메뉴 건너뛰기




Volumn 818, Issue , 2014, Pages 99-124

Tumor suppressing properties of rodent parvovirus NS1 proteins and their derivatives

Author keywords

Actin; Anti cancer activities; Cellular targets; Cytolysis; Cytoskeleton dynamics; DNA repair; ERM family proteins; Gelsolin; Host macromolecular synthesis shut off; Non structural protein NS1; Parvoviruses; Phosphoinositide dependent kinase 1 pathway; Post translational modifications; Signaling cascades; Tropomyosin

Indexed keywords

NONSTRUCTURAL PROTEIN 1; ONCOLYTIC PARVOVIRUS; POLYPEPTIDE; ANTINEOPLASTIC AGENT; NS1 PROTEIN, PARVOVIRUS; TUMOR SUPPRESSOR PROTEIN; VIRUS PROTEIN;

EID: 84921672283     PISSN: 00652598     EISSN: 22148019     Source Type: Book Series    
DOI: 10.1007/978-1-4471-6458-6_5     Document Type: Article
Times cited : (14)

References (110)
  • 1
    • 77951677941 scopus 로고    scopus 로고
    • Improved killing of human high-grade glioma cells by combining ionizing radiation with oncolytic parvovirus H-1 infection
    • Geletneky K, Hartkopf AD, Krempien R, Rommelaere J, Schlehofer JR (2010) Improved killing of human high-grade glioma cells by combining ionizing radiation with oncolytic parvovirus H-1 infection. J Biomed Biotechnol 2010:350748
    • (2010) J Biomed Biotechnol , vol.2010 , pp. 350748
    • Geletneky, K.1    Hartkopf, A.D.2    Krempien, R.3    Rommelaere, J.4    Schlehofer, J.R.5
  • 2
    • 78650191743 scopus 로고    scopus 로고
    • Therapeutic implications of the enhanced short and long-term cytotoxicity of radiation treatment followed by oncolytic parvovirus H-1 infection in high-grade glioma cells
    • Geletneky K, Hartkopf AD, Krempien R, Rommelaere J, Schlehofer JR (2010) Therapeutic implications of the enhanced short and long-term cytotoxicity of radiation treatment followed by oncolytic parvovirus H-1 infection in high-grade glioma cells. Bioeng Bugs 1:429-433
    • (2010) Bioeng Bugs , vol.1 , pp. 429-433
    • Geletneky, K.1    Hartkopf, A.D.2    Krempien, R.3    Rommelaere, J.4    Schlehofer, J.R.5
  • 3
    • 78149488438 scopus 로고    scopus 로고
    • Regression of advanced rat and human gliomas by local or systemic treatment with oncolytic parvovirus H-1 in rat models
    • Geletneky K, Kiprianova I, Ayache A, Koch R, Herrero YCM, Deleu L et al (2010) Regression of advanced rat and human gliomas by local or systemic treatment with oncolytic parvovirus H-1 in rat models. Neuro Oncol 12:804-814
    • (2010) Neuro Oncol , vol.12 , pp. 804-814
    • Geletneky, K.1    Kiprianova, I.2    Ayache, A.3    Koch, R.4    Herrero, Y.C.M.5    Deleu, L.6
  • 4
    • 0025816045 scopus 로고
    • Antineoplastic activity of parvoviruses
    • Rommelaere J, Cornelis JJ (1991) Antineoplastic activity of parvoviruses. J Virol Methods 33:233-251
    • (1991) J Virol Methods , vol.33 , pp. 233-251
    • Rommelaere, J.1    Cornelis, J.J.2
  • 6
    • 84858608281 scopus 로고    scopus 로고
    • Phase I/IIa study of intratumoral/intracerebral or intravenous/ intracerebral administration of Parvovirus H-1 (ParvOryx) in patients with progressive primary or recurrent glioblastoma multiforme: ParvOryx01 protocol
    • Geletneky K, Huesing J, Rommelaere J, Schlehofer JR, Leuchs B, Dahm M et al (2012) Phase I/IIa study of intratumoral/intracerebral or intravenous/intracerebral administration of Parvovirus H-1 (ParvOryx) in patients with progressive primary or recurrent glioblastoma multiforme: ParvOryx01 protocol. BMC Cancer 12:99
    • (2012) BMC Cancer , vol.12 , pp. 99
    • Geletneky, K.1    Huesing, J.2    Rommelaere, J.3    Schlehofer, J.R.4    Leuchs, B.5    Dahm, M.6
  • 7
    • 0023065751 scopus 로고
    • The autonomously replicating parvoviruses of vertebrates
    • Cotmore SF, Tattersall P (1987) The autonomously replicating parvoviruses of vertebrates. Adv Virus Res 33:91-174
    • (1987) Adv Virus Res , vol.33 , pp. 91-174
    • Cotmore, S.F.1    Tattersall, P.2
  • 8
    • 85145154923 scopus 로고    scopus 로고
    • Regulation of non-structural protein functions by differential synthesis, modification and trafficking
    • Kerr CSB, Linden ME, Parrish CR, Cotmore SF (eds) Edward Arnold, Ltd, London
    • Nüesch JPF (2006) Regulation of non-structural protein functions by differential synthesis, modification and trafficking. In: Kerr CSB, Linden ME, Parrish CR, Cotmore SF (eds) Parvoviruses. Edward Arnold, Ltd, London, pp 275-290
    • (2006) Parvoviruses , pp. 275-290
    • Nüesch, J.P.F.1
  • 9
    • 0033526831 scopus 로고    scopus 로고
    • Phosphorylation of the viral nonstructural protein NS1 during MVMp infection of A9 cells
    • Corbau R, Salom N, Rommelaere J, Nuesch JP (1999) Phosphorylation of the viral nonstructural protein NS1 during MVMp infection of A9 cells. Virology 259:402-415
    • (1999) Virology , vol.259 , pp. 402-415
    • Corbau, R.1    Salom, N.2    Rommelaere, J.3    Nuesch, J.P.4
  • 10
    • 0034610239 scopus 로고    scopus 로고
    • Regulation of MVM NS1 by protein kinase C: Impact of mutagenesis at consensus phosphorylation sites on replicative functions and cytopathic effects
    • Corbau R, Duverger V, Rommelaere J, Nuesch JP (2000) Regulation of MVM NS1 by protein kinase C: impact of mutagenesis at consensus phosphorylation sites on replicative functions and cytopathic effects. Virology 278:151-167
    • (2000) Virology , vol.278 , pp. 151-167
    • Corbau, R.1    Duverger, V.2    Rommelaere, J.3    Nuesch, J.P.4
  • 11
    • 0031714793 scopus 로고    scopus 로고
    • Biochemical activities of minute virus of mice nonstructural protein NS1 are modulated in vitro by the phosphorylation state of the polypeptide
    • Nuesch JP, Corbau R, Tattersall P, Rommelaere J (1998) Biochemical activities of minute virus of mice nonstructural protein NS1 are modulated In vitro by the phosphorylation state of the polypeptide. J Virol 72:8002-8012
    • (1998) J Virol , vol.72 , pp. 8002-8012
    • Nuesch, J.P.1    Corbau, R.2    Tattersall, P.3    Rommelaere, J.4
  • 12
    • 0034968465 scopus 로고    scopus 로고
    • Initiation of minute virus of mice DNA replication is regulated at the level of origin unwinding by atypical protein kinase C phosphorylation of NS1
