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Volumn 16, Issue 8, 2014, Pages 1179-1200

An L2 SUMO interacting motif is important for PML localization and infection of human papillomavirus type 16

Author keywords

[No Author keywords available]

Indexed keywords

L1 PROTEIN; L2 PROTEIN; PROMYELOCYTIC LEUKEMIA PROTEIN; SUMO PROTEIN; UNCLASSIFIED DRUG; VIRUS PROTEIN; CAPSID PROTEIN; L2 PROTEIN, HUMAN PAPILLOMAVIRUS TYPE 16; NUCLEAR PROTEIN; ONCOPROTEIN; PML PROTEIN, HUMAN; SUMO 1 PROTEIN; SUMO2 PROTEIN, HUMAN; TRANSCRIPTION FACTOR; TUMOR SUPPRESSOR PROTEIN; VIRUS ANTIGEN; ZINC FINGER PROTEIN;

EID: 84904986129     PISSN: 14625814     EISSN: 14625822     Source Type: Journal    
DOI: 10.1111/cmi.12271     Document Type: Article
Times cited : (29)

References (98)
  • 1
    • 0026329210 scopus 로고
    • Structures of bovine and human papillomaviruses. Analysis by cryoelectron microscopy and three-dimensional image reconstruction
    • Baker, T.S., Newcomb, W.W., Olson, N.H., Cowsert, L.M., Olson, C., and Brown, J.C. (1991) Structures of bovine and human papillomaviruses. Analysis by cryoelectron microscopy and three-dimensional image reconstruction. Biophys J 60: 1445-1456.
    • (1991) Biophys J , vol.60 , pp. 1445-1456
    • Baker, T.S.1    Newcomb, W.W.2    Olson, N.H.3    Cowsert, L.M.4    Olson, C.5    Brown, J.C.6
  • 2
    • 0141680274 scopus 로고    scopus 로고
    • Dissection of human papillomavirus type 33L2 domains involved in nuclear domains (ND) 10 homing and reorganization
    • Becker, K.A., Florin, L., Sapp, C., and Sapp, M. (2003) Dissection of human papillomavirus type 33L2 domains involved in nuclear domains (ND) 10 homing and reorganization. Virology 314: 161-167.
    • (2003) Virology , vol.314 , pp. 161-167
    • Becker, K.A.1    Florin, L.2    Sapp, C.3    Sapp, M.4
  • 3
    • 0347634431 scopus 로고    scopus 로고
    • Nuclear localization but not PML protein is required for incorporation of the papillomavirus minor capsid protein L2 into virus-like particles
    • Becker, K.A., Florin, L., Sapp, C., Maul, G.G., and Sapp, M. (2004) Nuclear localization but not PML protein is required for incorporation of the papillomavirus minor capsid protein L2 into virus-like particles. J Virol 78: 1121-1128.
    • (2004) J Virol , vol.78 , pp. 1121-1128
    • Becker, K.A.1    Florin, L.2    Sapp, C.3    Maul, G.G.4    Sapp, M.5
  • 4
    • 70049114748 scopus 로고    scopus 로고
    • Target cell cyclophilins facilitate human papillomavirus type 16 infection
    • Bienkowska-Haba, M., Patel, H.D., and Sapp, M. (2009a) Target cell cyclophilins facilitate human papillomavirus type 16 infection. PLoS Pathog 5: e1000524.
    • (2009) PLoS Pathog , vol.5
    • Bienkowska-Haba, M.1    Patel, H.D.2    Sapp, M.3
  • 5
    • 70049114748 scopus 로고    scopus 로고
    • Target cell cyclophilins facilitate human papillomavirus type 16 infection
    • Bienkowska-Haba, M., Patel, H.D., and Sapp, M. (2009b) Target cell cyclophilins facilitate human papillomavirus type 16 infection. PLoS Pathog 5: e1000524.
    • (2009) PLoS Pathog , vol.5
    • Bienkowska-Haba, M.1    Patel, H.D.2    Sapp, M.3
  • 6
    • 84866170686 scopus 로고    scopus 로고
    • Cyclophilins facilitate dissociation of the HPV16 capsid protein L1 from the L2/DNA complex following virus entry
    • Bienkowska-Haba, M., Williams, C., Kim, S.M., Garcea, R.L., and Sapp, M. (2012) Cyclophilins facilitate dissociation of the HPV16 capsid protein L1 from the L2/DNA complex following virus entry. J Virol 86: 9875-9887.
    • (2012) J Virol , vol.86 , pp. 9875-9887
    • Bienkowska-Haba, M.1    Williams, C.2    Kim, S.M.3    Garcea, R.L.4    Sapp, M.5
  • 7
    • 0029736651 scopus 로고    scopus 로고
    • PIC1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia
    • Boddy, M.N., Howe, K., Etkin, L.D., Solomon, E., and Freemont, P.S. (1996) PIC1, a novel ubiquitin-like protein which interacts with the PML component of a multiprotein complex that is disrupted in acute promyelocytic leukaemia. Oncogene 13: 971-982.
    • (1996) Oncogene , vol.13 , pp. 971-982
    • Boddy, M.N.1    Howe, K.2    Etkin, L.D.3    Solomon, E.4    Freemont, P.S.5
  • 8
    • 80053459914 scopus 로고    scopus 로고
    • A viral ubiquitin ligase has substrate preferential SUMO targeted ubiquitin ligase activity that counteracts intrinsic antiviral defence
    • Boutell, C., Cuchet-Lourenco, D., Vanni, E., Orr, A., Glass, M., McFarlane, S., and Everett, R.D. (2011) A viral ubiquitin ligase has substrate preferential SUMO targeted ubiquitin ligase activity that counteracts intrinsic antiviral defence. PLoS Pathog 7: e1002245.
    • (2011) PLoS Pathog , vol.7
    • Boutell, C.1    Cuchet-Lourenco, D.2    Vanni, E.3    Orr, A.4    Glass, M.5    McFarlane, S.6    Everett, R.D.7
  • 9
    • 84858271333 scopus 로고    scopus 로고
    • The papillomavirus virion: a machine built to hide molecular Achilles' heels
    • Buck, C.B., and Trus, B.L. (2012) The papillomavirus virion: a machine built to hide molecular Achilles' heels. Adv Exp Med Biol 726: 403-422.
