메뉴 건너뛰기




Volumn 6, Issue 11, 2014, Pages 4536-4570

Structure, function and dynamics in adenovirus maturation

Author keywords

Adenovirus; DNA sliding; Infectivity; Protease; Uncoating; Virus stability

Indexed keywords

ACTIN; CORE PROTEIN; CYTOKERATIN 18; DOUBLE STRANDED DNA; PROTEINASE; RHODAMINE 110; SCAFFOLD PROTEIN; TUBULIN; VIMENTIN; VIRUS DNA; VIRAL PROTEIN;

EID: 84912544572     PISSN: None     EISSN: 19994915     Source Type: Journal    
DOI: 10.3390/v6114536     Document Type: Review
Times cited : (101)

References (145)
  • 1
    • 34447539077 scopus 로고    scopus 로고
    • Adenoviridae: The viruses and their replication
    • Knipe, D.M., Howley, P.M., Griffin, D.E., Lamb, R.A., Martin, M.A., Eds, 5th ed. Lippincott Williams & Wilkins: Philadelphia, PA, USA
    • Berk, A.J. Adenoviridae: The viruses and their replication. In Fields Virology, 5th ed.; Knipe, D.M., Howley, P.M., Griffin, D.E., Lamb, R.A., Martin, M.A., Eds.; Lippincott Williams & Wilkins: Philadelphia, PA, USA, 2007; pp. 2355-2394.
    • (2007) Fields Virology , pp. 2355-2394
    • Berk, A.J.1
  • 2
    • 84856053806 scopus 로고    scopus 로고
    • Family Adenoviridae
    • Virus Taxonomy: Classification and Nomenclature of Viruses. Ninth Report of the International Committee on Taxonomy of Viruses; King, A., Adams, M., Carstens, E., Lefkowitz, E., Eds Elsevier: San Diego, CA, USA
    • Harrach, B.; Benkő, M.; Both, G.; Brown, M.; Davison, A.; Echavarría, M.; Hess, M.; Jones, M.; Kajon, A.; Lehmkuhl, H.; et al. Family Adenoviridae. In Virus Taxonomy: Classification and Nomenclature of Viruses. Ninth Report of the International Committee on Taxonomy of Viruses; King, A., Adams, M., Carstens, E., Lefkowitz, E., Eds.; Elsevier: San Diego, CA, USA, 2011; pp. 95-111.
    • (2011) Elsevier: San Diego, CA, USA , pp. 95-111
    • Harrach, B.1    Benkő, M.2    Both, G.3    Brown, M.4    Davison, A.5    Echavarría, M.6    Hess, M.7    Jones, M.8    Kajon, A.9    Lehmkuhl, H.10
  • 3
    • 68249099660 scopus 로고    scopus 로고
    • New insights on adenovirus as vaccine vectors
    • Lasaro, M.O.; Ertl, H.C. New insights on adenovirus as vaccine vectors. Mol. Ther. 2009, 17, 1333-1339.
    • (2009) Mol. Ther , vol.17 , pp. 1333-1339
    • Lasaro, M.O.1    Ertl, H.C.2
  • 5
    • 76349110981 scopus 로고    scopus 로고
    • Current issues and future directions of oncolytic adenoviruses
    • Yamamoto, M.; Curiel, D.T. Current issues and future directions of oncolytic adenoviruses. Mol. Ther. 2010, 18, 243-250.
    • (2010) Mol. Ther , vol.18 , pp. 243-250
    • Yamamoto, M.1    Curiel, D.T.2
  • 7
    • 84861540383 scopus 로고    scopus 로고
    • Latest Insights on Adenovirus Structure and Assembly
    • San Martín, C. Latest Insights on Adenovirus Structure and Assembly. Viruses 2012, 4, 847-877.
    • (2012) Viruses , vol.4 , pp. 847-877
    • San Martín, C.1
  • 8
    • 77956098333 scopus 로고    scopus 로고
    • Atomic structure of human adenovirus by cryo-EM reveals interactions among protein networks
    • Liu, H.; Jin, L.; Koh, S.B.; Atanasov, I.; Schein, S.; Wu, L.; Zhou, Z.H. Atomic structure of human adenovirus by cryo-EM reveals interactions among protein networks. Science 2010, 329, 1038-1043.
    • (2010) Science , vol.329 , pp. 1038-1043
    • Liu, H.1    Jin, L.2    Koh, S.B.3    Atanasov, I.4    Schein, S.5    Wu, L.6    Zhou, Z.H.7
  • 9
    • 77956128250 scopus 로고    scopus 로고
    • Crystal structure of human adenovirus at 3.5 A resolution
    • Reddy, V.S.; Natchiar, S.K.; Stewart, P.L.; Nemerow, G.R. Crystal structure of human adenovirus at 3.5 A resolution. Science 2010, 329, 1071-1075.
    • (2010) Science , vol.329 , pp. 1071-1075
    • Reddy, V.S.1    Natchiar, S.K.2    Stewart, P.L.3    Nemerow, G.R.4
  • 10
    • 84905979871 scopus 로고    scopus 로고
    • Structures and organization of adenovirus cement proteins provide insights into the role of capsid maturation in virus entry and infection
    • Reddy, V.S.; Nemerow, G.R. Structures and organization of adenovirus cement proteins provide insights into the role of capsid maturation in virus entry and infection. Proc. Natl. Acad. Sci. USA 2014, 111, 11715-11720.
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 11715-11720
    • Reddy, V.S.1    Nemerow, G.R.2
  • 11
    • 84908555950 scopus 로고    scopus 로고
    • New structural model of adenoviral cement proteins is not yet concrete
    • Campos, S.K. New structural model of adenoviral cement proteins is not yet concrete. Proc. Natl. Acad. Sci. USA 2014, 111, E4542-E4543.
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. E4542-E4543
    • Campos, S.K.1
  • 12
    • 33845411897 scopus 로고    scopus 로고
    • Visualization of α-helices in a 6 Å resolution cryoEM structure of adenovirus allows refinement of capsid protein assignments
    • Saban, S.D.; Silvestry, M.; Nemerow, G.R.; Stewart, P.L. Visualization of α-helices in a 6 Å resolution cryoEM structure of adenovirus allows refinement of capsid protein assignments. J. Virol. 2006, 80, 12049-12059.
    • (2006) J. Virol , vol.80 , pp. 12049-12059
    • Saban, S.D.1    Silvestry, M.2    Nemerow, G.R.3    Stewart, P.L.4
  • 15
    • 79960432721 scopus 로고    scopus 로고
    • Adenovirus structural protein IIIa is involved in the serotype specificity of viral DNA packaging
    • Ma, H.C.; Hearing, P. Adenovirus structural protein IIIa is involved in the serotype specificity of viral DNA packaging. J. Virol. 2011, 85, 7849-7855.
    • (2011) J. Virol , vol.85 , pp. 7849-7855
    • Ma, H.C.1    Hearing, P.2
  • 17
    • 0027496645 scopus 로고
    • Stepwise dismantling of adenovirus 2 during entry into cells
    • Greber, U.F.; Willetts, M.; Webster, P.; Helenius, A. Stepwise dismantling of adenovirus 2 during entry into cells. Cell 1993, 75, 477-486.
    • (1993) Cell , vol.75 , pp. 477-486
    • Greber, U.F.1    Willetts, M.2    Webster, P.3    Helenius, A.4
  • 18
    • 0022348579 scopus 로고
    • Molecular composition of the adenovirus type 2 virion
    • Van Oostrum, J.; Burnett, R.M. Molecular composition of the adenovirus type 2 virion. J. Virol. 1985, 56, 439-448.
    • (1985) J. Virol , vol.56 , pp. 439-448
    • Van Oostrum, J.1    Burnett, R.M.2
  • 19
    • 84899010486 scopus 로고    scopus 로고
    • Adenovirus composition, proteolysis, and disassembly studied by in-depth qualitative and quantitative proteomics
    • Benevento, M.; di Palma, S.; Snijder, J.; Moyer, C.L.; Reddy, V.S.; Nemerow, G.R.; Heck, A.J. Adenovirus composition, proteolysis, and disassembly studied by in-depth qualitative and quantitative proteomics. J. Biol. Chem. 2014, 289, 11421-11430.
