메뉴 건너뛰기




Volumn 41, Issue 2, 2015, Pages 238-260

Bridging the past and the future of virology: Surface plasmon resonance as a powerful tool to investigate virus/host interactions

Author keywords

Protein protein interactions; Virus binding assays; Virus receptors

Indexed keywords

ANTIVIRUS AGENT; CELL SURFACE RECEPTOR; VACCINE; VIRUS ENVELOPE PROTEIN; VIRUS PROTEIN; PROTEIN BINDING;

EID: 84929728689     PISSN: 1040841X     EISSN: 15497828     Source Type: Journal    
DOI: 10.3109/1040841X.2013.826177     Document Type: Review
Times cited : (22)

References (276)
  • 1
    • 78650056746 scopus 로고    scopus 로고
    • Domain swapping reveals complement control protein modules critical for imparting cofactor and Decay-Accelerating activities in vaccinia virus complement control protein
    • Ahmad M, Raut S, Pyaram K, et al. (2010). Domain swapping reveals complement control protein modules critical for imparting cofactor and Decay-Accelerating activities in vaccinia virus complement control protein. J Immunol 185:6128-37
    • (2010) J Immunol , vol.185 , pp. 6128-6137
    • Ahmad, M.1    Raut, S.2    Pyaram, K.3
  • 2
    • 70349254552 scopus 로고    scopus 로고
    • IDentification of coagulation factor (F)X binding sites on the aDenovirus serotype 5 hexon: Effect of mutagenesis on FX interactions and gene transfer
    • Alba R, Bradshaw AC, Parker AL, et al. (2009). IDentification of coagulation factor (F)X binding sites on the aDenovirus serotype 5 hexon: effect of mutagenesis on FX interactions and gene transfer. Blood 114:965-71
    • (2009) Blood , vol.114 , pp. 965-971
    • Alba, R.1    Bradshaw, A.C.2    Parker, A.L.3
  • 3
    • 33645819161 scopus 로고    scopus 로고
    • A chemokine-binding domain in the tumor necrosis factor receptor from variola (smallpox) virus
    • Alejo A, Ruiz-Arguello MB, Ho Y, et al. (2006). A chemokine-binding domain in the tumor necrosis factor receptor from variola (smallpox) virus. Proc Natl Acad Sci U S A 103:5995-6000
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 5995-6000
    • Alejo, A.1    Ruiz-Arguello, M.B.2    Ho, Y.3
  • 4
    • 77953888539 scopus 로고    scopus 로고
    • Highly sensitive analysis of the interaction between HIV-1 Gag and phosphoinositiDe Derivatives based on surface plasmon resonance
    • Anraku K, Fukuda R, Takamune N, et al. (2010). Highly sensitive analysis of the interaction between HIV-1 Gag and phosphoinositiDe Derivatives based on surface plasmon resonance. Biochemistry 49: 5109-16
    • (2010) Biochemistry , vol.49 , pp. 5109-5116
    • Anraku, K.1    Fukuda, R.2    Takamune, N.3
  • 5
    • 0035892118 scopus 로고    scopus 로고
    • Receptor engagement by viral interleukin-6 encoDed by Kaposi sarcomaassociated herpesvirus
    • Aoki Y, Narazaki M, Kishimoto T, Tosato G. (2001). Receptor engagement by viral interleukin-6 encoDed by Kaposi sarcomaassociated herpesvirus. Blood 98:3042-9
    • (2001) Blood , vol.98 , pp. 3042-3049
    • Aoki, Y.1    Narazaki, M.2    Kishimoto, T.3    Tosato, G.4
  • 6
    • 38949213433 scopus 로고    scopus 로고
    • Structure and function of A41, a vaccinia virus chemokine binding protein
    • Bahar MW, Kenyon JC, Putz MM, et al. (2008). Structure and function of A41, a vaccinia virus chemokine binding protein. PLoS Pathog 4:e5
    • (2008) PLoS Pathog , vol.4 , pp. e5
    • Bahar, M.W.1    Kenyon, J.C.2    Putz, M.M.3
  • 7
    • 78649441078 scopus 로고    scopus 로고
    • Physical interaction between the herpes simplex virus type 1 exonuclease, UL12, and the DNA double-strand break-sensing MRN complex
    • Balasubramanian N, Bai P, Buchek G, et al. (2010). Physical interaction between the herpes simplex virus type 1 exonuclease, UL12, and the DNA double-strand break-sensing MRN complex. J Virol 84: 12504-14
    • (2010) J Virol , vol.84 , pp. 12504-12514
    • Balasubramanian, N.1    Bai, P.2    Buchek, G.3
  • 8
    • 0031662140 scopus 로고    scopus 로고
    • The use of variable Density self-Assembled monolayers to probe the structure of a target molecule
    • Bamdad C. (1998) the use of variable Density self-Assembled monolayers to probe the structure of a target molecule. Biophys J 75: 1989-96
    • (1998) Biophys J , vol.75 , pp. 1989-1996
    • Bamdad, C.1
  • 9
    • 0036431899 scopus 로고    scopus 로고
    • Ionic interaction of the HIV-1 V3 domain with CCR5 and Deregulation of T lymphocyte function
    • Baritaki S, Zafiropoulos A, Sioumpara M, et al. (2002). Ionic interaction of the HIV-1 V3 domain with CCR5 and Deregulation of T lymphocyte function. Biochem Biophys Res Commun 298:574-80
    • (2002) Biochem Biophys Res Commun , vol.298 , pp. 574-580
    • Baritaki, S.1    Zafiropoulos, A.2    Sioumpara, M.3
  • 10
    • 17044457135 scopus 로고    scopus 로고
    • Cellular binding of hepatitis C virus envelope glycoprotein E2 requires cell surface heparan sulfate
    • Barth H, Schafer C, Adah MI, et al. (2003). Cellular binding of hepatitis C virus envelope glycoprotein E2 requires cell surface heparan sulfate. J Biol Chem 278:41003-12
    • (2003) J Biol Chem , vol.278 , pp. 41003-41012
    • Barth, H.1    Schafer, C.2    Adah, M.I.3
  • 11
    • 33750356630 scopus 로고    scopus 로고
    • Viral and cellular Determinants of the hepatitis C virus envelope-heparan sulfate interaction
    • Barth H, Schnober EK, Zhang F, et al. (2006). Viral and cellular Determinants of the hepatitis C virus envelope-heparan sulfate interaction. J Virol 80:10579-90
    • (2006) J Virol , vol.80 , pp. 10579-10590
    • Barth, H.1    Schnober, E.K.2    Zhang, F.3
  • 12
    • 0035910468 scopus 로고    scopus 로고
    • Utilization of sialic acid as a coreceptor enhances reovirus attachment by multistep adhesion strengthening
    • Barton ES, Connolly JL, Forrest JC, et al. (2001). Utilization of sialic acid as a coreceptor enhances reovirus attachment by multistep adhesion strengthening. J Biol Chem 276:2200-11
    • (2001) J Biol Chem , vol.276 , pp. 2200-2211
    • Barton, E.S.1    Connolly, J.L.2    Forrest, J.C.3
  • 13
    • 0035900713 scopus 로고    scopus 로고
    • The viral CC chemokinebinding protein vCCI inhibits monocyte chemoattractant protein-1 activity by masking its CCR2B-binding site
    • Beck CG, StuDer C, Zuber JF, et al. (2001) the viral CC chemokinebinding protein vCCI inhibits monocyte chemoattractant protein-1 activity by masking its CCR2B-binding site. J Biol Chem 276: 43270-6
    • (2001) J Biol Chem , vol.276 , pp. 43270-43276
    • Beck, C.G.1    Studer, C.2    Zuber, J.F.3
  • 14
    • 0033591844 scopus 로고    scopus 로고
    • Potential drugs against cervical cancer: Zinc-ejecting inhibitors of the human papillomavirus type 16 E6 oncoprotein
    • BeerheiDe W, Bernard HU, Tan YJ, et al. (1999). Potential drugs against cervical cancer: zinc-ejecting inhibitors of the human papillomavirus type 16 E6 oncoprotein. J Natl Cancer Inst 91:1211-20
    • (1999) J Natl Cancer Inst , vol.91 , pp. 1211-1220
    • Beerheide, W.1    Bernard, H.U.2    Tan, Y.J.3
  • 15
    • 4143153933 scopus 로고    scopus 로고
    • Kinetic analysis of the interactions between vaccinia virus complement control protein and human complement proteins C3b and C4b
    • Bernet J, Mullick J, Panse Y, et al. (2004). Kinetic analysis of the interactions between vaccinia virus complement control protein and human complement proteins C3b and C4b. J Virol 78:9446-57
    • (2004) J Virol , vol.78 , pp. 9446-9457
    • Bernet, J.1    Mullick, J.2    Panse, Y.3
  • 16
    • 67649407509 scopus 로고    scopus 로고
    • The cell biology of HIV-1 virion genesis
    • Bieniasz PD. (2009) the cell biology of HIV-1 virion genesis. Cell Host Microbe 5:550-8
    • (2009) Cell Host Microbe , vol.5 , pp. 550-558
    • Bieniasz, P.D.1
  • 17
    • 10744224401 scopus 로고    scopus 로고
    • MoDe of action for linear peptiDe inhibitors of HIV-1 gp120 interactions
    • Biorn AC, Cocklin S, Madani N, et al. (2004). MoDe of action for linear peptiDe inhibitors of HIV-1 gp120 interactions. Biochemistry 43: 1928-38
    • (2004) Biochemistry , vol.43 , pp. 1928-1938
    • Biorn, A.C.1    Cocklin, S.2    Madani, N.3
  • 18
    • 0035159830 scopus 로고    scopus 로고
    • Cell surface heparan sulfate is a receptor for human herpesvirus 8 and interacts with envelope glycoprotein K8.1
    • Birkmann A, Mahr K, Ensser A, et al. (2001). Cell surface heparan sulfate is a receptor for human herpesvirus 8 and interacts with envelope glycoprotein K8.1. J Virol 75:11583-93
    • (2001) J Virol , vol.75 , pp. 11583-11593
    • Birkmann, A.1    Mahr, K.2    Ensser, A.3
  • 19
    • 0037237790 scopus 로고    scopus 로고
    • SynDecan captures, protects, and transmits HIV to T lymphocytes
    • Bobardt MD, Saphire AC, Hung HC, et al. (2003). SynDecan captures, protects, and transmits HIV to T lymphocytes. Immunity 18:27-39
    • (2003) Immunity , vol.18 , pp. 27-39
    • Bobardt, M.D.1    Saphire, A.C.2    Hung, H.C.3
  • 20
    • 79953224896 scopus 로고    scopus 로고
    • Interaction of the influenza A virus polymerase PB2 C-terminal region with importin {alpha} isoforms proviDes insights into host adaptation and polymerase assembly
    • Boivin S, Hart DJ. (2011). Interaction of the influenza A virus polymerase PB2 C-terminal region with importin {alpha} isoforms proviDes insights into host adaptation and polymerase assembly. J Biol Chem 286:10439-48
    • (2011) J Biol Chem , vol.286 , pp. 10439-10448
    • Boivin, S.1    Hart, D.J.2
  • 21
    • 34147094622 scopus 로고    scopus 로고
    • Potent T cell agonism mediated by a very rapid TCR/pMHC interaction
    • Boulter JM, Schmitz N, Sewell AK, et al. (2007). Potent T cell agonism mediated by a very rapid TCR/pMHC interaction. Eur J Immunol 37: 798-806
    • (2007) Eur J Immunol , vol.37 , pp. 798-806
    • Boulter, J.M.1    Schmitz, N.2    Sewell, A.K.3
  • 22
    • 23644449725 scopus 로고    scopus 로고
    • The intrinsically disorDered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolDed
    • Bourhis JM, Receveur-Brechot V, Oglesbee M, et al. (2005) the intrinsically disorDered C-terminal domain of the measles virus nucleoprotein interacts with the C-terminal domain of the phosphoprotein via two distinct sites and remains predominantly unfolDed. Protein Sci 14:1975-92
    • (2005) Protein Sci , vol.14 , pp. 1975-1992
    • Bourhis, J.M.1    Receveur-Brechot, V.2    Oglesbee, M.3
  • 23
    • 79959923466 scopus 로고    scopus 로고
    • Cells under siege: Viral glycoprotein interactions at the cell surface
    • BowDen TA, Yvonne Jones E, Stuart DI. (2011). Cells unDer siege: viral glycoprotein interactions at the cell surface. J Struct Biol 175:120-6
    • (2011) J Struct Biol , vol.175 , pp. 120-126
    • Bowden, T.A.1    Yvonne Jones, E.2    Stuart, D.I.3
  • 24
    • 79952446758 scopus 로고    scopus 로고
    • Computational biology approaches for selecting host-pathogen drug targets
    • Brown JR, Magid-Slav M, Sanseau P, Rajpal DK. (2011). Computational biology approaches for selecting host-pathogen drug targets. Drug Discov Today 16:229-36
    • (2011) Drug Discov Today , vol.16 , pp. 229-236
    • Brown, J.R.1    Magid-Slav, M.2    Sanseau, P.3    Rajpal, D.K.4
  • 25
    • 77953545354 scopus 로고    scopus 로고
    • BSA conjugates bearing multiple copies of the basic domain of HIV-1 Tat: Prototype for the Development of multitarget inhibitors of extracellular Tat
    • Bugatti A, ChioDelli P, Rosenbluh J, et al. (2010). BSA conjugates bearing multiple copies of the basic domain of HIV-1 Tat: prototype for the Development of multitarget inhibitors of extracellular Tat. Antiviral Res 87:30-9
    • (2010) Antiviral Res , vol.87 , pp. 30-39
    • Bugatti, A.1    Chiodelli, P.2    Rosenbluh, J.3
  • 26
    • 84872342951 scopus 로고    scopus 로고
    • Molecular interaction studies of HIV-1 matrix protein p17 and heparin: IDentification of the heparin-binding motif of p17 as a target for the Development of multitarget antagonists
    • Bugatti A, Giagulli C, Urbinati C, et al. (2013). Molecular interaction studies of HIV-1 matrix protein p17 and heparin: iDentification of the heparin-binding motif of p17 as a target for the Development of multitarget antagonists. J Biol Chem 288:1150-61
    • (2013) J Biol Chem , vol.288 , pp. 1150-1161
    • Bugatti, A.1    Giagulli, C.2    Urbinati, C.3
  • 27
    • 34447277610 scopus 로고    scopus 로고
    • Heparin-mimicking sulfonic acid polymers as multitarget inhibitors of human immunoDeficiency virus type 1 Tat and gp120 proteins
    • Bugatti A, Urbinati C, Ravelli C, et al. (2007). Heparin-mimicking sulfonic acid polymers as multitarget inhibitors of human immunoDeficiency virus type 1 Tat and gp120 proteins. Antimicrob Agents Chemother 51:2337-45
    • (2007) Antimicrob Agents Chemother , vol.51 , pp. 2337-2345
    • Bugatti, A.1    Urbinati, C.2    Ravelli, C.3
  • 28
    • 84865980040 scopus 로고    scopus 로고
    • HIV-1 matrix protein p17 promotes angiogenesis via chemokine receptors CXCR1 and CXCR2
    • Caccuri F, Giagulli C, Bugatti A, et al. (2012). HIV-1 matrix protein p17 promotes angiogenesis via chemokine receptors CXCR1 and CXCR2, Proc Natl Acad Sci U S A 109: 14580-5
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 14580-14585
    • Caccuri, F.1    Giagulli, C.2    Bugatti, A.3
  • 29
    • 0035915992 scopus 로고    scopus 로고
    • Orthopoxvirus IL-18 binding proteins: Affinities and antagonist activities
    • CalDerara S, Xiang Y, Moss B. (2001). Orthopoxvirus IL-18 binding proteins: affinities and antagonist activities. Virology 279:22-6
    • (2001) Virology , vol.279 , pp. 22-26
    • Calderara, S.1    Xiang, Y.2    Moss, B.3
  • 30
    • 0029063466 scopus 로고
    • Kinetics and thermodynamics of virus binding to receptor. Studies with rhinovirus, intercellular adhesion molecule-1 (ICAM-1), and surface plasmon resonance
    • Casasnovas JM, Springer TA. (1995). Kinetics and thermodynamics of virus binding to receptor. Studies with rhinovirus, intercellular adhesion molecule-1 (ICAM-1), and surface plasmon resonance. J Biol Chem 270:13216-24
    • (1995) J Biol Chem , vol.270 , pp. 13216-13224
    • Casasnovas, J.M.1    Springer, T.A.2
  • 31
    • 14844333201 scopus 로고    scopus 로고
    • The N-terminus of HIV-1 Tat protein is essential for Tat-TAR RNA interaction
    • Chaloin O, Peter JC, Briand JP, et al. (2005) the N-terminus of HIV-1 Tat protein is essential for Tat-TAR RNA interaction. Cell Mol Life Sci 62:355-61
    • (2005) Cell Mol Life Sci , vol.62 , pp. 355-361
    • Chaloin, O.1    Peter, J.C.2    Briand, J.P.3
  • 32
    • 33747854509 scopus 로고    scopus 로고
    • Azurin, Plasmodium falciparum malaria and HIV/AIDS: Inhibition of parasitic and viral growth by Azurin
    • Chaudhari A, Fialho AM, Ratner D, et al. (2006). Azurin, Plasmodium falciparum malaria and HIV/AIDS: inhibition of parasitic and viral growth by Azurin. Cell Cycle 5:1642-8
    • (2006) Cell Cycle , vol.5 , pp. 1642-1648
    • Chaudhari, A.1    Fialho, A.M.2    Ratner, D.3
  • 33
    • 11144227044 scopus 로고    scopus 로고
    • Mass spectroscopic characterization of the coronavirus infectious bronchitis virus nucleoprotein and elucidation of the role of phosphorylation in RNA binding by using surface plasmon resonance
    • Chen H, Gill A, Dove BK, et al. (2005a). Mass spectroscopic characterization of the coronavirus infectious bronchitis virus nucleoprotein and elucidation of the role of phosphorylation in RNA binding by using surface plasmon resonance. J Virol 79:1164-79
