{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,6]],"date-time":"2026-10-06T17:38:27Z","timestamp":1791308307593,"version":"4.3.1"},"reference-count":112,"publisher":"Public Library of Science (PLoS)","issue":"7","license":[{"start":{"date-parts":[[2010,7,8]],"date-time":"2010-07-08T00:00:00Z","timestamp":1278547200000},"content-version":"unspecified","delay-in-days":0,"URL":"http:\/\/creativecommons.org\/licenses\/by\/4.0\/"}],"content-domain":{"domain":["www.plospathogens.org"],"crossmark-restriction":false},"short-container-title":["PLoS Pathog"],"DOI":"10.1371\/journal.ppat.1000984","type":"journal-article","created":{"date-parts":[[2010,7,8]],"date-time":"2010-07-08T16:49:16Z","timestamp":1278607756000},"page":"e1000984","update-policy":"https:\/\/doi.org\/10.1371\/journal.ppat.corrections_policy","source":"Crossref","is-referenced-by-count":82,"title":["Vaccinia Virus\u2013Encoded Ribonucleotide Reductase Subunits Are Differentially Required for Replication and Pathogenesis"],"prefix":"10.1371","volume":"6","author":[{"given":"Don B.","family":"Gammon","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Branawan","family":"Gowrishankar","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sophie","family":"Duraffour","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Graciela","family":"Andrei","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Chris","family":"Upton","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David H.","family":"Evans","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"340","published-online":{"date-parts":[[2010,7,8]]},"reference":[{"key":"ref1","doi-asserted-by":"crossref","first-page":"681","DOI":"10.1146\/annurev.biochem.75.103004.142443","article-title":"Ribonucleotide reductases.","volume":"75","author":"P Nordlund","year":"2006","journal-title":"Annu Rev Biochem"},{"key":"ref2","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/S1570-9639(04)00054-8","article-title":"Structure, function, and mechanism of ribonucleotide reductases.","volume":"1699","author":"M Kolberg","year":"2004","journal-title":"Biochim Biophys Acta"},{"key":"ref3","doi-asserted-by":"crossref","first-page":"5604","DOI":"10.1074\/jbc.M512962200","article-title":"Euglena gracilis ribonucleotide reductase: the eukaryote class II enzyme and the possible antiquity of eukaryote B12 dependence.","volume":"281","author":"E Torrents","year":"2006","journal-title":"J Biol Chem"},{"key":"ref4","doi-asserted-by":"crossref","first-page":"23746","DOI":"10.1074\/jbc.274.34.23746","article-title":"Evidence by mutagenesis that Tyr(370) of the mouse ribonucleotide reductase R2 protein is the connecting link in the intersubunit radical transfer pathway.","volume":"274","author":"U Rova","year":"1999","journal-title":"J Biol Chem"},{"key":"ref5","doi-asserted-by":"crossref","first-page":"2421","DOI":"10.1021\/cr020436s","article-title":"Quantum chemical studies of radical-containing enzymes.","volume":"103","author":"F Himo","year":"2003","journal-title":"Chem Rev"},{"key":"ref6","doi-asserted-by":"crossref","first-page":"2167","DOI":"10.1021\/cr020421u","article-title":"Radical initiation in the class I ribonucleotide reductase: long-range proton-coupled electron transfer?","volume":"103","author":"J Stubbe","year":"2003","journal-title":"Chem Rev"},{"key":"ref7","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1038\/345593a0","article-title":"Three-dimensional structure of the free radical protein of ribonucleotide reductase.","volume":"345","author":"P Nordlund","year":"1990","journal-title":"Nature"},{"key":"ref8","doi-asserted-by":"crossref","first-page":"4267","DOI":"10.1021\/bi00013a016","article-title":"Evidence