    • Nuesch JP, Christensen J, Rommelaere J (2001) Initiation of minute virus of mice DNA replication is regulated at the level of origin unwinding by atypical protein kinase C phosphorylation of NS1. J Virol 75:5730-5739
    • (2001) J Virol , vol.75 , pp. 5730-5739
    • Nuesch, J.P.1    Christensen, J.2    Rommelaere, J.3
  • 13
    • 0037213242 scopus 로고    scopus 로고
    • Regulation of minute virus of mice NS1 replicative functions by atypical PKClambda in vivo
    • Nuesch JP, Lachmann S, Corbau R, Rommelaere J (2003) Regulation of minute virus of mice NS1 replicative functions by atypical PKClambda in vivo. J Virol 77:433-442
    • (2003) J Virol , vol.77 , pp. 433-442
    • Nuesch, J.P.1    Lachmann, S.2    Corbau, R.3    Rommelaere, J.4
  • 14
    • 0032815926 scopus 로고    scopus 로고
    • DNA unwinding functions of minute virus of mice NS1 protein are modulated specifically by the lambda isoform of protein kinase C
    • Dettwiler S, Rommelaere J, Nuesch JP (1999) DNA unwinding functions of minute virus of mice NS1 protein are modulated specifically by the lambda isoform of protein kinase C. J Virol 73:7410-7420
    • (1999) J Virol , vol.73 , pp. 7410-7420
    • Dettwiler, S.1    Rommelaere, J.2    Nuesch, J.P.3
  • 15
    • 0037744681 scopus 로고    scopus 로고
    • Novel PKCeta is required to activate replicative functions of the major nonstructural protein NS1 of minute virus of mice
    • Lachmann S, Rommeleare J, Nuesch JP (2003) Novel PKCeta is required to activate replicative functions of the major nonstructural protein NS1 of minute virus of mice. J Virol 77:8048-8060
    • (2003) J Virol , vol.77 , pp. 8048-8060
    • Lachmann, S.1    Rommeleare, J.2    Nuesch, J.P.3
  • 16
    • 79959365543 scopus 로고    scopus 로고
    • Targeting PDK1 in cancer
    • Raimondi C, Falasca M (2011) Targeting PDK1 in cancer. Curr Med Chem 18:2763-2769
    • (2011) Curr Med Chem , vol.18 , pp. 2763-2769
    • Raimondi, C.1    Falasca, M.2
  • 17
    • 84863304315 scopus 로고    scopus 로고
    • Molecular pathways: Rodent parvoviruses-mechanisms of oncolysis and prospects for clinical cancer treatment
    • Nuesch JP, Lacroix J, Marchini A, Rommelaere J (2012) Molecular pathways: rodent parvoviruses-mechanisms of oncolysis and prospects for clinical cancer treatment. Clin Cancer Res 18:3516-3523
    • (2012) Clin Cancer Res , vol.18 , pp. 3516-3523
    • Nuesch, J.P.1    Lacroix, J.2    Marchini, A.3    Rommelaere, J.4
  • 18
    • 77952737333 scopus 로고    scopus 로고
    • Through its nonstructural protein NS1, parvovirus H-1 induces apoptosis via accumulation of reactive oxygen species
    • Hristov G, Kramer M, Li J, El-Andaloussi N, Mora R, Daeffler L et al (2010) Through its nonstructural protein NS1, parvovirus H-1 induces apoptosis via accumulation of reactive oxygen species. J Virol 84:5909-5922
    • (2010) J Virol , vol.84 , pp. 5909-5922
    • Hristov, G.1    Kramer, M.2    Li, J.3    El-Andaloussi, N.4    Mora, R.5    Daeffler, L.6
  • 19
    • 0035050285 scopus 로고    scopus 로고
    • Effective infection, apoptotic cell killing and gene transfer of human hepatoma cells but not primary hepatocytes by parvovirus H1 and derived vectors
    • Moehler M, Blechacz B, Weiskopf N, Zeidler M, Stremmel W, Rommelaere J et al (2001) Effective infection, apoptotic cell killing and gene transfer of human hepatoma cells but not primary hepatocytes by parvovirus H1 and derived vectors. Cancer Gene Ther 8:158-167
    • (2001) Cancer Gene Ther , vol.8 , pp. 158-167
    • Moehler, M.1    Blechacz, B.2    Weiskopf, N.3    Zeidler, M.4    Stremmel, W.5    Rommelaere, J.6
  • 20
    • 0032743996 scopus 로고    scopus 로고
    • Parvovirus H-1-induced cell death: Influence of intracellular NAD consumption on the regulation of necrosis and apoptosis
    • Ran Z, Rayet B, Rommelaere J, Faisst S (1999) Parvovirus H-1-induced cell death: influence of intracellular NAD consumption on the regulation of necrosis and apoptosis. Virus Res 65:161-174
    • (1999) Virus Res , vol.65 , pp. 161-174
    • Ran, Z.1    Rayet, B.2    Rommelaere, J.3    Faisst, S.4
  • 21
    • 0031691259 scopus 로고    scopus 로고
    • Induction of programmed cell death by parvovirus H-1 in U937 cells: Connection with the tumor necrosis factor alpha signalling pathway
    • Rayet B, Lopez-Guerrero JA, Rommelaere J, Dinsart C (1998) Induction of programmed cell death by parvovirus H-1 in U937 cells: connection with the tumor necrosis factor alpha signalling pathway. J Virol 72:8893-8903
    • (1998) J Virol , vol.72 , pp. 8893-8903
    • Rayet, B.1    Lopez-Guerrero, J.A.2    Rommelaere, J.3    Dinsart, C.4
  • 22
    • 54349126677 scopus 로고    scopus 로고
    • Killing of p53-deficient hepatoma cells by parvovirus H-1 and chemotherapeutics requires promyelocytic leukemia protein
    • Sieben M, Herzer K, Zeidler M, Heinrichs V, Leuchs B, Schuler M et al (2008) Killing of p53-deficient hepatoma cells by parvovirus H-1 and chemotherapeutics requires promyelocytic leukemia protein. World J Gastroenterol 14:3819-3828
    • (2008) World J Gastroenterol , vol.14 , pp. 3819-3828
    • Sieben, M.1    Herzer, K.2    Zeidler, M.3    Heinrichs, V.4    Leuchs, B.5    Schuler, M.6
  • 23
    • 34247170947 scopus 로고    scopus 로고
    • Cytosolic activation of cathepsins mediates parvovirus H-1-induced killing of cisplatin and TRAIL-resistant glioma cells
    • Di Piazza M, Mader C, Geletneky K, Herrero YCM, Weber E, Schlehofer J et al (2007) Cytosolic activation of cathepsins mediates parvovirus H-1-induced killing of cisplatin and TRAIL-resistant glioma cells. J Virol 81:4186-4198
    • (2007) J Virol , vol.81 , pp. 4186-4198
    • Di Piazza, M.1    Mader, C.2    Geletneky, K.3    Herrero, Y.C.M.4    Weber, E.5    Schlehofer, J.6
  • 24
    • 84884687913 scopus 로고    scopus 로고
    • Vesicular transport of progeny parvovirus particles through ER and Golgi regulates maturation and cytolysis
    • Bar S, Rommelaere J, Nuesch JP (2013) Vesicular transport of progeny parvovirus particles through ER and Golgi regulates maturation and cytolysis. PLoS Pathog 9:e1003605
    • (2013) PLoS Pathog , vol.9
    • Bar, S.1    Rommelaere, J.2    Nuesch, J.P.3
  • 25
    • 0025080463 scopus 로고
    • Programmed killing of human cells by means of an inducible clone of parvoviral genes encoding non-structural proteins