    • (2005) J Virol , vol.79 , pp. 1164-1179
    • Chen, H.1    Gill, A.2    Dove, B.K.3
  • 34
    • 21044456863 scopus 로고    scopus 로고
    • Cinanserin is an inhibitor of the 3C-like proteinase of severe acute respiratory syndrome coronavirus and strongly reduces virus replication in vitro
    • Chen L, Gui C, Luo X, et al. (2005b). Cinanserin is an inhibitor of the 3C-like proteinase of severe acute respiratory syndrome coronavirus and strongly reduces virus replication in vitro. J Virol 79:7095-103
    • (2005) J Virol , vol.79 , pp. 7095-7103
    • Chen, L.1    Gui, C.2    Luo, X.3
  • 35
    • 78650676082 scopus 로고    scopus 로고
    • Herpes simplex virus type 1 helicase-primase: DNA binding and consequent protein oligomerization and primase activation
    • Chen Y, Bai P, Mackay S, et al. (2012). Herpes simplex virus type 1 helicase-primase: DNA binding and consequent protein oligomerization and primase activation. J Virol 85:968-78
    • (2012) J Virol , vol.85 , pp. 968-978
    • Chen, Y.1    Bai, P.2    Mackay, S.3
  • 36
    • 13944272188 scopus 로고    scopus 로고
    • Function of HAb18G/CD147 in invasion of host cells by severe acute respiratory syndrome coronavirus
    • Chen Z, Mi L, Xu J, et al. (2005c). Function of HAb18G/CD147 in invasion of host cells by severe acute respiratory syndrome coronavirus. J Infect Dis 191:755-60
    • (2005) J Infect Dis , vol.191 , pp. 755-760
    • Chen, Z.1    Mi, L.2    Xu, J.3
  • 37
    • 33846155913 scopus 로고    scopus 로고
    • Structure-based maximal affinity moDel predicts small-molecule druggability
    • Cheng AC, Coleman RG, Smyth KT, et al. (2007). Structure-based maximal affinity moDel predicts small-molecule druggability. Nat Biotechnol 25:71-5
    • (2007) Nat Biotechnol , vol.25 , pp. 71-75
    • Cheng, A.C.1    Coleman, R.G.2    Smyth, K.T.3
  • 38
    • 84855849822 scopus 로고    scopus 로고
    • Fusion of Epstein-Barr virus with epithelial cells can be triggered by alphavbeta5 in addition to alphavbeta6 and alphavbeta8, and integrin binding triggers a conformational change in glycoproteins gHgL
    • Chesnokova LS, Hutt-Fletcher LM. (2011). Fusion of Epstein-Barr virus with epithelial cells can be triggered by alphavbeta5 in addition to alphavbeta6 and alphavbeta8, and integrin binding triggers a conformational change in glycoproteins gHgL. J Virol 85:13214-23
    • (2011) J Virol , vol.85 , pp. 13214-13223
    • Chesnokova, L.S.1    Hutt-Fletcher, L.M.2
  • 39
    • 42049118274 scopus 로고    scopus 로고
    • The function of coreceptor as a basis for the kinetic dissection of HIV type 1 envelope proteinmediated cell fusion
    • Chien MP, Jiang S, Chang DK. (2008) the function of coreceptor as a basis for the kinetic dissection of HIV type 1 envelope proteinmediated cell fusion. FASEB J 22:1179-92
    • (2008) FASEB J , vol.22 , pp. 1179-1192
    • Chien, M.P.1    Jiang, S.2    Chang, D.K.3
  • 40
    • 0029896207 scopus 로고    scopus 로고
    • Nucleic acid binding by zinc finger-like motif of human papillomavirus type 16 E7 oncoprotein
    • Chinami M, Inoue M, Masunaga K, et al. (1996). Nucleic acid binding by zinc finger-like motif of human papillomavirus type 16 E7 oncoprotein. J Virol Methods 59:173-6
    • (1996) J Virol Methods , vol.59 , pp. 173-176
    • Chinami, M.1    Inoue, M.2    Masunaga, K.3
  • 41
    • 84862019025 scopus 로고    scopus 로고
    • Sialic acid associated with alphavbeta3 integrin mediates HIV-1 Tat protein interaction and endothelial cell proangiogenic activation
    • ChioDelli P, Urbinati C, Mitola S, et al. (2012). Sialic acid associated with alphavbeta3 integrin mediates HIV-1 Tat protein interaction and endothelial cell proangiogenic activation. J Biol Chem 287:20456-66
    • (2012) J Biol Chem , vol.287 , pp. 20456-20466
    • Chiodelli, P.1    Urbinati, C.2    Mitola, S.3
  • 42
    • 0031711520 scopus 로고    scopus 로고
    • Inhibition of PrKX, a novel protein kinase, and the cyclic AMP-DepenDent protein kinase PKA by the regulatory proteins of aDeno-Associated virus type 2
    • Chiorini JA, Zimmermann B, Yang L, et al. (1998). Inhibition of PrKX, a novel protein kinase, and the cyclic AMP-DepenDent protein kinase PKA by the regulatory proteins of aDeno-Associated virus type 2. Mol Cell Biol 18:5921-9
    • (1998) Mol Cell Biol , vol.18 , pp. 5921-5929
    • Chiorini, J.A.1    Zimmermann, B.2    Yang, L.3
  • 43
    • 84874708174 scopus 로고    scopus 로고
    • The ubiquitinproteasome system in positive-strand RNA virus infection
    • Choi AG, Wong J, Marchant D, Luo H. (2012) the ubiquitinproteasome system in positive-strand RNA virus infection. Rev Med Virol 23:85-96
    • (2012) Rev Med Virol , vol.23 , pp. 85-96
    • Choi, A.G.1    Wong, J.2    Marchant, D.3    Luo, H.4
  • 44
    • 2942620427 scopus 로고    scopus 로고
    • Quantitative analysis of the interaction between the envelope protein domains and the core protein of human hepatitis B virus
    • Choi KJ, Lim CW, Yoon MY, et al. (2004). Quantitative analysis of the interaction between the envelope protein domains and the core protein of human hepatitis B virus. Biochem Biophys Res Commun 319: 959-66
    • (2004) Biochem Biophys Res Commun , vol.319 , pp. 959-966
    • Choi, K.J.1    Lim, C.W.2    Yoon, M.Y.3
  • 45
    • 33947433186 scopus 로고    scopus 로고
    • Broad-spectrum anti-human immunoDeficiency virus (HIV) potential of a peptiDe HIV type 1 entry inhibitor
    • Cocklin S, Gopi H, Querido B, et al. (2007). Broad-spectrum anti-human immunoDeficiency virus (HIV) potential of a peptiDe HIV type 1 entry inhibitor. J Virol 81:3645-8
    • (2007) J Virol , vol.81 , pp. 3645-3648
    • Cocklin, S.1    Gopi, H.2    Querido, B.3
  • 46
    • 79957572426 scopus 로고    scopus 로고
    • Cell entry and trafficking of human aDenovirus bound to blood factor X is Determined by the fiber serotype and not hexon:heparan sulfate interaction
    • Corjon S, Gonzalez G, Henning P, et al. (2011). Cell entry and trafficking of human aDenovirus bound to blood factor X is Determined by the fiber serotype and not hexon:heparan sulfate interaction. PLoS One 6:e18205
    • (2011) PLoS One , vol.6 , pp. e18205
    • Corjon, S.1    Gonzalez, G.2    Henning, P.3
  • 47
    • 2142810118 scopus 로고    scopus 로고
    • Binding of an influenza A virus to a neomembrane measured by surface plasmon resonance
    • Critchley P, Dimmock NJ. (2004). Binding of an influenza A virus to a neomembrane measured by surface plasmon resonance. Bioorg Med Chem 12:2773-80
    • (2004) Bioorg Med Chem , vol.12 , pp. 2773-2780
    • Critchley, P.1    Dimmock, N.J.2
  • 48
    • 47249111824 scopus 로고    scopus 로고
    • The HIV-1 envelope glycoprotein gp120 features four heparan sulfate binding domains, including the co-receptor binding site
    • Crublet E, Andrieu JP, Vives RR, Lortat-Jacob H. (2008) the HIV-1 envelope glycoprotein gp120 features four heparan sulfate binding domains, including the co-receptor binding site. J Biol Chem 283: 15193-200
    • (2008) J Biol Chem , vol.283 , pp. 15193-15200
    • Crublet, E.1    Andrieu, J.P.2    Vives, R.R.3    Lortat-Jacob, H.4
  • 49
    • 77949392990 scopus 로고    scopus 로고
    • Structure of aDenovirus type 21 knob in complex with CD46 reveals key differences in receptor contacts among species B aDenoviruses
    • Cupelli K, Muller S, Persson BD, et al. (2010). Structure of aDenovirus type 21 knob in complex with CD46 reveals key differences in receptor contacts among species B aDenoviruses. J Virol 84: 3189-200
    • (2010) J Virol , vol.84 , pp. 3189-3200
    • Cupelli, K.1    Muller, S.2    Persson, B.D.3
  • 50
    • 0032502813 scopus 로고    scopus 로고
    • ATPinDepenDent DNA unwinding by the aDenovirus single-stranDed DNA binding protein requires a flexible DNA binding loop
    • Dekker J, Kanellopoulos PN, Van Oosterhout JA, et al. (1998). ATPinDepenDent DNA unwinding by the aDenovirus single-stranDed DNA binding protein requires a flexible DNA binding loop. J Mol Biol 277: 825-38
    • (1998) J Mol Biol , vol.277 , pp. 825-838
    • Dekker, J.1    Kanellopoulos, P.N.2    Van Oosterhout, J.A.3
  • 51
    • 27144483814 scopus 로고    scopus 로고
    • An aptamer that neutralizes R5 strains of human immunoDeficiency virus type 1 blocks gp120-CCR5 interaction
    • Dey AK, Khati M, Tang M, et al. (2005). An aptamer that neutralizes R5 strains of human immunoDeficiency virus type 1 blocks gp120-CCR5 interaction. J Virol 79:13806-10
    • (2005) J Virol , vol.79 , pp. 13806-13810
    • Dey, A.K.1    Khati, M.2    Tang, M.3
  • 52
    • 67249085575 scopus 로고    scopus 로고
    • Structure-based stabilization of HIV-1 gp120 enhances humoral immune responses to the induced coreceptor binding site
    • Dey B, Svehla K, Xu L, et al. (2009). Structure-based stabilization of HIV-1 gp120 enhances humoral immune responses to the induced coreceptor binding site. PLoS Pathog 5:e1000445
    • (2009) PLoS Pathog , vol.5 , pp. e1000445
    • Dey, B.1    Svehla, K.2    Xu, L.3
  • 53
    • 33846242147 scopus 로고    scopus 로고
    • Coupled ATP and DNA binding of aDeno-Associated virus Rep40 helicase
    • Dignam SS, Collaco RF, Bieszczad J, et al. (2007). Coupled ATP and DNA binding of aDeno-Associated virus Rep40 helicase. Biochemistry 46:568-76
    • (2007) Biochemistry , vol.46 , pp. 568-576
    • Dignam, S.S.1    Collaco, R.F.2    Bieszczad, J.3
  • 54
    • 1542374062 scopus 로고    scopus 로고
    • Valency of antibody binding to virions and its Determination by surface plasmon resonance
    • Dimmock NJ, Hardy SA. (2004). Valency of antibody binding to virions and its Determination by surface plasmon resonance. Rev Med Virol 14:123-35
    • (2004) Rev Med Virol , vol.14 , pp. 123-135
    • Dimmock, N.J.1    Hardy, S.A.2
  • 55
    • 33646240071 scopus 로고    scopus 로고
    • Disparate thermodynamics governing T cell receptor-MHC-I interactions implicate extrinsic factors in guiding MHC restriction
    • Ely LK, Beddoe T, Clements CS, et al. (2006). Disparate thermodynamics governing T cell receptor-MHC-I interactions implicate extrinsic factors in guiding MHC restriction. Proc Natl Acad Sci U S A 103:6641-6
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 6641-6646
    • Ely, L.K.1    Beddoe, T.2    Clements, C.S.3
  • 56
    • 33749330704 scopus 로고    scopus 로고
    • Functional association between viral and cellular transcription during influenza virus infection
    • Engelhardt OG, Fodor E. (2006). Functional association between viral and cellular transcription during influenza virus infection. Rev Med Virol 16:329-45
    • (2006) Rev Med Virol , vol.16 , pp. 329-345
    • Engelhardt, O.G.1    Fodor, E.2
  • 57
    • 2942530949 scopus 로고    scopus 로고
    • IDentification of residues in an orthopoxvirus interleukin-18 binding protein involved in ligand binding and species specificity
    • Esteban DJ, Buller RM. (2004). IDentification of residues in an orthopoxvirus interleukin-18 binding protein involved in ligand binding and species specificity. Virology 323:197-207
    • (2004) Virology , vol.323 , pp. 197-207
    • Esteban, D.J.1    Buller, R.M.2
  • 58
    • 2442658926 scopus 로고    scopus 로고
    • Interleukin-18 and glycosaminoglycan binding by a protein encoDed by Variola virus
    • Esteban DJ, Nuara AA, Buller RM. (2004). Interleukin-18 and glycosaminoglycan binding by a protein encoDed by Variola virus. J Gen Virol 85:1291-9
    • (2004) J Gen Virol , vol.85 , pp. 1291-1299
    • Esteban, D.J.1    Nuara, A.A.2    Buller, R.M.3
  • 59
    • 0030930191 scopus 로고    scopus 로고
    • The UL8 subunit of the heterotrimeric herpes simplex virus type 1 helicaseprimase is required for the unwinding of single strand DNAbinding protein (ICP8)-coated DNA substrates
    • Falkenberg M, Bushnell DA, Elias P, Lehman IR. (1997) the UL8 subunit of the heterotrimeric herpes simplex virus type 1 helicaseprimase is required for the unwinding of single strand DNAbinding protein (ICP8)-coated DNA substrates. J Biol Chem 272: 22766-70
    • (1997) J Biol Chem , vol.272 , pp. 22766-22770
    • Falkenberg, M.1    Bushnell, D.A.2    Elias, P.3    Lehman, I.R.4
  • 60
    • 84857306337 scopus 로고    scopus 로고
    • Biochemically Defined HIV-1 envelope glycoprotein variant immunogens display differential binding and neutralizing specificities to the CD4-binding site
    • Feng Y, McKee K, Tran K, et al. (2011). Biochemically Defined HIV-1 envelope glycoprotein variant immunogens display differential binding and neutralizing specificities to the CD4-binding site. J Biol Chem 287:5673-86
    • (2011) J Biol Chem , vol.287 , pp. 5673-5686
    • Feng, Y.1    McKee, K.2    Tran, K.3
  • 61
    • 77952298465 scopus 로고    scopus 로고
    • The highly virulent variola and monkeypox viruses express secreted inhibitors of type i interferon
    • FernanDez De Marco MDel M, Alejo A, Hudson P, et al. (2009) the highly virulent variola and monkeypox viruses express secreted inhibitors of type I interferon. FASEB J 24:1479-88
    • (2009) FASEB J , vol.24 , pp. 1479-1488
    • De Fernandez, M.M.M.1    Alejo, A.2    Hudson, P.3
  • 62
    • 20444475372 scopus 로고    scopus 로고
    • Mechanism of transcription factor recruitment by acidic activators
    • Ferreira ME, Hermann S, Prochasson P, et al. (2005). Mechanism of transcription factor recruitment by acidic activators. J Biol Chem 280: 21779-84
    • (2005) J Biol Chem , vol.280 , pp. 21779-21784
    • Ferreira, M.E.1    Hermann, S.2    Prochasson, P.3
  • 63
    • 0032840985 scopus 로고    scopus 로고
    • Structural and functional characterization of an epitope in the conserved C-terminal region of HIV-1 gp120
    • Ferrer M, SulliVan BJ, Godbout KL, et al. (1999). Structural and functional characterization of an epitope in the conserved C-terminal region of HIV-1 gp120. J Pept Res 54:32-42
    • (1999) J Pept Res , vol.54 , pp. 32-42
    • Ferrer, M.1    Sullivan, B.J.2    Godbout, K.L.3
  • 65
    • 0029620850 scopus 로고
    • Aspects of molecular interaction between HIV p17 and human gamma interferon
    • Flamminio G, Caruso A, Poiesi C, et al. (1995). Aspects of molecular interaction between HIV p17 and human gamma interferon. AIDS Res Hum Retroviruses 11:1441-7
    • (1995) AIDS Res Hum Retroviruses , vol.11 , pp. 1441-1447
    • Flamminio, G.1    Caruso, A.2    Poiesi, C.3
  • 66
    • 79953778055 scopus 로고    scopus 로고
    • Surface plasmon resonance analysis of the binding of high-risk mucosal HPV E6 oncoproteins to the PDZ1 domain of the tight junction protein MAGI-1
    • Fournane S, Charbonnier S, Chapelle A, et al. (2010). Surface plasmon resonance analysis of the binding of high-risk mucosal HPV E6 oncoproteins to the PDZ1 domain of the tight junction protein MAGI-1. J Mol Recognit 24:511-23
    • (2010) J Mol Recognit , vol.24 , pp. 511-523
    • Fournane, S.1    Charbonnier, S.2    Chapelle, A.3
  • 67
    • 41649090223 scopus 로고    scopus 로고
    • A fusion-intermediate state of HIV-1 gp41 targeted by broadly neutralizing antibodies
    • Frey G, Peng H, Rits-Volloch S, et al. (2008). A fusion-intermediate state of HIV-1 gp41 targeted by broadly neutralizing antibodies. Proc Natl Acad Sci U S A 105:3739-44
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 3739-3744
    • Frey, G.1    Peng, H.2    Rits-Volloch, S.3
  • 68