by site-directed mutagenesis supports long-range electron transfer in mouse ribonucleotide reductase.","volume":"34","author":"U Rova","year":"1995","journal-title":"Biochemistry"},{"key":"ref9","doi-asserted-by":"crossref","first-page":"2037","DOI":"10.1002\/j.1460-2075.1986.tb04461.x","article-title":"Identification of the stable free radical tyrosine residue in ribonucleotide reductase.","volume":"5","author":"A Larsson","year":"1986","journal-title":"EMBO J"},{"key":"ref10","doi-asserted-by":"crossref","first-page":"20655","DOI":"10.1074\/jbc.271.34.20655","article-title":"Two conserved tyrosine residues in protein R1 participate in an intermolecular electron transfer in ribonucleotide reductase.","volume":"271","author":"M Ekberg","year":"1996","journal-title":"J Biol Chem"},{"key":"ref11","doi-asserted-by":"crossref","first-page":"4801","DOI":"10.1021\/bi00135a009","article-title":"Site-directed mutagenesis and deletion of the carboxyl terminus of Escherichia coli ribonucleotide reductase protein R2. Effects on catalytic activity and subunit interaction.","volume":"31","author":"I Climent","year":"1992","journal-title":"Biochemistry"},{"key":"ref12","doi-asserted-by":"crossref","first-page":"5452","DOI":"10.1021\/bi00475a007","article-title":"S-phase-specific expression of mammalian ribonucleotide reductase R1 and R2 subunit mRNAs.","volume":"29","author":"S Bjorklund","year":"1990","journal-title":"Biochemistry"},{"key":"ref13","doi-asserted-by":"crossref","first-page":"9114","DOI":"10.1016\/S0021-9258(17)39337-7","article-title":"Cell cycle-dependent expression of mammalian ribonucleotide reductase. Differential regulation of the two subunits.","volume":"260","author":"Y Engstrom","year":"1985","journal-title":"J Biol Chem"},{"key":"ref14","doi-asserted-by":"crossref","first-page":"10796","DOI":"10.1074\/jbc.M312482200","article-title":"S Phase-specific transcription of the mouse ribonucleotide reductase R2 gene requires both a proximal repressive E2F-binding site and an upstream promoter activating region.","volume":"279","author":"AL Chabes","year":"2004","journal-title":"J Biol Chem"},{"key":"ref15","doi-asserted-by":"crossref","first-page":"3925","DOI":"10.1073\/pnas.0330774100","article-title":"Mouse ribonucleotide reductase R2 protein: a new target for anaphase-promoting complex-Cdh1-mediated proteolysis.","volume":"100","author":"AL Chabes","year":"2003","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref16","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1038\/35003506","article-title":"A ribonucleotide reductase gene involved in a p53-dependent cell-cycle checkpoint for DNA damage.","volume":"404","author":"H Tanaka","year":"2000","journal-title":"Nature"},{"key":"ref17","doi-asserted-by":"crossref","first-page":"40647","DOI":"10.1074\/jbc.M106088200","article-title":"Mammalian p53R2 protein forms an active ribonucleotide reductase in vitro with the R1 protein, which is expressed both in resting cells in response to DNA damage and in proliferating cells.","volume":"276","author":"O Guittet","year":"2001","journal-title":"J Biol Chem"},{"key":"ref18","doi-asserted-by":"crossref","first-page":"1","DOI":"10.1016\/j.canlet.2008.07.019","article-title":"Regulation of p53R2 and its role as potential target for cancer therapy.","volume":"276","author":"X Wang","year":"2009","journal-title":"Cancer Lett"},{"key":"ref19","doi-asserted-by":"crossref","first-page":"776","DOI":"10.1038\/ng2040","article-title":"Mutation of RRM2B, encoding p53-controlled ribonucleotide reductase (p53R2), causes severe mitochondrial DNA depletion.","volume":"39","author":"A