    • (2012) Adv Exp Med Biol , vol.726 , pp. 403-422
    • Buck, C.B.1    Trus, B.L.2
  • 10
    • 0346688642 scopus 로고    scopus 로고
    • Efficient intracellular assembly of papillomaviral vectors
    • Buck, C.B., Pastrana, D.V., Lowy, D.R., and Schiller, J.T. (2004) Efficient intracellular assembly of papillomaviral vectors. J Virol 78: 751-757.
    • (2004) J Virol , vol.78 , pp. 751-757
    • Buck, C.B.1    Pastrana, D.V.2    Lowy, D.R.3    Schiller, J.T.4
  • 12
    • 84867881070 scopus 로고    scopus 로고
    • Principles of polyoma- and papillomavirus uncoating
    • Cerqueira, C., and Schelhaas, M. (2012) Principles of polyoma- and papillomavirus uncoating. Med Microbiol Immunol 201: 427-436.
    • (2012) Med Microbiol Immunol , vol.201 , pp. 427-436
    • Cerqueira, C.1    Schelhaas, M.2
  • 13
    • 84885419211 scopus 로고    scopus 로고
    • Heparin increases the infectivity of Human Papillomavirus Type 16 independent of cell surface proteoglycans and induces L1 epitope exposure
    • Cerqueira, C., Liu, Y., Kuhling, L., Chai, W., Hafezi, W., van Kuppevelt, T.H., etal. (2013) Heparin increases the infectivity of Human Papillomavirus Type 16 independent of cell surface proteoglycans and induces L1 epitope exposure. Cell Microbiol 15: 1818-1836.
    • (2013) Cell Microbiol , vol.15 , pp. 1818-1836
    • Cerqueira, C.1    Liu, Y.2    Kuhling, L.3    Chai, W.4    Hafezi, W.5    van Kuppevelt, T.H.6
  • 14
    • 0026769936 scopus 로고
    • Viral E1 and E2 proteins support replication of homologous and heterologous papillomaviral origins
    • Chiang, C.M., Ustav, M., Stenlund, A., Ho, T.F., Broker, T.R., and Chow, L.T. (1992) Viral E1 and E2 proteins support replication of homologous and heterologous papillomaviral origins. Proc Natl Acad Sci USA 89: 5799-5803.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 5799-5803
    • Chiang, C.M.1    Ustav, M.2    Stenlund, A.3    Ho, T.F.4    Broker, T.R.5    Chow, L.T.6
  • 15
    • 7644237129 scopus 로고    scopus 로고
    • The L2 minor capsid protein of human papillomavirus type 16 interacts with a network of nuclear import receptors
    • Darshan, M.S., Lucchi, J., Harding, E., and Moroianu, J. (2004) The L2 minor capsid protein of human papillomavirus type 16 interacts with a network of nuclear import receptors. J Virol 78: 12179-12188.
    • (2004) J Virol , vol.78 , pp. 12179-12188
    • Darshan, M.S.1    Lucchi, J.2    Harding, E.3    Moroianu, J.4
  • 17
    • 0031984638 scopus 로고    scopus 로고
    • The papillomavirus minor capsid protein, L2, induces localization of the major capsid protein, L1, and the viral transcription/replication protein, E2, to PML oncogenic domains
    • Day, P.M., Roden, R.B., Lowy, D.R., and Schiller, J.T. (1998) The papillomavirus minor capsid protein, L2, induces localization of the major capsid protein, L1, and the viral transcription/replication protein, E2, to PML oncogenic domains. J Virol 72: 142-150.
    • (1998) J Virol , vol.72 , pp. 142-150
    • Day, P.M.1    Roden, R.B.2    Lowy, D.R.3    Schiller, J.T.4
  • 18
    • 4644352291 scopus 로고    scopus 로고
    • Establishment of papillomavirus infection is enhanced by promyelocytic leukemia protein (PML) expression
    • Day, P.M., Baker, C.C., Lowy, D.R., and Schiller, J.T. (2004) Establishment of papillomavirus infection is enhanced by promyelocytic leukemia protein (PML) expression. Proc Natl Acad Sci USA 101: 14252-14257.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 14252-14257
    • Day, P.M.1    Baker, C.C.2    Lowy, D.R.3    Schiller, J.T.4
  • 19
    • 84875523072 scopus 로고    scopus 로고
    • Identification of a role for the trans-Golgi network in human papillomavirus 16 pseudovirus infection
    • Day, P.M., Thompson, C.D., Schowalter, R.M., Lowy, D.R., and Schiller, J.T. (2013) Identification of a role for the trans-Golgi network in human papillomavirus 16 pseudovirus infection. J Virol 87: 3862-3870.
    • (2013) J Virol , vol.87 , pp. 3862-3870
    • Day, P.M.1    Thompson, C.D.2    Schowalter, R.M.3    Lowy, D.R.4    Schiller, J.T.5
  • 20
    • 14744285753 scopus 로고    scopus 로고
    • The papillomavirus life cycle
    • Doorbar, J. (2005) The papillomavirus life cycle. J Clin Virol 32 (Suppl. 1): S7-S15.
    • (2005) J Clin Virol , vol.32 , Issue.SUPPL. 1
    • Doorbar, J.1
  • 21
    • 0030614485 scopus 로고    scopus 로고
    • Identification of the alpha6 integrin as a candidate receptor for papillomaviruses
    • Evander, M., Frazer, I.H., Payne, E., Qi, Y.M., Hengst, K., and McMillan, N.A. (1997) Identification of the alpha6 integrin as a candidate receptor for papillomaviruses. J Virol 71: 2449-2456.
    • (1997) J Virol , vol.71 , pp. 2449-2456
    • Evander, M.1    Frazer, I.H.2    Payne, E.3    Qi, Y.M.4    Hengst, K.5    McMillan, N.A.6
  • 22
    • 0035969103 scopus 로고    scopus 로고
    • DNA viruses and viral proteins that interact with PML nuclear bodies
    • Everett, R.D. (2001) DNA viruses and viral proteins that interact with PML nuclear bodies. Oncogene 29: 7266-7273.