    • 79955968096 scopus 로고    scopus 로고
    • ADenovirus E3-19K proteins of different serotypes and subgroups have similar, yet distinct, immunomodulatory functions toward major histocompatibility class i molecules
    • Fu J, Li L, Bouvier M. (2011). ADenovirus E3-19K proteins of different serotypes and subgroups have similar, yet distinct, immunomodulatory functions toward major histocompatibility class I molecules. J Biol Chem 286:17631-9
    • (2011) J Biol Chem , vol.286 , pp. 17631-17639
    • Fu, J.1    Li, L.2    Bouvier, M.3
  • 69
    • 36749009635 scopus 로고    scopus 로고
    • Kinetic eviDence for a ligand-binding-induced conformational transition in the T cell receptor
    • Gakamsky DM, Lewitzki E, Grell E, et al. (2007). Kinetic eviDence for a ligand-binding-induced conformational transition in the T cell receptor. Proc Natl Acad Sci U S A 104:16639-44
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 16639-16644
    • Gakamsky, D.M.1    Lewitzki, E.2    Grell, E.3
  • 70
    • 76749147768 scopus 로고    scopus 로고
    • Role of membranotropic sequences from herpes simplex virus type i glycoproteins B and H in the fusion process
    • Galdiero S, Falanga A, Vitiello G, et al. (2010). Role of membranotropic sequences from herpes simplex virus type I glycoproteins B and H in the fusion process. Biochim Biophys Acta 1798:579-91
    • (2010) Biochim Biophys Acta , vol.1798 , pp. 579-591
    • Galdiero, S.1    Falanga, A.2    Vitiello, G.3
  • 71
    • 0037016045 scopus 로고    scopus 로고
    • ADenovirus protein involved in virus internalization recruits ubiquitin-protein ligases
    • Galinier R, Gout E, Lortat-Jacob H, et al. (2002). ADenovirus protein involved in virus internalization recruits ubiquitin-protein ligases. Biochemistry 41:14299-305
    • (2002) Biochemistry , vol.41 , pp. 14299-14305
    • Galinier, R.1    Gout, E.2    Lortat-Jacob, H.3
  • 72
    • 2542422996 scopus 로고    scopus 로고
    • SynDecans and HIV-1 pathogenesis
    • Gallay P. (2004). SynDecans and HIV-1 pathogenesis. Microbes Infect 6: 617-22
    • (2004) Microbes Infect , vol.6 , pp. 617-622
    • Gallay, P.1
  • 73
    • 0141924820 scopus 로고    scopus 로고
    • Rev binds specifically to a purine loop in the SL1 region of the HIV-1 leaDer RNA
    • Gallego J, Greatorex J, Zhang H, et al. (2003). Rev binds specifically to a purine loop in the SL1 region of the HIV-1 leaDer RNA. J Biol Chem 278:40385-91
    • (2003) J Biol Chem , vol.278 , pp. 40385-40391
    • Gallego, J.1    Greatorex, J.2    Zhang, H.3
  • 74
    • 77955654922 scopus 로고    scopus 로고
    • Structural characterization of the Hepatitis C Virus NS3 protease from genotype 3a: The basis of the genotype 1b vs 3a inhibitor potency shift
    • Gallo M, Bottomley MJ, Pennestri M, et al. (2010). Structural characterization of the Hepatitis C Virus NS3 protease from genotype 3a: the basis of the genotype 1b vs. 3a inhibitor potency shift. Virology 405:424-38
    • (2010) Virology , vol.405 , pp. 424-438
    • Gallo, M.1    Bottomley, M.J.2    Pennestri, M.3
  • 75
    • 33745691892 scopus 로고    scopus 로고
    • Theta-Defensins prevent HIV-1 Env-mediated fusion by binding gp41 and blocking 6-helix bundle formation
    • Gallo SA, Wang W, Rawat SS, et al. (2006) theta-Defensins prevent HIV-1 Env-mediated fusion by binding gp41 and blocking 6-helix bundle formation. J Biol Chem 281:18787-92
    • (2006) J Biol Chem , vol.281 , pp. 18787-18792
    • Gallo, S.A.1    Wang, W.2    Rawat, S.S.3
  • 76
    • 17944363138 scopus 로고    scopus 로고
    • Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding
    • Garrus JE, von Schwedler UK, Pornillos OW, et al. (2001). Tsg101 and the vacuolar protein sorting pathway are essential for HIV-1 budding. Cell 107:55-65
    • (2001) Cell , vol.107 , pp. 55-65
    • Garrus, J.E.1    Von Schwedler, U.K.2    Pornillos, O.W.3
  • 77
    • 0029008438 scopus 로고
    • Stable chelating linkage for reversible immobilization of oligohistidine tagged proteins in the BIAcore surface plasmon resonance Detector
    • Gershon PD, Khilko S. (1995). Stable chelating linkage for reversible immobilization of oligohistidine tagged proteins in the BIAcore surface plasmon resonance Detector. J Immunol Methods 183: 65-76
    • (1995) J Immunol Methods , vol.183 , pp. 65-76
    • Gershon, P.D.1    Khilko, S.2
  • 78
    • 84868138485 scopus 로고    scopus 로고
    • Role of the HIV-1 matrix protein in Gag intracellular trafficking and targeting to the plasma membrane for virus assembly
    • Ghanam RH, Samal AB, FernanDez TF, Saad JS. (2012). Role of the HIV-1 matrix protein in Gag intracellular trafficking and targeting to the plasma membrane for virus assembly. Front Microbiol 3:55
    • (2012) Front Microbiol , vol.3 , pp. 55
    • Ghanam, R.H.1    Samal, A.B.2    Fernandez, T.F.3    Saad, J.S.4
  • 79
    • 84858035209 scopus 로고    scopus 로고
    • HIV-1 matrix protein p17 binds to the IL-8 receptor CXCR1 and shows IL-8-like chemokine activity on monocytes through Rho/ROCK activation
    • Giagulli C, Magiera AK, Bugatti A, et al. (2012). HIV-1 matrix protein p17 binds to the IL-8 receptor CXCR1 and shows IL-8-like chemokine activity on monocytes through Rho/ROCK activation. Blood 119: 2274-83
    • (2012) Blood , vol.119 , pp. 2274-2283
    • Giagulli, C.1    Magiera, A.K.2    Bugatti, A.3
  • 80
    • 0035871105 scopus 로고    scopus 로고
    • HIV-1 reverse transcriptase interaction with moDel RNA-DNA duplexes
    • Gorshkova, II, Rausch JW, Le Grice SF, Crouch RJ. (2001). HIV-1 reverse transcriptase interaction with moDel RNA-DNA duplexes. Anal Biochem 291:198-206
    • (2001) Anal Biochem , vol.291 , pp. 198-206
    • Gorshkova, I.I.1    Rausch, J.W.2    Le Grice, S.F.3    Crouch, R.J.4
  • 81
    • 60149111426 scopus 로고    scopus 로고
    • The shaping of T cell receptor recognition by self-tolerance
    • Gras S, Burrows SR, Kjer-Nielsen L, et al. (2009) the shaping of T cell receptor recognition by self-tolerance. Immunity 30:193-203
    • (2009) Immunity , vol.30 , pp. 193-203
    • Gras, S.1    Burrows, S.R.2    Kjer-Nielsen, L.3
  • 82
    • 77954411152 scopus 로고    scopus 로고
    • Allelic polymorphism in the T cell receptor and its impact on immune responses
    • Gras S, Chen Z, Miles JJ, et al. (2010). Allelic polymorphism in the T cell receptor and its impact on immune responses. J Exp Med 207: 1555-67
    • (2010) J Exp Med , vol.207 , pp. 1555-1567
    • Gras, S.1    Chen, Z.2    Miles, J.J.3
  • 83
    • 79952090349 scopus 로고    scopus 로고
    • Interaction of host cellular proteins with components of the hepatitis Delta virus
    • Greco-Stewart V, Pelchat M. (2010). Interaction of host cellular proteins with components of the hepatitis Delta virus. Viruses 2:189-212
    • (2010) Viruses , vol.2 , pp. 189-212
    • Greco-Stewart, V.1    Pelchat, M.2
  • 84
    • 70349869162 scopus 로고    scopus 로고
    • Influence of coagulation factor x on in vitro and in vivo gene Delivery by aDenovirus (Ad) 5, Ad35, and chimeric Ad5/Ad35 vectors
    • Greig JA, Buckley SM, Waddington SN, et al. (2009). Influence of coagulation factor x on in vitro and in vivo gene Delivery by aDenovirus (Ad) 5, Ad35, and chimeric Ad5/Ad35 vectors. Mol Ther 17:1683-91
    • (2009) Mol Ther , vol.17 , pp. 1683-1691
    • Greig, J.A.1    Buckley, S.M.2    Waddington, S.N.3
  • 85
    • 34547114262 scopus 로고    scopus 로고
    • Reovirus binding Determinants in junctional adhesion molecule-A
    • Guglielmi KM, Kirchner E, Holm GH, et al. (2007). Reovirus binding Determinants in junctional adhesion molecule-A. J Biol Chem 282: 17930-40
    • (2007) J Biol Chem , vol.282 , pp. 17930-17940
    • Guglielmi, K.M.1    Kirchner, E.2    Holm, G.H.3
  • 86
    • 33846667903 scopus 로고    scopus 로고
    • Duplex strand joining reactions catalyzed by vaccinia virus DNA polymerase
    • Hamilton MD, Nuara AA, Gammon DB, et al. (2007). Duplex strand joining reactions catalyzed by vaccinia virus DNA polymerase. Nucleic Acids Res 35:143-51
    • (2007) Nucleic Acids Res , vol.35 , pp. 143-151
    • Hamilton, M.D.1    Nuara, A.A.2    Gammon, D.B.3
  • 87
    • 77951959240 scopus 로고    scopus 로고
    • HIV-1 Tat and host AFF4 recruit two transcription elongation factors into a bifunctional complex for coordinated activation of HIV-1 transcription
    • He N, Liu M, Hsu J, et al. (2010). HIV-1 Tat and host AFF4 recruit two transcription elongation factors into a bifunctional complex for coordinated activation of HIV-1 transcription. Mol Cell 38:428-38
    • (2010) Mol Cell , vol.38 , pp. 428-438
    • He, N.1    Liu, M.2    Hsu, J.3
  • 88
    • 37849042508 scopus 로고    scopus 로고
    • Mechanism of inhibition of HIV-1 reverse transcriptase by the novel broad-range DNA polymerase inhibitor N-{2-[4-(aminosulfonyl)phenyl]ethyl}-2-(2-thienyl)acetamiDe
    • Herschhorn A, Oz-Gleenberg I, Hizi A. (2008a). Mechanism of inhibition of HIV-1 reverse transcriptase by the novel broad-range DNA polymerase inhibitor N-{2-[4-(aminosulfonyl)phenyl]ethyl}-2-(2-thienyl)acetamiDe. Biochemistry 47:490-502
    • (2008) Biochemistry , vol.47 , pp. 490-502
    • Herschhorn, A.1    Oz-Gleenberg, I.2    Hizi, A.3
  • 89
    • 43549095213 scopus 로고    scopus 로고
    • Quantitative analysis of the interactions between HIV-1 integrase and retroviral reverse transcriptases
    • Herschhorn A, Oz-Gleenberg I, Hizi A. (2008b). Quantitative analysis of the interactions between HIV-1 integrase and retroviral reverse transcriptases. Biochem J 412: 163-70
    • (2008) Biochem J , vol.412 , pp. 163-170
    • Herschhorn, A.1    Oz-Gleenberg, I.2    Hizi, A.3
  • 90
    • 35648960384 scopus 로고    scopus 로고
    • Binding kinetics of influenza viruses to sialic acid-containing carbohydrates
    • Hidari KI, Shimada S, Suzuki Y, Suzuki T. (2007). Binding kinetics of influenza viruses to sialic acid-containing carbohydrates. Glycoconj J 24:583-90
    • (2007) Glycoconj J , vol.24 , pp. 583-590
    • Hidari, K.I.1    Shimada, S.2    Suzuki, Y.3    Suzuki, T.4
  • 91
    • 82855163961 scopus 로고    scopus 로고
    • DC-SIGN increases the affinity of HIV-1 envelope glycoprotein interaction with CD4
    • Hijazi K, Wang Y, Scala C, et al. (2011). DC-SIGN increases the affinity of HIV-1 envelope glycoprotein interaction with CD4. PLoS One 6: e28307
    • (2011) PLoS One , vol.6 , pp. e28307
    • Hijazi, K.1    Wang, Y.2    Scala, C.3
  • 92
    • 0346434163 scopus 로고    scopus 로고
    • Two distinct transport motifs in the aDenovirus E3/10.4-14.5 proteins act in concert to downmodulate apoptosis receptors and the epiDermal growth factor receptor
    • Hilgendorf A, Lindberg J, Ruzsics Z, et al. (2003). Two distinct transport motifs in the aDenovirus E3/10.4-14.5 proteins act in concert to downmodulate apoptosis receptors and the epiDermal growth factor receptor. J Biol Chem 278:51872-84
    • (2003) J Biol Chem , vol.278 , pp. 51872-51884
    • Hilgendorf, A.1    Lindberg, J.2    Ruzsics, Z.3
  • 93
    • 20344403493 scopus 로고    scopus 로고
    • The oligomeric structure of vaccinia viral envelope protein A27L is essential for binding to heparin and heparan sulfates on cell surfaces: A structural and functional approach using site-specific mutagenesis
    • Ho Y, Hsiao JC, Yang MH, et al. (2005) the oligomeric structure of vaccinia viral envelope protein A27L is essential for binding to heparin and heparan sulfates on cell surfaces: a structural and functional approach using site-specific mutagenesis. J Mol Biol 349:1060-71
    • (2005) J Mol Biol , vol.349 , pp. 1060-1071
    • Ho, Y.1    Hsiao, J.C.2    Yang, M.H.3
  • 94
    • 77957338656 scopus 로고    scopus 로고
    • Interaction of viruses with host cell molecular motors
    • Hsieh MJ, White PJ, Pouton CW. (2010). Interaction of viruses with host cell molecular motors. Curr Opin Biotechnol 21:633-9
    • (2010) Curr Opin Biotechnol , vol.21 , pp. 633-639
    • Hsieh, M.J.1    White, P.J.2    Pouton, C.W.3
  • 95
    • 70350492302 scopus 로고    scopus 로고
    • Elucidation of the stability and functional regions of the human coronavirus OC43 nucleocapsid protein
    • Huang CY, Hsu YL, Chiang WL, Hou MH. (2009). Elucidation of the stability and functional regions of the human coronavirus OC43 nucleocapsid protein. Protein Sci 18:2209-18
    • (2009) Protein Sci , vol.18 , pp. 2209-2218
    • Huang, C.Y.1    Hsu, Y.L.2    Chiang, W.L.3    Hou, M.H.4
  • 96
    • 40649128534 scopus 로고    scopus 로고
    • Epitope mapping and use of epitope-specific antisera to characterize the VP5 binding site in rotavirus SA11 NSP4
    • Hyser JM, Zeng CQ, Beharry Z, et al. (2008). Epitope mapping and use of epitope-specific antisera to characterize the VP5 binding site in rotavirus SA11 NSP4. Virology 373:211-28
    • (2008) Virology , vol.373 , pp. 211-228
    • Hyser, J.M.1    Zeng, C.Q.2    Beharry, Z.3
  • 97
    • 0035910754 scopus 로고    scopus 로고
    • Control of mitochondrial membrane permeabilization by aDenine nucleotiDe translocator interacting with HIV-1 viral protein rR and Bcl-2
    • Jacotot E, Ferri KF, El Hamel C, et al. (2001). Control of mitochondrial membrane permeabilization by aDenine nucleotiDe translocator interacting with HIV-1 viral protein rR and Bcl-2. J Exp Med 193: 509-19
    • (2001) J Exp Med , vol.193 , pp. 509-519
    • Jacotot, E.1    Ferri, K.F.2    El Hamel, C.3
  • 98
    • 38549142580 scopus 로고    scopus 로고
    • RNA unwinding activity of the hepatitis C virus NS3 helicase is modulated by the NS5B polymerase
    • Jennings TA, Chen Y, Sikora D, et al. (2008). RNA unwinding activity of the hepatitis C virus NS3 helicase is modulated by the NS5B polymerase. Biochemistry 47:1126-35
    • (2008) Biochemistry , vol.47 , pp. 1126-1135
    • Jennings, T.A.1    Chen, Y.2    Sikora, D.3
  • 99
    • 39049114500 scopus 로고    scopus 로고
    • Novel paradigms for drug discovery: Computational multitarget screening
    • Jenwitheesuk E, Horst JA, Rivas KL, et al. (2008). Novel paradigms for drug discovery: computational multitarget screening. Trends Pharmacol Sci 29:62-71
    • (2008) Trends Pharmacol Sci , vol.29 , pp. 62-71
    • Jenwitheesuk, E.1    Horst, J.A.2    Rivas, K.L.3
  • 100
    • 81455159239 scopus 로고    scopus 로고
    • The binding of hepatitis B virus X protein to glioma-Associated oncogene homologue 1 and its biological characterization in vitro
    • Jo BB, Jeong MS, Park SY, et al. (2011) the binding of hepatitis B virus X protein to glioma-Associated oncogene homologue 1 and its biological characterization in vitro. Appl Biochem Biotechnol 165: 109-22
    • (2011) Appl Biochem Biotechnol , vol.165 , pp. 109-122
    • Jo, B.B.1    Jeong, M.S.2    Park, S.Y.3
  • 101
    • 84857082116 scopus 로고    scopus 로고
    • Respiratory syncytial virus glycoprotein G interacts with DC-SIGN and L-SIGN to activate ERK1 and ERK2
    • Johnson TR, McLellan JS, Graham BS. (2011). Respiratory syncytial virus glycoprotein G interacts with DC-SIGN and L-SIGN to activate ERK1 and ERK2. J Virol 86:1339-47
    • (2011) J Virol , vol.86 , pp. 1339-1347
    • Johnson, T.R.1    McLellan, J.S.2    Graham, B.S.3
  • 102
    • 28444469838 scopus 로고    scopus 로고
    • Surface plasmon resonance imaging-based protein arrays for high-throughput screening of protein-protein interaction inhibitors