Bourdon","year":"2007","journal-title":"Nat Genet"},{"key":"ref20","doi-asserted-by":"crossref","first-page":"7834","DOI":"10.1074\/jbc.M512894200","article-title":"Regulation of mammalian ribonucleotide reduction and dNTP pools after DNA damage and in resting cells.","volume":"281","author":"P Hakansson","year":"2006","journal-title":"J Biol Chem"},{"key":"ref21","doi-asserted-by":"crossref","first-page":"77","DOI":"10.1023\/A:1008192616923","article-title":"Iridovirus homologues of cellular genes\u2013implications for the molecular evolution of large DNA viruses.","volume":"21","author":"CA Tidona","year":"2000","journal-title":"Virus Genes"},{"key":"ref22","doi-asserted-by":"crossref","first-page":"411","DOI":"10.1016\/0042-6822(91)90860-E","article-title":"The sequences of the ribonucleotide reductase genes from African swine fever virus show considerable homology with those of the orthopoxvirus, vaccinia virus.","volume":"184","author":"M Boursnell","year":"1991","journal-title":"Virology"},{"key":"ref23","doi-asserted-by":"crossref","first-page":"1581","DOI":"10.1099\/0022-1317-66-7-1581","article-title":"The ribonucleotide reductase induced by herpes simplex virus type 1 involves minimally a complex of two polypeptides (136K and 38K).","volume":"66(Pt 7)","author":"MC Frame","year":"1985","journal-title":"J Gen Virol"},{"key":"ref24","doi-asserted-by":"crossref","first-page":"519","DOI":"10.1128\/JVI.62.2.519-527.1988","article-title":"Vaccinia virus-encoded ribonucleotide reductase: sequence conservation of the gene for the small subunit and its amplification in hydroxyurea-resistant mutants.","volume":"62","author":"M Slabaugh","year":"1988","journal-title":"J Virol"},{"key":"ref25","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/0042-6822(88)90627-7","article-title":"Nucleotide sequence and molecular genetic analysis of the large subunit of ribonucleotide reductase encoded by vaccinia virus.","volume":"164","author":"LA Tengelsen","year":"1988","journal-title":"Virology"},{"key":"ref26","first-page":"5228","article-title":"Ribonucleotide reductase and cell proliferation. I. Variations of ribonucleotide reductase activity with tumor growth rate in a series of rat hepatomas.","volume":"245","author":"HL Elford","year":"1970","journal-title":"J Biol Chem"},{"key":"ref27","doi-asserted-by":"crossref","first-page":"17","DOI":"10.2217\/17460913.2.1.17","article-title":"Human monkeypox: an emerging zoonotic disease.","volume":"2","author":"S Parker","year":"2007","journal-title":"Future Microbiol"},{"key":"ref28","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1097\/QCO.0b013e3282f44c74","article-title":"Cowpox virus infection: an emerging health threat.","volume":"21","author":"RM Vorou","year":"2008","journal-title":"Curr Opin Infect Dis"},{"key":"ref29","doi-asserted-by":"crossref","first-page":"507","DOI":"10.1128\/JVI.52.2.507-514.1984","article-title":"Vaccinia virus induces ribonucleotide reductase in primate cells.","volume":"52","author":"MB Slabaugh","year":"1984","journal-title":"J Virol"},{"key":"ref30","doi-asserted-by":"crossref","first-page":"1889","DOI":"10.1128\/JVI.62.6.1889-1897.1988","article-title":"Sequence and transcriptional analysis of the vaccinia virus HindIII I fragment.","volume":"62","author":"JF Schmitt","year":"1988","journal-title":"J Virol"},{"key":"ref31","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1128\/JVI.52.2.501-506.1984","article-title":"Vaccinia virus-induced ribonucleotide reductase can be distinguished from host cell activity.","volume":"52","author":"MB Slabaugh","year":"1984","journal-title":"J