    • (2001) Oncogene , vol.29 , pp. 7266-7273
    • Everett, R.D.1
  • 23
    • 34347348272 scopus 로고    scopus 로고
    • PML and PML nuclear bodies: implications in antiviral defence
    • Everett, R.D., and Chelbi-Alix, M.K. (2007) PML and PML nuclear bodies: implications in antiviral defence. Biochimie 89: 819-830.
    • (2007) Biochimie , vol.89 , pp. 819-830
    • Everett, R.D.1    Chelbi-Alix, M.K.2
  • 24
    • 0036776336 scopus 로고    scopus 로고
    • Assembly and translocation of papillomavirus capsid proteins
    • Florin, L., Sapp, C., Streeck, R.E., and Sapp, M. (2002a) Assembly and translocation of papillomavirus capsid proteins. J Virol 76: 10009-10014.
    • (2002) J Virol , vol.76 , pp. 10009-10014
    • Florin, L.1    Sapp, C.2    Streeck, R.E.3    Sapp, M.4
  • 25
    • 0036061103 scopus 로고    scopus 로고
    • Reorganization of nuclear domain 10 induced by papillomavirus capsid protein l2
    • Florin, L., Schafer, F., Sotlar, K., Streeck, R.E., and Sapp, M. (2002b) Reorganization of nuclear domain 10 induced by papillomavirus capsid protein l2. Virology 295: 97-107.
    • (2002) Virology , vol.295 , pp. 97-107
    • Florin, L.1    Schafer, F.2    Sotlar, K.3    Streeck, R.E.4    Sapp, M.5
  • 26
    • 33745251121 scopus 로고    scopus 로고
    • Identification of a dynein interacting domain in the papillomavirus minor capsid protein L2
    • Florin, L., Becker, K.A., Lambert, C., Nowak, T., Sapp, C., Strand, D., etal. (2006) Identification of a dynein interacting domain in the papillomavirus minor capsid protein L2. J Virol 80: 6691-6696.
    • (2006) J Virol , vol.80 , pp. 6691-6696
    • Florin, L.1    Becker, K.A.2    Lambert, C.3    Nowak, T.4    Sapp, C.5    Strand, D.6
  • 27
    • 84867846134 scopus 로고    scopus 로고
    • Host-cell factors involved in papillomavirus entry
    • Florin, L., Sapp, M., and Spoden, G.A. (2012) Host-cell factors involved in papillomavirus entry. Med Microbiol Immunol 201: 437-448.
    • (2012) Med Microbiol Immunol , vol.201 , pp. 437-448
    • Florin, L.1    Sapp, M.2    Spoden, G.A.3
  • 28
    • 78649396592 scopus 로고    scopus 로고
    • The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition
    • Gareau, J.R., and Lima, C.D. (2010) The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition. Nat Rev Mol Cell Biol 11: 861-871.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 861-871
    • Gareau, J.R.1    Lima, C.D.2
  • 29
    • 0035156505 scopus 로고    scopus 로고
    • Human papillomavirus infection requires cell surface heparan sulfate
    • Giroglou, T., Florin, L., Schäfer, F., Streeck, R.E., and Sapp, M. (2001) Human papillomavirus infection requires cell surface heparan sulfate. J Virol 75: 1565-1570.
    • (2001) J Virol , vol.75 , pp. 1565-1570
    • Giroglou, T.1    Florin, L.2    Schäfer, F.3    Streeck, R.E.4    Sapp, M.5
  • 32
    • 52049125935 scopus 로고    scopus 로고
    • Papillomavirus 3' UTR regulatory elements
    • Graham, S.V. (2008) Papillomavirus 3' UTR regulatory elements. Front Biosci 13: 5646-5663.
    • (2008) Front Biosci , vol.13 , pp. 5646-5663
    • Graham, S.V.1
  • 33
    • 3543046736 scopus 로고    scopus 로고
    • A functional variant of SUMO4, a new IκBα modifier, is associated with type 1 diabetes
    • Guo, D., Li, M., Zhang, Y., Yang, P., Eckenrode, S., Hopkins, D., etal. (2004) A functional variant of SUMO4, a new IκBα modifier, is associated with type 1 diabetes. Nat Genet 36: 837-841.
    • (2004) Nat Genet , vol.36 , pp. 837-841
    • Guo, D.1    Li, M.2    Zhang, Y.3    Yang, P.4    Eckenrode, S.5    Hopkins, D.6
  • 34
    • 14244260623 scopus 로고    scopus 로고
    • Defining the SUMO-modified proteome by multiple approaches in Saccharomyces cerevisiae
    • Hannich, J.T., Lewis, A., Kroetz, M.B., Li, S.J., Heide, H., Emili, A., and Hochstrasser, M. (2005) Defining the SUMO-modified proteome by multiple approaches in Saccharomyces cerevisiae. J Biol Chem 280: 4102-4110.
    • (2005) J Biol Chem , vol.280 , pp. 4102-4110
    • Hannich, J.T.1    Lewis, A.2    Kroetz, M.B.3    Li, S.J.4    Heide, H.5    Emili, A.6    Hochstrasser, M.7
  • 36
    • 0037022173 scopus 로고    scopus 로고
    • Structure and dynamics of a helical hairpin and loop region in annexin 12: a site-directed spin labeling study
    • Isas, J.M., Langen, R., Haigler, H.T., and Hubbell, W.L. (2002) Structure and dynamics of a helical hairpin and loop region in annexin 12: a site-directed spin labeling study. Biochemistry 41: 1464-1473.