    • Jung SO, Ro HS, Kho BH, et al. (2005). Surface plasmon resonance imaging-based protein arrays for high-throughput screening of protein-protein interaction inhibitors. Proteomics 5:4427-31
    • (2005) Proteomics , vol.5 , pp. 4427-4431
    • Jung, S.O.1    Ro, H.S.2    Kho, B.H.3
  • 103
    • 52049111184 scopus 로고    scopus 로고
    • Viral infection and human disease-insights from minimotifs
    • Kadaveru K, Vyas J, Schiller MR. (2008). Viral infection and human disease-insights from minimotifs. Front Biosci 13:6455-71
    • (2008) Front Biosci , vol.13 , pp. 6455-6471
    • Kadaveru, K.1    Vyas, J.2    Schiller, M.R.3
  • 104
    • 56049108120 scopus 로고    scopus 로고
    • Phosphorylation of hepatitis B virus core C-terminally truncated protein (Cp149) by PKC increases capsid assembly and stability
    • Kang H, Yu J, Jung G. (2008). Phosphorylation of hepatitis B virus core C-terminally truncated protein (Cp149) by PKC increases capsid assembly and stability. Biochem J 416:47-54
    • (2008) Biochem J , vol.416 , pp. 47-54
    • Kang, H.1    Yu, J.2    Jung, G.3
  • 105
    • 78650599993 scopus 로고    scopus 로고
    • Epstein-Barr virus-encoDed EBNA-5 forms trimolecular protein complexes with MDM2 and p53 and inhibits the transactivating function of p53
    • Kashuba E, Yurchenko M, Yenamandra SP, et al. (2010). Epstein-Barr virus-encoDed EBNA-5 forms trimolecular protein complexes with MDM2 and p53 and inhibits the transactivating function of p53. Int J Cancer 128:817-25
    • (2010) Int J Cancer , vol.128 , pp. 817-825
    • Kashuba, E.1    Yurchenko, M.2    Yenamandra, S.P.3
  • 106
    • 77952068704 scopus 로고    scopus 로고
    • Are scoring functions in proteinprotein docking ready to predict interactomes? Clues from a novel binding affinity benchmark
    • Kastritis PL, Bonvin AM. (2010). Are scoring functions in proteinprotein docking ready to predict interactomes? Clues from a novel binding affinity benchmark. J Proteome Res 9:2216-25
    • (2010) J Proteome Res , vol.9 , pp. 2216-2225
    • Kastritis, P.L.1    Bonvin, A.M.2
  • 107
    • 12344292308 scopus 로고    scopus 로고
    • Parvovirus B19 does not bind to membrane-Associated globosiDe in vitro
    • Kaufmann B, Baxa U, Chipman PR, et al. (2005). Parvovirus B19 does not bind to membrane-Associated globosiDe in vitro. Virology 332: 189-98
    • (2005) Virology , vol.332 , pp. 189-198
    • Kaufmann, B.1    Baxa, U.2    Chipman, P.R.3
  • 108
    • 0027205314 scopus 로고
    • Direct Detection of major histocompatibility complex class i binding to antigenic peptiDes using surface plasmon resonance. PeptiDe immobilization and characterization of binding specificity
    • Khilko SN, Corr M, Boyd LF, et al. (1993). Direct Detection of major histocompatibility complex class I binding to antigenic peptiDes using surface plasmon resonance. PeptiDe immobilization and characterization of binding specificity. J Biol Chem 268: 15425-34
    • (1993) J Biol Chem , vol.268 , pp. 15425-15434
    • Khilko, S.N.1    Corr, M.2    Boyd, L.F.3
  • 109
    • 77953009742 scopus 로고    scopus 로고
    • Vaccines with MF59 adjuVant expand the antibody repertoire to target protective sites of panDemic avian H5N1 influenza virus
    • Khurana S, Chearwae W, Castellino F, et al. (2010). Vaccines with MF59 adjuVant expand the antibody repertoire to target protective sites of panDemic avian H5N1 influenza virus. Sci Transl Med 2: 15ra5
    • (2010) Sci Transl Med , vol.2 , pp. 15ra5
    • Khurana, S.1    Chearwae, W.2    Castellino, F.3
  • 110
    • 34249950861 scopus 로고    scopus 로고
    • Immunogenicity of recombinant human immunoDeficiency virus type 1-like particles expressing gp41 Derivatives in a pre-fusion state
    • Kim M, Qiao Z, Yu J, et al. (2007). Immunogenicity of recombinant human immunoDeficiency virus type 1-like particles expressing gp41 Derivatives in a pre-fusion state. Vaccine 25:5102-14
    • (2007) Vaccine , vol.25 , pp. 5102-5114
    • Kim, M.1    Qiao, Z.2    Yu, J.3
  • 111
    • 1442355476 scopus 로고    scopus 로고
    • RNA aptamers that bind the nucleocapsid protein contain pseudoknots
    • Kim MY, Jeong S. (2003). RNA aptamers that bind the nucleocapsid protein contain pseudoknots. Mol Cells 16:413-17
    • (2003) Mol Cells , vol.16 , pp. 413-417
    • Kim, M.Y.1    Jeong, S.2
  • 112
    • 0036296520 scopus 로고    scopus 로고
    • Selection and stabilization of the RNA aptamers against the human immunoDeficiency virus type-1 nucleocapsid protein
    • Kim SJ, Kim MY, Lee JH, et al. (2002). Selection and stabilization of the RNA aptamers against the human immunoDeficiency virus type-1 nucleocapsid protein. Biochem Biophys Res Commun 291: 925-31
    • (2002) Biochem Biophys Res Commun , vol.291 , pp. 925-931
    • Kim, S.J.1    Kim, M.Y.2    Lee, J.H.3
  • 113
    • 0033999577 scopus 로고    scopus 로고
    • IDentification of contact residues and Definition of the CAR-binding site of aDenovirus type 5 fiber protein
    • Kirby I, Davison E, Beavil AJ, et al. (2000). IDentification of contact residues and Definition of the CAR-binding site of aDenovirus type 5 fiber protein. J Virol 74:2804-13
    • (2000) J Virol , vol.74 , pp. 2804-2813
    • Kirby, I.1    Davison, E.2    Beavil, A.J.3
  • 114
    • 0034960354 scopus 로고    scopus 로고
    • ADenovirus type 9 fiber knob binds to the coxsackie B virus-ADenovirus receptor (CAR) with lower affinity than fiber knobs of other CAR-binding aDenovirus serotypes
    • Kirby I, Lord R, Davison E, et al. (2001). ADenovirus type 9 fiber knob binds to the coxsackie B virus-ADenovirus receptor (CAR) with lower affinity than fiber knobs of other CAR-binding aDenovirus serotypes. J Virol 75:7210-14
    • (2001) J Virol , vol.75 , pp. 7210-7214
    • Kirby, I.1    Lord, R.2    Davison, E.3
  • 115
    • 72849130164 scopus 로고    scopus 로고
    • The requirement for cellular transportin 3 (TNPO3 or TRN-SR2) during infection maps to human immunoDeficiency virus type 1 capsid and not integrase
    • Krishnan L, Matreyek KA, Oztop I, et al. (2010) the requirement for cellular transportin 3 (TNPO3 or TRN-SR2) during infection maps to human immunoDeficiency virus type 1 capsid and not integrase. J Virol 84:397-406
    • (2010) J Virol , vol.84 , pp. 397-406
    • Krishnan, L.1    Matreyek, K.A.2    Oztop, I.3
  • 116
    • 55749098114 scopus 로고    scopus 로고
    • Tyrosine-sulfate isosteres of CCR5 N-terminus as tools for studying HIV-1 entry
    • Lam SN, Acharya P, Wyatt R, et al. (2008). Tyrosine-sulfate isosteres of CCR5 N-terminus as tools for studying HIV-1 entry. Bioorg Med Chem 16:10113-20
    • (2008) Bioorg Med Chem , vol.16 , pp. 10113-10120
    • Lam, S.N.1    Acharya, P.2    Wyatt, R.3
  • 117
    • 67649221447 scopus 로고    scopus 로고
    • Orf virus-encoDed chemokine-binding protein is a potent inhibitor of inflammatory monocyte recruitment in a mouse skin moDel
    • Lateef Z, Baird MA, Wise LM, et al. (2009). Orf virus-encoDed chemokine-binding protein is a potent inhibitor of inflammatory monocyte recruitment in a mouse skin moDel. J Gen Virol 90:1477-82
    • (2009) J Gen Virol , vol.90 , pp. 1477-1482
    • Lateef, Z.1    Baird, M.A.2    Wise, L.M.3
  • 118
    • 0032514905 scopus 로고    scopus 로고
    • Determination of the affinity and kinetic constants for the interaction between the human virus echovirus 11 and its cellular receptor, CD55
    • Lea SM, Powell RM, McKee T, et al. (1998). Determination of the affinity and kinetic constants for the interaction between the human virus echovirus 11 and its cellular receptor, CD55. J Biol Chem 273: 30443-7
    • (1998) J Biol Chem , vol.273 , pp. 30443-30447
    • Lea, S.M.1    Powell, R.M.2    McKee, T.3
  • 119
    • 1442326743 scopus 로고    scopus 로고
    • Interactions of HIV-1 proteins gp120 and Nef with cellular partners Define a novel allosteric paradigm
    • Leavitt SA, Schon A, Klein JC, et al. (2004). Interactions of HIV-1 proteins gp120 and Nef with cellular partners Define a novel allosteric paradigm. Curr Protein Pept Sci 5:1-8
    • (2004) Curr Protein Pept Sci , vol.5 , pp. 1-8
    • Leavitt, S.A.1    Schon, A.2    Klein, J.C.3
  • 120
    • 75949120950 scopus 로고    scopus 로고
    • Hepatitis B virus core interacts with the host cell nucleolar protein, nucleophosmin 1
    • Lee SJ, Shim HY, Hsieh A, et al. (2009). Hepatitis B virus core interacts with the host cell nucleolar protein, nucleophosmin 1. J Microbiol 47: 746-52
    • (2009) J Microbiol , vol.47 , pp. 746-752
    • Lee, S.J.1    Shim, H.Y.2    Hsieh, A.3
  • 121
    • 68949094007 scopus 로고    scopus 로고
    • Multivalent binding of carbohydrates by the human alpha-Defensin, HD5
    • Lehrer RI, Jung G, Ruchala P, et al. (2009). Multivalent binding of carbohydrates by the human alpha-Defensin, HD5. J Immunol 183: 480-90
    • (2009) J Immunol , vol.183 , pp. 480-490
    • Lehrer, R.I.1    Jung, G.2    Ruchala, P.3
  • 122
    • 42049095483 scopus 로고    scopus 로고
    • Sulfated K5 Escherichia coli polysacchariDe Derivatives as wiDe-range inhibitors of genital types of human papillomavirus
    • Lembo D, Donalisio M, Rusnati M, et al. (2008). Sulfated K5 Escherichia coli polysacchariDe Derivatives as wiDe-range inhibitors of genital types of human papillomavirus. Antimicrob Agents Chemother 52:1374-81
    • (2008) Antimicrob Agents Chemother , vol.52 , pp. 1374-1381
    • Lembo, D.1    Donalisio, M.2    Rusnati, M.3
  • 123
    • 70349560033 scopus 로고    scopus 로고
    • Factors affecting protein-glycan specificity: Effect of spacers and incubation time
    • Lewallen DM, Siler D, Iyer SS. (2009). Factors affecting protein-glycan specificity: effect of spacers and incubation time. Chembiochem 10: 1486-9
    • (2009) Chembiochem , vol.10 , pp. 1486-1489
    • Lewallen, D.M.1    Siler, D.2    Iyer, S.S.3
  • 124
    • 34548494357 scopus 로고    scopus 로고
    • The K15 protein of Kaposis sarcoma-Associated herpesvirus recruits the endocytic regulator intersectin 2 through a selective SH3 domain interaction
    • Lim CS, Seet BT, Ingham RJ, et al. (2007) the K15 protein of Kaposis sarcoma-Associated herpesvirus recruits the endocytic regulator intersectin 2 through a selective SH3 domain interaction. Biochemistry 46:9874-85
    • (2007) Biochemistry , vol.46 , pp. 9874-9885
    • Lim, C.S.1    Seet, B.T.2    Ingham, R.J.3
  • 125
    • 0034214208 scopus 로고    scopus 로고
    • Characterization of the helix clamp motif of HIV-1 reverse transcriptase using MALDI-TOF MS and surface plasmon resonance
    • Lin S, Long S, Ramirez SM, et al. (2000). Characterization of the helix clamp motif of HIV-1 reverse transcriptase using MALDI-TOF MS and surface plasmon resonance. Anal Chem 72:2635-40
    • (2000) Anal Chem , vol.72 , pp. 2635-2640
    • Lin, S.1    Long, S.2    Ramirez, S.M.3
  • 127
    • 84867231810 scopus 로고    scopus 로고
    • Deciphering novel host-herpesvirus interactions by virion proteomics
    • Lippe R. (2012). Deciphering novel host-herpesvirus interactions by virion proteomics. Front Microbiol 3:181
    • (2012) Front Microbiol , vol.3 , pp. 181
    • Lippe, R.1
  • 128
    • 33947622234 scopus 로고    scopus 로고
    • Allele-And locus-specific recognition of class i MHC molecules by the immunomodulatory E3-19K protein from aDenovirus
    • Liu H, Fu J, Bouvier M. (2007). Allele-And locus-specific recognition of class I MHC molecules by the immunomodulatory E3-19K protein from aDenovirus. J Immunol 178:4567-75
    • (2007) J Immunol , vol.178 , pp. 4567-4575
    • Liu, H.1    Fu, J.2    Bouvier, M.3
  • 129
    • 65249185539 scopus 로고    scopus 로고
    • Structure of the HIV-1 gp41 membrane-proximal ectodomain region in a putative prefusion conformation
    • Liu J, Deng Y, Dey AK, et al. (2009a). Structure of the HIV-1 gp41 membrane-proximal ectodomain region in a putative prefusion conformation. Biochemistry 48:2915-23
    • (2009) Biochemistry , vol.48 , pp. 2915-2923
    • Liu, J.1    Deng, Y.2    Dey, A.K.3
  • 130
    • 60149089457 scopus 로고    scopus 로고
    • Determinants of stability for the E6 protein of papillomavirus type 16
    • Liu Y, Cherry JJ, Dineen JV, et al. (2009b). Determinants of stability for the E6 protein of papillomavirus type 16. J Mol Biol 386:1123-37
    • (2009) J Mol Biol , vol.386 , pp. 1123-1137
    • Liu, Y.1    Cherry, J.J.2    Dineen, J.V.3
  • 131
    • 33747366901 scopus 로고    scopus 로고
    • Analysis of the interaction between RGD-expressing aDenovirus type 5 fiber knob domains and alphavbeta3 integrin reveals distinct binding profiles and intracellular trafficking
    • Lord R, Parsons M, Kirby I, et al. (2006). Analysis of the interaction between RGD-expressing aDenovirus type 5 fiber knob domains and alphavbeta3 integrin reveals distinct binding profiles and intracellular trafficking. J Gen Virol 87:2497-505
    • (2006) J Gen Virol , vol.87 , pp. 2497-2505
    • Lord, R.1    Parsons, M.2    Kirby, I.3
  • 132
    • 0035937833 scopus 로고    scopus 로고
    • Kinetic analysis of aDenovirus fiber binding to its receptor reveals an avidity mechanism for trimeric receptor-ligand interactions
    • Lortat-Jacob H, Chouin E, Cusack S, Van Raaij MJ. (2001). Kinetic analysis of aDenovirus fiber binding to its receptor reveals an avidity mechanism for trimeric receptor-ligand interactions. J Biol Chem 276: 9009-15
    • (2001) J Biol Chem , vol.276 , pp. 9009-9015
    • Lortat-Jacob, H.1    Chouin, E.2    Cusack, S.3    Van Raaij, M.J.4
  • 133
    • 4344612246 scopus 로고    scopus 로고
    • Nucleocapsid protein of SARS coronavirus tightly binds to human cyclophilin A
    • Luo C, Luo H, Zheng S, et al. (2004a). Nucleocapsid protein of SARS coronavirus tightly binds to human cyclophilin A. Biochem Biophys Res Commun 321:557-65
    • (2004) Biochem Biophys Res Commun , vol.321 , pp. 557-565
    • Luo, C.1    Luo, H.2    Zheng, S.3
  • 134
    • 18044405160 scopus 로고    scopus 로고
    • The nucleocapsid protein of SARS coronavirus has a high binding affinity to the human cellular heterogeneous nuclear ribonucleoprotein A1
    • Luo H, Chen Q, Chen J, et al. (2005) the nucleocapsid protein of SARS coronavirus has a high binding affinity to the human cellular heterogeneous nuclear ribonucleoprotein A1. FEBS Lett 579:2623-8
    • (2005) FEBS Lett , vol.579 , pp. 2623-2628
    • Luo, H.1    Chen, Q.2    Chen, J.3
  • 135
    • 30944445006 scopus 로고    scopus 로고
    • Severe acute respiratory syndrome coronavirus membrane protein interacts with nucleocapsid protein mostly through their carboxyl termini by electrostatic attraction
    • Luo H, Wu D, Shen C, et al. (2006). Severe acute respiratory syndrome coronavirus membrane protein interacts with nucleocapsid protein mostly through their carboxyl termini by electrostatic attraction. Int J Biochem Cell Biol 38:589-99
    • (2006) Int J Biochem Cell Biol , vol.38 , pp. 589-599
    • Luo, H.1    Wu, D.2    Shen, C.3
  • 136
    • 6344222994 scopus 로고    scopus 로고
    • In vitro biochemical and thermodynamic characterization of nucleocapsid protein of SARS
    • Luo H, Ye F, Sun T, et al. (2004b). In vitro biochemical and thermodynamic characterization of nucleocapsid protein of SARS. Biophys Chem 112:15-25
    • (2004) Biophys Chem , vol.112 , pp. 15-25
    • Luo, H.1    Ye, F.2    Sun, T.3
  • 137
    • 1642494724 scopus 로고    scopus 로고
    • Fcgamma receptor-like activity of hepatitis C virus core protein
    • Maillard P, Lavergne JP, Siberil S, et al. (2004). Fcgamma receptor-like activity of hepatitis C virus core protein. J Biol Chem 279:2430-7