    • (2014) J. Biol. Chem , vol.289 , pp. 11421-11430
    • Benevento, M.1    di Palma, S.2    Snijder, J.3    Moyer, C.L.4    Reddy, V.S.5    Nemerow, G.R.6    Heck, A.J.7
  • 20
    • 0021111527 scopus 로고
    • The structure of nucleoprotein cores released from adenovirions
    • Vayda, M.E.; Rogers, A.E.; Flint, S.J. The structure of nucleoprotein cores released from adenovirions. Nucleic Acids Res. 1983, 11, 441-460.
    • (1983) Nucleic Acids Res , vol.11 , pp. 441-460
    • Vayda, M.E.1    Rogers, A.E.2    Flint, S.J.3
  • 21
    • 0020063146 scopus 로고
    • Structure of adenovirus chromatin
    • Mirza, M.A.; Weber, J. Structure of adenovirus chromatin. Biochim. Biophys. Acta 1982, 696, 76-86.
    • (1982) Biochim. Biophys. Acta , vol.696 , pp. 76-86
    • Mirza, M.A.1    Weber, J.2
  • 22
    • 84864284194 scopus 로고    scopus 로고
    • Adenovirus receptors: Implications for targeting of viral vectors
    • Arnberg, N. Adenovirus receptors: Implications for targeting of viral vectors. Trends Pharmacol. Sci. 2012, 33, 442-448.
    • (2012) Trends Pharmacol. Sci , vol.33 , pp. 442-448
    • Arnberg, N.1
  • 23
    • 0027166647 scopus 로고
    • Integrins αvβ3 and αvβ5 promote adenovirus internalization but not virus attachment
    • Wickham, T.J.; Mathias, P.; Cheresh, D.A.; Nemerow, G.R. Integrins αvβ3 and αvβ5 promote adenovirus internalization but not virus attachment. Cell 1993, 73, 309-319.
    • (1993) Cell , vol.73 , pp. 309-319
    • Wickham, T.J.1    Mathias, P.2    Cheresh, D.A.3    Nemerow, G.R.4
  • 24
    • 0033942486 scopus 로고    scopus 로고
    • The first step of adenovirus type 2 disassembly occurs at the cell surface, independently of endocytosis and escape to the cytosol
    • Nakano, M.Y.; Boucke, K.; Suomalainen, M.; Stidwill, R.P.; Greber, U.F. The first step of adenovirus type 2 disassembly occurs at the cell surface, independently of endocytosis and escape to the cytosol. J. Virol. 2000, 74, 7085-7095.
    • (2000) J. Virol , vol.74 , pp. 7085-7095
    • Nakano, M.Y.1    Boucke, K.2    Suomalainen, M.3    Stidwill, R.P.4    Greber, U.F.5
  • 25
    • 70350322305 scopus 로고    scopus 로고
    • Cryo-electron microscopy structure of an adenovirus-integrin complex indicates conformational changes in both penton base and integrin
    • Lindert, S.; Silvestry, M.; Mullen, T.M.; Nemerow, G.R.; Stewart, P.L. Cryo-electron microscopy structure of an adenovirus-integrin complex indicates conformational changes in both penton base and integrin. J. Virol. 2009, 83, 11491-11501.
    • (2009) J. Virol , vol.83 , pp. 11491-11501
    • Lindert, S.1    Silvestry, M.2    Mullen, T.M.3    Nemerow, G.R.4    Stewart, P.L.5
  • 26
    • 78650070473 scopus 로고    scopus 로고
    • Stepwise loss of fluorescent core protein V from human adenovirus during entry into cells
    • Puntener, D.; Engelke, M.F.; Ruzsics, Z.; Strunze, S.; Wilhelm, C.; Greber, U.F. Stepwise loss of fluorescent core protein V from human adenovirus during entry into cells. J. Virol. 2011, 85, 481-496.
    • (2011) J. Virol , vol.85 , pp. 481-496
    • Puntener, D.1    Engelke, M.F.2    Ruzsics, Z.3    Strunze, S.4    Wilhelm, C.5    Greber, U.F.6
  • 27
    • 13444311651 scopus 로고    scopus 로고
    • Adenovirus protein VI mediates membrane disruption following capsid disassembly
    • Wiethoff, C.M.; Wodrich, H.; Gerace, L.; Nemerow, G.R. Adenovirus protein VI mediates membrane disruption following capsid disassembly. J. Virol. 2005, 79, 1992-2000.
    • (2005) J. Virol , vol.79 , pp. 1992-2000
    • Wiethoff, C.M.1    Wodrich, H.2    Gerace, L.3    Nemerow, G.R.4
  • 29
    • 80051887181 scopus 로고    scopus 로고
    • Drifting motions of the adenovirus receptor CAR and immobile integrins initiate virus uncoating and membrane lytic protein exposure
    • Burckhardt, C.J.; Suomalainen, M.; Schoenenberger, P.; Boucke, K.; Hemmi, S.; Greber, U.F. Drifting motions of the adenovirus receptor CAR and immobile integrins initiate virus uncoating and membrane lytic protein exposure. Cell Host Microbe 2011, 10, 105-117.
    • (2011) Cell Host Microbe , vol.10 , pp. 105-117
    • Burckhardt, C.J.1    Suomalainen, M.2    Schoenenberger, P.3    Boucke, K.4    Hemmi, S.5    Greber, U.F.6
  • 30
    • 77952577600 scopus 로고    scopus 로고
    • An N-terminal domain of adenovirus protein VI fragments membranes by inducing positive membrane curvature
    • Maier, O.; Galan, D.L.; Wodrich, H.; Wiethoff, C.M. An N-terminal domain of adenovirus protein VI fragments membranes by inducing positive membrane curvature. Virology 2010, 402, 11-19.
    • (2010) Virology , vol.402 , pp. 11-19
    • Maier, O.1    Galan, D.L.2    Wodrich, H.3    Wiethoff, C.M.4
  • 31
    • 84886031698 scopus 로고    scopus 로고
    • A direct and versatile assay measuring membrane penetration of adenovirus in single cells
    • Suomalainen, M.; Luisoni, S.; Boucke, K.; Bianchi, S.; Engel, D.A.; Greber, U.F. A direct and versatile assay measuring membrane penetration of adenovirus in single cells. J. Virol. 2013, 87, 12367-12379.
    • (2013) J. Virol , vol.87 , pp. 12367-12379
    • Suomalainen, M.1    Luisoni, S.2    Boucke, K.3    Bianchi, S.4    Engel, D.A.5    Greber, U.F.6
  • 32
    • 75149142941 scopus 로고    scopus 로고
    • Adenovirus transport via direct interaction of cytoplasmic dynein with the viral capsid hexon subunit
    • Bremner, K.H.; Scherer, J.; Yi, J.; Vershinin, M.; Gross, S.P.; Vallee, R.B. Adenovirus transport via direct interaction of cytoplasmic dynein with the viral capsid hexon subunit. Cell Host Microbe 2009, 6, 523-535.
    • (2009) Cell Host Microbe , vol.6 , pp. 523-535
    • Bremner, K.H.1    Scherer, J.2    Yi, J.3    Vershinin, M.4    Gross, S.P.5    Vallee, R.B.6
  • 34
    • 0035195085 scopus 로고    scopus 로고
    • Import of adenovirus DNA involves the nuclear pore complex receptor CAN/Nup214 and histone H1
    • Trotman, L.C.; Mosberger, N.; Fornerod, M.; Stidwill, R.P.; Greber, U.F. Import of adenovirus DNA involves the nuclear pore complex receptor CAN/Nup214 and histone H1. Nat. Cell Biol. 2001, 3, 1092-1100.
    • (2001) Nat. Cell Biol , vol.3 , pp. 1092-1100
    • Trotman, L.C.1    Mosberger, N.2    Fornerod, M.3    Stidwill, R.P.4    Greber, U.F.5
  • 35
    • 0033593811 scopus 로고    scopus 로고
    • Microtubule-dependent plus- and minus end-directed motilities are competing processes for nuclear targeting of adenovirus
    • Suomalainen, M.; Nakano, M.Y.; Keller, S.; Boucke, K.; Stidwill, R.P.; Greber, U.F. Microtubule-dependent plus- and minus end-directed motilities are competing processes for nuclear targeting of adenovirus. J. Cell Biol. 1999, 144, 657-672.