    • Caillet-Fauquet P, Perros M, Brandenburger A, Spegelaere P, Rommelaere J (1990) Programmed killing of human cells by means of an inducible clone of parvoviral genes encoding non-structural proteins. EMBO J 9:2989-2995
    • (1990) EMBO J , vol.9 , pp. 2989-2995
    • Caillet-Fauquet, P.1    Perros, M.2    Brandenburger, A.3    Spegelaere, P.4    Rommelaere, J.5
  • 26
    • 0028040382 scopus 로고
    • The cytotoxicity of the autonomous parvovirus minute virus of mice nonstructural proteins in FR3T3 rat cells depends on oncogene expression
    • Mousset S, Ouadrhiri Y, Caillet-Fauquet P, Rommelaere J (1994) The cytotoxicity of the autonomous parvovirus minute virus of mice nonstructural proteins in FR3T3 rat cells depends on oncogene expression. J Virol 68:6446-6453
    • (1994) J Virol , vol.68 , pp. 6446-6453
    • Mousset, S.1    Ouadrhiri, Y.2    Caillet-Fauquet, P.3    Rommelaere, J.4
  • 27
    • 0030738386 scopus 로고    scopus 로고
    • Parvovirus initiation factor PIF: A novel human DNA-binding factor which coordinately recognizes two ACGT motifs
    • Christensen J, Cotmore SF, Tattersall P (1997) Parvovirus initiation factor PIF: a novel human DNA-binding factor which coordinately recognizes two ACGT motifs. J Virol 71:5733-5741
    • (1997) J Virol , vol.71 , pp. 5733-5741
    • Christensen, J.1    Cotmore, S.F.2    Tattersall, P.3
  • 28
    • 0031031923 scopus 로고    scopus 로고
    • A novel cellular site-specific DNA-binding protein cooperates with the viral NS1 polypeptide to initiate parvovirus DNA replication
    • Christensen J, Cotmore SF, Tattersall P (1997) A novel cellular site-specific DNA-binding protein cooperates with the viral NS1 polypeptide to initiate parvovirus DNA replication. J Virol 71:1405-1416
    • (1997) J Virol , vol.71 , pp. 1405-1416
    • Christensen, J.1    Cotmore, S.F.2    Tattersall, P.3
  • 29
    • 0026802053 scopus 로고
    • In vitro excision and replication of 50 telomeres of minute virus of mice DNA from cloned palindromic concatemer junctions
    • Cotmore SF, Nuesch JP, Tattersall P (1992) In vitro excision and replication of 50 telomeres of minute virus of mice DNA from cloned palindromic concatemer junctions. Virology 190:365-377
    • (1992) Virology , vol.190 , pp. 365-377
    • Cotmore, S.F.1    Nuesch, J.P.2    Tattersall, P.3
  • 30
    • 0027405966 scopus 로고
    • Asymmetric resolution of a parvovirus palindrome in vitro
    • Cotmore SF, Nuesch JP, Tattersall P (1993) Asymmetric resolution of a parvovirus palindrome in vitro. J Virol 67:1579-1589
    • (1993) J Virol , vol.67 , pp. 1579-1589
    • Cotmore, S.F.1    Nuesch, J.P.2    Tattersall, P.3
  • 31
    • 0028146087 scopus 로고
    • An asymmetric nucleotide in the parvoviral 30 hairpin directs segregation of a single active origin of DNA replication
    • Cotmore SF, Tattersall P (1994) An asymmetric nucleotide in the parvoviral 30 hairpin directs segregation of a single active origin of DNA replication. EMBO J 13:4145-4152
    • (1994) EMBO J , vol.13 , pp. 4145-4152
    • Cotmore, S.F.1    Tattersall, P.2
  • 32
    • 0033977269 scopus 로고    scopus 로고
    • Two widely spaced initiator binding sites create an HMG1-dependent parvovirus rolling-hairpin replication origin
    • Cotmore SF, Christensen J, Tattersall P (2000) Two widely spaced initiator binding sites create an HMG1-dependent parvovirus rolling-hairpin replication origin. J Virol 74:1332-1341
    • (2000) J Virol , vol.74 , pp. 1332-1341
    • Cotmore, S.F.1    Christensen, J.2    Tattersall, P.3
  • 33
    • 0026657913 scopus 로고
    • Terminal regions of the NS-1 protein of the parvovirus minute virus of mice are involved in cytotoxicity and promoter trans inhibition
    • Legendre D, Rommelaere J (1992) Terminal regions of the NS-1 protein of the parvovirus minute virus of mice are involved in cytotoxicity and promoter trans inhibition. J Virol 66:5705-5713
    • (1992) J Virol , vol.66 , pp. 5705-5713
    • Legendre, D.1    Rommelaere, J.2
  • 34
    • 0025039287 scopus 로고
    • Mutation of lysine 405 to serine in the parvovirus H-1 NS1 abolishes its functions for viral DNA replication, late promoter trans activation, and cytotoxicity
    • Li X, Rhode SL 3rd (1990) Mutation of lysine 405 to serine in the parvovirus H-1 NS1 abolishes its functions for viral DNA replication, late promoter trans activation, and cytotoxicity. J Virol 64:4654-4660
    • (1990) J Virol , vol.64 , pp. 4654-4660
    • Li, X.1    Rhode III, S.L.2
  • 35
    • 0022180651 scopus 로고
    • Trans-Activation of parvovirus P38 promoter by the 76 K noncapsid protein
    • Rhode SL 3rd (1985) trans-Activation of parvovirus P38 promoter by the 76 K noncapsid protein. J Virol 55:886-889
    • (1985) J Virol , vol.55 , pp. 886-889
    • Rhode III, S.L.1
  • 36
    • 0025064272 scopus 로고
    • NS-1 and NS-2 proteins may act synergistically in the cytopathogenicity of parvovirus MVMp
    • Brandenburger A, Legendre D, Avalosse B, Rommelaere J (1990) NS-1 and NS-2 proteins may act synergistically in the cytopathogenicity of parvovirus MVMp. Virology 174:576-584
    • (1990) Virology , vol.174 , pp. 576-584
    • Brandenburger, A.1    Legendre, D.2    Avalosse, B.3    Rommelaere, J.4
  • 37
    • 9944228589 scopus 로고    scopus 로고
    • Selective alterations of the host cell architecture upon infection with parvovirus minute virus of mice
    • Nuesch JP, Lachmann S, Rommelaere J (2005) Selective alterations of the host cell architecture upon infection with parvovirus minute virus of mice. Virology 331:159-174
    • (2005) Virology , vol.331 , pp. 159-174
    • Nuesch, J.P.1    Lachmann, S.2    Rommelaere, J.3
  • 38
    • 0242492883 scopus 로고    scopus 로고
    • Modulation of minute virus of mice cytotoxic activities through site-directed mutagenesis within the NS coding region
    • Daeffler L, Horlein R, Rommelaere J, Nuesch JP (2003) Modulation of minute virus of mice cytotoxic activities through site-directed mutagenesis within the NS coding region. J Virol 77:12466-12478
    • (2003) J Virol , vol.77 , pp. 12466-12478
    • Daeffler, L.1    Horlein, R.2    Rommelaere, J.3    Nuesch, J.P.4
  • 39
    • 0036284381 scopus 로고    scopus 로고