    • (2004) J Biol Chem , vol.279 , pp. 2430-2437
    • Maillard, P.1    Lavergne, J.P.2    Siberil, S.3
  • 138
    • 34047179944 scopus 로고    scopus 로고
    • Analysis of protein-DNA interactions using surface plasmon resonance
    • Majka J, Speck C. (2007). Analysis of protein-DNA interactions using surface plasmon resonance. Adv Biochem Eng Biotechnol 104:13-36
    • (2007) Adv Biochem Eng Biotechnol , vol.104 , pp. 13-36
    • Majka, J.1    Speck, C.2
  • 139
    • 1542327649 scopus 로고    scopus 로고
    • P-protein of Chandipura virus is an N-protein-specific chaperone that acts at the nucleation stage
    • Majumdar A, Bhattacharya R, Basak S, et al. (2004). P-protein of Chandipura virus is an N-protein-specific chaperone that acts at the nucleation stage. Biochemistry 43:2863-70
    • (2004) Biochemistry , vol.43 , pp. 2863-2870
    • Majumdar, A.1    Bhattacharya, R.2    Basak, S.3
  • 140
    • 52449110328 scopus 로고    scopus 로고
    • Detection of the active components of calf thymus nuclear proteins (TNP), histones that are binding with high affinity to HIV-1 envelope proteins and CD4 molecules
    • Mamikonyan G, Kiyatkin A, Movsesyan N, et al. (2008). Detection of the active components of calf thymus nuclear proteins (TNP), histones that are binding with high affinity to HIV-1 envelope proteins and CD4 molecules. Curr HIV Res 6:318-26
    • (2008) Curr HIV Res , vol.6 , pp. 318-326
    • Mamikonyan, G.1    Kiyatkin, A.2    Movsesyan, N.3
  • 141
    • 46349091910 scopus 로고    scopus 로고
    • Monitoring of influenza virus hemagglutinin in process samples using weak affinity ligands and surface plasmon resonance
    • ManDenius CF, Wang R, AlDen A, et al. (2008). Monitoring of influenza virus hemagglutinin in process samples using weak affinity ligands and surface plasmon resonance. Anal Chim Acta 623:66-75
    • (2008) Anal Chim Acta , vol.623 , pp. 66-75
    • Mandenius, C.F.1    Wang, R.2    Alden, A.3
  • 142
    • 0032566903 scopus 로고    scopus 로고
    • SH3-Domain binding function of HIV-1 Nef is required for association with a PAKrelated kinase
    • Manninen A, Hiipakka M, Vihinen M, et al. (1998). SH3-Domain binding function of HIV-1 Nef is required for association with a PAKrelated kinase. Virology 250:273-82
    • (1998) Virology , vol.250 , pp. 273-282
    • Manninen, A.1    Hiipakka, M.2    Vihinen, M.3
  • 143
    • 7244251651 scopus 로고    scopus 로고
    • The Kaposis sarcomaassociated herpesvirus complement control protein mimics human molecular mechanisms for inhibition of the complement system
    • Mark L, Lee WH, Spiller OB, et al. (2004) the Kaposis sarcomaassociated herpesvirus complement control protein mimics human molecular mechanisms for inhibition of the complement system. J Biol Chem 279:45093-101
    • (2004) J Biol Chem , vol.279 , pp. 45093-45101
    • Mark, L.1    Lee, W.H.2    Spiller, O.B.3
  • 144
    • 0035927442 scopus 로고    scopus 로고
    • Probing the interaction of Dengue virus envelope protein with heparin: Assessment of glycosaminoglycan-Derived inhibitors
    • Marks RM, Lu H, Sundaresan R, et al. (2001). Probing the interaction of Dengue virus envelope protein with heparin: assessment of glycosaminoglycan-Derived inhibitors. J Med Chem 44:2178-87
    • (2001) J Med Chem , vol.44 , pp. 2178-2187
    • Marks, R.M.1    Lu, H.2    Sundaresan, R.3
  • 145
    • 18744403973 scopus 로고    scopus 로고
    • Interaction with CD4 and antibodies to CD4-induced epitopes of the envelope gp120 from a microglial cell-Adapted human immunoDeficiency virus type 1 isolate
    • Martin-Garcia J, Cocklin S, Chaiken IM, Gonzalez-Scarano F. (2005). Interaction with CD4 and antibodies to CD4-induced epitopes of the envelope gp120 from a microglial cell-Adapted human immunoDeficiency virus type 1 isolate. J Virol 79:6703-13
    • (2005) J Virol , vol.79 , pp. 6703-6713
    • Martin-Garcia, J.1    Cocklin, S.2    Chaiken, I.M.3    Gonzalez-Scarano, F.4
  • 146
    • 13244266915 scopus 로고    scopus 로고
    • Myristoyl moiety of HIV Nef is involved in regulation of the interaction with calmodulin in vivo
    • Matsubara M, Jing T, Kawamura K, et al. (2005). Myristoyl moiety of HIV Nef is involved in regulation of the interaction with calmodulin in vivo. Protein Sci 14:494-503
    • (2005) Protein Sci , vol.14 , pp. 494-503
    • Matsubara, M.1    Jing, T.2    Kawamura, K.3
  • 147
    • 0034725699 scopus 로고    scopus 로고
    • Two distinct binding affinities of poliovirus for its cellular receptor
    • McDermott Jr BM, Rux AH, Eisenberg RJ, et al. (2000). Two distinct binding affinities of poliovirus for its cellular receptor. J Biol Chem 275:23089-96
    • (2000) J Biol Chem , vol.275 , pp. 23089-23096
    • McDermott, B.M.1    Rux, A.H.2    Eisenberg, R.J.3
  • 149
    • 33845999225 scopus 로고    scopus 로고
    • Variola virus IL-18 binding protein interacts with three human IL-18 residues that are part of a binding site for human IL-18 receptor alpha subunit
    • Meng X, Leman M, Xiang Y. (2007). Variola virus IL-18 binding protein interacts with three human IL-18 residues that are part of a binding site for human IL-18 receptor alpha subunit. Virology 358:211-20
    • (2007) Virology , vol.358 , pp. 211-220
    • Meng, X.1    Leman, M.2    Xiang, Y.3
  • 150
    • 79251518600 scopus 로고    scopus 로고
    • Genetic and structural basis for selection of a ubiquitous T cell receptor Deployed in Epstein-Barr virus infection
    • Miles JJ, Bulek AM, Cole DK, et al. (2010). Genetic and structural basis for selection of a ubiquitous T cell receptor Deployed in Epstein-Barr virus infection. PLoS Pathog 6:e1001198
    • (2010) PLoS Pathog , vol.6 , pp. e1001198
    • Miles, J.J.1    Bulek, A.M.2    Cole, D.K.3
  • 151
    • 79957892660 scopus 로고    scopus 로고
    • Glycosaminoglycans mediate retention of the poxvirus type i interferon binding protein at the cell surface to locally block interferon antiviral responses
    • Montanuy I, Alejo A, Alcami A. (2011). Glycosaminoglycans mediate retention of the poxvirus type I interferon binding protein at the cell surface to locally block interferon antiviral responses. FASEB J 26: 1960-71
    • (2011) FASEB J , vol.26 , pp. 1960-1971
    • Montanuy, I.1    Alejo, A.2    Alcami, A.3
  • 152
    • 84867594415 scopus 로고    scopus 로고
    • Exploitation of lipid components by viral and host proteins for hepatitis C virus infection
    • Moriishi K, Matsuura Y. (2012). Exploitation of lipid components by viral and host proteins for hepatitis C virus infection. Front Microbiol 3:54
    • (2012) Front Microbiol , vol.3 , pp. 54
    • Moriishi, K.1    Matsuura, Y.2
  • 153
    • 0033920212 scopus 로고    scopus 로고
    • Selective interactions of polyanions with basic surfaces on human immunoDeficiency virus type 1 gp120
    • Moulard M, Lortat-Jacob H, Mondor I, et al. (2000). Selective interactions of polyanions with basic surfaces on human immunoDeficiency virus type 1 gp120. J Virol 74:1948-60
    • (2000) J Virol , vol.74 , pp. 1948-1960
    • Moulard, M.1    Lortat-Jacob, H.2    Mondor, I.3
  • 154
    • 77649218586 scopus 로고    scopus 로고
    • Structure of the HCMV UL16-MICB complex elucidates select binding of a viral immunoevasin to diverse NKG2D ligands
    • Muller S, Zocher G, Steinle A, Stehle T. (2010). Structure of the HCMV UL16-MICB complex elucidates select binding of a viral immunoevasin to diverse NKG2D ligands. PLoS Pathog 6:e1000723
    • (2010) PLoS Pathog , vol.6 , pp. e1000723
    • Muller, S.1    Zocher, G.2    Steinle, A.3    Stehle, T.4
  • 155
    • 33947544434 scopus 로고    scopus 로고
    • An Alix fragment potently inhibits HIV-1 budding: Characterization of binding to retroviral YPXL late domains
    • Munshi UM, Kim J, Nagashima K, et al. (2007). An Alix fragment potently inhibits HIV-1 budding: characterization of binding to retroviral YPXL late domains. J Biol Chem 282:3847-55
    • (2007) J Biol Chem , vol.282 , pp. 3847-3855
    • Munshi, U.M.1    Kim, J.2    Nagashima, K.3
  • 157
    • 13744251677 scopus 로고    scopus 로고
    • Kinetics of HCV envelope proteins interaction with CD81 large extracellular loop
    • Nakajima H, Cocquerel L, Kiyokawa N, et al. (2005). Kinetics of HCV envelope proteins interaction with CD81 large extracellular loop. Biochem Biophys Res Commun 328:1091-100
    • (2005) Biochem Biophys Res Commun , vol.328 , pp. 1091-1100
    • Nakajima, H.1    Cocquerel, L.2    Kiyokawa, N.3
  • 158
    • 45549105566 scopus 로고    scopus 로고
    • Dynamic interaction of the measles virus hemagglutinin with its receptor signaling lymphocytic activation molecule (SLAM, CD150
    • Navaratnarajah CK, Vongpunsawad S, Oezguen N, et al. (2008). Dynamic interaction of the measles virus hemagglutinin with its receptor signaling lymphocytic activation molecule (SLAM, CD150). J Biol Chem 283:11763-71
    • (2008) J Biol Chem , vol.283 , pp. 11763-11771
    • Navaratnarajah, C.K.1    Vongpunsawad, S.2    Oezguen, N.3
  • 159
    • 84856298523 scopus 로고    scopus 로고
    • Biosensor-based approach to the iDentification of protein kinase ligands with dual-site moDes of action
    • Navratilova I, Macdonald G, Robinson C, et al. (2012). Biosensor-based approach to the iDentification of protein kinase ligands with dual-site moDes of action. J Biomol Screen 17:183-93
    • (2012) J Biomol Screen , vol.17 , pp. 183-193
    • Navratilova, I.1    Macdonald, G.2    Robinson, C.3
  • 160
    • 33947666565 scopus 로고    scopus 로고
    • Thermodynamic benchmark study using Biacore technology
    • Navratilova I, Papalia GA, Rich RL, et al. (2007) thermodynamic benchmark study using Biacore technology. Anal Biochem 364: 67-77
    • (2007) Anal Biochem , vol.364 , pp. 67-77
    • Navratilova, I.1    Papalia, G.A.2    Rich, R.L.3
  • 161
    • 15444376596 scopus 로고    scopus 로고
    • Solubilization, stabilization, and purification of chemokine receptors using biosensor technology
    • Navratilova I, Sodroski J, Myszka DG. (2005). Solubilization, stabilization, and purification of chemokine receptors using biosensor technology. Anal Biochem 339:271-81
    • (2005) Anal Biochem , vol.339 , pp. 271-281
    • Navratilova, I.1    Sodroski, J.2    Myszka, D.G.3
  • 162
    • 0348011822 scopus 로고    scopus 로고
    • Purification and protein interaction assays of the VP16C transcription activation domain
    • Nedialkov YA, Shooltz DD, Triezenberg SJ. (2003). Purification and protein interaction assays of the VP16C transcription activation domain. Methods Enzymol 370:522-35
    • (2003) Methods Enzymol , vol.370 , pp. 522-535
    • Nedialkov, Y.A.1    Shooltz, D.D.2    Triezenberg, S.J.3
  • 163
    • 1842635751 scopus 로고    scopus 로고
    • Quantitative assessment of in vitro interactions implicates TATA-binding protein as a target of the VP16C transcriptional activation region
    • Nedialkov YA, Triezenberg SJ. (2004). Quantitative assessment of in vitro interactions implicates TATA-binding protein as a target of the VP16C transcriptional activation region. Arch Biochem Biophys 425: 77-86
    • (2004) Arch Biochem Biophys , vol.425 , pp. 77-86
    • Nedialkov, Y.A.1    Triezenberg, S.J.2
  • 164
    • 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, 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 , pp. e7
    • Negrete, O.A.1    Wolf, M.C.2    Aguilar, H.C.3
  • 165
    • 84872367900 scopus 로고    scopus 로고
    • Comparative analysis of virus-host interactomes with a mammalian high-throughput protein complementation assay based on Gaussia princeps luciferase
    • Neveu G, Cassonnet P, Vidalain PO, et al. (2012). Comparative analysis of virus-host interactomes with a mammalian high-throughput protein complementation assay based on Gaussia princeps luciferase. Methods 58:349-59
    • (2012) Methods , vol.58 , pp. 349-359
    • Neveu, G.1    Cassonnet, P.2    Vidalain, P.O.3
  • 166
    • 0034845560 scopus 로고    scopus 로고
    • The vaccinia virus A41L protein is a soluble 30 kDa glycoprotein that affects virus virulence
    • Ng A, Tscharke DC, Reading PC, Smith GL. (2001) the vaccinia virus A41L protein is a soluble 30 kDa glycoprotein that affects virus virulence. J Gen Virol 82:2095-105
    • (2001) J Gen Virol , vol.82 , pp. 2095-2105
    • Ng, A.1    Tscharke, D.C.2    Reading, P.C.3    Smith, G.L.4
  • 167
    • 84860526518 scopus 로고    scopus 로고
    • Influenza polymerase activity correlates with the strength of interaction between nucleoprotein and PB2 through the host-specific residue K/E627
    • Ng AK, Chan WH, Choi ST, et al. (2012). Influenza polymerase activity correlates with the strength of interaction between nucleoprotein and PB2 through the host-specific residue K/E627. PLoS One 7: e36415
    • (2012) PLoS One , vol.7 , pp. e36415
    • Ng, A.K.1    Chan, W.H.2    Choi, S.T.3
  • 168
    • 54049146687 scopus 로고    scopus 로고
    • Structure of the influenza virus A H5N1 nucleoprotein: Implications for RNA binding, oligomerization, and vaccine Design
    • Ng AK, Zhang H, Tan K, et al. (2008). Structure of the influenza virus A H5N1 nucleoprotein: implications for RNA binding, oligomerization, and vaccine Design. FASEB J 22:3638-47
    • (2008) FASEB J , vol.22 , pp. 3638-3647
    • Ng, A.K.1    Zhang, H.2    Tan, K.3
  • 169
    • 78651242668 scopus 로고    scopus 로고
    • The GD1a glycan is a cellular receptor for aDenoviruses causing epiDemic keratoconjunctivitis
    • Nilsson EC, Storm RJ, Bauer J, et al. (2010) the GD1a glycan is a cellular receptor for aDenoviruses causing epiDemic keratoconjunctivitis. Nat Med 17:105-9
    • (2010) Nat Med , vol.17 , pp. 105-109
    • Nilsson, E.C.1    Storm, R.J.2    Bauer, J.3
  • 170
    • 34547111812 scopus 로고    scopus 로고
    • Subcellular localization and physiological significance of intracellular mannan-binding protein
    • Nonaka M, Ma BY, Ohtani M, et al. (2007). Subcellular localization and physiological significance of intracellular mannan-binding protein. J Biol Chem 282:17908-20
    • (2007) J Biol Chem , vol.282 , pp. 17908-17920
    • Nonaka, M.1    Ma, B.Y.2    Ohtani, M.3
  • 171
    • 67649364152 scopus 로고    scopus 로고
    • Mechanisms of receptor/coreceptormediated entry of enveloped viruses
    • Nowak SA, Chou T. (2009). Mechanisms of receptor/coreceptormediated entry of enveloped viruses. Biophys J 96:2624-36
    • (2009) Biophys J , vol.96 , pp. 2624-2636
    • Nowak, S.A.1    Chou, T.2
  • 172
    • 77649106809 scopus 로고    scopus 로고
    • 1a/1b subtype profiling of nonnucleosiDe polymerase inhibitors of hepatitis C virus
    • Nyanguile O, Devogelaere B, Vijgen L, et al. (2010). 1a/1b subtype profiling of nonnucleosiDe polymerase inhibitors of hepatitis C virus. J Virol 84:2923-34
    • (2010) J Virol , vol.84 , pp. 2923-2934
    • Nyanguile, O.1    Devogelaere, B.2    Vijgen, L.3
  • 173
    • 0034049693 scopus 로고    scopus 로고
    • Thermodynamic and kinetic analyses for unDerstanding sequence-specific DNA recognition
    • Oda M, Nakamura H. (2000) thermodynamic and kinetic analyses for unDerstanding sequence-specific DNA recognition. Genes Cells 5: 319-26
    • (2000) Genes Cells , vol.5 , pp. 319-326
    • Oda, M.1    Nakamura, H.2
  • 174
    • 80051922422 scopus 로고    scopus 로고
    • Poxvirus A46 protein binds to TIR domain-containing Mal/TIRAP via an alpha-helical sub-domain