    • (1999) J. Cell Biol , vol.144 , pp. 657-672
    • Suomalainen, M.1    Nakano, M.Y.2    Keller, S.3    Boucke, K.4    Stidwill, R.P.5    Greber, U.F.6
  • 37
    • 66049143447 scopus 로고    scopus 로고
    • Accurate single-day titration of adenovirus vectors based on equivalence of protein VII nuclear dots and infectious particles
    • Walkiewicz, M.P.; Morral, N.; Engel, D.A. Accurate single-day titration of adenovirus vectors based on equivalence of protein VII nuclear dots and infectious particles. J. Virol. Methods 2009, 159, 251-258.
    • (2009) J. Virol. Methods , vol.159 , pp. 251-258
    • Walkiewicz, M.P.1    Morral, N.2    Engel, D.A.3
  • 38
    • 0031660669 scopus 로고    scopus 로고
    • Encapsidation of viral DNA requires the adenovirus L1 52/55-kilodalton protein
    • Gustin, K.E.; Imperiale, M.J. Encapsidation of viral DNA requires the adenovirus L1 52/55-kilodalton protein. J. Virol. 1998, 72, 7860-7870.
    • (1998) J. Virol , vol.72 , pp. 7860-7870
    • Gustin, K.E.1    Imperiale, M.J.2
  • 39
    • 84880368657 scopus 로고    scopus 로고
    • The Adenovirus L4-22K Protein Has Distinct Functions in the Posttranscriptional Regulation of Gene Expression and Encapsidation of the Viral Genome
    • Guimet, D.; Hearing, P. The Adenovirus L4-22K Protein Has Distinct Functions in the Posttranscriptional Regulation of Gene Expression and Encapsidation of the Viral Genome. J. Virol. 2013, 87, 7688-7699.
    • (2013) J. Virol , vol.87 , pp. 7688-7699
    • Guimet, D.1    Hearing, P.2
  • 40
    • 84878535432 scopus 로고    scopus 로고
    • The Adenovirus L4-33K Protein Regulates both Late Gene Expression Patterns and Viral DNA Packaging
    • Wu, K.; Guimet, D.; Hearing, P. The Adenovirus L4-33K Protein Regulates both Late Gene Expression Patterns and Viral DNA Packaging. J. Virol. 2013, 87, 6739-6747.
    • (2013) J. Virol , vol.87 , pp. 6739-6747
    • Wu, K.1    Guimet, D.2    Hearing, P.3
  • 41
    • 79956158034 scopus 로고    scopus 로고
    • Characterization of Empty adenovirus particles assembled in the absence of a functional adenovirus IVa2 protein
    • Ostapchuk, P.; Almond, M.; Hearing, P. Characterization of Empty adenovirus particles assembled in the absence of a functional adenovirus IVa2 protein. J. Virol. 2011, 85, 5524-5531.
    • (2011) J. Virol , vol.85 , pp. 5524-5531
    • Ostapchuk, P.1    Almond, M.2    Hearing, P.3
  • 42
    • 0034006742 scopus 로고    scopus 로고
    • Interaction of the adenovirus IVa2 protein with viral packaging sequences
    • Zhang, W.; Imperiale, M.J. Interaction of the adenovirus IVa2 protein with viral packaging sequences. J. Virol. 2000, 74, 2687-2693.
    • (2000) J. Virol , vol.74 , pp. 2687-2693
    • Zhang, W.1    Imperiale, M.J.2
  • 43
    • 13944275170 scopus 로고    scopus 로고
    • Functional interaction of the adenovirus IVa2 protein with adenovirus type 5 packaging sequences
    • Ostapchuk, P.; Yang, J.; Auffarth, E.; Hearing, P. Functional interaction of the adenovirus IVa2 protein with adenovirus type 5 packaging sequences. J. Virol. 2005, 79, 2831-2838.
    • (2005) J. Virol , vol.79 , pp. 2831-2838
    • Ostapchuk, P.1    Yang, J.2    Auffarth, E.3    Hearing, P.4
  • 44
    • 13444259754 scopus 로고    scopus 로고
    • Analysis of the interaction of the adenovirus L1 52/55-kilodalton and IVa2 proteins with the packaging sequence in vivo and in vitro
    • Perez-Romero, P.; Tyler, R.E.; Abend, J.R.; Dus, M.; Imperiale, M.J. Analysis of the interaction of the adenovirus L1 52/55-kilodalton and IVa2 proteins with the packaging sequence in vivo and in vitro. J. Virol. 2005, 79, 2366-2374.
    • (2005) J. Virol , vol.79 , pp. 2366-2374
    • Perez-Romero, P.1    Tyler, R.E.2    Abend, J.R.3    Dus, M.4    Imperiale, M.J.5
  • 45
    • 33745780727 scopus 로고    scopus 로고
    • The L4 22-kilodalton protein plays a role in packaging of the adenovirus genome
    • Ostapchuk, P.; Anderson, M.E.; Chandrasekhar, S.; Hearing, P. The L4 22-kilodalton protein plays a role in packaging of the adenovirus genome. J. Virol. 2006, 80, 6973-6981.
    • (2006) J. Virol , vol.80 , pp. 6973-6981
    • Ostapchuk, P.1    Anderson, M.E.2    Chandrasekhar, S.3    Hearing, P.4
  • 46
    • 0026757420 scopus 로고
    • Adenovirus L1 52- and 55-kilodalton proteins are present within assembling virions and colocalize with nuclear structures distinct from replication centers
    • Hasson, T.B.; Ornelles, D.A.; Shenk, T. Adenovirus L1 52- and 55-kilodalton proteins are present within assembling virions and colocalize with nuclear structures distinct from replication centers. J. Virol. 1992, 66, 6133-6142.
    • (1992) J. Virol , vol.66 , pp. 6133-6142
    • Hasson, T.B.1    Ornelles, D.A.2    Shenk, T.3
  • 47
    • 0015970702 scopus 로고
    • V. Young Virions, Structural Intermediate Between Top Components and Aged Virions
    • Ishibashi, M.; Maizel, J.V., Jr. The polypeptides of adenovirus. V. Young virions, structural intermediate between top components and aged virions. Virology 1974, 57, 409-424.
    • (1974) Virology , vol.57 , pp. 409-424
    • Ishibashi, M.1    Maizel, J.V.2
  • 48
    • 84912559464 scopus 로고    scopus 로고
    • Adenoviruses: Basic Biology to Gene Therapy; Seth, P., Ed.; R.G. Landes: Austin, TX, USA
    • Weber, J.M. Role of endoprotease in adenovirus infection. In Adenoviruses: Basic Biology to Gene Therapy; Seth, P., Ed.; R.G. Landes: Austin, TX, USA, 1999; pp. 79-83.
    • (1999) Role of Endoprotease in Adenovirus Infection , pp. 79-83
    • Weber, J.M.1
  • 49
    • 0028883978 scopus 로고
    • The adenovirus protease is required for virus entry into host cells
    • Cotten, M.; Weber, J.M. The adenovirus protease is required for virus entry into host cells. Virology 1995, 213, 494-502.
    • (1995) Virology , vol.213 , pp. 494-502
    • Cotten, M.1    Weber, J.M.2
  • 50
    • 56149117291 scopus 로고    scopus 로고
    • Infectious adenovirus type 2 transport through early but not late endosomes
    • Gastaldelli, M.; Imelli, N.; Boucke, K.; Amstutz, B.; Meier, O.; Greber, U.F. Infectious adenovirus type 2 transport through early but not late endosomes. Traffic 2008, 9, 2265-2278.
    • (2008) Traffic , vol.9 , pp. 2265-2278
    • Gastaldelli, M.1    Imelli, N.2    Boucke, K.3    Amstutz, B.4    Meier, O.5    Greber, U.F.6
  • 51
    • 0017237714 scopus 로고
    • Genetic analysis of adenovirus type 2 III. Temperature Sensitivity of Processing Viral Proteins
    • Weber, J. Genetic analysis of adenovirus type 2 III. Temperature sensitivity of processing viral proteins. J. Virol. 1976, 17, 462-471.