    • (2002) Biochemistry , vol.41 , pp. 1464-1473
    • Isas, J.M.1    Langen, R.2    Haigler, H.T.3    Hubbell, W.L.4
  • 37
    • 84755161558 scopus 로고    scopus 로고
    • Inhibition of nuclear entry of HPV16 pseudovirus-packaged DNA by an anti-HPV16 L2 neutralizing antibody
    • Ishii, Y., Tanaka, K., Kondo, K., Takeuchi, T., Mori, S., and Kanda, T. (2010) Inhibition of nuclear entry of HPV16 pseudovirus-packaged DNA by an anti-HPV16 L2 neutralizing antibody. Virology 406: 181-188.
    • (2010) Virology , vol.406 , pp. 181-188
    • Ishii, Y.1    Tanaka, K.2    Kondo, K.3    Takeuchi, T.4    Mori, S.5    Kanda, T.6
  • 38
    • 3943099375 scopus 로고    scopus 로고
    • Protein modification by SUMO
    • Johnson, E.S. (2004) Protein modification by SUMO. Annu Rev Biochem 73: 355-382.
    • (2004) Annu Rev Biochem , vol.73 , pp. 355-382
    • Johnson, E.S.1
  • 39
    • 0033605153 scopus 로고    scopus 로고
    • The L1 major capsid protein of human papillomavirus type 11 recombinant virus-like particles interacts with heparin and cell-surface glycosaminoglycans on human keratinocytes
    • Joyce, J., Tung, J., Przysiecki, C., Cook, J., Lehman, E., Sands, J., etal. (1999) The L1 major capsid protein of human papillomavirus type 11 recombinant virus-like particles interacts with heparin and cell-surface glycosaminoglycans on human keratinocytes. J Biol Chem 274: 5810-5822.
    • (1999) J Biol Chem , vol.274 , pp. 5810-5822
    • Joyce, J.1    Tung, J.2    Przysiecki, C.3    Cook, J.4    Lehman, E.5    Sands, J.6
  • 40
    • 0032080337 scopus 로고    scopus 로고
    • Characterization of a second member of the sentrin family of ubiquitin-like proteins
    • Kamitani, T., Kito, K., Nguyen, H.P., Fukuda-Kamitani, T., and Yeh, E.T. (1998) Characterization of a second member of the sentrin family of ubiquitin-like proteins. J Biol Chem 273: 11349-11353.
    • (1998) J Biol Chem , vol.273 , pp. 11349-11353
    • Kamitani, T.1    Kito, K.2    Nguyen, H.P.3    Fukuda-Kamitani, T.4    Yeh, E.T.5
  • 42
    • 30344481121 scopus 로고    scopus 로고
    • A membrane-destabilizing peptide in capsid protein L2 is required for egress of papillomavirus genomes from endosomes
    • Kämper, N., Day, P.M., Nowak, T., Selinka, H.C., Florin, L., Bolscher, J., etal. (2006) A membrane-destabilizing peptide in capsid protein L2 is required for egress of papillomavirus genomes from endosomes. J Virol 80: 759-768.
    • (2006) J Virol , vol.80 , pp. 759-768
    • Kämper, N.1    Day, P.M.2    Nowak, T.3    Selinka, H.C.4    Florin, L.5    Bolscher, J.6
  • 43
    • 34547683267 scopus 로고    scopus 로고
    • SUMO junction-what's your function? New insights through SUMO-interacting motifs
    • Kerscher, O., Felberbaum, R., and Hochstrasser, M. (2007) SUMO junction-what's your function? New insights through SUMO-interacting motifs. EMBO Rep 8: 550-555.
    • (2007) EMBO Rep , vol.8 , pp. 550-555
    • Kerscher, O.1    Felberbaum, R.2    Hochstrasser, M.3
  • 44
    • 77954982420 scopus 로고    scopus 로고
    • Role of noncovalent SUMO binding by the human cytomegalovirus IE2 transactivator in lytic growth
    • Kim, E.T., Kim, Y.E., Huh, Y.H., and Ahn, J.H. (2010) Role of noncovalent SUMO binding by the human cytomegalovirus IE2 transactivator in lytic growth. J Virol 84: 8111-8123.
    • (2010) J Virol , vol.84 , pp. 8111-8123
    • Kim, E.T.1    Kim, Y.E.2    Huh, Y.H.3    Ahn, J.H.4
  • 45
    • 0027304830 scopus 로고
    • The biology of human papillomaviruses: from warts to cancer
    • Laimins, L.A. (1993) The biology of human papillomaviruses: from warts to cancer. Infect Agents Dis 2: 74-86.
    • (1993) Infect Agents Dis , vol.2 , pp. 74-86
    • Laimins, L.A.1
  • 47
    • 0034850163 scopus 로고    scopus 로고
    • Enhancement of capsid gene expression: preparing the human papillomavirus type 16 major structural gene L1 for DNA vaccination purposes
    • Leder, C., Kleinschmidt, J.A., Wiethe, C., and Muller, M. (2001) Enhancement of capsid gene expression: preparing the human papillomavirus type 16 major structural gene L1 for DNA vaccination purposes. J Virol 75: 9201-9209.
    • (2001) J Virol , vol.75 , pp. 9201-9209
    • Leder, C.1    Kleinschmidt, J.A.2    Wiethe, C.3    Muller, M.4
  • 48
    • 84876931306 scopus 로고    scopus 로고
    • Genome-wide siRNA screen identifies the retromer as a cellular entry factor for human papillomavirus
    • Lipovsky, A., Popa, A., Pimienta, G., Wyler, M., Bhan, A., Kuruvilla, L., etal. (2013) Genome-wide siRNA screen identifies the retromer as a cellular entry factor for human papillomavirus. Proc Natl Acad Sci USA 110: 7452-7457.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 7452-7457
    • Lipovsky, A.1    Popa, A.2    Pimienta, G.3    Wyler, M.4    Bhan, A.5    Kuruvilla, L.6
  • 49
    • 67349087384 scopus 로고    scopus 로고
    • Sumo-2/3-ylation following in vitro modeled ischemia is reduced in delayed ischemic tolerance
    • Loftus, L.T., Gala, R., Yang, T., Jessick, V.J., Ashley, M.D., Ordonez, A.N., etal. (2009) Sumo-2/3-ylation following in vitro modeled ischemia is reduced in delayed ischemic tolerance. Brain Res 1272: 71-80.