    • Oda S, Franklin E, Khan AR. (2011). Poxvirus A46 protein binds to TIR domain-containing Mal/TIRAP via an alpha-helical sub-domain. Mol Immunol 48:2144-50
    • (2011) Mol Immunol , vol.48 , pp. 2144-2150
    • Oda, S.1    Franklin, E.2    Khan, A.R.3
  • 175
    • 41149173078 scopus 로고    scopus 로고
    • A single-Amino-Acid mutation in hepatitis C virus NS5A disrupting FKBP8 interaction impairs viral replication
    • Okamoto T, Omori H, Kaname Y, et al. (2008). A single-Amino-Acid mutation in hepatitis C virus NS5A disrupting FKBP8 interaction impairs viral replication. J Virol 82:3480-9
    • (2008) J Virol , vol.82 , pp. 3480-3489
    • Okamoto, T.1    Omori, H.2    Kaname, Y.3
  • 176
    • 0037176876 scopus 로고    scopus 로고
    • Immobilized small Deoxyribozyme to distinguish RNA secondary structures
    • Okumoto Y, Ohmichi T, Sugimoto N. (2002). Immobilized small Deoxyribozyme to distinguish RNA secondary structures. Biochemistry 41:2769-73
    • (2002) Biochemistry , vol.41 , pp. 2769-2773
    • Okumoto, Y.1    Ohmichi, T.2    Sugimoto, N.3
  • 177
    • 79953248134 scopus 로고    scopus 로고
    • The critical protein interactions and structures that elicit growth Deregulation in cancer and viral replication Wiley
    • Ou HD, May AP, OShea CC. (2010) the critical protein interactions and structures that elicit growth Deregulation in cancer and viral replication. Wiley Interdiscip Rev Syst Biol Med 3:48-73
    • (2010) Interdiscip Rev Syst Biol Med , vol.3 , pp. 48-73
    • Ou, H.D.1    May, A.P.2    Oshea, C.C.3
  • 178
    • 9344221638 scopus 로고    scopus 로고
    • RC-101, a retrocyclin-1 analogue with enhanced activity against primary HIV type 1 isolates
    • Owen SM, Rudolph DL, Wang W, et al. (2004). RC-101, a retrocyclin-1 analogue with enhanced activity against primary HIV type 1 isolates. AIDS Res Hum Retroviruses 20:1157-65
    • (2004) AIDS Res Hum Retroviruses , vol.20 , pp. 1157-1165
    • Owen, S.M.1    Rudolph, D.L.2    Wang, W.3
  • 179
    • 1842329730 scopus 로고    scopus 로고
    • Basal transcription factors TBP and TFIIB and the viral coactivator E1A 13S bind with distinct affinities and kinetics to the transactivation domain of NF-kappaB p65
    • Paal K, Baeuerle PA, Schmitz ML. (1997). Basal transcription factors TBP and TFIIB and the viral coactivator E1A 13S bind with distinct affinities and kinetics to the transactivation domain of NF-kappaB p65. Nucleic Acids Res 25:1050-5
    • (1997) Nucleic Acids Res , vol.25 , pp. 1050-1055
    • Paal, K.1    Baeuerle, P.A.2    Schmitz, M.L.3
  • 180
    • 79251559368 scopus 로고    scopus 로고
    • Construction and characterization of insect cell-Derived influenza VLP: Cell binding, fusion, and EGFP incorporation
    • Pan YS, Wei HJ, Chang CC, et al. (2010). Construction and characterization of insect cell-Derived influenza VLP: cell binding, fusion, and EGFP incorporation. J Biomed Biotechnol 2010:506363
    • (2010) J Biomed Biotechnol , vol.2010 , pp. 506363
    • Pan, Y.S.1    Wei, H.J.2    Chang, C.C.3
  • 181
    • 0031961907 scopus 로고    scopus 로고
    • Direct measurement of the substrate preference of uracil-DNA glycosylase
    • Panayotou G, Brown T, Barlow T, et al. (1998). Direct measurement of the substrate preference of uracil-DNA glycosylase. J Biol Chem 273: 45-50
    • (1998) J Biol Chem , vol.273 , pp. 45-50
    • Panayotou, G.1    Brown, T.2    Barlow, T.3
  • 182
    • 18844443671 scopus 로고    scopus 로고
    • The binding affinity of double-stranDed RNA motifs to HIV-1 Tat protein affects transactivation and the neutralizing capacity of anti-Tat antibodies elicited after intranasal immunization
    • Partidos CD, Hoebeke J, Moreau E, et al. (2005) the binding affinity of double-stranDed RNA motifs to HIV-1 Tat protein affects transactivation and the neutralizing capacity of anti-Tat antibodies elicited after intranasal immunization. Eur J Immunol 35:1521-9
    • (2005) Eur J Immunol , vol.35 , pp. 1521-1529
    • Partidos, C.D.1    Hoebeke, J.2    Moreau, E.3
  • 183
    • 27244449002 scopus 로고    scopus 로고
    • Concanavalin A binding to HIV envelope protein is less sensitive to mutations in glycosylation sites than monoclonal antibody 2G12
    • Pashov A, MacLeod S, Saha R, et al. (2005). Concanavalin A binding to HIV envelope protein is less sensitive to mutations in glycosylation sites than monoclonal antibody 2G12. Glycobiology 15:994-1001
    • (2005) Glycobiology , vol.15 , pp. 994-1001
    • Pashov, A.1    Macleod, S.2    Saha, R.3
  • 184
    • 12844264099 scopus 로고    scopus 로고
    • Hepatitis A virus proteinase 3C binding to viral RNA: Correlation with substrate binding and enzyme dimerization
    • Peters H, Kusov YY, Meyer S, et al. (2005). Hepatitis A virus proteinase 3C binding to viral RNA: correlation with substrate binding and enzyme dimerization. Biochem J 385:363-70
    • (2005) Biochem J , vol.385 , pp. 363-370
    • Peters, H.1    Kusov, Y.Y.2    Meyer, S.3
  • 185
    • 33646167688 scopus 로고    scopus 로고
    • Structural and functional insights into the interaction of echoviruses and Decayaccelerating factor
    • Pettigrew DM, Williams DT, Kerrigan D, et al. (2006). Structural and functional insights into the interaction of echoviruses and Decayaccelerating factor. J Biol Chem 281:5169-77
    • (2006) J Biol Chem , vol.281 , pp. 5169-5177
    • Pettigrew, D.M.1    Williams, D.T.2    Kerrigan, D.3
  • 186
    • 78650639889 scopus 로고    scopus 로고
    • The Kaposis sarcomaassociated herpes virus G protein-coupled receptor contains an immunoreceptor tyrosine-based inhibitory motif that activates Shp2
    • Philpott N, Bakken T, Pennell C, et al. (2011) the Kaposis sarcomaassociated herpes virus G protein-coupled receptor contains an immunoreceptor tyrosine-based inhibitory motif that activates Shp2,. J Virol 85:1140-4
    • (2011) J Virol , vol.85 , pp. 1140-1144
    • Philpott, N.1    Bakken, T.2    Pennell, C.3
  • 187
    • 38049088409 scopus 로고    scopus 로고
    • Characterization of DNA-binding activity of Z alpha domains from poxviruses and the importance of the beta-wing regions in converting B-DNA to Z-DNA
    • Quyen DV, Ha SC, Lowenhaupt K, et al. (2007). Characterization of DNA-binding activity of Z alpha domains from poxviruses and the importance of the beta-wing regions in converting B-DNA to Z-DNA. Nucleic Acids Res 35:7714-20
    • (2007) Nucleic Acids Res , vol.35 , pp. 7714-7720
    • Quyen, D.V.1    Ha, S.C.2    Lowenhaupt, K.3
  • 188
    • 2642580665 scopus 로고    scopus 로고
    • Target specificity of human immunoDeficiency virus type 1 NCp7 requires an intact conformation of its CCHC N-terminal zinc finger
    • Ramboarina S, Druillennec S, Morellet N, et al. (2004). Target specificity of human immunoDeficiency virus type 1 NCp7 requires an intact conformation of its CCHC N-terminal zinc finger. J Virol 78: 6682-7
    • (2004) J Virol , vol.78 , pp. 6682-6687
    • Ramboarina, S.1    Druillennec, S.2    Morellet, N.3
  • 189
    • 34247550827 scopus 로고    scopus 로고
    • MoDe of inhibition of HIV-1 Integrase by a C-terminal domain-specific monoclonal antibody
    • Ramcharan J, Colleluori DM, Merkel G, et al. (2006). MoDe of inhibition of HIV-1 Integrase by a C-terminal domain-specific monoclonal antibody. Retrovirology 3:34
    • (2006) Retrovirology , vol.3 , pp. 34
    • Ramcharan, J.1    Colleluori, D.M.2    Merkel, G.3
  • 190
    • 67649400809 scopus 로고    scopus 로고
    • Initiation of hepatitis C virus infection requires the dynamic microtubule network: Role of the viral nucleocapsid protein
    • RoohVand F, Maillard P, Lavergne JP, et al. (2009). Initiation of hepatitis C virus infection requires the dynamic microtubule network: role of the viral nucleocapsid protein. J Biol Chem 284:13778-91
    • (2009) J Biol Chem , vol.284 , pp. 13778-13791
    • Roohvand, F.1    Maillard, P.2    Lavergne, J.P.3
  • 191
    • 70349634195 scopus 로고    scopus 로고
    • Exploiting Surface Plasmon Resonance (SPR) technology for the iDentification of fibroblast growth factor-2 (FGF2) antagonists endowed with antiangiogenic activity
    • Rusnati M, Bugatti A, Mitola S, et al. (2009). Exploiting Surface Plasmon Resonance (SPR) technology for the iDentification of fibroblast growth factor-2 (FGF2) antagonists endowed with antiangiogenic activity. Sensors (Basel) 9:6471-503
    • (2009) Sensors (Basel , vol.9 , pp. 6471-6503
    • Rusnati, M.1    Bugatti, A.2    Mitola, S.3
  • 192
    • 0036323246 scopus 로고    scopus 로고
    • HIV-1 Tat protein: A target for the Development of anti-AIDS therapies
    • Rusnati M, Presta M. (2002). HIV-1 Tat protein: a target for the Development of anti-AIDS therapies. Drug Fut 27:481-493
    • (2002) Drug Fut , vol.27 , pp. 481-493
    • Rusnati, M.1    Presta, M.2
  • 193
    • 0035933826 scopus 로고    scopus 로고
    • Pentosan polysulfate as an inhibitor of extracellular HIV-1 Tat
    • Rusnati M, Urbinati C, Caputo A, et al. (2001). Pentosan polysulfate as an inhibitor of extracellular HIV-1 Tat. J Biol Chem 276: 22420-5
    • (2001) J Biol Chem , vol.276 , pp. 22420-22425
    • Rusnati, M.1    Urbinati, C.2    Caputo, A.3
  • 194
    • 0036317974 scopus 로고    scopus 로고
    • Rapid progression to simian AIDS can be accompanied by selection of CD4-inDepenDent gp120 variants with impaired ability to bind CD4
    • Ryzhova E, Whitbeck JC, Canziani G, et al. (2002). Rapid progression to simian AIDS can be accompanied by selection of CD4-inDepenDent gp120 variants with impaired ability to bind CD4. J Virol 76:7903-9
    • (2002) J Virol , vol.76 , pp. 7903-7909
    • Ryzhova, E.1    Whitbeck, J.C.2    Canziani, G.3
  • 195
    • 33745944661 scopus 로고    scopus 로고
    • Development and characterization of ten monoclonal anti-Vpr antibodies
    • Sabbah EN, Delaunay T, Varin A, et al. (2006). Development and characterization of ten monoclonal anti-Vpr antibodies. AIDS Res Hum Retroviruses 22:630-9
    • (2006) AIDS Res Hum Retroviruses , vol.22 , pp. 630-639
    • Sabbah, E.N.1    Delaunay, T.2    Varin, A.3
  • 196
    • 0032883325 scopus 로고    scopus 로고
    • Hepatitis C virus core protein binds to apolipoprotein AII and its secretion is modulated by fibrates
    • Sabile A, Perlemuter G, Bono F, et al. (1999). Hepatitis C virus core protein binds to apolipoprotein AII and its secretion is modulated by fibrates. Hepatology 30:1064-76
    • (1999) Hepatology , vol.30 , pp. 1064-1076
    • Sabile, A.1    Perlemuter, G.2    Bono, F.3
  • 197
    • 43749114947 scopus 로고    scopus 로고
    • Podophyllotoxin directly binds a hinge domain in E2 of HPV and inhibits an E2/E7 interaction in vitro
    • Saitoh T, Kuramochi K, Imai T, et al. (2008). Podophyllotoxin directly binds a hinge domain in E2 of HPV and inhibits an E2/E7 interaction in vitro. Bioorg Med Chem 16:5815-25
    • (2008) Bioorg Med Chem , vol.16 , pp. 5815-5825
    • Saitoh, T.1    Kuramochi, K.2    Imai, T.3
  • 198
    • 0037200110 scopus 로고    scopus 로고
    • Distinct kinetics for binding of the CD46 and SLAM receptors to overlapping sites in the measles virus hemagglutinin protein
    • Santiago C, Bjorling E, Stehle T, Casasnovas JM. (2002). Distinct kinetics for binding of the CD46 and SLAM receptors to overlapping sites in the measles virus hemagglutinin protein. J Biol Chem 277: 32294-301
    • (2002) J Biol Chem , vol.277 , pp. 32294-32301
    • Santiago, C.1    Bjorling, E.2    Stehle, T.3    Casasnovas, J.M.4
  • 199
    • 0035423431 scopus 로고    scopus 로고
    • Kinetic analysis of the interactions of complement receptor 2 (CR2, CD21) with its ligands C3d, iC3b, and the EBV glycoprotein gp350/220
    • Sarrias MR, Franchini S, Canziani G, et al. (2001). Kinetic analysis of the interactions of complement receptor 2 (CR2, CD21) with its ligands C3d, iC3b, and the EBV glycoprotein gp350/220. J Immunol 167:1490-9
    • (2001) J Immunol , vol.167 , pp. 1490-1499
    • Sarrias, M.R.1    Franchini, S.2    Canziani, G.3
  • 200
    • 65449159794 scopus 로고    scopus 로고
    • Binding site Detection and druggability inDex from first principles
    • Seco J, Luque FJ, Barril X. (2009). Binding site Detection and druggability inDex from first principles. J Med Chem 52:2363-71
    • (2009) J Med Chem , vol.52 , pp. 2363-2371
    • Seco, J.1    Luque, F.J.2    Barril, X.3
  • 201
    • 0035839571 scopus 로고    scopus 로고
    • Glycosaminoglycan binding properties of the myxoma virus CC-chemokine inhibitor, M-T1
    • Seet BT, Barrett J, Robichaud J, et al. (2001a). Glycosaminoglycan binding properties of the myxoma virus CC-chemokine inhibitor, M-T1. J Biol Chem 276:30504-13
    • (2001) J Biol Chem , vol.276 , pp. 30504-30513
    • Seet, B.T.1    Barrett, J.2    Robichaud, J.3
  • 202
    • 0035979206 scopus 로고    scopus 로고
    • Molecular Determinants for CC-chemokine recognition by a poxvirus CC-chemokine inhibitor
    • Seet BT, Singh R, Paavola C, et al. (2001b). Molecular Determinants for CC-chemokine recognition by a poxvirus CC-chemokine inhibitor. Proc Natl Acad Sci U S A 98:9008-13
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 9008-9013
    • Seet, B.T.1    Singh, R.2    Paavola, C.3
  • 203
    • 33845946967 scopus 로고    scopus 로고
    • Structural and mutational analysis of human Ad37 and canine aDenovirus 2 fiber heads in complex with the D1 domain of coxsackie and aDenovirus receptor
    • Seiradake E, Lortat-Jacob H, Billet O, et al. (2006). Structural and mutational analysis of human Ad37 and canine aDenovirus 2 fiber heads in complex with the D1 domain of coxsackie and aDenovirus receptor. J Biol Chem 281:33704-16
    • (2006) J Biol Chem , vol.281 , pp. 33704-33716
    • Seiradake, E.1    Lortat-Jacob, H.2    Billet, O.3
  • 204
    • 48249150347 scopus 로고    scopus 로고
    • Integrins alpha1beta1 and alpha2beta1 are receptors for the rotavirus enterotoxin
    • Seo NS, Zeng CQ, Hyser JM, et al. (2008). Integrins alpha1beta1 and alpha2beta1 are receptors for the rotavirus enterotoxin. Proc Natl Acad Sci U S A 105:8811-18
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 8811-8818
    • Seo, N.S.1    Zeng, C.Q.2    Hyser, J.M.3
  • 205
    • 40149102826 scopus 로고    scopus 로고
    • Hepatitis C virus NS5A protein binds the SH3 domain of the Fyn tyrosine kinase with high affinity: Mutagenic analysis of residues within the SH3 domain that contribute to the interaction
    • Shelton H, Harris M. (2008). Hepatitis C virus NS5A protein binds the SH3 domain of the Fyn tyrosine kinase with high affinity: mutagenic analysis of residues within the SH3 domain that contribute to the interaction. Virol J 5:24
    • (2008) Virol J , vol.5 , pp. 24
    • Shelton, H.1    Harris, M.2
  • 206
    • 0029919176 scopus 로고    scopus 로고
    • IDentification and characterization of an S-ADenosyl-L-methionine: Delta 24-sterol-C-methyltransferase cDNA from soybean
    • Shi J, Gonzales RA, Bhattacharyya MK. (1996). IDentification and characterization of an S-ADenosyl-L-methionine: Delta 24-sterol-C-methyltransferase cDNA from soybean. J Biol Chem 271:9384-9
    • (1996) J Biol Chem , vol.271 , pp. 9384-9389
    • Shi, J.1    Gonzales, R.A.2    Bhattacharyya, M.K.3
  • 207
    • 73649099861 scopus 로고    scopus 로고
    • A turn-like structure KKPE segment mediates the specific binding of viral protein A27 to heparin and heparan sulfate on cell surfaces