    • (1976) J. Virol , vol.17 , pp. 462-471
    • Weber, J.1
  • 52
    • 0030027458 scopus 로고    scopus 로고
    • Characterization of three components of human adenovirus proteinase activity in vitro
    • Mangel, W.F.; Toledo, D.L.; Brown, M.T.; Martin, J.H.; McGrath, W.J. Characterization of three components of human adenovirus proteinase activity in vitro. J. Biol. Chem. 1996, 271, 536-543.
    • (1996) J. Biol. Chem , vol.271 , pp. 536-543
    • Mangel, W.F.1    Toledo, D.L.2    Brown, M.T.3    Martin, J.H.4    McGrath, W.J.5
  • 54
    • 0019508862 scopus 로고
    • Processing of the adenovirus terminal protein
    • Challberg, M.D.; Kelly, T.J., Jr. Processing of the adenovirus terminal protein. J. Virol. 1981, 38, 272-277.
    • (1981) J. Virol , vol.38 , pp. 272-277
    • Challberg, M.D.1    Kelly, T.J.2
  • 55
    • 0242351787 scopus 로고    scopus 로고
    • Genetic content and evolution of adenoviruses
    • Davison, A.J.; Benkő, M.; Harrach, B. Genetic content and evolution of adenoviruses. J. Gen. Virol. 2003, 84, 2895-2908.
    • (2003) J. Gen. Virol , vol.84 , pp. 2895-2908
    • Davison, A.J.1    Benkő, M.2    Harrach, B.3
  • 56
    • 0027171113 scopus 로고
    • The active adenovirus protease is the intact L3 23K protein
    • Webster, A.; Kemp, G. The active adenovirus protease is the intact L3 23K protein. J. Gen. Virol. 1993, 74, 1415-1420.
    • (1993) J. Gen. Virol , vol.74 , pp. 1415-1420
    • Webster, A.1    Kemp, G.2
  • 57
    • 0025291078 scopus 로고
    • The proteinase polypeptide of adenovirus serotype 2 virions
    • Anderson, C.W. The proteinase polypeptide of adenovirus serotype 2 virions. Virology 1990, 177, 259-272.
    • (1990) Virology , vol.177 , pp. 259-272
    • Anderson, C.W.1
  • 58
    • 0030591441 scopus 로고    scopus 로고
    • Different modes of inhibition of human adenovirus proteinase, probably a cysteine proteinase, by bovine pancreatic trypsin inhibitor
    • Brown, M.T.; McGrath, W.J.; Toledo, D.L.; Mangel, W.F. Different modes of inhibition of human adenovirus proteinase, probably a cysteine proteinase, by bovine pancreatic trypsin inhibitor. FEBS Lett. 1996, 388, 233-237.
    • (1996) FEBS Lett , vol.388 , pp. 233-237
    • Brown, M.T.1    McGrath, W.J.2    Toledo, D.L.3    Mangel, W.F.4
  • 59
    • 15244353527 scopus 로고    scopus 로고
    • Interaction of the adenovirus major core protein precursor, pVII, with the viral DNA packaging machinery
    • Zhang, W.; Arcos, R. Interaction of the adenovirus major core protein precursor, pVII, with the viral DNA packaging machinery. Virology 2005, 334, 194-202.
    • (2005) Virology , vol.334 , pp. 194-202
    • Zhang, W.1    Arcos, R.2
  • 60
    • 84892462480 scopus 로고    scopus 로고
    • Processing of the L1 52/55k protein by the adenovirus protease: A new substrate and new insights into virion maturation
    • Pérez-Berná, A.J.; Mangel, W.F.; McGrath, W.J.; Graziano, V.; Flint, J.; San Martín, C. Processing of the L1 52/55k protein by the adenovirus protease: A new substrate and new insights into virion maturation. J. Virol. 2014, 88, 1513-1524.
    • (2014) J. Virol , vol.88 , pp. 1513-1524
    • Pérez-Berná, A.J.1    Mangel, W.F.2    McGrath, W.J.3    Graziano, V.4    Flint, J.5    San Martín, C.6
  • 62
    • 0027548474 scopus 로고
    • Expression and purification of the adenovirus proteinase polypeptide and of a synthetic proteinase substrate
    • Anderson, C.W. Expression and purification of the adenovirus proteinase polypeptide and of a synthetic proteinase substrate. Protein Express. Purif. 1993, 4, 8-15.
    • (1993) Protein Express. Purif , vol.4 , pp. 8-15
    • Anderson, C.W.1
  • 64
    • 0027509951 scopus 로고
    • The adenovirus protease is activated by a virus-coded disulphide-linked peptide
    • Webster, A.; Hay, R.T.; Kemp, G. The adenovirus protease is activated by a virus-coded disulphide-linked peptide. Cell 1993, 72, 97-104.
    • (1993) Cell , vol.72 , pp. 97-104
    • Webster, A.1    Hay, R.T.2    Kemp, G.3
  • 65
    • 0029070235 scopus 로고
    • Proline 137 is critical for adenovirus protease encapsidation and activation but not enzyme activity
    • Rancourt, C.; Keyvani-Amineh, H.; Sircar, S.; Labrecque, P.; Weber, J.M. Proline 137 is critical for adenovirus protease encapsidation and activation but not enzyme activity. Virology 1995, 209, 167-173.
    • (1995) Virology , vol.209 , pp. 167-173
    • Rancourt, C.1    Keyvani-Amineh, H.2    Sircar, S.3    Labrecque, P.4    Weber, J.M.5
  • 66
    • 70449378795 scopus 로고    scopus 로고
    • Genetic reconstitution of the human adenovirus type 2 temperature-sensitive 1 mutant defective in endosomal escape
    • Imelli, N.; Ruzsics, Z.; Puntener, D.; Gastaldelli, M.; Greber, U.F. Genetic reconstitution of the human adenovirus type 2 temperature-sensitive 1 mutant defective in endosomal escape. Virol. J. 2009, 6, 174.
    • (2009) Virol. J , vol.6 , pp. 174
    • Imelli, N.1    Ruzsics, Z.2    Puntener, D.3    Gastaldelli, M.4    Greber, U.F.5
  • 67
    • 16944366766 scopus 로고    scopus 로고
    • Cleavage efficiency by adenovirus protease is site-dependent
    • Diouri, M.; Keyvani-Amineh, H.; Geoghegan, K.F.; Weber, J.M. Cleavage efficiency by adenovirus protease is site-dependent. J. Biol. Chem. 1996, 271, 32511-32514.
    • (1996) J. Biol. Chem , vol.271 , pp. 32511-32514
    • Diouri, M.1    Keyvani-Amineh, H.2    Geoghegan, K.F.3    Weber, J.M.4
  • 68
    • 0024817679 scopus 로고
    • Characterization of the adenovirus proteinase: Substrate specificity
    • Webster, A.; Russell, S.; Talbot, P.; Russell, W.C.; Kemp, G.D. Characterization of the adenovirus proteinase: Substrate specificity. J. Gen. Virol. 1989, 70, 3225-3234.
    • (1989) J. Gen. Virol , vol.70 , pp. 3225-3234
    • Webster, A.1    Russell, S.2    Talbot, P.3    Russell, W.C.4    Kemp, G.D.5
  • 69
    • 0030808927 scopus 로고    scopus 로고
    • Role of preterminal protein processing in adenovirus replication
    • Webster, A.; Leith, I.R.; Nicholson, J.; Hounsell, J.; Hay, R.T. Role of preterminal protein processing in adenovirus replication. J. Virol. 1997, 71, 6381-6389.
    • (1997) J. Virol , vol.71 , pp. 6381-6389
    • Webster, A.1    Leith, I.R.2    Nicholson, J.3    Hounsell, J.4    Hay, R.T.5
  • 70
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: A novel method for fast and accurate multiple sequence alignment
    • Notredame, C.; Higgins, D.G.; Heringa, J. T-Coffee: A novel method for fast and accurate multiple sequence alignment. J. Mol. Biol. 2000, 302, 205-217.