    • (2009) Brain Res , vol.1272 , pp. 71-80
    • Loftus, L.T.1    Gala, R.2    Yang, T.3    Jessick, V.J.4    Ashley, M.D.5    Ordonez, A.N.6
  • 50
    • 0029905422 scopus 로고    scopus 로고
    • Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics
    • Mchaourab, H.S., Lietzow, M.A., Hideg, K., and Hubbell, W.L. (1996) Motion of spin-labeled side chains in T4 lysozyme. Correlation with protein structure and dynamics. Biochemistry 35: 7692-7704.
    • (1996) Biochemistry , vol.35 , pp. 7692-7704
    • Mchaourab, H.S.1    Lietzow, M.A.2    Hideg, K.3    Hubbell, W.L.4
  • 51
    • 84855205694 scopus 로고    scopus 로고
    • The high risk HPV16 L2 minor capsid protein has multiple transport signals that mediate its nucleocytoplasmic traffic
    • Mamoor, S., Onder, Z., Karanam, B., Kwak, K., Bordeaux, J., Crosby, L., etal. (2012) The high risk HPV16 L2 minor capsid protein has multiple transport signals that mediate its nucleocytoplasmic traffic. Virology 422: 413-424.
    • (2012) Virology , vol.422 , pp. 413-424
    • Mamoor, S.1    Onder, Z.2    Karanam, B.3    Kwak, K.4    Bordeaux, J.5    Crosby, L.6
  • 52
    • 77957959661 scopus 로고    scopus 로고
    • Modification of human papillomavirus minor capsid protein L2 by sumoylation
    • Marusic, M.B., Mencin, N., Licen, M., Banks, L., and Grm, H.S. (2010) Modification of human papillomavirus minor capsid protein L2 by sumoylation. J Virol 84: 11585-11589.
    • (2010) J Virol , vol.84 , pp. 11585-11589
    • Marusic, M.B.1    Mencin, N.2    Licen, M.3    Banks, L.4    Grm, H.S.5
  • 53
    • 0030455748 scopus 로고    scopus 로고
    • A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex
    • Matunis, M.J., Coutavas, E., and Blobel, G. (1996) A novel ubiquitin-like modification modulates the partitioning of the Ran-GTPase-activating protein RanGAP1 between the cytosol and the nuclear pore complex. J Cell Biol 135: 1457-1470.
    • (1996) J Cell Biol , vol.135 , pp. 1457-1470
    • Matunis, M.J.1    Coutavas, E.2    Blobel, G.3
  • 54
    • 44449109533 scopus 로고    scopus 로고
    • Mechanism and consequences for paralog-specific sumoylation of ubiquitin-specific protease 25
    • Meulmeester, E., Kunze, M., Hsiao, H.H., Urlaub, H., and Melchior, F. (2008) Mechanism and consequences for paralog-specific sumoylation of ubiquitin-specific protease 25. Mol Cell 30: 610-619.
    • (2008) Mol Cell , vol.30 , pp. 610-619
    • Meulmeester, E.1    Kunze, M.2    Hsiao, H.H.3    Urlaub, H.4    Melchior, F.5
  • 55
    • 34548848530 scopus 로고    scopus 로고
    • Small ubiquitin-related modifier (SUMO)-specific proteases: profiling the specificities and activities of human SENPs
    • Mikolajczyk, J., Drag, M., Bekes, M., Cao, J.T., Ronai, Z., and Salvesen, G.S. (2007) Small ubiquitin-related modifier (SUMO)-specific proteases: profiling the specificities and activities of human SENPs. J Biol Chem 282: 26217-26224.
    • (2007) J Biol Chem , vol.282 , pp. 26217-26224
    • Mikolajczyk, J.1    Drag, M.2    Bekes, M.3    Cao, J.T.4    Ronai, Z.5    Salvesen, G.S.6
  • 56
    • 0034680441 scopus 로고    scopus 로고
    • Covalent modification of p73α by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif
    • Minty, A., Dumont, X., Kaghad, M., and Caput, D. (2000) Covalent modification of p73α by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif. J Biol Chem 275: 36316-36323.
    • (2000) J Biol Chem , vol.275 , pp. 36316-36323
    • Minty, A.1    Dumont, X.2    Kaghad, M.3    Caput, D.4
  • 57
    • 0037119997 scopus 로고    scopus 로고
    • Atomic model of the papillomavirus capsid
    • Modis, Y., Trus, B.L., and Harrison, S.C. (2002) Atomic model of the papillomavirus capsid. EMBO J 21: 4754-4762.
    • (2002) EMBO J , vol.21 , pp. 4754-4762
    • Modis, Y.1    Trus, B.L.2    Harrison, S.C.3
  • 59
    • 0030588674 scopus 로고    scopus 로고
    • Protection against Fas/APO-1- and tumor necrosis factor-mediated cell death by a novel protein, sentrin
    • Okura, T., Gong, L., Kamitani, T., Wada, T., Okura, I., Wei, C.F., etal. (1996) Protection against Fas/APO-1- and tumor necrosis factor-mediated cell death by a novel protein, sentrin. J Immunol 157: 4277-4281.
    • (1996) J Immunol , vol.157 , pp. 4277-4281
    • Okura, T.1    Gong, L.2    Kamitani, T.3    Wada, T.4    Okura, I.5    Wei, C.F.6
  • 60
    • 64749093273 scopus 로고    scopus 로고
    • Direct binding of CoREST1 to SUMO-2/3 contributes to gene-specific repression by the LSD1/CoREST1/HDAC complex
    • Ouyang, J., Shi, Y., Valin, A., Xuan, Y., and Gill, G. (2009) Direct binding of CoREST1 to SUMO-2/3 contributes to gene-specific repression by the LSD1/CoREST1/HDAC complex. Mol Cell 34: 45-154.