    • Shih PC, Yang MS, Lin SC, et al. (2009). A turn-like structure KKPE segment mediates the specific binding of viral protein A27 to heparin and heparan sulfate on cell surfaces. J Biol Chem 284: 36535-46
    • (2009) J Biol Chem , vol.284 , pp. 36535-36546
    • Shih, P.C.1    Yang, M.S.2    Lin, S.C.3
  • 208
    • 0037134868 scopus 로고    scopus 로고
    • Chemically induced hairpin formation in DNA monolayers
    • Smith EA, Kyo M, Kumasawa H, et al. (2002). Chemically induced hairpin formation in DNA monolayers. J Am Chem Soc 124: 6810-11
    • (2002) J Am Chem Soc , vol.124 , pp. 6810-6811
    • Smith, E.A.1    Kyo, M.2    Kumasawa, H.3
  • 209
    • 0035346801 scopus 로고    scopus 로고
    • Virokines: Novel immunomodulatory agents
    • Smith SA, Kotwal GJ. (2001). Virokines: novel immunomodulatory agents. Expert Opin Biol Ther 1:343-57
    • (2001) Expert Opin Biol Ther , vol.1 , pp. 343-357
    • Smith, S.A.1    Kotwal, G.J.2
  • 210
    • 0141907308 scopus 로고    scopus 로고
    • Mapping of regions within the vaccinia virus complement control protein involved in dose-DepenDent binding to key complement components and heparin using surface plasmon resonance
    • Smith SA, Sreenivasan R, Krishnasamy G, et al. (2003). Mapping of regions within the vaccinia virus complement control protein involved in dose-DepenDent binding to key complement components and heparin using surface plasmon resonance. Biochim Biophys Acta 1650:30-9
    • (2003) Biochim Biophys Acta , vol.1650 , pp. 30-39
    • Smith, S.A.1    Sreenivasan, R.2    Krishnasamy, G.3
  • 211
    • 84870711846 scopus 로고    scopus 로고
    • HIV-1 p6-A structured to flexible multifunctional membrane-interacting protein
    • Solbak SM, Reksten TR, Hahn F, et al. (2012). HIV-1 p6-A structured to flexible multifunctional membrane-interacting protein. Biochim Biophys Acta 1828:816-23
    • (2012) Biochim Biophys Acta , vol.1828 , pp. 816-823
    • Solbak, S.M.1    Reksten, T.R.2    Hahn, F.3
  • 212
    • 77957259243 scopus 로고    scopus 로고
    • The intriguing cyclophilin A-HIV-1 Vpr interaction: Prolyl cis/trans isomerisation catalysis and specific binding
    • Solbak SM, Reksten TR, Wray V, et al. (2010) the intriguing cyclophilin A-HIV-1 Vpr interaction: prolyl cis/trans isomerisation catalysis and specific binding. BMC Struct Biol 10:31
    • (2010) BMC Struct Biol , vol.10 , pp. 31
    • Solbak, S.M.1    Reksten, T.R.2    Wray, V.3
  • 213
    • 83655181384 scopus 로고    scopus 로고
    • The hostpathogen interaction of human cyclophilin A and HIV-1 Vpr requires specific N-terminal and novel C-terminal domains
    • Solbak SM, Wray V, Horvli O, et al. (2011) the hostpathogen interaction of human cyclophilin A and HIV-1 Vpr requires specific N-terminal and novel C-terminal domains. BMC Struct Biol 11:49
    • (2011) BMC Struct Biol , vol.11 , pp. 49
    • Solbak, S.M.1    Wray, V.2    Horvli, O.3
  • 214
    • 75149162038 scopus 로고    scopus 로고
    • Formal reasoning on qualitative moDels of coinfection of HIV and Tuberculosis and HAART therapy
    • Sorathiya A, Bracciali A, Lio P. (2010). Formal reasoning on qualitative moDels of coinfection of HIV and Tuberculosis and HAART therapy. BMC Bioinformatics 11:S67
    • (2010) BMC Bioinformatics , vol.11 , pp. S67
    • Sorathiya, A.1    Bracciali, A.2    Lio, P.3
  • 215
    • 33750083654 scopus 로고    scopus 로고
    • Characterisation of the RNA binding properties of the coronavirus infectious bronchitis virus nucleocapsid protein amino-terminal region
    • Spencer KA, Hiscox JA. (2006). Characterisation of the RNA binding properties of the coronavirus infectious bronchitis virus nucleocapsid protein amino-terminal region. FEBS Lett 580:5993-8
    • (2006) FEBS Lett , vol.580 , pp. 5993-5998
    • Spencer, K.A.1    Hiscox, J.A.2
  • 216
    • 0037646403 scopus 로고    scopus 로고
    • Functional activity of the complement regulator encoDed by Kaposis sarcoma-Associated herpesvirus
    • Spiller OB, Blackbourn DJ, Mark L, et al. (2003). Functional activity of the complement regulator encoDed by Kaposis sarcoma-Associated herpesvirus. J Biol Chem 278:9283-9
    • (2003) J Biol Chem , vol.278 , pp. 9283-9289
    • Spiller, O.B.1    Blackbourn, D.J.2    Mark, L.3
  • 217
    • 41149107316 scopus 로고    scopus 로고
    • The human cytomegalovirus Fc receptor gp68 binds the Fc CH2-CH3 interface of immunoglobulin G
    • Sprague ER, Reinhard H, Cheung EJ, et al. (2008) the human cytomegalovirus Fc receptor gp68 binds the Fc CH2-CH3 interface of immunoglobulin G. J Virol 82:3490-9
    • (2008) J Virol , vol.82 , pp. 3490-3499
    • Sprague, E.R.1    Reinhard, H.2    Cheung, E.J.3
  • 218
    • 48849094143 scopus 로고    scopus 로고
    • Interactions of human cytomegalovirus proteins with the nuclear transport machinery
    • Stamminger T. (2008). Interactions of human cytomegalovirus proteins with the nuclear transport machinery. Curr Top Microbiol Immunol 325:167-85
    • (2008) Curr Top Microbiol Immunol , vol.325 , pp. 167-185
    • Stamminger, T.1
  • 219
    • 36049000440 scopus 로고    scopus 로고
    • Measuring the binding stoichiometry of HIV-1 Gag to very-low-Density oligonucleotiDe surfaces using surface plasmon resonance spectroscopy
    • Stephen AG, Datta SA, Worthy KM, et al. (2007). Measuring the binding stoichiometry of HIV-1 Gag to very-low-Density oligonucleotiDe surfaces using surface plasmon resonance spectroscopy. J Biomol Tech 18:259-66
    • (2007) J Biomol Tech , vol.18 , pp. 259-266
    • Stephen, A.G.1    Datta, S.A.2    Worthy, K.M.3
  • 220
    • 50249084524 scopus 로고    scopus 로고
    • Combinatorial optimization of a CD4-mimetic miniprotein and cocrystal structures with HIV-1 gp120 envelope glycoprotein
    • Stricher F, Huang CC, Descours A, et al. (2008). Combinatorial optimization of a CD4-mimetic miniprotein and cocrystal structures with HIV-1 gp120 envelope glycoprotein. J Mol Biol 382:510-24
    • (2008) J Mol Biol , vol.382 , pp. 510-524
    • Stricher, F.1    Huang, C.C.2    Descours, A.3
  • 221
    • 84855774532 scopus 로고    scopus 로고
    • Monitoring influenza hemagglutinin and glycan interactions using surface plasmon resonance
    • Suenaga E, Mizuno H, Penmetcha KK. (2012). Monitoring influenza hemagglutinin and glycan interactions using surface plasmon resonance. Biosens Bioelectron 32:195-201
    • (2012) Biosens Bioelectron , vol.32 , pp. 195-201
    • Suenaga, E.1    Mizuno, H.2    Penmetcha, K.K.3
  • 222
    • 37849000389 scopus 로고    scopus 로고
    • HIV-1 broadly neutralizing antibody extracts its epitope from a kinked gp41 ectodomain region on the viral membrane
    • Sun ZY, Oh KJ, Kim M, et al. (2008). HIV-1 broadly neutralizing antibody extracts its epitope from a kinked gp41 ectodomain region on the viral membrane. Immunity 28:52-63
    • (2008) Immunity , vol.28 , pp. 52-63
    • Sun, Z.Y.1    Oh, K.J.2    Kim, M.3
  • 223
    • 0036330262 scopus 로고    scopus 로고
    • A study of the vaccinia virus interferon-gamma receptor and its contribution to virus virulence
    • Symons JA, Tscharke DC, Price N, Smith GL. (2002). A study of the vaccinia virus interferon-gamma receptor and its contribution to virus virulence. J Gen Virol 83:1953-64
    • (2002) J Gen Virol , vol.83 , pp. 1953-1964
    • Symons, J.A.1    Tscharke, D.C.2    Price, N.3    Smith, G.L.4
  • 224
    • 0347989408 scopus 로고    scopus 로고
    • Topoisomerase i dissociates human immunoDeficiency virus type 1 reverse transcriptase from genomic RNAs
    • Takahashi H, Sawa H, Hasegawa H, et al. (2004). Topoisomerase I dissociates human immunoDeficiency virus type 1 reverse transcriptase from genomic RNAs. Biochem Biophys Res Commun 313: 1073-8
    • (2004) Biochem Biophys Res Commun , vol.313 , pp. 1073-1078
    • Takahashi, H.1    Sawa, H.2    Hasegawa, H.3
  • 225
    • 81155131430 scopus 로고    scopus 로고
    • Nuclear exportin receptor CAS regulates the NPI-1-mediated nuclear import of HIV-1 Vpr
    • Takeda E, Murakami T, Matsuda G, et al. (2011). Nuclear exportin receptor CAS regulates the NPI-1-mediated nuclear import of HIV-1 Vpr. PLoS One 6:e27815
    • (2011) PLoS One , vol.6 , pp. e27815
    • Takeda, E.1    Murakami, T.2    Matsuda, G.3
  • 226
    • 0029880005 scopus 로고    scopus 로고
    • A surface plasmon resonance assay for the binding of influenza virus hemagglutinin to its sialic acid receptor
    • Takemoto DK, Skehel JJ, Wiley DC. (1996). A surface plasmon resonance assay for the binding of influenza virus hemagglutinin to its sialic acid receptor. Virology 217:452-8
    • (1996) Virology , vol.217 , pp. 452-458
    • Takemoto, D.K.1    Skehel, J.J.2    Wiley, D.C.3
  • 227
    • 0034712884 scopus 로고    scopus 로고
    • Selective binding of hepatitis C virus core protein to synthetic oligonucleotiDes corresponding to the 5 untranslated region of the viral genome
    • Tanaka Y, Shimoike T, Ishii K, et al. (2000). Selective binding of hepatitis C virus core protein to synthetic oligonucleotiDes corresponding to the 5 untranslated region of the viral genome. Virology 270:229-36
    • (2000) Virology , vol.270 , pp. 229-236
    • Tanaka, Y.1    Shimoike, T.2    Ishii, K.3
  • 228
    • 84857037520 scopus 로고    scopus 로고
    • Oligomerization paths of the nucleoprotein of influenza A virus
    • Tarus B, Bakowiez O, Chenavas S, et al. (2012). Oligomerization paths of the nucleoprotein of influenza A virus. Biochimie 94:776-85
    • (2012) Biochimie , vol.94 , pp. 776-785
    • Tarus, B.1    Bakowiez, O.2    Chenavas, S.3
  • 229
    • 78049507903 scopus 로고    scopus 로고
    • Glycosphingolipids as receptors for non-enveloped viruses
    • Taube S, Jiang M, Wobus CE. (2010). Glycosphingolipids as receptors for non-enveloped viruses. Viruses 2:1011-49
    • (2010) Viruses , vol.2 , pp. 1011-1049
    • Taube, S.1    Jiang, M.2    Wobus, C.E.3
  • 230
    • 79956141898 scopus 로고    scopus 로고
    • Subversion of the actin cytoskeleton during viral infection
    • Taylor MP, Koyuncu OO, Enquist LW. (2011). Subversion of the actin cytoskeleton during viral infection. Nat Rev Microbiol 9:427-39
    • (2011) Nat Rev Microbiol , vol.9 , pp. 427-439
    • Taylor, M.P.1    Koyuncu, O.O.2    Enquist, L.W.3
  • 231
    • 33746424849 scopus 로고    scopus 로고
    • Human monoclonal antibody combination against SARS coronavirus: Synergy and coverage of escape mutants
    • ter Meulen J, Van Den Brink EN, Poon LL, et al 2006. Human monoclonal antibody combination against SARS coronavirus: synergy and coverage of escape mutants. PLoS Med. 3. e237
    • (2006) PLoS Med , vol.3 , pp. e237
    • Ter Meulen, J.1    Van Den Brink, E.N.2    Poon, L.L.3
  • 232
    • 56349124125 scopus 로고    scopus 로고
    • Heparin-like glycosaminoglycans prevent the infection of measles virus in SLAM-negative cell lines
    • Terao-Muto Y, Yoneda M, Seki T, et al. (2008). Heparin-like glycosaminoglycans prevent the infection of measles virus in SLAM-negative cell lines. Antiviral Res 80:370-6
    • (2008) Antiviral Res , vol.80 , pp. 370-376
    • Terao-Muto, Y.1    Yoneda, M.2    Seki, T.3
  • 233
    • 0037436346 scopus 로고    scopus 로고
    • Ebola virus matrix protein VP40 interaction with human cellular factors Tsg101 and Nedd4
    • Timmins J, Schoehn G, Ricard-Blum S, et al. (2003). Ebola virus matrix protein VP40 interaction with human cellular factors Tsg101 and Nedd4. J Mol Biol 326:493-502
    • (2003) J Mol Biol , vol.326 , pp. 493-502
    • Timmins, J.1    Schoehn, G.2    Ricard-Blum, S.3
  • 234
    • 84857077947 scopus 로고    scopus 로고
    • Avidity binding of human aDenovirus serotypes 3 and 7 to the membrane cofactor CD46 triggers infection
    • Trinh HV, Lesage G, Chennamparampil V, et al. (2012). Avidity binding of human aDenovirus serotypes 3 and 7 to the membrane cofactor CD46 triggers infection. J Virol 86:1623-37
    • (2012) J Virol , vol.86 , pp. 1623-1637
    • Trinh, H.V.1    Lesage, G.2    Chennamparampil, V.3
  • 235
    • 33747790535 scopus 로고    scopus 로고
    • Template-based coiled-coil antigens elicit neutralizing antibodies to the SARS-coronavirus
    • Tripet B, Kao DJ, Jeffers SA, et al. (2006). Template-based coiled-coil antigens elicit neutralizing antibodies to the SARS-coronavirus. J Struct Biol 155:176-94
    • (2006) J Struct Biol , vol.155 , pp. 176-194
    • Tripet, B.1    Kao, D.J.2    Jeffers, S.A.3
  • 236
    • 84868091515 scopus 로고    scopus 로고
    • Aminoacylase 3 binds to and cleaves the N-terminus of the hepatitis C virus core protein
    • Tsirulnikov K, Abuladze N, Vahi R, et al. (2012). Aminoacylase 3 binds to and cleaves the N-terminus of the hepatitis C virus core protein. FEBS Lett 586:3799-804
    • (2012) FEBS Lett , vol.586 , pp. 3799-3804
    • Tsirulnikov, K.1    Abuladze, N.2    Vahi, R.3
  • 237
    • 33845629453 scopus 로고    scopus 로고
    • Mathematical virology: A novel approach to the structure and assembly of viruses
    • Twarock R. (2006). Mathematical virology: a novel approach to the structure and assembly of viruses. Philos Transact A Math Phys Eng Sci 364:3357-73
    • (2006) Philos Transact A Math Phys Eng Sci , vol.364 , pp. 3357-3373
    • Twarock, R.1
  • 238
    • 26244434388 scopus 로고    scopus 로고
    • Alpha(v)beta3-integrinDepenDent activation of focal adhesion kinase mediates NF-kappaB activation and motogenic activity by HIV-1 Tat in endothelial cells
    • Urbinati C, Bugatti A, Giacca M, et al. (2005). alpha(v)beta3-integrinDepenDent activation of focal adhesion kinase mediates NF-kappaB activation and motogenic activity by HIV-1 Tat in endothelial cells. J Cell Sci 118:3949-58
    • (2005) J Cell Sci , vol.118 , pp. 3949-3958
    • Urbinati, C.1    Bugatti, A.2    Giacca, M.3
  • 239
    • 2942625991 scopus 로고    scopus 로고
    • Chemically sulfated Escherichia coli K5 polysacchariDe Derivatives as extracellular HIV-1 Tat protein antagonists
    • Urbinati C, Bugatti A, Oreste P, et al. (2004). Chemically sulfated Escherichia coli K5 polysacchariDe Derivatives as extracellular HIV-1 Tat protein antagonists. FEBS Lett 568:171-7
    • (2004) FEBS Lett , vol.568 , pp. 171-177
    • Urbinati, C.1    Bugatti, A.2    Oreste, P.3
  • 240
    • 56349167518 scopus 로고    scopus 로고
    • Polyanionic drugs and viral oncogenesis: A novel approach to control infection, tumor-Associated inflammation and angiogenesis
    • Urbinati C, ChioDelli P, Rusnati M. (2008). Polyanionic drugs and viral oncogenesis: a novel approach to control infection, tumor-Associated inflammation and angiogenesis. Molecules 13:2758-85
    • (2008) Molecules , vol.13 , pp. 2758-2785
    • Urbinati, C.1    Chiodelli, P.2    Rusnati, M.3
  • 241
    • 33845439562 scopus 로고    scopus 로고
    • Surface plasmon resonance biosensor for direct Detection of antibody against Epstein-Barr virus
    • Vaisocherova H, Mrkvova K, Piliarik M, et al. (2007). Surface plasmon resonance biosensor for direct Detection of antibody against Epstein-Barr virus. Biosens Bioelectron 22:1020-6
    • (2007) Biosens Bioelectron , vol.22 , pp. 1020-1026
    • Vaisocherova, H.1    Mrkvova, K.2    Piliarik, M.3
  • 242
    • 0033580814 scopus 로고    scopus 로고
    • Real-time kinetics of HIV-1 Rev-Rev response element interactions. Definition of minimal binding sites on RNA and protein and stoichiometric analysis
    • Van Ryk DI, Venkatesan S. (1999). Real-time kinetics of HIV-1 Rev-Rev response element interactions. Definition of minimal binding sites on RNA and protein and stoichiometric analysis. J Biol Chem 274: 17452-63