Virol"},{"key":"ref32","doi-asserted-by":"crossref","first-page":"29512","DOI":"10.1074\/jbc.273.45.29512","article-title":"Allosteric regulation of vaccinia virus ribonucleotide reductase, analyzed by simultaneous monitoring of its four activities.","volume":"273","author":"SP Hendricks","year":"1998","journal-title":"J Biol Chem"},{"key":"ref33","doi-asserted-by":"crossref","first-page":"7093","DOI":"10.1074\/jbc.M006232200","article-title":"Mouse ribonucleotide reductase control: influence of substrate binding upon interactions with allosteric effectors.","volume":"276","author":"K Chimploy","year":"2001","journal-title":"J Biol Chem"},{"key":"ref34","doi-asserted-by":"crossref","first-page":"625","DOI":"10.1016\/0042-6822(90)90119-C","article-title":"Insertional inactivation of the large subunit of ribonucleotide reductase encoded by vaccinia virus is associated with reduced virulence in vivo.","volume":"174","author":"SJ Child","year":"1990","journal-title":"Virology"},{"key":"ref35","doi-asserted-by":"crossref","first-page":"27415","DOI":"10.1074\/jbc.270.46.27415","article-title":"Roles of vaccinia virus ribonucleotide reductase and glutaredoxin in DNA precursor biosynthesis.","volume":"270","author":"I Rajagopal","year":"1995","journal-title":"J Biol Chem"},{"key":"ref36","doi-asserted-by":"crossref","first-page":"233","DOI":"10.1016\/0378-1119(96)00192-8","article-title":"A vaccinia virus transfer vector using a GUS reporter gene inserted into the I4L locus.","volume":"172","author":"PM Howley","year":"1996","journal-title":"Gene"},{"key":"ref37","doi-asserted-by":"crossref","first-page":"2617","DOI":"10.1128\/JVI.66.5.2617-2630.1992","article-title":"Molecular attenuation of vaccinia virus: mutant generation and animal characterization.","volume":"66","author":"MS Lee","year":"1992","journal-title":"J Virol"},{"key":"ref38","doi-asserted-by":"crossref","first-page":"4236","DOI":"10.1128\/JVI.02255-08","article-title":"The 3\u2032-to-5\u2032 exonuclease activity of vaccinia virus DNA polymerase is essential and plays a role in promoting virus genetic recombination.","volume":"83","author":"DB Gammon","year":"2009","journal-title":"J Virol"},{"key":"ref39","doi-asserted-by":"crossref","first-page":"9743","DOI":"10.1016\/S0021-9258(19)50155-7","article-title":"A single amino acid substitution abolishes feedback inhibition of vaccinia virus thymidine kinase.","volume":"267","author":"ME Black","year":"1992","journal-title":"J Biol Chem"},{"key":"ref40","doi-asserted-by":"crossref","first-page":"5922","DOI":"10.1128\/JVI.02723-07","article-title":"Vaccinia virus DNA ligase recruits cellular topoisomerase II to sites of viral replication and assembly.","volume":"82","author":"YC Lin","year":"2008","journal-title":"J Virol"},{"key":"ref41","doi-asserted-by":"crossref","first-page":"563","DOI":"10.1016\/j.chom.2009.11.005","article-title":"Cellular DNA ligase I is recruited to cytoplasmic vaccinia virus factories and masks the role of the vaccinia ligase in viral DNA replication.","volume":"6","author":"N Paran","year":"2009","journal-title":"Cell Host Microbe"},{"key":"ref42","doi-asserted-by":"crossref","first-page":"410","DOI":"10.1016\/0042-6822(90)90338-R","article-title":"The vaccinia virus HindIII F fragment: nucleotide sequence of the left 6.2 kb.","volume":"178","author":"NA Roseman","year":"1990","journal-title":"Virology"},{"key":"ref43","doi-asserted-by":"crossref","first-page":"1900","DOI":"10.1158\/0008-5472.CAN-05-2656","article-title":"Structurally dependent redox property of ribonucleotide reductase subunit p53R2.","volume":"66","author":"L Xue","year":"2006","journal-title":"Cancer Res"},{"key":"ref44","doi-asserted-by":"crossref","first-page":"506","DOI":"10.1128\/JVI.60.2.506-514.1986","article-title":"Hydroxyurea-resistant