    • Parvovirus initiator protein NS1 and RPA coordinate replication fork progression in a reconstituted DNA replication system
    • Christensen J, Tattersall P (2002) Parvovirus initiator protein NS1 and RPA coordinate replication fork progression in a reconstituted DNA replication system. J Virol 76:6518-6531
    • (2002) J Virol , vol.76 , pp. 6518-6531
    • Christensen, J.1    Tattersall, P.2
  • 40
    • 0031957916 scopus 로고    scopus 로고
    • Identification of a novel cellular TPR-containing protein, SGT, that interacts with the nonstructural protein NS1 of parvovirus H-1
    • Cziepluch C, Kordes E, Poirey R, Grewenig A, Rommelaere J, Jauniaux JC (1998) Identification of a novel cellular TPR-containing protein, SGT, that interacts with the nonstructural protein NS1 of parvovirus H-1. J Virol 72:4149-4156
    • (1998) J Virol , vol.72 , pp. 4149-4156
    • Cziepluch, C.1    Kordes, E.2    Poirey, R.3    Grewenig, A.4    Rommelaere, J.5    Jauniaux, J.C.6
  • 41
    • 0032889252 scopus 로고    scopus 로고
    • A novel heterogeneous nuclear ribonucleoproteinlike protein interacts with NS1 of the minute virus of mice
    • Harris CE, Boden RA, Astell CR (1999) A novel heterogeneous nuclear ribonucleoproteinlike protein interacts with NS1 of the minute virus of mice. J Virol 73:72-80
    • (1999) J Virol , vol.73 , pp. 72-80
    • Harris, C.E.1    Boden, R.A.2    Astell, C.R.3
  • 42
    • 0028961938 scopus 로고
    • Transcriptional activation by the parvoviral nonstructural protein NS-1 is mediated via a direct interaction with Sp1
    • Krady JK, Ward DC (1995) Transcriptional activation by the parvoviral nonstructural protein NS-1 is mediated via a direct interaction with Sp1. Mol Cell Biol 15:524-533
    • (1995) Mol Cell Biol , vol.15 , pp. 524-533
    • Krady, J.K.1    Ward, D.C.2
  • 43
    • 0032518479 scopus 로고    scopus 로고
    • An Sp1-binding site and TATA element are sufficient to support full transactivation by proximally bound NS1 protein of minute virus of mice
    • Lorson C, Pearson J, Burger L, Pintel DJ (1998) An Sp1-binding site and TATA element are sufficient to support full transactivation by proximally bound NS1 protein of minute virus of mice. Virology 240:326-337
    • (1998) Virology , vol.240 , pp. 326-337
    • Lorson, C.1    Pearson, J.2    Burger, L.3    Pintel, D.J.4
  • 44
    • 33646439683 scopus 로고    scopus 로고
    • NS1 interaction with CKII alpha: Novel protein complex mediating parvovirus-induced cytotoxicity
    • Nuesch JP, Rommelaere J (2006) NS1 interaction with CKII alpha: novel protein complex mediating parvovirus-induced cytotoxicity. J Virol 80:4729-4739
    • (2006) J Virol , vol.80 , pp. 4729-4739
    • Nuesch, J.P.1    Rommelaere, J.2
  • 45
    • 34547629250 scopus 로고    scopus 로고
    • A viral adaptor protein modulating casein kinase II activity induces cytopathic effects in permissive cells
    • Nuesch JP, Rommelaere J (2007) A viral adaptor protein modulating casein kinase II activity induces cytopathic effects in permissive cells. Proc Natl Acad Sci U S A 104:12482-12487
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 12482-12487
    • Nuesch, J.P.1    Rommelaere, J.2
  • 46
    • 13444270802 scopus 로고    scopus 로고
    • Expression profiling of human hepatoma cells reveals global repression of genes involved in cell proliferation, growth, and apoptosis upon infection with parvovirus H-1
    • Li J, Werner E, Hergenhahn M, Poirey R, Luo Z, Rommelaere J et al (2005) Expression profiling of human hepatoma cells reveals global repression of genes involved in cell proliferation, growth, and apoptosis upon infection with parvovirus H-1. J Virol 79:2274-2286
    • (2005) J Virol , vol.79 , pp. 2274-2286
    • Li, J.1    Werner, E.2    Hergenhahn, M.3    Poirey, R.4    Luo, Z.5    Rommelaere, J.6
  • 47
    • 78449264186 scopus 로고    scopus 로고
    • Parvovirus minute virus of mice induces a DNA damage response that facilitates viral replication
    • Adeyemi RO, Landry S, Davis ME, Weitzman MD, Pintel DJ (2010) Parvovirus minute virus of mice induces a DNA damage response that facilitates viral replication. PLoS Pathog 6:e1001141
    • (2010) PLoS Pathog , vol.6
    • Adeyemi, R.O.1    Landry, S.2    Davis, M.E.3    Weitzman, M.D.4    Pintel, D.J.5
  • 48
    • 0035051929 scopus 로고    scopus 로고
    • In vivo accumulation of cyclin A and cellular replication factors in autonomous parvovirus minute virus of mice-associated replication bodies
    • Bashir T, Rommelaere J, Cziepluch C (2001) In vivo accumulation of cyclin A and cellular replication factors in autonomous parvovirus minute virus of mice-associated replication bodies. J Virol 75:4394-4398
    • (2001) J Virol , vol.75 , pp. 4394-4398
    • Bashir, T.1    Rommelaere, J.2    Cziepluch, C.3
  • 49
    • 78751706652 scopus 로고    scopus 로고
    • Recruitment of DNA replication and damage response proteins to viral replication centers during infection with NS2 mutants of Minute Virus of Mice (MVM)
    • Ruiz Z, Mihaylov IS, Cotmore SF, Tattersall P (2011) Recruitment of DNA replication and damage response proteins to viral replication centers during infection with NS2 mutants of Minute Virus of Mice (MVM). Virology 410:375-384
    • (2011) Virology , vol.410 , pp. 375-384
    • Ruiz, Z.1    Mihaylov, I.S.2    Cotmore, S.F.3    Tattersall, P.4
  • 50
    • 84864386141 scopus 로고    scopus 로고
    • Replication of minute virus of mice in murine cells is facilitated by virally induced depletion of p21
    • Adeyemi RO, Pintel DJ (2012) Replication of minute virus of mice in murine cells is facilitated by virally induced depletion of p21. J Virol 86:8328-8332
    • (2012) J Virol , vol.86 , pp. 8328-8332
    • Adeyemi, R.O.1    Pintel, D.J.2
  • 51
    • 0029003455 scopus 로고
    • The nonstructural proteins of the autonomous parvovirus minute virus of mice interfere with the cell cycle, inducing accumulation in G2
    • Op De Beeck A, Anouja F, Mousset S, Rommelaere J, Caillet-Fauquet P (1995) The nonstructural proteins of the autonomous parvovirus minute virus of mice interfere with the cell cycle, inducing accumulation in G2. Cell Growth Differ 6:781-787
    • (1995) Cell Growth Differ , vol.6 , pp. 781-787