    • (2009) Mol Cell , vol.34 , pp. 45-154
    • Ouyang, J.1    Shi, Y.2    Valin, A.3    Xuan, Y.4    Gill, G.5
  • 62
    • 84878199077 scopus 로고    scopus 로고
    • The evolving field of human papillomavirus receptor research: a review of binding and entry
    • doi:10.1128/JVI.00330-13
    • Raff, A.B., Woodham, A.W., Raff, L.M., Skeate, J.G., Yan, L., Da Silva, D.M., etal. (2013) The evolving field of human papillomavirus receptor research: a review of binding and entry. J Virol. doi:10.1128/JVI.00330-13
    • (2013) J Virol
    • Raff, A.B.1    Woodham, A.W.2    Raff, L.M.3    Skeate, J.G.4    Yan, L.5    Da Silva, D.M.6
  • 63
    • 31944439998 scopus 로고    scopus 로고
    • Cleavage of the papillomavirus minor capsid protein, L2, at a furin consensus site is necessary for infection
    • Richards, R.M., Lowy, D.R., Schiller, J.T., and Day, P.M. (2006) Cleavage of the papillomavirus minor capsid protein, L2, at a furin consensus site is necessary for infection. Proc Natl Acad Sci USA 103: 1522-1527.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 1522-1527
    • Richards, R.M.1    Lowy, D.R.2    Schiller, J.T.3    Day, P.M.4
  • 65
    • 9644302502 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans interact exclusively with conformationally intact HPV L1 assemblies: basis for a virus-like particle ELISA
    • Rommel, O., Dillner, J., Fligge, C., Bergsdorf, C., Wang, X., Selinka, H.C., and Sapp, M. (2005) Heparan sulfate proteoglycans interact exclusively with conformationally intact HPV L1 assemblies: basis for a virus-like particle ELISA. J Med Virol 75: 114-121.
    • (2005) J Med Virol , vol.75 , pp. 114-121
    • Rommel, O.1    Dillner, J.2    Fligge, C.3    Bergsdorf, C.4    Wang, X.5    Selinka, H.C.6    Sapp, M.7
  • 66
    • 0034054669 scopus 로고    scopus 로고
    • Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3
    • Saitoh, H., and Hinchey, J. (2000) Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3. J Biol Chem 275: 6252-6258.
    • (2000) J Biol Chem , vol.275 , pp. 6252-6258
    • Saitoh, H.1    Hinchey, J.2
  • 67
    • 59349098016 scopus 로고    scopus 로고
    • Structure, attachment and entry of polyoma- and papillomaviruses
    • Sapp, M., and Day, P.M. (2009) Structure, attachment and entry of polyoma- and papillomaviruses. Virology 384: 400-409.
    • (2009) Virology , vol.384 , pp. 400-409
    • Sapp, M.1    Day, P.M.2
  • 68
    • 0028618317 scopus 로고
    • Analysis of type-restricted and cross-reactive epitopes on virus-like particles of human papillomavirus type 33 and in infected tissues using monoclonal antibodies to the major capsid protein
    • Sapp, M., Kraus, U., Volpers, C., Snijders, P.J., Walboomers, J.M., and Streeck, R.E. (1994) Analysis of type-restricted and cross-reactive epitopes on virus-like particles of human papillomavirus type 33 and in infected tissues using monoclonal antibodies to the major capsid protein. J Gen Virol 75: 3375-3383.
    • (1994) J Gen Virol , vol.75 , pp. 3375-3383
    • Sapp, M.1    Kraus, U.2    Volpers, C.3    Snijders, P.J.4    Walboomers, J.M.5    Streeck, R.E.6
  • 69
    • 84876901328 scopus 로고    scopus 로고
    • HPV virions hitchhike a ride on retromer complexes
    • Sapp, M.J. (2013) HPV virions hitchhike a ride on retromer complexes. Proc Natl Acad Sci USA 110: 7116-7117.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 7116-7117
    • Sapp, M.J.1
  • 71
    • 84861207605 scopus 로고    scopus 로고
    • Entry of human papillomavirus type 16 by actin-dependent, clathrin- and lipid raft-independent endocytosis
    • Schelhaas, M., Shah, B., Holzer, M., Blattmann, P., Kuhling, L., Day, P.M., etal. (2012) Entry of human papillomavirus type 16 by actin-dependent, clathrin- and lipid raft-independent endocytosis. PLoS Pathog 8: e1002657.
    • (2012) PLoS Pathog , vol.8
    • Schelhaas, M.1    Shah, B.2    Holzer, M.3    Blattmann, P.4    Kuhling, L.5    Day, P.M.6
  • 72
    • 78650282789 scopus 로고    scopus 로고
    • Identification of the dynein light chains required for human papillomavirus infection
    • Schneider, M.A., Spoden, G.A., Florin, L., and Lambert, C. (2011) Identification of the dynein light chains required for human papillomavirus infection. Cell Microbiol 13: 32-47.
    • (2011) Cell Microbiol , vol.13 , pp. 32-47
    • Schneider, M.A.1    Spoden, G.A.2    Florin, L.3    Lambert, C.4
  • 73
    • 52049104181 scopus 로고    scopus 로고
    • HPV-16 RNA processing
    • Schwartz, S. (2008) HPV-16 RNA processing. Front Biosci 13: 5880-5891.
    • (2008) Front Biosci , vol.13 , pp. 5880-5891
    • Schwartz, S.1
  • 74
    • 0041837510 scopus 로고    scopus 로고
    • Nuclear and unclear functions of SUMO
    • Seeler, J.-S., and Dejean, A. (2003) Nuclear and unclear functions of SUMO. Nat Rev Mol Cell Biol 4: 690-699.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 690-699
    • Seeler, J.-S.1    Dejean, A.2
  • 75
    • 58149096433 scopus 로고    scopus 로고
    • Structure of the small ubiquitin-like modifier (SUMO)-interacting motif of MBD1-containing chromatin-associated factor 1 bound to SUMO-3
    • Sekiyama, N., Ikegami, T., Yamane, T., Ikeguchi, M., Uchimura, Y., Baba, D., etal. (2008) Structure of the small ubiquitin-like modifier (SUMO)-interacting motif of MBD1-containing chromatin-associated factor 1 bound to SUMO-3. J Biol Chem 283: 35966-35975.