    • (1999) J Biol Chem , vol.274 , pp. 17452-17463
    • Van Ryk, D.I.1    Venkatesan, S.2
  • 243
    • 0028170783 scopus 로고
    • Preferential antibody recognition of structurally distinct HIV-1 gp120 molecules
    • VanCott TC, Bethke FR, Kalyanaraman V, et al. (1994). Preferential antibody recognition of structurally distinct HIV-1 gp120 molecules. J Acquir Immune Defic Syndr 7:1103-15
    • (1994) J Acquir Immune Defic Syndr , vol.7 , pp. 1103-1115
    • Vancott, T.C.1    Bethke, F.R.2    Kalyanaraman, V.3
  • 244
    • 85043488048 scopus 로고    scopus 로고
    • Interactions of HIV-1 antibodies 2F5 and 4E10 with a gp41 epitope prebound to host and viral membrane moDel systems
    • Veiga AS, PattenDen LK, Fletcher JM, et al. (2009). Interactions of HIV-1 antibodies 2F5 and 4E10 with a gp41 epitope prebound to host and viral membrane moDel systems. Chembiochem 10:1032-44
    • (2009) Chembiochem , vol.10 , pp. 1032-1044
    • Veiga, A.S.1    Pattenden, L.K.2    Fletcher, J.M.3
  • 245
    • 84860895143 scopus 로고    scopus 로고
    • Enhancement of chemokine function as an immunomodulatory strategy employed by human herpesviruses
    • Viejo-Borbolla A, Martinez-Martin N, Nel HJ, et al. (2012). Enhancement of chemokine function as an immunomodulatory strategy employed by human herpesviruses. PLoS Pathog 8: e1002497
    • (2012) PLoS Pathog , vol.8 , pp. e1002497
    • Viejo-Borbolla, A.1    Martinez-Martin, N.2    Nel, H.J.3
  • 246
    • 37149031663 scopus 로고    scopus 로고
    • Viral proteomics: Global evaluation of viruses and their interaction with the host
    • Viswanathan K, Fruh K. (2007). Viral proteomics: global evaluation of viruses and their interaction with the host. Expert Rev Proteomics 4: 815-29
    • (2007) Expert Rev Proteomics , vol.4 , pp. 815-829
    • Viswanathan, K.1    Fruh, K.2
  • 247
    • 79960846480 scopus 로고    scopus 로고
    • Structural and functional insights into IkappaB-Alpha/HIV-1 Tat interaction
    • Vitagliano L, Fiume G, Scognamiglio PL, et al. (2011). Structural and functional insights into IkappaB-Alpha/HIV-1 Tat interaction. Biochimie 93:1592-600
    • (2011) Biochimie , vol.93 , pp. 1592-1600
    • Vitagliano, L.1    Fiume, G.2    Scognamiglio, P.L.3
  • 248
    • 38849134279 scopus 로고    scopus 로고
    • ADenovirus serotype 5 hexon mediates liver gene transfer
    • Waddington SN, McVey JH, Bhella D, et al. (2008). ADenovirus serotype 5 hexon mediates liver gene transfer. Cell 132:397-409
    • (2008) Cell , vol.132 , pp. 397-409
    • Waddington, S.N.1    McVey, J.H.2    Bhella, D.3
  • 249
    • 78651260394 scopus 로고    scopus 로고
    • Desmoglein 2 is a receptor for aDenovirus serotypes 3 7, 11 and 14
    • Wang H, Li ZY, Liu Y, et al. (2010a). Desmoglein 2 is a receptor for aDenovirus serotypes 3, 7, 11 and 14. Nat Med 17:96-104
    • (2010) Nat Med , vol.17 , pp. 96-104
    • Wang, H.1    Li, Z.Y.2    Liu, Y.3
  • 250
    • 36349037234 scopus 로고    scopus 로고
    • IDentification of CD46 binding sites within the aDenovirus serotype 35 fiber knob
    • Wang H, Liaw YC, Stone D, et al. (2007). IDentification of CD46 binding sites within the aDenovirus serotype 35 fiber knob. J Virol 81: 12785-92
    • (2007) J Virol , vol.81 , pp. 12785-12792
    • Wang, H.1    Liaw, Y.C.2    Stone, D.3
  • 251
    • 77952196908 scopus 로고    scopus 로고
    • Interactions of SARS coronavirus nucleocapsid protein with the host cell proteasome subunit p42
    • Wang Q, Li C, Zhang Q, et al. (2010b). Interactions of SARS coronavirus nucleocapsid protein with the host cell proteasome subunit p42. Virol J 7:99
    • (2010) Virol J , vol.7 , pp. 99
    • Wang, Q.1    Li, C.2    Zhang, Q.3
  • 252
    • 0037407586 scopus 로고    scopus 로고
    • Retrocyclin, an antiretroviral theta-Defensin, is a lectin
    • Wang W, Cole AM, Hong T, et al. (2003). Retrocyclin, an antiretroviral theta-Defensin, is a lectin. J Immunol 170:4708-16
    • (2003) J Immunol , vol.170 , pp. 4708-4716
    • Wang, W.1    Cole, A.M.2    Hong, T.3
  • 253
    • 0030310583 scopus 로고    scopus 로고
    • Binding kinetics and bioassay of RRE mRNA fragments to a peptiDe containing the recognition domain of HIV-1 Rev
    • West ML, Ramsdale TE. (1996). Binding kinetics and bioassay of RRE mRNA fragments to a peptiDe containing the recognition domain of HIV-1 Rev. Biomed Pept Proteins Nucleic Acids 2:85-8
    • (1996) Biomed Pept Proteins Nucleic Acids , vol.2 , pp. 85-88
    • West, M.L.1    Ramsdale, T.E.2
  • 254
    • 65549142692 scopus 로고    scopus 로고
    • IDentifying and characterizing a functional HIV-1 reverse transcriptase-binding site on integrase
    • Wilkinson TA, Januszyk K, Phillips ML, et al. (2009). IDentifying and characterizing a functional HIV-1 reverse transcriptase-binding site on integrase. J Biol Chem 284:7931-9
    • (2009) J Biol Chem , vol.284 , pp. 7931-7939
    • Wilkinson, T.A.1    Januszyk, K.2    Phillips, M.L.3
  • 255
    • 0031032593 scopus 로고    scopus 로고
    • Specificity and affinity of binding of herpes simplex virus type 2 glycoprotein B to glycosaminoglycans
    • Williams RK, Straus SE. (1997). Specificity and affinity of binding of herpes simplex virus type 2 glycoprotein B to glycosaminoglycans. J Virol 71:1375-80
    • (1997) J Virol , vol.71 , pp. 1375-1380
    • Williams, R.K.1    Straus, S.E.2
  • 256
    • 0031777344 scopus 로고    scopus 로고
    • Examination of the kinetics of herpes simplex virus glycoprotein D binding to the herpesvirus entry mediator, using surface plasmon resonance
    • Willis SH, Rux AH, Peng C, et al. (1998). Examination of the kinetics of herpes simplex virus glycoprotein D binding to the herpesvirus entry mediator, using surface plasmon resonance. J Virol 72:5937-47
    • (1998) J Virol , vol.72 , pp. 5937-5947
    • Willis, S.H.1    Rux, A.H.2    Peng, C.3
  • 257
    • 78751681564 scopus 로고    scopus 로고
    • IDentification of high-Affinity PB1-Derived peptiDes with enhanced affinity to the PA protein of influenza A virus polymerase
    • WunDerlich K, Juozapaitis M, Ranadheera C, et al. (2011). IDentification of high-Affinity PB1-Derived peptiDes with enhanced affinity to the PA protein of influenza A virus polymerase. Antimicrob Agents Chemother 55:696-702
    • (2011) Antimicrob Agents Chemother , vol.55 , pp. 696-702
    • Wunderlich, K.1    Juozapaitis, M.2    Ranadheera, C.3
  • 258
    • 0037320267 scopus 로고    scopus 로고
    • Molluscum contagiosum virus interleukin-18 (IL-18) binding protein is secreted as a full-length form that binds cell surface glycosaminoglycans through the C-terminal tail and a furincleaved form with only the IL-18 binding domain
    • Xiang Y, Moss B. (2003). Molluscum contagiosum virus interleukin-18 (IL-18) binding protein is secreted as a full-length form that binds cell surface glycosaminoglycans through the C-terminal tail and a furincleaved form with only the IL-18 binding domain. J Virol 77:2623-30
    • (2003) J Virol , vol.77 , pp. 2623-2630
    • Xiang, Y.1    Moss, B.2
  • 259
    • 0034015712 scopus 로고    scopus 로고
    • HIV-1 gp41 by N-domain binds the potential receptor protein P45
    • Xiao Y, Wu W, Dierich MP, Chen Y. (2000). HIV-1 gp41 by N-domain binds the potential receptor protein P45. Int Arch Allergy Immunol 121:253-7
    • (2000) Int Arch Allergy Immunol , vol.121 , pp. 253-257
    • Xiao, Y.1    Wu, W.2    Dierich, M.P.3    Chen, Y.4
  • 260
    • 0034653439 scopus 로고    scopus 로고
    • Distinct cellular receptor interactions in poliovirus and rhinoviruses
    • Xing L, Tjarnlund K, Lindqvist B, et al. (2000). Distinct cellular receptor interactions in poliovirus and rhinoviruses. EMBO J 19:1207-16
    • (2000) EMBO J , vol.19 , pp. 1207-1216
    • Xing, L.1    Tjarnlund, K.2    Lindqvist, B.3
  • 261
    • 41149162586 scopus 로고    scopus 로고
    • IDentification of hot spots in the variola virus complement inhibitor (SPICE) for human complement regulation
    • Yadav VN, Pyaram K, Mullick J, Sahu A. (2008). IDentification of hot spots in the variola virus complement inhibitor (SPICE) for human complement regulation. J Virol 82:3283-94
    • (2008) J Virol , vol.82 , pp. 3283-3294
    • Yadav, V.N.1    Pyaram, K.2    Mullick, J.3    Sahu, A.4
  • 262
    • 55949092847 scopus 로고    scopus 로고
    • A novel strategy for analyzing RNAprotein interactions by surface plasmon resonance biosensor
    • Yang Y, Wang Q, Guo D. (2008). A novel strategy for analyzing RNAprotein interactions by surface plasmon resonance biosensor. Mol Biotechnol 40:87-93
    • (2008) Mol Biotechnol , vol.40 , pp. 87-93
    • Yang, Y.1    Wang, Q.2    Guo, D.3
  • 263
    • 2342573669 scopus 로고    scopus 로고
    • Theta Defensins protect cells from infection by herpes simplex virus by inhibiting viral adhesion and entry
    • Yasin B, Wang W, Pang M, et al. (2004) theta Defensins protect cells from infection by herpes simplex virus by inhibiting viral adhesion and entry. J Virol 78:5147-56
    • (2004) J Virol , vol.78 , pp. 5147-5156
    • Yasin, B.1    Wang, W.2    Pang, M.3
  • 264
    • 0033614815 scopus 로고    scopus 로고
    • Divalent cations stimulate preferential recognition of a viral DNA end by HIV-1 integrase
    • Yi J, Asante-Appiah E, Skalka AM. (1999). Divalent cations stimulate preferential recognition of a viral DNA end by HIV-1 integrase. Biochemistry 38:8458-68
    • (1999) Biochemistry , vol.38 , pp. 8458-8468
    • Yi, J.1    Asante-Appiah, E.2    Skalka, A.M.3
  • 265
    • 84864554412 scopus 로고    scopus 로고
    • Epstein-Barr virus IL-10 engages IL-10R1 by a two-step mechanism leading to altered signaling properties
    • Yoon SI, Jones BC, Logsdon NJ, et al. (2012). Epstein-Barr virus IL-10 engages IL-10R1 by a two-step mechanism leading to altered signaling properties. J Biol Chem 287:26586-95
    • (2012) J Biol Chem , vol.287 , pp. 26586-26595
    • Yoon, S.I.1    Jones, B.C.2    Logsdon, N.J.3
  • 266
    • 33748705342 scopus 로고    scopus 로고
    • Detection of Ebola virus envelope using monoclonal and polyclonal antibodies in ELISA, surface plasmon resonance and a quartz crystal microbalance immunosensor
    • Yu JS, Liao HX, Gerdon AE, et al. (2006). Detection of Ebola virus envelope using monoclonal and polyclonal antibodies in ELISA, surface plasmon resonance and a quartz crystal microbalance immunosensor. J Virol Methods 137:219-28
    • (2006) J Virol Methods , vol.137 , pp. 219-228
    • Yu, J.S.1    Liao, H.X.2    Gerdon, A.E.3
  • 267
    • 18844406437 scopus 로고    scopus 로고
    • Kinetic analysis of the interactions of human papillomavirus E6 oncoproteins with the ubiquitin ligase E6AP using surface plasmon resonance
    • Zanier K, Charbonnier S, Baltzinger M, et al. (2005). Kinetic analysis of the interactions of human papillomavirus E6 oncoproteins with the ubiquitin ligase E6AP using surface plasmon resonance. J Mol Biol 349:401-12
    • (2005) J Mol Biol , vol.349 , pp. 401-412
    • Zanier, K.1    Charbonnier, S.2    Baltzinger, M.3
  • 268
    • 74649086278 scopus 로고    scopus 로고
    • E6 proteins from diverse papillomaviruses self-Associate both in vitro and in vivo
    • Zanier K, Ruhlmann C, Melin F, et al. (2009). E6 proteins from diverse papillomaviruses self-Associate both in vitro and in vivo. J Mol Biol 396:90-104
    • (2009) J Mol Biol , vol.396 , pp. 90-104
    • Zanier, K.1    Ruhlmann, C.2    Melin, F.3
  • 269
    • 0037092977 scopus 로고    scopus 로고
    • A highly stable covalent conjugated heparin biochip for heparin-protein interaction studies
    • Zhang F, Fath M, Marks R, Linhardt RJ. (2002). A highly stable covalent conjugated heparin biochip for heparin-protein interaction studies. Anal Biochem 304:271-3
    • (2002) Anal Biochem , vol.304 , pp. 271-273
    • Zhang, F.1    Fath, M.2    Marks, R.3    Linhardt, R.J.4
  • 270
    • 84870014650 scopus 로고    scopus 로고
    • The stem region of premembrane protein plays an important role in the virus surface protein rearrangement during Dengue maturation
    • Zhang Q, Hunke C, Yau YH, et al. (2012) the stem region of premembrane protein plays an important role in the virus surface protein rearrangement during Dengue maturation. J Biol Chem 287: 40525-34
    • (2012) J Biol Chem , vol.287 , pp. 40525-40534
    • Zhang, Q.1    Hunke, C.2    Yau, Y.H.3
  • 271
    • 0347930801 scopus 로고    scopus 로고
    • Use of surface plasmon resonance for the measurement of low affinity binding interactions between HSP72 and measles virus nucleocapsid protein
    • Zhang X, Oglesbee M. (2003). Use of surface plasmon resonance for the measurement of low affinity binding interactions between HSP72 and measles virus nucleocapsid protein. Biol Proced Online 5:170-81
    • (2003) Biol Proced Online , vol.5 , pp. 170-181
    • Zhang, X.1    Oglesbee, M.2
  • 272
    • 77954214955 scopus 로고    scopus 로고
    • APOBEC3G directly binds Hepatitis B virus core protein in cell and cell free systems
    • Zhao D, Wang X, Lou G, et al. (2010). APOBEC3G directly binds Hepatitis B virus core protein in cell and cell free systems. Virus Res 151:213-19
    • (2010) Virus Res , vol.151 , pp. 213-219
    • Zhao, D.1    Wang, X.2    Lou, G.3
  • 273
    • 23844440296 scopus 로고    scopus 로고
    • IDentification of N-phenyl-N0-2 2, 6, 6-tetramethyl-piperidin-4-yl)-oxalamiDes as a new class of HIV-1 entry inhibitors that prevent gp120 binding to CD4
    • Zhao Q, Ma L, Jiang S, et al. (2005). IDentification of N-phenyl-N0-(2, 2, 6, 6-tetramethyl-piperidin-4-yl)-oxalamiDes as a new class of HIV-1 entry inhibitors that prevent gp120 binding to CD4. Virology 339:213-25
    • (2005) Virology , vol.339 , pp. 213-225
    • Zhao, Q.1    Ma, L.2    Jiang, S.3
  • 274
    • 47049088603 scopus 로고    scopus 로고
    • The nucleocapsid protein of severe acute respiratory syndrome coronavirus inhibits cell cytokinesis and proliferation by interacting with translation elongation factor 1alpha
    • Zhou B, Liu J, Wang Q, et al. (2008) the nucleocapsid protein of severe acute respiratory syndrome coronavirus inhibits cell cytokinesis and proliferation by interacting with translation elongation factor 1alpha. J Virol 82:6962-71
    • (2008) J Virol , vol.82 , pp. 6962-6971
    • Zhou, B.1    Liu, J.2    Wang, Q.3
  • 275
    • 66749106440 scopus 로고    scopus 로고
    • HIV-1 Tat proteininduced rapid and reversible Decrease in [3H]dopamine uptake: Dissociation of [3H]dopamine uptake and [3H]2beta-carbomethoxy-3-beta-(4-fluorophenyl)tropane (WIN 35 428) binding in rat striatal synaptosomes
    • Zhu J, Mactutus CF, Wallace DR, Booze RM. (2009). HIV-1 Tat proteininduced rapid and reversible Decrease in [3H]dopamine uptake: dissociation of [3H]dopamine uptake and [3H]2beta-carbomethoxy-3-beta-(4-fluorophenyl)tropane (WIN 35 428) binding in rat striatal synaptosomes. J Pharmacol Exp Ther 329:1071-83
    • (2009) J Pharmacol Exp Ther , vol.329 , pp. 1071-1083
    • Zhu, J.1    Mactutus, C.F.2    Wallace, D.R.3    Booze, R.M.4
  • 276
    • 78650754124 scopus 로고    scopus 로고
    • Virus assembly, allostery and antivirals
    • Zlotnick A, Mukhopadhyay S. (2011). Virus assembly, allostery and antivirals. Trends Microbiol 19:14-23
    • (2011) Trends Microbiol , vol.19 , pp. 14-23
    • Zlotnick, A.1    Mukhopadhyay, S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.