    • Op De Beeck, A.1    Anouja, F.2    Mousset, S.3    Rommelaere, J.4    Caillet-Fauquet, P.5
  • 54
    • 0023746443 scopus 로고
    • Minute virus of mice non-structural protein NS-1 is necessary and sufficient for trans-activation of the viral P39 promoter
    • Doerig C, Hirt B, Beard P, Antonietti JP (1988) Minute virus of mice non-structural protein NS-1 is necessary and sufficient for trans-activation of the viral P39 promoter. J Gen Virol 69(Pt 10):2563-2573
    • (1988) J Gen Virol , vol.69 , Issue.PART 10 , pp. 2563-2573
    • Doerig, C.1    Hirt, B.2    Beard, P.3    Antonietti, J.P.4
  • 55
    • 0025073223 scopus 로고
    • Nonstructural protein of parvoviruses B19 and minute virus of mice controls transcription
    • Doerig C, Hirt B, Antonietti JP, Beard P (1990) Nonstructural protein of parvoviruses B19 and minute virus of mice controls transcription. J Virol 64:387-396
    • (1990) J Virol , vol.64 , pp. 387-396
    • Doerig, C.1    Hirt, B.2    Antonietti, J.P.3    Beard, P.4
  • 56
    • 0026804644 scopus 로고
    • Expression of functional parvoviral NS1 from recombinant vaccinia virus: Effects of mutations in the nucleotide-binding motif
    • Nuesch JP, Cotmore SF, Tattersall P (1992) Expression of functional parvoviral NS1 from recombinant vaccinia virus: effects of mutations in the nucleotide-binding motif. Virology 191:406-416
    • (1992) Virology , vol.191 , pp. 406-416
    • Nuesch, J.P.1    Cotmore, S.F.2    Tattersall, P.3
  • 57
    • 0036059242 scopus 로고    scopus 로고
    • Caspase activation is required for permissive replication of Aleutian mink disease parvovirus in vitro
    • Best SM, Wolfinbarger JB, Bloom ME (2002) Caspase activation is required for permissive replication of Aleutian mink disease parvovirus in vitro. Virology 292:224-234
    • (2002) Virology , vol.292 , pp. 224-234
    • Best, S.M.1    Wolfinbarger, J.B.2    Bloom, M.E.3
  • 58
    • 1542375390 scopus 로고    scopus 로고
    • Caspase activation during virus infection: More than just the kiss of death?
    • Best SM, Bloom ME (2004) Caspase activation during virus infection: more than just the kiss of death? Virology 320:191-194
    • (2004) Virology , vol.320 , pp. 191-194
    • Best, S.M.1    Bloom, M.E.2
  • 59
    • 38849111120 scopus 로고    scopus 로고
    • Parvovirus interference with intracellular signalling: Mechanism of PKCeta activation in MVM-infected A9 fibroblasts
    • Lachmann S, Bar S, Rommelaere J, Nuesch JP (2008) Parvovirus interference with intracellular signalling: mechanism of PKCeta activation in MVM-infected A9 fibroblasts. Cell Microbiol 10:755-769
    • (2008) Cell Microbiol , vol.10 , pp. 755-769
    • Lachmann, S.1    Bar, S.2    Rommelaere, J.3    Nuesch, J.P.4
  • 60
    • 0025174652 scopus 로고
    • Sensitization of transformed rat cells to parvovirus MVMp is restricted to specific oncogenes
    • Salome N, van Hille B, Duponchel N, Meneguzzi G, Cuzin F, Rommelaere J et al (1990) Sensitization of transformed rat cells to parvovirus MVMp is restricted to specific oncogenes. Oncogene 5:123-130
    • (1990) Oncogene , vol.5 , pp. 123-130
    • Salome, N.1    Van Hille, B.2    Duponchel, N.3    Meneguzzi, G.4    Cuzin, F.5    Rommelaere, J.6
  • 61
    • 50849129909 scopus 로고    scopus 로고
    • Vesicular egress of non-enveloped lytic parvoviruses depends on gelsolin functioning
    • Bar S, Daeffler L, Rommelaere J, Nuesch JP (2008) Vesicular egress of non-enveloped lytic parvoviruses depends on gelsolin functioning. PLoS Pathog 4:e1000126
    • (2008) PLoS Pathog , vol.4
    • Bar, S.1    Daeffler, L.2    Rommelaere, J.3    Nuesch, J.P.4
  • 62
    • 66149093119 scopus 로고    scopus 로고
    • Ezrin-radixin-moesin family proteins are involved in parvovirus replication and spreading
    • Nuesch JP, Bar S, Lachmann S, Rommelaere J (2009) Ezrin-radixin-moesin family proteins are involved in parvovirus replication and spreading. J Virol 83:5854-5863
    • (2009) J Virol , vol.83 , pp. 5854-5863
    • Nuesch, J.P.1    Bar, S.2    Lachmann, S.3    Rommelaere, J.4
  • 63
    • 58149161889 scopus 로고    scopus 로고
    • Viral proteins killing tumor cells: New weapons in the fight against cancer
    • Nuesch JP, Bar S, Rommelaere J (2008) Viral proteins killing tumor cells: new weapons in the fight against cancer. Cancer Biol Ther 7:1374-1376
    • (2008) Cancer Biol Ther , vol.7 , pp. 1374-1376
    • Nuesch, J.P.1    Bar, S.2    Rommelaere, J.3
  • 64
    • 0029143369 scopus 로고
    • Minute virus of mice transcriptional activator protein NS1 binds directly to the transactivation region of the viral P38 promoter in a strictly ATP-dependent manner
    • Christensen J, Cotmore SF, Tattersall P (1995) Minute virus of mice transcriptional activator protein NS1 binds directly to the transactivation region of the viral P38 promoter in a strictly ATP-dependent manner. J Virol 69:5422-5430
    • (1995) J Virol , vol.69 , pp. 5422-5430
    • Christensen, J.1    Cotmore, S.F.2    Tattersall, P.3
  • 65
    • 0028136544 scopus 로고
    • Mutations in the NTP-binding motif of minute virus of mice (MVM) NS-1 protein uncouple ATPase and DNA helicase functions
    • Jindal HK, Yong CB, Wilson GM, Tam P, Astell CR (1994) Mutations in the NTP-binding motif of minute virus of mice (MVM) NS-1 protein uncouple ATPase and DNA helicase functions. J Biol Chem 269:3283-3289
    • (1994) J Biol Chem , vol.269 , pp. 3283-3289
    • Jindal, H.K.1    Yong, C.B.2    Wilson, G.M.3    Tam, P.4    Astell, C.R.5
  • 66
    • 0032506101 scopus 로고    scopus 로고
    • Amino acids 16-275 of minute virus of mice NS1 include a domain that specifically binds (ACCA)2-3-containing DNA
    • Mouw M, Pintel DJ (1998) Amino acids 16-275 of minute virus of mice NS1 include a domain that specifically binds (ACCA)2-3-containing DNA. Virology 251:123-131
    • (1998) Virology , vol.251 , pp. 123-131
    • Mouw, M.1    Pintel, D.J.2
  • 67
    • 0027496233 scopus 로고
    • Nuclear targeting of the parvoviral replicator molecule NS1: Evidence for self-association prior to nuclear transport
    • Nuesch JP, Tattersall P (1993) Nuclear targeting of the parvoviral replicator molecule NS1: evidence for self-association prior to nuclear transport. Virology 196:637-651
