, 407–411.
    • (1996) . J. Gen. Virol , vol.77 , pp. 407-411
    • Linn, M.L.1    Aaskov, J.G.2    Suhrbier, A.3
  • 185
    • 84899083438 scopus 로고    scopus 로고
    • Closing the Gap between Viral and Noninfectious Arthritis
    • Ryman, K.D.; Klimstra, W.B. Closing the Gap between Viral and Noninfectious Arthritis. Proc. Natl. Acad. Sci. USA 2014, 111, 5767–5768.
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 5767-5768
    • Ryman, K.D.1    Klimstra, W.B.2
  • 187
    • 84888024884 scopus 로고    scopus 로고
    • Chronic Joint Disease Caused by Persistent Chikungunya Virus Infection is Controlled by the Adaptive Immune Response
    • Hawman, D.W.; Stoermer, K.A.; Montgomery, S.A.; Pal, P.; Oko, L.; Diamond, M.S.; Morrison, T.E. Chronic Joint Disease Caused by Persistent Chikungunya Virus Infection is Controlled by the Adaptive Immune Response. J. Virol. 2013, 87, 13878–13888.
    • (2013) J. Virol , vol.87 , pp. 13878-13888
    • Hawman, D.W.1    Stoermer, K.A.2    Montgomery, S.A.3    Pal, P.4    Oko, L.5    Diamond, M.S.6    Morrison, T.E.7


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