vaccinia virus: overproduction of ribonucleotide reductase.","volume":"60","author":"MB Slabaugh","year":"1986","journal-title":"J Virol"},{"key":"ref45","doi-asserted-by":"crossref","first-page":"261","DOI":"10.1016\/j.surg.2004.04.029","article-title":"Retrovirally mediated RNA interference targeting the M2 subunit of ribonucleotide reductase: A novel therapeutic strategy in pancreatic cancer.","volume":"136","author":"MS Duxbury","year":"2004","journal-title":"Surgery"},{"key":"ref46","doi-asserted-by":"crossref","first-page":"1502","DOI":"10.1016\/S0026-895X(25)09608-7","article-title":"Identification of enzymes catalyzing two-step phosphorylation of cidofovir and the effect of cytomegalovirus infection on their activities in host cells.","volume":"50","author":"T Cihlar","year":"1996","journal-title":"Mol Pharmacol"},{"key":"ref47","doi-asserted-by":"crossref","first-page":"1563","DOI":"10.1016\/0006-2952(96)00100-1","article-title":"Kinetic analysis of the interaction of cidofovir diphosphate with human cytomegalovirus DNA polymerase.","volume":"51","author":"X Xiong","year":"1996","journal-title":"Biochem Pharmacol"},{"key":"ref48","doi-asserted-by":"crossref","first-page":"3153","DOI":"10.1128\/AAC.49.8.3153-3162.2005","article-title":"Mechanism of inhibition of vaccinia virus DNA polymerase by cidofovir diphosphate.","volume":"49","author":"WC Magee","year":"2005","journal-title":"Antimicrob Agents Chemother"},{"key":"ref49","doi-asserted-by":"crossref","first-page":"586","DOI":"10.1128\/AAC.01172-07","article-title":"Cidofovir and (S)-9-[3-hydroxy-(2-phosphonomethoxy)propyl]adenine are highly effective inhibitors of vaccinia virus DNA polymerase when incorporated into the template strand.","volume":"52","author":"WC Magee","year":"2008","journal-title":"Antimicrob Agents Chemother"},{"key":"ref50","doi-asserted-by":"crossref","first-page":"572","DOI":"10.1128\/AAC.01257-08","article-title":"Activities of certain 5-substituted 4\u2032-thiopyrimidine nucleosides against orthopoxvirus infections.","volume":"53","author":"ER Kern","year":"2009","journal-title":"Antimicrob Agents Chemother"},{"key":"ref51","doi-asserted-by":"crossref","first-page":"1795","DOI":"10.1128\/AAC.01447-06","article-title":"Selective phosphorylation of antiviral drugs by vaccinia virus thymidine kinase.","volume":"51","author":"MN Prichard","year":"2007","journal-title":"Antimicrob Agents Chemother"},{"key":"ref52","doi-asserted-by":"crossref","first-page":"4323","DOI":"10.1128\/JVI.67.7.4323-4336.1993","article-title":"Genetic characterization of the vaccinia virus DNA polymerase: cytosine arabinoside resistance requires a variable lesion conferring phosphonoacetate resistance in conjunction with an invariant mutation localized to the 3\u2032-5\u2032 exonuclease domain.","volume":"67","author":"JA Taddie","year":"1993","journal-title":"J Virol"},{"key":"ref53","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1016\/j.virol.2007.02.005","article-title":"Mapping and phenotypic analysis of spontaneous isatin-beta-thiosemicarbazone resistant mutants of vaccinia virus.","volume":"363","author":"SG Cresawn","year":"2007","journal-title":"Virology"},{"key":"ref54","doi-asserted-by":"crossref","first-page":"1615","DOI":"10.1002\/j.1460-2075.1988.tb02987.x","article-title":"Immunocytochemical evidence for the cytoplasmic localization and differential expression during the cell cycle of the M1 and M2 subunits of mammalian ribonucleotide reductase.","volume":"7","author":"Y Engstrom","year":"1988","journal-title":"EMBO