    • (2008) J Biol Chem , vol.283 , pp. 35966-35975
    • Sekiyama, N.1    Ikegami, T.2    Yamane, T.3    Ikeguchi, M.4    Uchimura, Y.5    Baba, D.6
  • 76
    • 35148819635 scopus 로고    scopus 로고
    • Inhibition of transfer to secondary receptors by heparan sulfate-binding drug or antibody induces noninfectious uptake of human papillomavirus
    • Selinka, H.-C., Florin, L., Patel, H.D., Freitag, K., Schmidtke, M., Makarov, V.A., and Sapp, M. (2007) Inhibition of transfer to secondary receptors by heparan sulfate-binding drug or antibody induces noninfectious uptake of human papillomavirus. J Virol 81: 10970-10980.
    • (2007) J Virol , vol.81 , pp. 10970-10980
    • Selinka, H.-C.1    Florin, L.2    Patel, H.D.3    Freitag, K.4    Schmidtke, M.5    Makarov, V.A.6    Sapp, M.7
  • 77
    • 0345599103 scopus 로고    scopus 로고
    • Different heparan sulfate proteoglycans serve as cellular receptors for human papillomaviruses
    • Shafti-Keramat, S., Handisurya, A., Kriehuber, E., Meneguzzi, G., Slupetzky, K., and Kirnbauer, R. (2003) Different heparan sulfate proteoglycans serve as cellular receptors for human papillomaviruses. J Virol 77: 13125-13135.
    • (2003) J Virol , vol.77 , pp. 13125-13135
    • Shafti-Keramat, S.1    Handisurya, A.2    Kriehuber, E.3    Meneguzzi, G.4    Slupetzky, K.5    Kirnbauer, R.6
  • 78
    • 5144219680 scopus 로고    scopus 로고
    • Identification of a SUMO-binding motif that recognizes SUMO-modified proteins
    • Song, J., Durrin, L.K., Wilkinson, T.A., Krontiris, T.G., and Chen, Y. (2004) Identification of a SUMO-binding motif that recognizes SUMO-modified proteins. Proc Natl Acad Sci USA 101: 4373-14378.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 4373-14378
    • Song, J.1    Durrin, L.K.2    Wilkinson, T.A.3    Krontiris, T.G.4    Chen, Y.5
  • 79
    • 28844455305 scopus 로고    scopus 로고
    • Small ubiquitin-like modifier (SUMO) recognition of a SUMO binding motif: a reversal of the bound orientation
    • Song, J., Zhang, Z., Hu, W., and Chen, Y. (2005) Small ubiquitin-like modifier (SUMO) recognition of a SUMO binding motif: a reversal of the bound orientation. J Biol Chem 280: 40122-40129.
    • (2005) J Biol Chem , vol.280 , pp. 40122-40129
    • Song, J.1    Zhang, Z.2    Hu, W.3    Chen, Y.4
  • 80
    • 53749105515 scopus 로고    scopus 로고
    • Clathrin- and caveolin-independent entry of human papillomavirus type 16 - involvement of tetraspanin-enriched microdomains (TEMs)
    • Spoden, G., Freitag, K., Husmann, M., Boller, K., Sapp, M., Lambert, C., and Florin, L. (2008) Clathrin- and caveolin-independent entry of human papillomavirus type 16 - involvement of tetraspanin-enriched microdomains (TEMs). PLoS ONE 3: e3313.
    • (2008) PLoS ONE , vol.3
    • Spoden, G.1    Freitag, K.2    Husmann, M.3    Boller, K.4    Sapp, M.5    Lambert, C.6    Florin, L.7
  • 81
    • 84880351887 scopus 로고    scopus 로고
    • The Human Papillomaviruses Type 16, 18, and 31 share similar endocytic requirements for entry
    • Spoden, G., Kuhling, L., Cordes, N., Frenzel, B., Sapp, M., Boller, K., etal. (2013) The Human Papillomaviruses Type 16, 18, and 31 share similar endocytic requirements for entry. J Virol 87: 7765-7773.
    • (2013) J Virol , vol.87 , pp. 7765-7773
    • Spoden, G.1    Kuhling, L.2    Cordes, N.3    Frenzel, B.4    Sapp, M.5    Boller, K.6
  • 83
    • 59649087451 scopus 로고    scopus 로고
    • Phospho-regulated SUMO interaction modules connect the SUMO system to CK2 signaling
    • Stehmeier, P., and Muller, S. (2009) Phospho-regulated SUMO interaction modules connect the SUMO system to CK2 signaling. Mol Cell 33: 400-409.
    • (2009) Mol Cell , vol.33 , pp. 400-409
    • Stehmeier, P.1    Muller, S.2
  • 84
    • 84891602166 scopus 로고    scopus 로고
    • Sp100 provides intrinsic immunity against human papillomavirus infection
    • Stepp, W.H., Meyers, J.M., and McBride, A.A. (2013) Sp100 provides intrinsic immunity against human papillomavirus infection. MBio 4: 845-857.
    • (2013) MBio , vol.4 , pp. 845-857
    • Stepp, W.H.1    Meyers, J.M.2    McBride, A.A.3
  • 85
    • 28844486080 scopus 로고    scopus 로고
    • EasySpin, a comprehensive software package for spectral simulation and analysis in EPR
    • Stoll, S., and Schweiger, A. (2006) EasySpin, a comprehensive software package for spectral simulation and analysis in EPR. J Magn Reson 178: 42-55.
    • (2006) J Magn Reson , vol.178 , pp. 42-55
    • Stoll, S.1    Schweiger, A.2
  • 86
    • 84860891623 scopus 로고    scopus 로고
    • Essential roles for soluble virion-associated heparan sulfonated proteoglycans and growth factors in human papillomavirus infections
    • Surviladze, Z., Dziduszko, A., and Ozbun, M.A. (2012) Essential roles for soluble virion-associated heparan sulfonated proteoglycans and growth factors in human papillomavirus infections. PLoS Pathog 8: e1002519.