    • (2000) J. Mol. Biol , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.G.2    Heringa, J.3
  • 71
    • 65449188232 scopus 로고    scopus 로고
    • Jalview Version 2-A multiple sequence alignment editor and analysis workbench
    • Waterhouse, A.M.; Procter, J.B.; Martin, D.M.; Clamp, M.; Barton, G.J. Jalview Version 2-A multiple sequence alignment editor and analysis workbench. Bioinformatics 2009, 25, 1189-1191.
    • (2009) Bioinformatics , vol.25 , pp. 1189-1191
    • Waterhouse, A.M.1    Procter, J.B.2    Martin, D.M.3    Clamp, M.4    Barton, G.J.5
  • 72
    • 0020679785 scopus 로고
    • Rhodamine-based compounds as fluorogenic substrates for serine proteases
    • Leytus, S.P.; Melhado, L.L.; Mangel, W.F. Rhodamine-based compounds as fluorogenic substrates for serine proteases. Biochem. J. 1983, 209, 299-307.
    • (1983) Biochem. J , vol.209 , pp. 299-307
    • Leytus, S.P.1    Melhado, L.L.2    Mangel, W.F.3
  • 73
    • 0020852609 scopus 로고
    • New class of sensitive, specific, and selective substrates for serine proteinases: Fluorogenic, amino acid peptide derivatives of Rhodamine
    • Leytus, S.P.; Patterson, W.L.; Mangel, W.F. New class of sensitive, specific, and selective substrates for serine proteinases: Fluorogenic, amino acid peptide derivatives of Rhodamine. Biochem. J. 1983, 215, 253-260.
    • (1983) Biochem. J , vol.215 , pp. 253-260
    • Leytus, S.P.1    Patterson, W.L.2    Mangel, W.F.3
  • 74
    • 0024831007 scopus 로고
    • Characterization of the adenovirus proteinase; development and use of a specific peptide assay
    • Webster, A.; Russell, W.C.; Kemp, G.D. Characterization of the adenovirus proteinase; development and use of a specific peptide assay. J. Gen. Virol. 1989, 70, 3215-3223.
    • (1989) J. Gen. Virol , vol.70 , pp. 3215-3223
    • Webster, A.1    Russell, W.C.2    Kemp, G.D.3
  • 75
    • 0027390796 scopus 로고
    • Viral DNA and a viral peptide can act as cofactors of adenovirus virion proteinase activity
    • Mangel, W.F.; McGrath, W.J.; Toledo, D.L.; Anderson, C.W. Viral DNA and a viral peptide can act as cofactors of adenovirus virion proteinase activity. Nature 1993, 361, 274-275.
    • (1993) Nature , vol.361 , pp. 274-275
    • Mangel, W.F.1    McGrath, W.J.2    Toledo, D.L.3    Anderson, C.W.4
  • 76
    • 0029913726 scopus 로고    scopus 로고
    • Characterization of human adenovirus proteinase activity in disrupted virus particles
    • McGrath, W.J.; Abola, A.P.; Toledo, D.L.; Brown, M.T.; Mangel, W.F. Characterization of human adenovirus proteinase activity in disrupted virus particles. Virology 1996, 217, 131-138.
    • (1996) Virology , vol.217 , pp. 131-138
    • McGrath, W.J.1    Abola, A.P.2    Toledo, D.L.3    Brown, M.T.4    Mangel, W.F.5
  • 77
    • 20544448487 scopus 로고    scopus 로고
    • Interaction of the adenovirus proteinase with protein cofactors with high negative charge densities
    • Bajpayee, N.S.; McGrath, W.J.; Mangel, W.F. Interaction of the adenovirus proteinase with protein cofactors with high negative charge densities. Biochemistry 2005, 44, 8721-8729.
    • (2005) Biochemistry , vol.44 , pp. 8721-8729
    • Bajpayee, N.S.1    McGrath, W.J.2    Mangel, W.F.3
  • 79
    • 0028983898 scopus 로고
    • Crystal structure of a conserved protease that binds DNA: The bleomycin hydrolase, Gal6
    • Joshua-Tor, L.; Xu, H.E.; Johnston, S.A.; Rees, D.C. Crystal structure of a conserved protease that binds DNA: The bleomycin hydrolase, Gal6. Science 1995, 269, 945-950.
    • (1995) Science , vol.269 , pp. 945-950
    • Joshua-Tor, L.1    Xu, H.E.2    Johnston, S.A.3    Rees, D.C.4
  • 80
    • 0023003219 scopus 로고
    • Progressive reorganization of the host cell cytoskeleton during adenovirus infection
    • Staufenbiel, M.; Epple, P.; Deppert, W. Progressive reorganization of the host cell cytoskeleton during adenovirus infection. J. Virol. 1986, 60, 1186-1191.
    • (1986) J. Virol , vol.60 , pp. 1186-1191
    • Staufenbiel, M.1    Epple, P.2    Deppert, W.3
  • 81
    • 0027167564 scopus 로고
    • The adenovirus L3 23-Kilodalton proteinase cleaves the amino-terminal head domain from cytokeratin 18 and disrupts the cytokeratin network of HeLa cells
    • Chen, P.H.; Ornelles, D.A.; Shenk, T. The adenovirus L3 23-Kilodalton proteinase cleaves the amino-terminal head domain from cytokeratin 18 and disrupts the cytokeratin network of HeLa cells. J. Virol. 1993, 67, 3507-3514.
    • (1993) J. Virol , vol.67 , pp. 3507-3514
    • Chen, P.H.1    Ornelles, D.A.2    Shenk, T.3
  • 82
    • 2242494519 scopus 로고    scopus 로고
    • Actin can act as a cofactor for a viral proteinase, in the cleavage of the cytoskeleton
    • Brown, M.T.; McBride, K.M.; Baniecki, M.L.; Reich, N.C.; Marriott, G.; Mangel, W.F. Actin can act as a cofactor for a viral proteinase, in the cleavage of the cytoskeleton. J. Biol. Chem. 2002, 277, 46298-46303.
    • (2002) J. Biol. Chem , vol.277 , pp. 46298-46303
    • Brown, M.T.1    McBride, K.M.2    Baniecki, M.L.3    Reich, N.C.4    Marriott, G.5    Mangel, W.F.6
  • 84
    • 0019419218 scopus 로고
    • Gene and mRNA for precursor polypeptide VI from adenovirus type 2
    • Akusjarvi, G.; Persson, H.J. Gene and mRNA for precursor polypeptide VI from adenovirus type 2. J. Virol. 1981, 38, 469-482.
    • (1981) J. Virol , vol.38 , pp. 469-482
    • Akusjarvi, G.1    Persson, H.J.2
  • 85
    • 0027217232 scopus 로고
    • Organization of the avian adenovirus genome and the structure of its endopeptidase
    • Cai, F.; Weber, J.M. Organization of the avian adenovirus genome and the structure of its endopeptidase. Virology 1993, 196, 358-362.
    • (1993) Virology , vol.196 , pp. 358-362
    • Cai, F.1    Weber, J.M.2
  • 86
    • 0030198630 scopus 로고    scopus 로고
    • Preparation and crystallization of a complex between human adenovirus serotype 2 proteinase and its 11-amino-acid cofactor pVIc
    • McGrath, W.J.; Ding, J.; Sweet, R.M.; Mangel, W.F. Preparation and crystallization of a complex between human adenovirus serotype 2 proteinase and its 11-amino-acid cofactor pVIc. J. Struct. Biol. 1996, 117, 77-79.
    • (1996) J. Struct. Biol , vol.117 , pp. 77-79
    • McGrath, W.J.1    Ding, J.2    Sweet, R.M.3    Mangel, W.F.4
  • 87
    • 0029914251 scopus 로고    scopus 로고
    • Crystal structure of the human adenovirus proteinase with its 11 amino acid cofactor
    • Ding, J.; McGrath, W.J.; Sweet, R.M.; Mangel, W.F. Crystal structure of the human adenovirus proteinase with its 11 amino acid cofactor. EMBO J. 1996, 15, 1778-1783.