J"},{"key":"ref55","doi-asserted-by":"crossref","first-page":"17801","DOI":"10.1073\/pnas.0808198105","article-title":"Ribonucleotide reduction is a cytosolic process in mammalian cells independently of DNA damage.","volume":"105","author":"G Pontarin","year":"2008","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref56","doi-asserted-by":"crossref","first-page":"863","DOI":"10.1002\/j.1460-2075.1984.tb01897.x","article-title":"Localization of ribonucleotide reductase in mammalian cells.","volume":"3","author":"Y Engstrom","year":"1984","journal-title":"EMBO J"},{"key":"ref57","doi-asserted-by":"crossref","first-page":"3859","DOI":"10.1021\/jm00076a015","article-title":"R2 C-terminal peptide inhibition of mammalian and yeast ribonucleotide reductase.","volume":"36","author":"A Fisher","year":"1993","journal-title":"J Med Chem"},{"key":"ref58","doi-asserted-by":"crossref","first-page":"36","DOI":"10.1021\/jm000335r","article-title":"Toward a rational design of peptide inhibitors of ribonucleotide reductase: structure-function and modeling studies.","volume":"44","author":"BA Pender","year":"2001","journal-title":"J Med Chem"},{"key":"ref59","doi-asserted-by":"crossref","first-page":"533","DOI":"10.1038\/370533a0","article-title":"Structure of ribonucleotide reductase protein R1.","volume":"370","author":"U Uhlin","year":"1994","journal-title":"Nature"},{"key":"ref60","doi-asserted-by":"crossref","first-page":"695","DOI":"10.1038\/372695a0","article-title":"A potent peptidomimetic inhibitor of HSV ribonucleotide reductase with antiviral activity in vivo.","volume":"372","author":"M Liuzzi","year":"1994","journal-title":"Nature"},{"key":"ref61","doi-asserted-by":"crossref","first-page":"365","DOI":"10.1016\/j.jmb.2006.03.035","article-title":"The first holocomplex structure of ribonucleotide reductase gives new insight into its mechanism of action.","volume":"359","author":"M Uppsten","year":"2006","journal-title":"J Mol Biol"},{"key":"ref62","doi-asserted-by":"crossref","first-page":"1539","DOI":"10.1038\/sj.onc.1207272","article-title":"RNA interference targeting the M2 subunit of ribonucleotide reductase enhances pancreatic adenocarcinoma chemosensitivity to gemcitabine.","volume":"23","author":"MS Duxbury","year":"2004","journal-title":"Oncogene"},{"key":"ref63","doi-asserted-by":"crossref","first-page":"25","DOI":"10.1016\/j.tibs.2008.09.008","article-title":"Tinkering with a viral ribonucleotide reductase.","volume":"34","author":"D Lembo","year":"2009","journal-title":"Trends Biochem Sci"},{"key":"ref64","doi-asserted-by":"crossref","first-page":"16820","DOI":"10.1074\/jbc.M701310200","article-title":"p53R2-dependent ribonucleotide reduction provides deoxyribonucleotides in quiescent human fibroblasts in the absence of induced DNA damage.","volume":"282","author":"G Pontarin","year":"2007","journal-title":"J Biol Chem"},{"key":"ref65","doi-asserted-by":"crossref","first-page":"440","DOI":"10.1038\/ng1212","article-title":"Impaired function of p53R2 in Rrm2b-null mice causes severe renal failure through attenuation of dNTP pools.","volume":"34","author":"T Kimura","year":"2003","journal-title":"Nat Genet"},{"key":"ref66","doi-asserted-by":"crossref","first-page":"351","DOI":"10.1099\/0022-1317-74-3-351","article-title":"Ribonucleotide reductase-deficient mutants of pseudorabies virus are avirulent for pigs and induce partial protective immunity.","volume":"74(Pt 3)","author":"N de Wind","year":"1993","journal-title":"J Gen Virol"},{"key":"ref67","doi-asserted-by":"crossref","first-page":"2607","DOI":"10.1099\/0022-1317-69-10-2607","article-title":"Ribonucleotide reductase encoded by herpes simplex virus is a determinant of the pathogenicity of the virus in mice