    • (2012) PLoS Pathog , vol.8
    • Surviladze, Z.1    Dziduszko, A.2    Ozbun, M.A.3
  • 87
    • 43049093756 scopus 로고    scopus 로고
    • RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation
    • Tatham, M.H., Geoffroy, M.C., Shen, L., Plechanovova, A., Hattersley, N., Jaffray, E.G., etal. (2008) RNF4 is a poly-SUMO-specific E3 ubiquitin ligase required for arsenic-induced PML degradation. Nat Cell Biol 10: 538-546.
    • (2008) Nat Cell Biol , vol.10 , pp. 538-546
    • Tatham, M.H.1    Geoffroy, M.C.2    Shen, L.3    Plechanovova, A.4    Hattersley, N.5    Jaffray, E.G.6
  • 88
    • 54549084341 scopus 로고    scopus 로고
    • New insights into the role of the subnuclear structure ND10 for viral infection
    • Tavalai, N., and Stamminger, T. (2008) New insights into the role of the subnuclear structure ND10 for viral infection. Biochim Biophys Acta 1783: 2207-2221.
    • (2008) Biochim Biophys Acta , vol.1783 , pp. 2207-2221
    • Tavalai, N.1    Stamminger, T.2
  • 89
    • 79955047081 scopus 로고    scopus 로고
    • Interplay between herpesvirus infection and host defense by PML nuclear bodies
    • Tavalai, N., and Stamminger, T. (2009) Interplay between herpesvirus infection and host defense by PML nuclear bodies. Viruses 1: 1240-1264.
    • (2009) Viruses , vol.1 , pp. 1240-1264
    • Tavalai, N.1    Stamminger, T.2
  • 90
    • 79959553618 scopus 로고    scopus 로고
    • Crosstalk between viruses and PML nuclear bodies: a network-based approach
    • Van Damme, E., and Van Ostade, X. (2011) Crosstalk between viruses and PML nuclear bodies: a network-based approach. Front Biosci 17: 2910-2920.
    • (2011) Front Biosci , vol.17 , pp. 2910-2920
    • Van Damme, E.1    Van Ostade, X.2
  • 91
    • 76449092386 scopus 로고    scopus 로고
    • SUMO chains: polymeric signals
    • Vertegaal, A.C. (2010) SUMO chains: polymeric signals. Biochem Soc Trans 38: 46-49.
    • (2010) Biochem Soc Trans , vol.38 , pp. 46-49
    • Vertegaal, A.C.1
  • 92
    • 0028807569 scopus 로고
    • Conformational and linear epitopes on virus-like particles of human papillomavirus type 33 identified by monoclonal antibodies to the minor capsid protein L2
    • Volpers, C., Sapp, M., Snijders, P.J., Walboomers, J.M., and Streeck, R.E. (1995) Conformational and linear epitopes on virus-like particles of human papillomavirus type 33 identified by monoclonal antibodies to the minor capsid protein L2. J Gen Virol 76: 2661-2667.
    • (1995) J Gen Virol , vol.76 , pp. 2661-2667
    • Volpers, C.1    Sapp, M.2    Snijders, P.J.3    Walboomers, J.M.4    Streeck, R.E.5
  • 93
    • 84856487109 scopus 로고    scopus 로고
    • The story so far: post-translational regulation of peroxisome proliferator-activated receptors by ubiquitination and SUMOylation
    • Wadosky, K.M., and Willis, M.S. (2011) The story so far: post-translational regulation of peroxisome proliferator-activated receptors by ubiquitination and SUMOylation. Am J Physiol Heart Circ Physiol 302: H515-H526.
    • (2011) Am J Physiol Heart Circ Physiol , vol.302
    • Wadosky, K.M.1    Willis, M.S.2
  • 94
    • 80052341054 scopus 로고    scopus 로고
    • Disruption of PML nuclear bodies is mediated by ORF61 SUMO-interacting motifs and required for varicella-zoster virus pathogenesis in skin
    • Wang, L., Oliver, S.L., Sommer, M., Rajamani, J., Reichelt, M., and Arvin, A.M. (2011) Disruption of PML nuclear bodies is mediated by ORF61 SUMO-interacting motifs and required for varicella-zoster virus pathogenesis in skin. PLoS Pathog 7: e1002157.
    • (2011) PLoS Pathog , vol.7
    • Wang, L.1    Oliver, S.L.2    Sommer, M.3    Rajamani, J.4    Reichelt, M.5    Arvin, A.M.6
  • 95
    • 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., and Barton, G.J. (2009) Jalview Version 2 - a multiple sequence alignment editor and analysis workbench. Bioinformatics 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
  • 96
    • 84905030219 scopus 로고    scopus 로고
    • Human pathogens and the host cell SUMOylation system
    • Wimmer, P., Schreiner, S., and Dobner, T. (2012) Human pathogens and the host cell SUMOylation system. J Virol 7: 211-225.
    • (2012) J Virol , vol.7 , pp. 211-225
    • Wimmer, P.1    Schreiner, S.2    Dobner, T.3
  • 97
    • 84865156591 scopus 로고    scopus 로고
    • The S100A10 subunit of the annexin A2 heterotetramer facilitates L2-mediated human papillomavirus infection
    • Woodham, A.W., Da Silva, D.M., Skeate, J.G., Raff, A.B., Ambroso, M.R., Brand, H.E., etal. (2012) The S100A10 subunit of the annexin A2 heterotetramer facilitates L2-mediated human papillomavirus infection. PLoS ONE 7: e43519.
    • (2012) PLoS ONE , vol.7
    • Woodham, A.W.1    Da Silva, D.M.2    Skeate, J.G.3    Raff, A.B.4    Ambroso, M.R.5    Brand, H.E.6
  • 98
    • 77950643586 scopus 로고    scopus 로고
    • The SUMO E3 ligase activity of Pc2 is coordinated through a SUMO interaction motif
    • Yang, S.H., and Sharrocks, A.D. (2010) The SUMO E3 ligase activity of Pc2 is coordinated through a SUMO interaction motif. Mol Cell Biol 30: 2193-2205.
    • (2010) Mol Cell Biol , vol.30 , pp. 2193-2205
    • Yang, S.H.1    Sharrocks, A.D.2


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