    • (1996) EMBO J , vol.15 , pp. 1778-1783
    • Ding, J.1    McGrath, W.J.2    Sweet, R.M.3    Mangel, W.F.4
  • 88
    • 0038644484 scopus 로고    scopus 로고
    • Crystallographic structure at 1.6-Å resolution of the human adenovirus proteinase in a covalent complex with its 11-amino-acid peptide cofactor: Insights on a new fold
    • McGrath, W.J.; Ding, J.; Sweet, R.M.; Mangel, W.F. Crystallographic structure at 1.6-Å resolution of the human adenovirus proteinase in a covalent complex with its 11-amino-acid peptide cofactor: Insights on a new fold. Biochem. Biophys. Acta 2003, 1648, 1-11.
    • (2003) Biochem. Biophys. Acta , vol.1648 , pp. 1-11
    • McGrath, W.J.1    Ding, J.2    Sweet, R.M.3    Mangel, W.F.4
  • 89
    • 0030807451 scopus 로고    scopus 로고
    • Temporal and spatial control of the adenovirus proteinase by both a peptide and the viral DNA
    • Mangel, W.F.; Toledo, D.L.; Ding, J.; Sweet, R.M.; McGrath, W.J. Temporal and spatial control of the adenovirus proteinase by both a peptide and the viral DNA. Trends Biochem. Sci. 1997, 22, 393-398.
    • (1997) Trends Biochem. Sci , vol.22 , pp. 393-398
    • Mangel, W.F.1    Toledo, D.L.2    Ding, J.3    Sweet, R.M.4    McGrath, W.J.5
  • 91
    • 0028674466 scopus 로고
    • Catalytic mechanism in papain family of cysteine peptidases
    • Storer, A.C.; Menard, R. Catalytic mechanism in papain family of cysteine peptidases. Methods Enzymol. 1994, 244, 486-500.
    • (1994) Methods Enzymol , vol.244 , pp. 486-500
    • Storer, A.C.1    Menard, R.2
  • 92
    • 0015497445 scopus 로고
    • Subtilisin; a stereochemical mechanism involving transition-state stabilization
    • Robertus, J.D.; Kraut, J.; Alden, R.A.; Birktoft, J.J. Subtilisin; a stereochemical mechanism involving transition-state stabilization. Biochemistry 1972, 11, 4293-4303.
    • (1972) Biochemistry , vol.11 , pp. 4293-4303
    • Robertus, J.D.1    Kraut, J.2    Alden, R.A.3    Birktoft, J.J.4
  • 93
    • 0017138215 scopus 로고
    • Binding of chloromethyl ketone substrate analogues to crystalline papain
    • Drenth, J.; Kalk, K.H.; Swen, H.M. Binding of chloromethyl ketone substrate analogues to crystalline papain. Biochemistry 1976, 15, 3731-3738.
    • (1976) Biochemistry , vol.15 , pp. 3731-3738
    • Drenth, J.1    Kalk, K.H.2    Swen, H.M.3
  • 94
    • 84872735707 scopus 로고    scopus 로고
    • Regulation of a viral proteinase by a peptide and DNA in one-dimensional space: III. Atomic resolution structure of the nascent form of the adenovirus proteinase
    • Baniecki, M.L.; McGrath, W.J.; Mangel, W.F. Regulation of a viral proteinase by a peptide and DNA in one-dimensional space: III. Atomic resolution structure of the nascent form of the adenovirus proteinase. J. Biol. Chem. 2013, 288, 2081-2091.
    • (2013) J. Biol. Chem , vol.288 , pp. 2081-2091
    • Baniecki, M.L.1    McGrath, W.J.2    Mangel, W.F.3
  • 96
    • 25144463726 scopus 로고    scopus 로고
    • Mapping a functional viral protein in solution using synchrotron X-ray footprinting technology
    • Gupta, S.; Mangel, W.F.; Sullivan, M.; Takamoto, K.G.; Chance, M.R. Mapping a functional viral protein in solution using synchrotron X-ray footprinting technology. Synchrotron Radiat. News 2005, 18, 25-34.
    • (2005) Synchrotron Radiat. News , vol.18 , pp. 25-34
    • Gupta, S.1    Mangel, W.F.2    Sullivan, M.3    Takamoto, K.G.4    Chance, M.R.5
  • 99
    • 0035807868 scopus 로고    scopus 로고
    • Roles of two conserved cysteine residues in the activation of human adenovirus proteinase
    • McGrath, W.J.; Baniecki, M.L.; Peters, E.; Green, D.T.; Mangel, W.F. Roles of two conserved cysteine residues in the activation of human adenovirus proteinase. Biochemistry 2001, 40, 14468-14474.
    • (2001) Biochemistry , vol.40 , pp. 14468-14474
    • McGrath, W.J.1    Baniecki, M.L.2    Peters, E.3    Green, D.T.4    Mangel, W.F.5
  • 100
    • 0036292317 scopus 로고    scopus 로고
    • In the virion, the 11-amino-acid peptide cofactor pVIc is covalently linked to the adenovirus proteinase
    • McGrath, W.J.; Aherne, K.S.; Mangel, W.F. In the virion, the 11-amino-acid peptide cofactor pVIc is covalently linked to the adenovirus proteinase. Virology 2002, 296, 234-240.
    • (2002) Virology , vol.296 , pp. 234-240
    • McGrath, W.J.1    Aherne, K.S.2    Mangel, W.F.3
  • 101
    • 0032479179 scopus 로고    scopus 로고
    • Anatomy of hot spots in protein interfaces
    • Bogan, A.A.; Thorn, K.S. Anatomy of hot spots in protein interfaces. J. Mol. Biol. 1998, 280, 1-9.
    • (1998) J. Mol. Biol , vol.280 , pp. 1-9
    • Bogan, A.A.1    Thorn, K.S.2
  • 102
    • 0020426755 scopus 로고
    • Nucleic acid-binding properties of adenovirus structural polypeptides
    • Russell, W.C.; Precious, B. Nucleic acid-binding properties of adenovirus structural polypeptides. J. Gen. Virol. 1982, 63, 69-79.
    • (1982) J. Gen. Virol , vol.63 , pp. 69-79
    • Russell, W.C.1    Precious, B.2
  • 103
    • 0017146579 scopus 로고
    • Ion effects on ligand-nucleic acid interactions
    • Record, M.T., Jr.; Lohman, M.L.; de Haseth, P. Ion effects on ligand-nucleic acid interactions. J. Mol. Biol. 1976, 107, 145-158.
    • (1976) J. Mol. Biol , vol.107 , pp. 145-158
    • Record, M.T.1    Lohman, M.L.2    de Haseth, P.3
  • 104
    • 84872701041 scopus 로고    scopus 로고
    • Regulation of a viral proteinase by a peptide and DNA in one-dimensional space: I. Binding to DNA and to hexon of the precursor to protein VI, pVI, of human adenovirus
    • Graziano, V.; McGrath, W.J.; Suomalainen, M.; Greber, U.F.; Freimuth, P.; Blainey, P.C.; Luo, G.; Xie, X.S.; Mangel, W.F. Regulation of a viral proteinase by a peptide and DNA in one-dimensional space: I. Binding to DNA and to hexon of the precursor to protein VI, pVI, of human adenovirus. J. Biol. Chem. 2013, 288, 2059-2067.
    • (2013) J. Biol. Chem , vol.288 , pp. 2059-2067
    • Graziano, V.1    McGrath, W.J.2    Suomalainen, M.3    Greber, U.F.4    Freimuth, P.5    Blainey, P.C.6    Luo, G.7    Xie, X.S.8    Mangel, W.F.9
  • 105
    • 0002917513 scopus 로고    scopus 로고
    • Principles of virion structure, function and assembly
    • Chiu, W., Burnett, R.M., Garcea, R.L., Eds.; Oxford University Press: Oxford, UK
    • Casjens, S. Principles of virion structure, function and assembly. In Structural Biology of Viruses; Chiu, W., Burnett, R.M., Garcea, R.L., Eds.; Oxford University Press: Oxford, UK, 1997; pp. 3-37.
    • (1997) Structural Biology of Viruses , pp. 3-37
    • Casjens, S.1
  • 106
    • 0042823481 scopus 로고    scopus 로고
    • Transport of nucleosome core particles in semidilute DNA solutions
    • Mangenot, S.; Keller, S.; Radler, J. Transport of nucleosome core particles in semidilute DNA solutions. Biophys. J. 2003, 85, 1817-1825.