and a valid antiviral target.","volume":"69(Pt 10)","author":"JM Cameron","year":"1988","journal-title":"J Gen Virol"},{"key":"ref68","doi-asserted-by":"crossref","first-page":"276","DOI":"10.1016\/0042-6822(89)90244-4","article-title":"A herpes simplex virus ribonucleotide reductase deletion mutant is defective for productive acute and reactivatable latent infections of mice and for replication in mouse cells.","volume":"173","author":"JG Jacobson","year":"1989","journal-title":"Virology"},{"key":"ref69","doi-asserted-by":"crossref","first-page":"3317","DOI":"10.1128\/JVI.68.5.3317-3323.1994","article-title":"Deletion of the varicella-zoster virus large subunit of ribonucleotide reductase impairs growth of virus in vitro.","volume":"68","author":"TC Heineman","year":"1994","journal-title":"J Virol"},{"key":"ref70","doi-asserted-by":"crossref","first-page":"270","DOI":"10.1016\/0042-6822(88)90421-7","article-title":"Oligopeptides inhibit the ribonucleotide reductase of herpes simplex virus by causing subunit separation.","volume":"162","author":"W McClements","year":"1988","journal-title":"Virology"},{"key":"ref71","doi-asserted-by":"crossref","first-page":"439","DOI":"10.1038\/321439a0","article-title":"Specific inhibition of herpesvirus ribonucleotide reductase by synthetic peptides.","volume":"321","author":"BM Dutia","year":"1986","journal-title":"Nature"},{"key":"ref72","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1002\/bip.10397","article-title":"Oligopeptide inhibition of class I ribonucleotide reductases.","volume":"71","author":"BS Cooperman","year":"2003","journal-title":"Biopolymers"},{"key":"ref73","doi-asserted-by":"crossref","first-page":"3359","DOI":"10.1099\/vir.0.19452-0","article-title":"The human cytomegalovirus UL45 gene product is a late, virion-associated protein and influences virus growth at low multiplicities of infection.","volume":"84","author":"M Patrone","year":"2003","journal-title":"J Gen Virol"},{"key":"ref74","doi-asserted-by":"crossref","first-page":"2713","DOI":"10.1099\/0022-1317-80-10-2713","article-title":"The U28 ORF of human herpesvirus-7 does not encode a functional ribonucleotide reductase R1 subunit.","volume":"80(Pt 10)","author":"Y Sun","year":"1999","journal-title":"J Gen Virol"},{"key":"ref75","doi-asserted-by":"crossref","first-page":"4278","DOI":"10.1128\/JVI.78.8.4278-4288.2004","article-title":"The ribonucleotide reductase R1 homolog of murine cytomegalovirus is not a functional enzyme subunit but is required for pathogenesis.","volume":"78","author":"D Lembo","year":"2004","journal-title":"J Virol"},{"key":"ref76","doi-asserted-by":"crossref","first-page":"11557","DOI":"10.1128\/JVI.74.24.11557-11565.2000","article-title":"Expression of an altered ribonucleotide reductase activity associated with the replication of murine cytomegalovirus in quiescent fibroblasts.","volume":"74","author":"D Lembo","year":"2000","journal-title":"J Virol"},{"key":"ref77","doi-asserted-by":"crossref","first-page":"303","DOI":"10.1126\/science.291.5502.303","article-title":"A ribonucleotide reductase homolog of cytomegalovirus and endothelial cell tropism.","volume":"291","author":"W Brune","year":"2001","journal-title":"Science"},{"key":"ref78","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/S0065-3527(05)65006-3","article-title":"A decade of advances in iridovirus research.","volume":"65","author":"T Williams","year":"2005","journal-title":"Adv Virus Res"},{"key":"ref79","article-title":"RNRdb: The ribonucleotide reductase database. version 1.0.","author":"D Lundin","year":"2005"},{"key":"ref80","doi-asserted-by":"crossref","first-page":"9244","DOI":"10.1128\/JVI.00945-06","article-title":"Genome