    • (1993) Virology , vol.196 , pp. 637-651
    • Nuesch, J.P.1    Tattersall, P.2
  • 68
    • 0029063821 scopus 로고
    • Sequence motifs in the replicator protein of parvovirus MVM essential for nicking and covalent attachment to the viral origin: Identification of the linking tyrosine
    • Nuesch JP, Cotmore SF, Tattersall P (1995) Sequence motifs in the replicator protein of parvovirus MVM essential for nicking and covalent attachment to the viral origin: identification of the linking tyrosine. Virology 209:122-135
    • (1995) Virology , vol.209 , pp. 122-135
    • Nuesch, J.P.1    Cotmore, S.F.2    Tattersall, P.3
  • 69
    • 0030842597 scopus 로고    scopus 로고
    • Inhibition of parvovirus minute virus of mice replication by a peptide involved in the oligomerization of nonstructural protein NS1
    • Pujol A, Deleu L, Nuesch JP, Cziepluch C, Jauniaux JC, Rommelaere J (1997) Inhibition of parvovirus minute virus of mice replication by a peptide involved in the oligomerization of nonstructural protein NS1. J Virol 71:7393-7403
    • (1997) J Virol , vol.71 , pp. 7393-7403
    • Pujol, A.1    Deleu, L.2    Nuesch, J.P.3    Cziepluch, C.4    Jauniaux, J.C.5    Rommelaere, J.6
  • 70
    • 0025992606 scopus 로고
    • Expression of minute virus of mice major nonstructural protein in insect cells: Purification and identification of ATPase and helicase activities
    • Wilson GM, Jindal HK, Yeung DE, Chen W, Astell CR (1991) Expression of minute virus of mice major nonstructural protein in insect cells: purification and identification of ATPase and helicase activities. Virology 185:90-98
    • (1991) Virology , vol.185 , pp. 90-98
    • Wilson, G.M.1    Jindal, H.K.2    Yeung, D.E.3    Chen, W.4    Astell, C.R.5
  • 71
    • 0027985384 scopus 로고
    • Targeting of promoters for trans activation by a carboxy-terminal domain of the NS-1 protein of the parvovirus minute virus of mice
    • Legendre D, Rommelaere J (1994) Targeting of promoters for trans activation by a carboxy-terminal domain of the NS-1 protein of the parvovirus minute virus of mice. J Virol 68:7974-7985
    • (1994) J Virol , vol.68 , pp. 7974-7985
    • Legendre, D.1    Rommelaere, J.2
  • 72
    • 0026748738 scopus 로고
    • Conserved sequence motifs in the initiator proteins for rolling circle DNA replication encoded by diverse replicons from eubacteria, eucaryotes and archaebacteria
    • Ilyina TV, Koonin EV (1992) Conserved sequence motifs in the initiator proteins for rolling circle DNA replication encoded by diverse replicons from eubacteria, eucaryotes and archaebacteria. Nucleic Acids Res 20:3279-3285
    • (1992) Nucleic Acids Res , vol.20 , pp. 3279-3285
    • Ilyina, T.V.1    Koonin, E.V.2
  • 73
    • 0025261685 scopus 로고
    • A new superfamily of putative NTP-binding domains encoded by genomes of small DNA and RNA viruses
    • Gorbalenya AE, Koonin EV, Wolf YI (1990) A new superfamily of putative NTP-binding domains encoded by genomes of small DNA and RNA viruses. FEBS Lett 262:145-148
    • (1990) FEBS Lett , vol.262 , pp. 145-148
    • Gorbalenya, A.E.1    Koonin, E.V.2    Wolf, Y.I.3
  • 74
    • 0036671409 scopus 로고    scopus 로고
    • Structural unity among viral origin binding proteins: Crystal structure of the nuclease domain of adeno-associated virus Rep
    • Hickman AB, Ronning DR, Kotin RM, Dyda F (2002) Structural unity among viral origin binding proteins: crystal structure of the nuclease domain of adeno-associated virus Rep. Mol Cell 10:327-337
    • (2002) Mol Cell , vol.10 , pp. 327-337
    • Hickman, A.B.1    Ronning, D.R.2    Kotin, R.M.3    Dyda, F.4
  • 75
    • 84886879224 scopus 로고    scopus 로고
    • Structure of the NS1 protein N-terminal origin-recognition/nickase domain from the emerging human bocavirus
    • Tewary SK, Zhao H, Shen W, Qiu J, Tang L (2013) Structure of the NS1 protein N-terminal origin-recognition/nickase domain from the emerging human bocavirus. J Virol 87(21): 11487-11493
    • (2013) J Virol , vol.87 , Issue.21 , pp. 11487-11493
    • Tewary, S.K.1    Zhao, H.2    Shen, W.3    Qiu, J.4    Tang, L.5
  • 76
    • 0028819067 scopus 로고
    • The NS1 polypeptide of the murine parvovirus minute virus of mice binds to DNA sequences containing the motif [ACCA]2-3
    • Cotmore SF, Christensen J, Nuesch JP, Tattersall P (1995) The NS1 polypeptide of the murine parvovirus minute virus of mice binds to DNA sequences containing the motif [ACCA]2-3. J Virol 69:1652-1660
    • (1995) J Virol , vol.69 , pp. 1652-1660
    • Cotmore, S.F.1    Christensen, J.2    Nuesch, J.P.3    Tattersall, P.4
  • 77
    • 0031706629 scopus 로고    scopus 로고
    • High-mobility group 1/2 proteins are essential for initiating rolling-circle-type DNA replication at a parvovirus hairpin origin
    • Cotmore SF, Tattersall P (1998) High-mobility group 1/2 proteins are essential for initiating rolling-circle-type DNA replication at a parvovirus hairpin origin. J Virol 72:8477-8484
    • (1998) J Virol , vol.72 , pp. 8477-8484
    • Cotmore, S.F.1    Tattersall, P.2
  • 78
    • 0024550638 scopus 로고
    • ATP-dependent assembly of double hexamers of SV40 T antigen at the viral origin of DNA replication
    • Mastrangelo IA, Hough PV, Wall JS, Dodson M, Dean FB, Hurwitz J (1989) ATP-dependent assembly of double hexamers of SV40 T antigen at the viral origin of DNA replication. Nature 338:658-662
    • (1989) Nature , vol.338 , pp. 658-662
    • Mastrangelo, I.A.1    Hough, P.V.2    Wall, J.S.3    Dodson, M.4    Dean, F.B.5    Hurwitz, J.6
  • 79
    • 0026587789 scopus 로고
    • Parvovirus H-1 P38 promoter requires the transactivation region (tar), an SP1 site, and a TATA box for full activity
    • Gu ML, Chen FX, Rhode SL (1992) Parvovirus H-1 P38 promoter requires the transactivation region (tar), an SP1 site, and a TATA box for full activity. Virology 187:10-17
    • (1992) Virology , vol.187 , pp. 10-17
    • Gu, M.L.1    Chen, F.X.2    Rhode, S.L.3
  • 80
    • 0026806865 scopus 로고
    • Trans-activation of H-1 parvovirus P38 promoter is correlated with increased binding of cellular protein(s) to the trans-activation responsive element (tar)