    • (2003) Biophys. J , vol.85 , pp. 1817-1825
    • Mangenot, S.1    Keller, S.2    Radler, J.3
  • 107
    • 59849102099 scopus 로고    scopus 로고
    • Adenoviruses: Update on structure and function
    • Russell, W.C. Adenoviruses: Update on structure and function. J. Gen. Virol. 2009, 90, 1-20.
    • (2009) J. Gen. Virol , vol.90 , pp. 1-20
    • Russell, W.C.1
  • 108
    • 84872699552 scopus 로고    scopus 로고
    • Regulation of a viral proteinase by a peptide and DNA in one-dimensional space: II. Adenovirus Proteinase is Activated in an Unusual One-dimensional Biochemical Reaction.
    • Graziano, V.; Luo, G.; Blainey, P.C.; Pérez-Berná, A.J.; McGrath, W.J.; Flint, S.J.; San Martín, C.; Xie, X.S.; Mangel, W.F. Regulation of a viral proteinase by a peptide and DNA in one-dimensional space: II. Adenovirus proteinase is activated in an unusual one-dimensional biochemical reaction. J. Biol. Chem. 2013, 288, 2068-2080.
    • (2013) J. Biol. Chem , vol.288 , pp. 2068-2080
    • Graziano, V.1    Luo, G.2    Blainey, P.C.3    Pérez-Berná, A.J.4    McGrath, W.J.5    Flint, S.J.6    San Martín, C.7    Xie, X.S.8    Mangel, W.F.9
  • 109
    • 0028099728 scopus 로고
    • Activation of adenovirus-coded protease and processing of preterminal protein
    • Webster, A.; Leith, I.R.; Hay, R.T. Activation of adenovirus-coded protease and processing of preterminal protein. J. Virol. 1994, 68, 7292-7300.
    • (1994) J. Virol , vol.68 , pp. 7292-7300
    • Webster, A.1    Leith, I.R.2    Hay, R.T.3
  • 110
    • 0023041995 scopus 로고
    • Identification of proteins and protein domains that contact DNA within adenovirus nucleoprotein cores by ultraviolet light crosslinking of oligonucleotides 32P-labelled in vivo
    • Chatterjee, P.K.; Vayda, M.E.; Flint, S.J. Identification of proteins and protein domains that contact DNA within adenovirus nucleoprotein cores by ultraviolet light crosslinking of oligonucleotides 32P-labelled in vivo. J. Mol. Biol. 1986, 188, 23-37.
    • (1986) J. Mol. Biol , vol.188 , pp. 23-37
    • Chatterjee, P.K.1    Vayda, M.E.2    Flint, S.J.3
  • 111
    • 0031792462 scopus 로고    scopus 로고
    • Virus assembly and disassembly: The adenovirus cysteine protease as a trigger factor
    • Greber, U.F. Virus assembly and disassembly: The adenovirus cysteine protease as a trigger factor. Rev. Med. Virol. 1998, 8, 213-222.
    • (1998) Rev. Med. Virol , vol.8 , pp. 213-222
    • Greber, U.F.1
  • 115
    • 0029131248 scopus 로고
    • Adenovirus infections in human immunodeficiency virus-positive patients: Clinical features and molecular epidemiology
    • Kohoo, S.H.; Bailey, A.S.; de Jong, J.C.; Mandal, B.K. Adenovirus infections in human immunodeficiency virus-positive patients: Clinical features and molecular epidemiology. J. Infect. Dis. 1995, 172, 629-637.
    • (1995) J. Infect. Dis , vol.172 , pp. 629-637
    • Kohoo, S.H.1    Bailey, A.S.2    de Jong, J.C.3    Mandal, B.K.4
  • 116
    • 0014260341 scopus 로고
    • Mycoplasma pneumonia and adenovirus respiratory illnesses in military and university personnel
    • Mogabgab, W.J. Mycoplasma pneumonia and adenovirus respiratory illnesses in military and university personnel. Am. Rev. Respir. Dis. 1968, 97, 345-358.
    • (1968) Am. Rev. Respir. Dis , vol.97 , pp. 345-358
    • Mogabgab, W.J.1
  • 119
    • 38449108684 scopus 로고    scopus 로고
    • Acute respiratory disease associated with adenovirus serotype 14-Four states, 2006-2007
    • Centers for Disease Control and Prevention (CDC). Acute respiratory disease associated with adenovirus serotype 14-Four states, 2006-2007. MMWR 2007, 56, 1181-1184.
    • (2007) MMWR , vol.56 , pp. 1181-1184
    • Centers for Disease Control and Prevention (CDC)1
  • 121
    • 0034934692 scopus 로고    scopus 로고
    • A new form of antiviral combination therapy predicted to prevent resistance from arising, and a model system to test it
    • Mangel, W.F.; McGrath, W.J.; Brown, M.T.; Baniecki, M.L.; Barnard, D.L.; Pang, Y.P. A new form of antiviral combination therapy predicted to prevent resistance from arising, and a model system to test it. Curr. Med. Chem. 2001, 8, 933-939.
    • (2001) Curr. Med. Chem , vol.8 , pp. 933-939
    • Mangel, W.F.1    McGrath, W.J.2    Brown, M.T.3    Baniecki, M.L.4    Barnard, D.L.5    Pang, Y.P.6
  • 122
    • 0004545922 scopus 로고    scopus 로고
    • Adenovirus proteinase-antiviral target for triple-combination therapy on a single enzyme: Potential inhibitor-binding sites
    • von der Helm, K., Korant, B.D., Cheronis, J.C., Eds.; Springer: Berlin, Germany
    • Mangel, W.F.; Toledo, D.L.; Brown, M.T.; Ding, J.; Sweet, R.M.; Barnard, D.L.; McGrath, W.J. Adenovirus proteinase-antiviral target for triple-combination therapy on a single enzyme: Potential inhibitor-binding sites. In Proteases as Targets for Therapy; von der Helm, K., Korant, B.D., Cheronis, J.C., Eds.; Springer: Berlin, Germany, 2000; Volume 140, pp. 145-158.
    • (2000) Proteases as Targets For Therapy , vol.140 , pp. 145-158
    • Mangel, W.F.1    Toledo, D.L.2    Brown, M.T.3    Ding, J.4    Sweet, R.M.5    Barnard, D.L.6    McGrath, W.J.7
  • 123
    • 0035800608 scopus 로고    scopus 로고
    • Discovery of a new inhibitor lead of adenovirus proteinase: Steps toward selective, irreversible inhibitors of cysteine proteinases
    • Pang, Y.-P.; Xu, K.; Kollmeyer, T.M.; Perola, E.; McGrath, W.J.; Green, D.T.; Mangel, W.F. Discovery of a new inhibitor lead of adenovirus proteinase: Steps toward selective, irreversible inhibitors of cysteine proteinases. FEBS Lett. 2001, 502, 93-97.
    • (2001) FEBS Lett , vol.502 , pp. 93-97
    • Pang, Y.-P.1    Xu, K.2    Kollmeyer, T.M.3    Perola, E.4    McGrath, W.J.5    Green, D.T.6    Mangel, W.F.7
  • 124
    • 84880700914 scopus 로고    scopus 로고
    • First generation inhibitors of the adenovirus proteinase
    • McGrath, W.J.; Graziano, V.; Mangel, W.F. First generation inhibitors of the adenovirus proteinase. FEBS Lett. 2013, 587, 2332-2339.
    • (2013) FEBS Lett , vol.587 , pp. 2332-2339
    • McGrath, W.J.1    Graziano, V.2    Mangel, W.F.3
  • 126
    • 77951298327 scopus 로고    scopus 로고
    • Virus particle maturation: Insights into elegantly programmed nanomachines
    • Johnson, J.E. Virus particle maturation: Insights into elegantly programmed nanomachines. Curr. Opin. Struct. Biol. 2010, 20, 210-216.
    • (2010) Curr. Opin. Struct. Biol , vol.20 , pp. 210-216
    • Johnson, J.E.1
  • 127
    • 67650912075 scopus 로고    scopus 로고
    • Cryo-electron microscopy structure of adenovirus type 2 temperature-sensitive mutant 1 reveals insight into the cell entry defect
    • Silvestry, M.; Lindert, S.; Smith, J.G.; Maier, O.; Wiethoff, C.M.; Nemerow, G.R.; Stewart, P.L. Cryo-electron microscopy structure of adenovirus type 2 temperature-sensitive mutant 1 reveals insight into the cell entry defect. J. Virol. 2009, 83, 7375-7383.