    • Gu ML, Rhode SL (1992) Trans-activation of H-1 parvovirus P38 promoter is correlated with increased binding of cellular protein(s) to the trans-activation responsive element (tar). Virology 190:116-123
    • (1992) Virology , vol.190 , pp. 116-123
    • Gu, M.L.1    Rhode, S.L.2
  • 81
    • 0031771850 scopus 로고    scopus 로고
    • Replicative functions of minute virus of mice NS1 protein are regulated in vitro by phosphorylation through protein kinase C
    • Nuesch JP, Dettwiler S, Corbau R, Rommelaere J (1998) Replicative functions of minute virus of mice NS1 protein are regulated in vitro by phosphorylation through protein kinase C. J Virol 72:9966-9977
    • (1998) J Virol , vol.72 , pp. 9966-9977
    • Nuesch, J.P.1    Dettwiler, S.2    Corbau, R.3    Rommelaere, J.4
  • 82
    • 84884950651 scopus 로고    scopus 로고
    • Synergistic combination of valproic acid and oncolytic parvovirus H-1PV as a potential therapy against cervical and pancreatic carcinomas
    • Li J, Bonifati S, Hristov G, Marttila T, Valmary-Degano S, Stanzel S et al (2013) Synergistic combination of valproic acid and oncolytic parvovirus H-1PV as a potential therapy against cervical and pancreatic carcinomas. EMBO Mol Med 5:1537-1555
    • (2013) EMBO Mol Med , vol.5 , pp. 1537-1555
    • Li, J.1    Bonifati, S.2    Hristov, G.3    Marttila, T.4    Valmary-Degano, S.5    Stanzel, S.6
  • 83
    • 53649106357 scopus 로고    scopus 로고
    • Dissecting the role of the 3-phosphoinositide-dependent protein kinase-1 (PDK1) signalling pathways
    • Bayascas JR (2008) Dissecting the role of the 3-phosphoinositide- dependent protein kinase-1 (PDK1) signalling pathways. Cell Cycle 7:2978-2982
    • (2008) Cell Cycle , vol.7 , pp. 2978-2982
    • Bayascas, J.R.1
  • 86
    • 18144413065 scopus 로고    scopus 로고
    • Targeting human glioblastoma cells: Comparison of nine viruses with oncolytic potential
    • Wollmann G, Tattersall P, van den Pol AN (2005) Targeting human glioblastoma cells: comparison of nine viruses with oncolytic potential. J Virol 79:6005-6022
    • (2005) J Virol , vol.79 , pp. 6005-6022
    • Wollmann, G.1    Tattersall, P.2    Van Den Pol, A.N.3
  • 87
    • 0036681993 scopus 로고    scopus 로고
    • The epidermal growth factor receptor pathway mediates resistance to sequential administration of radiation and chemotherapy in primary human glioblastoma cells in a RAS-dependent manner
    • Chakravarti A, Chakladar A, Delaney MA, Latham DE, Loeffler JS (2002) The epidermal growth factor receptor pathway mediates resistance to sequential administration of radiation and chemotherapy in primary human glioblastoma cells in a RAS-dependent manner. Cancer Res 62:4307-4315
    • (2002) Cancer Res , vol.62 , pp. 4307-4315
    • Chakravarti, A.1    Chakladar, A.2    Delaney, M.A.3    Latham, D.E.4    Loeffler, J.S.5
  • 88
    • 17144398831 scopus 로고    scopus 로고
    • Possible future issues in the treatment of glioblastomas: Special emphasis on cell migration and the resistance of migrating glioblastoma cells to apoptosis
    • Lefranc F, Brotchi J, Kiss R (2005) Possible future issues in the treatment of glioblastomas: special emphasis on cell migration and the resistance of migrating glioblastoma cells to apoptosis. J Clin Oncol 23:2411-2422
    • (2005) J Clin Oncol , vol.23 , pp. 2411-2422
    • Lefranc, F.1    Brotchi, J.2    Kiss, R.3
  • 89
    • 84857184141 scopus 로고    scopus 로고
    • Gene alterations in the PI3K/PTEN/AKT pathway as a mechanism of drug-resistance (review)
    • Hafsi S, Pezzino FM, Candido S, Ligresti G, Spandidos DA, Soua Z et al (2012) Gene alterations in the PI3K/PTEN/AKT pathway as a mechanism of drug-resistance (review). Int J Oncol 40:639-644
    • (2012) Int J Oncol , vol.40 , pp. 639-644
    • Hafsi, S.1    Pezzino, F.M.2    Candido, S.3    Ligresti, G.4    Spandidos, D.A.5    Soua, Z.6
  • 91
    • 34548052482 scopus 로고    scopus 로고
    • Combined oncolytic and vaccination activities of parvovirus H-1 in a metastatic tumor model
    • Raykov Z, Grekova S, Galabov AS, Balboni G, Koch U, Aprahamian M et al (2007) Combined oncolytic and vaccination activities of parvovirus H-1 in a metastatic tumor model. Oncol Rep 17:1493-1499
    • (2007) Oncol Rep , vol.17 , pp. 1493-1499
    • Raykov, Z.1    Grekova, S.2    Galabov, A.S.3    Balboni, G.4    Koch, U.5    Aprahamian, M.6
  • 92
    • 43049124141 scopus 로고    scopus 로고
    • Arming parvoviruses with CpG motifs to improve their oncosuppressive capacity
    • Raykov Z, Grekova S, Leuchs B, Aprahamian M, Rommelaere J (2008) Arming parvoviruses with CpG motifs to improve their oncosuppressive capacity. Int J Cancer 122:2880-2884
    • (2008) Int J Cancer , vol.122 , pp. 2880-2884
    • Raykov, Z.1    Grekova, S.2    Leuchs, B.3    Aprahamian, M.4    Rommelaere, J.5
  • 93
    • 78650609261 scopus 로고    scopus 로고
    • Enhancement of NK cell antitumor responses using an oncolytic parvovirus
    • Bhat R, Dempe S, Dinsart C, Rommelaere J (2011) Enhancement of NK cell antitumor responses using an oncolytic parvovirus. Int J Cancer 128:908-919
    • (2011) Int J Cancer , vol.128 , pp. 908-919
    • Bhat, R.1    Dempe, S.2    Dinsart, C.3    Rommelaere, J.4
  • 94
    • 84880956694 scopus 로고    scopus 로고
    • NK-cell-dependent killing of colon carcinoma cells is mediated by natural cytotoxicity receptors (NCRs) and stimulated by parvovirus infection of target cells
    • Bhat R, Rommelaere J (2013) NK-cell-dependent killing of colon carcinoma cells is mediated by natural cytotoxicity receptors (NCRs) and stimulated by parvovirus infection of target cells. BMC Cancer 13:367
    • (2013) BMC Cancer , vol.13 , pp. 367
    • Bhat, R.1    Rommelaere, J.2
  • 95
    • 23844451373 scopus 로고    scopus 로고
    • Parvovirus H-1-induced tumor cell death enhances human immune response in vitro via increased phagocytosis, maturation, and cross-presentation by dendritic cells
    • Moehler MH, Zeidler M, Wilsberg V, Cornelis JJ, Woelfel T, Rommelaere J et al (2005) Parvovirus H-1-induced tumor cell death enhances human immune response in vitro via increased phagocytosis, maturation, and cross-presentation by dendritic cells. Hum Gene Ther 16:996-1005
    • (2005) Hum Gene Ther , vol.16 , pp. 996-1005