    • (2009) J. Virol , vol.83 , pp. 7375-7383
    • Silvestry, M.1    Lindert, S.2    Smith, J.G.3    Maier, O.4    Wiethoff, C.M.5    Nemerow, G.R.6    Stewart, P.L.7
  • 129
    • 84898007672 scopus 로고    scopus 로고
    • The cleaved N-terminus of pVI binds peripentonal hexons in mature adenovirus
    • Snijder, J.; Benevento, M.; Moyer, C.L.; Reddy, V.; Nemerow, G.R.; Heck, A.J. The cleaved N-terminus of pVI binds peripentonal hexons in mature adenovirus. J. Mol. Biol. 2014, 426, 1971-1979.
    • (2014) J. Mol. Biol , vol.426 , pp. 1971-1979
    • Snijder, J.1    Benevento, M.2    Moyer, C.L.3    Reddy, V.4    Nemerow, G.R.5    Heck, A.J.6
  • 130
    • 0020570655 scopus 로고
    • Biological and structural studies with an adenovirus type 2 temperature-sensitive mutant defective for uncoating
    • Hannan, C.; Raptis, L.H.; Dery, C.V.; Weber, J. Biological and structural studies with an adenovirus type 2 temperature-sensitive mutant defective for uncoating. Intervirology 1983, 19, 213-223.
    • (1983) Intervirology , vol.19 , pp. 213-223
    • Hannan, C.1    Raptis, L.H.2    Dery, C.V.3    Weber, J.4
  • 132
    • 34147123766 scopus 로고    scopus 로고
    • DNA packaging and delivery machines in tailed bacteriophages
    • Johnson, J.E.; Chiu, W. DNA packaging and delivery machines in tailed bacteriophages. Curr. Opin. Struct. Biol. 2007, 17, 237-243.
    • (2007) Curr. Opin. Struct. Biol , vol.17 , pp. 237-243
    • Johnson, J.E.1    Chiu, W.2
  • 133
    • 0036403802 scopus 로고    scopus 로고
    • Poliovirus cell entry: Common structural themes in viral cell entry pathways
    • Hogle, J.M. Poliovirus cell entry: Common structural themes in viral cell entry pathways. Annu. Rev. Microbiol. 2002, 56, 677-702.
    • (2002) Annu. Rev. Microbiol , vol.56 , pp. 677-702
    • Hogle, J.M.1
  • 135
    • 34247116994 scopus 로고    scopus 로고
    • Sensing infection by adenovirus: Toll-like receptor-independent viral DNA recognition signals activation of the interferon regulatory factor 3 master regulator
    • Nociari, M.; Ocheretina, O.; Schoggins, J.W.; Falck-Pedersen, E. Sensing infection by adenovirus: Toll-like receptor-independent viral DNA recognition signals activation of the interferon regulatory factor 3 master regulator. J. Virol. 2007, 81, 4145-4157.
    • (2007) J. Virol , vol.81 , pp. 4145-4157
    • Nociari, M.1    Ocheretina, O.2    Schoggins, J.W.3    Falck-Pedersen, E.4
  • 136
    • 0029816095 scopus 로고    scopus 로고
    • Interaction of the adenovirus L1 52/55-kilodalton protein with the IVa2 gene product during infection
    • Gustin, K.E.; Lutz, P.; Imperiale, M.J. Interaction of the adenovirus L1 52/55-kilodalton protein with the IVa2 gene product during infection. J. Virol. 1996, 70, 6463-6467.
    • (1996) J. Virol , vol.70 , pp. 6463-6467
    • Gustin, K.E.1    Lutz, P.2    Imperiale, M.J.3
  • 137
    • 0017736844 scopus 로고
    • Identification of a protein linked to the ends of adenovirus DNA
    • Rekosh, D.M.; Russell, W.C.; Bellet, A.J.; Robinson, A.J. Identification of a protein linked to the ends of adenovirus DNA. Cell 1977, 11, 283-295.
    • (1977) Cell , vol.11 , pp. 283-295
    • Rekosh, D.M.1    Russell, W.C.2    Bellet, A.J.3    Robinson, A.J.4
  • 138
    • 0019486414 scopus 로고
    • Identification of the gene and mRNA for the adenovirus terminal protein precursor
    • Stillman, B.W.; Lewis, J.B.; Chow, L.T.; Mathews, M.B.; Smart, J.E. Identification of the gene and mRNA for the adenovirus terminal protein precursor. Cell 1981, 23, 497-508.
    • (1981) Cell , vol.23 , pp. 497-508
    • Stillman, B.W.1    Lewis, J.B.2    Chow, L.T.3    Mathews, M.B.4    Smart, J.E.5
  • 139
    • 0037270043 scopus 로고    scopus 로고
    • Adenovirus DNA replication
    • Current Topics in Microbiology and Immunology; Doerfler, W., Böhm, P., Eds.; Springer-Verlag: Heidelberg, Germany
    • Liu, H.; Naismith, J.H.; Hay, R.T. Adenovirus DNA replication. In Adenoviruses: Model and Vectors in Virus Host Interactions. Current Topics in Microbiology and Immunology; Doerfler, W., Böhm, P., Eds.; Springer-Verlag: Heidelberg, Germany, 2003; Volume 272, pp. 131-164.
    • (2003) In Adenoviruses: Model and Vectors in Virus Host Interactions , vol.272 , pp. 131-164
    • Liu, H.1    Naismith, J.H.2    Hay, R.T.3
  • 141
    • 0027985452 scopus 로고
    • A precursor terminal protein-trinucleotide intermediate during initiation of adenovirus DNA replication: Regeneration of molecular ends in vitro by a jumping back mechanism
    • King, A.J.; van der Vliet, P.C. A precursor terminal protein-trinucleotide intermediate during initiation of adenovirus DNA replication: Regeneration of molecular ends in vitro by a jumping back mechanism. EMBO J. 1994, 13, 5786-5792.
    • (1994) EMBO J , vol.13 , pp. 5786-5792
    • King, A.J.1    van der Vliet, P.C.2
  • 142
    • 0027066923 scopus 로고
    • Adenovirus DNA replication: The function of the covalently bound terminal protein
    • Pronk, R.; Stuiver, M.H.; van der Vliet, P.C. Adenovirus DNA replication: The function of the covalently bound terminal protein. Chromosoma 1992, 102, S39-S45.
    • (1992) Chromosoma , vol.102 , pp. S39-S45
    • Pronk, R.1    Stuiver, M.H.2    van der Vliet, P.C.3
  • 143
    • 84870689285 scopus 로고    scopus 로고
    • Reduced infectivity of adenovirus type 5 particles and degradation of entering viral genomes associated with incomplete processing of the preterminal protein
    • Kato, S.E.; Chahal, J.S.; Flint, S.J. Reduced infectivity of adenovirus type 5 particles and degradation of entering viral genomes associated with incomplete processing of the preterminal protein. J. Virol. 2012, 86, 13554-13565.
    • (2012) J. Virol , vol.86 , pp. 13554-13565
    • Kato, S.E.1    Chahal, J.S.2    Flint, S.J.3
  • 144
    • 84912566327 scopus 로고    scopus 로고
    • Cryo-EM enters a new era
    • Kuhlbrandt, W. Cryo-EM enters a new era. eLife 2014, 3, e03678.
    • (2014) eLife , vol.3
    • Kuhlbrandt, W.1
  • 145
    • 80052098908 scopus 로고    scopus 로고
    • Modern biomolecular mass spectrometry and its role in studying virus structure, dynamics, and assembly
    • Uetrecht, C.; Heck, A.J. Modern biomolecular mass spectrometry and its role in studying virus structure, dynamics, and assembly. Angew. Chem. Int. Ed. Engl. 2011, 50, 8248-8262.
    • (2011) Angew. Chem. Int. Ed. Engl , vol.50 , pp. 8248-8262
    • Uetrecht, C.1    Heck, A.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.