    • Moehler, M.H.1    Zeidler, M.2    Wilsberg, V.3    Cornelis, J.J.4    Woelfel, T.5    Rommelaere, J.6
  • 96
    • 77951933403 scopus 로고    scopus 로고
    • SMAD4: A predictive marker of PDAC cell permissiveness for oncolytic infection with parvovirus H-1PV
    • Dempe S, Stroh-Dege AY, Schwarz E, Rommelaere J, Dinsart C (2010) SMAD4: a predictive marker of PDAC cell permissiveness for oncolytic infection with parvovirus H-1PV. Int J Cancer 126:2914-2927
    • (2010) Int J Cancer , vol.126 , pp. 2914-2927
    • Dempe, S.1    Stroh-Dege, A.Y.2    Schwarz, E.3    Rommelaere, J.4    Dinsart, C.5
  • 97
    • 84885025161 scopus 로고    scopus 로고
    • Capacity of wild-type and chemokine-armed parvovirus H-1PV for inhibiting neo-angiogenesis
    • Lavie M, Struyf S, Stroh-Dege A, Rommelaere J, Van Damme J, Dinsart C (2013) Capacity of wild-type and chemokine-armed parvovirus H-1PV for inhibiting neo-angiogenesis. Virology 447:221-232
    • (2013) Virology , vol.447 , pp. 221-232
    • Lavie, M.1    Struyf, S.2    Stroh-Dege, A.3    Rommelaere, J.4    Van Damme, J.5    Dinsart, C.6
  • 98
    • 84884691678 scopus 로고    scopus 로고
    • Distinct host cell fates for human malignant melanoma targeted by oncolytic rodent parvoviruses
    • Vollmers EM, Tattersall P (2013) Distinct host cell fates for human malignant melanoma targeted by oncolytic rodent parvoviruses. Virology 446:37-48
    • (2013) Virology , vol.446 , pp. 37-48
    • Vollmers, E.M.1    Tattersall, P.2
  • 99
    • 84863746921 scopus 로고    scopus 로고
    • An in-frame deletion in the NS protein-coding sequence of parvovirus H-1PV efficiently stimulates export and infectivity of progeny virions
    • Weiss N, Stroh-Dege A, Rommelaere J, Dinsart C, Salome N (2012) An in-frame deletion in the NS protein-coding sequence of parvovirus H-1PV efficiently stimulates export and infectivity of progeny virions. J Virol 86:7554-7564
    • (2012) J Virol , vol.86 , pp. 7554-7564
    • Weiss, N.1    Stroh-Dege, A.2    Rommelaere, J.3    Dinsart, C.4    Salome, N.5
  • 101
    • 0034624998 scopus 로고    scopus 로고
    • Cyclin A activates the DNA polymerase delta -dependent elongation machinery in vitro: A parvovirus DNA replication model
    • Bashir T, Horlein R, Rommelaere J, Willwand K (2000) Cyclin A activates the DNA polymerase delta -dependent elongation machinery in vitro: A parvovirus DNA replication model. Proc Natl Acad Sci U S A 97:5522-5527
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 5522-5527
    • Bashir, T.1    Horlein, R.2    Rommelaere, J.3    Willwand, K.4
  • 102
    • 0032899123 scopus 로고    scopus 로고
    • Activation of promoter P4 of the autonomous parvovirus minute virus of mice at early S phase is required for productive infection
    • Deleu L, Pujol A, Faisst S, Rommelaere J (1999) Activation of promoter P4 of the autonomous parvovirus minute virus of mice at early S phase is required for productive infection. J Virol 73:3877-3885
    • (1999) J Virol , vol.73 , pp. 3877-3885
    • Deleu, L.1    Pujol, A.2    Faisst, S.3    Rommelaere, J.4
  • 103
    • 84863553090 scopus 로고    scopus 로고
    • Targeted and armed oncolytic poxviruses for cancer: The lead example of JX-594
    • Breitbach CJ, Thorne SH, Bell JC, Kirn DH (2012) Targeted and armed oncolytic poxviruses for cancer: the lead example of JX-594. Curr Pharm Biotechnol 13:1768-1772
    • (2012) Curr Pharm Biotechnol , vol.13 , pp. 1768-1772
    • Breitbach, C.J.1    Thorne, S.H.2    Bell, J.C.3    Kirn, D.H.4
  • 105
    • 0036948433 scopus 로고    scopus 로고
    • Toward maintaining the genome: DNA damage and replication checkpoints
    • Nyberg KA et al (2002) Toward maintaining the genome: DNA damage and replication checkpoints. Annu Rev Genet 36:617-656
    • (2002) Annu Rev Genet , vol.36 , pp. 617-656
    • Nyberg, K.A.1
  • 106
    • 0025228501 scopus 로고
    • Tropomyosins of human mammary epithelial cells: Consistent defects of expression in mammary carcinoma cell lines
    • Bhattacharya B et al (1990) Tropomyosins of human mammary epithelial cells: consistent defects of expression in mammary carcinoma cell lines. Cancer Res 50(7):2105-2112
    • (1990) Cancer Res , vol.50 , Issue.7 , pp. 2105-2112
    • Bhattacharya, B.1
  • 107
    • 84882870859 scopus 로고    scopus 로고
    • The intermediate filament network protein, vimentin, is required for parvoviral infection
    • Fay N, Pante N (2013) The intermediate filament network protein, vimentin, is required for parvoviral infection. Virology 444(1-2):181-190
    • (2013) Virology , vol.444 , Issue.1-2 , pp. 181-190
    • Fay, N.1    Pante, N.2
  • 108
    • 0023880478 scopus 로고
    • Transformation of human fibroblasts by ionizing radiation, a chemical carcinogen, or simian virus 40 correlates with an increase in susceptibility to the autonomous parvoviruses H-1 virus and minute virus of mice
    • Cornelis JJ et al (1988) Transformation of human fibroblasts by ionizing radiation, a chemical carcinogen, or simian virus 40 correlates with an increase in susceptibility to the autonomous parvoviruses H-1 virus and minute virus of mice. J Virol 62(5):1679-1686
    • (1988) J Virol , vol.62 , Issue.5 , pp. 1679-1686
    • Cornelis, J.J.1
  • 109
    • 81555222528 scopus 로고    scopus 로고
    • Interferon gamma improves the vaccination potential of oncolytic parvovirus H-1PV for the treatment of peritoneal carcinomatosis in pancreatic cancer
    • Grekova SP et al (2011) Interferon gamma improves the vaccination potential of oncolytic parvovirus H-1PV for the treatment of peritoneal carcinomatosis in pancreatic cancer. Cancer Biol Ther 12(10):888-895
    • (2011) Cancer Biol Ther , vol.12 , Issue.10 , pp. 888-895
    • Grekova, S.P.1
  • 110
    • 84906886248 scopus 로고    scopus 로고
    • PKCeta/Rdx-driven phosphorylation of PDK1: A novel mechanism promoting survival of cancer cells and permissiveness for parvovirus-induced lysis
    • submitted
    • Bar S, Rommelaere J, Nüesch JPF. PKCeta/Rdx-driven phosphorylation of PDK1: a novel mechanism promoting survival of cancer cells and permissiveness for parvovirus-induced lysis. Cell Host Microbe, submitted
    • Cell Host Microbe
    • Bar, S.1    Rommelaere, J.2    Nüesch, J.P.F.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.