of horsepox virus.","volume":"80","author":"ER Tulman","year":"2006","journal-title":"J Virol"},{"key":"ref81","doi-asserted-by":"crossref","first-page":"298","DOI":"10.1006\/viro.1999.0001","article-title":"The complete DNA sequence of myxoma virus.","volume":"264","author":"C Cameron","year":"1999","journal-title":"Virology"},{"key":"ref82","doi-asserted-by":"crossref","first-page":"319","DOI":"10.1006\/viro.1999.0002","article-title":"The complete genome sequence of shope (rabbit) fibroma virus.","volume":"264","author":"DO Willer","year":"1999","journal-title":"Virology"},{"key":"ref83","first-page":"980","article-title":"Wild-type p53 regulates human ribonucleotide reductase by protein-protein interaction with p53R2 as well as hRRM2 subunits.","volume":"63","author":"L Xue","year":"2003","journal-title":"Cancer Res"},{"key":"ref84","doi-asserted-by":"crossref","first-page":"16","DOI":"10.1158\/0008-5472.CAN-06-3200","article-title":"Ribonucleotide reductase small subunit p53R2 facilitates p21 induction of G1 arrest under UV irradiation.","volume":"67","author":"L Xue","year":"2007","journal-title":"Cancer Res"},{"key":"ref85","doi-asserted-by":"crossref","first-page":"2173","DOI":"10.1038\/onc.2009.84","article-title":"Ribonucleotide reductase small subunit p53R2 suppresses MEK-ERK activity by binding to ERK kinase 2.","volume":"28","author":"C Piao","year":"2009","journal-title":"Oncogene"},{"key":"ref86","doi-asserted-by":"crossref","first-page":"437","DOI":"10.1042\/BJ20031375","article-title":"The vaccinia virus-stimulated mitogen-activated protein kinase (MAPK) pathway is required for virus multiplication.","volume":"381","author":"AA Andrade","year":"2004","journal-title":"Biochem J"},{"key":"ref87","doi-asserted-by":"crossref","first-page":"67","DOI":"10.1186\/1471-2148-8-67","article-title":"Identification of multiple independent horizontal gene transfers into poxviruses using a comparative genomics approach.","volume":"8","author":"KA Bratke","year":"2008","journal-title":"BMC Evol Biol"},{"key":"ref88","doi-asserted-by":"crossref","first-page":"320","DOI":"10.1186\/1471-2148-8-320","article-title":"Phylogenetic evidence for extensive lateral acquisition of cellular genes by Nucleocytoplasmic large DNA viruses.","volume":"8","author":"J Filee","year":"2008","journal-title":"BMC Evol Biol"},{"key":"ref89","doi-asserted-by":"crossref","first-page":"1688","DOI":"10.1093\/molbev\/msl036","article-title":"A selective barrier to horizontal gene transfer in the T4-type bacteriophages that has preserved a core genome with the viral replication and structural genes.","volume":"23","author":"J Filee","year":"2006","journal-title":"Mol Biol Evol"},{"key":"ref90","doi-asserted-by":"crossref","first-page":"3974","DOI":"10.1128\/JB.181.13.3974-3980.1999","article-title":"Ribonucleotide reduction in Pseudomonas species: simultaneous presence of active enzymes from different classes.","volume":"181","author":"A Jordan","year":"1999","journal-title":"J Bacteriol"},{"key":"ref91","doi-asserted-by":"crossref","first-page":"979","DOI":"10.1093\/molbev\/msg107","article-title":"Genome-wide survey for genes horizontally transferred from cellular organisms to baculoviruses.","volume":"20","author":"AL Hughes","year":"2003","journal-title":"Mol Biol Evol"},{"key":"ref92","doi-asserted-by":"crossref","first-page":"7155","DOI":"10.1016\/S0021-9258(18)53159-8","article-title":"Vaccinia virus ribonucleotide reductase. Correlation between deoxyribonucleotide supply and demand.","volume":"268","author":"ML Howell","year":"1993","journal-title":"J Biol Chem"},{"key":"ref93","doi-asserted-by":"crossref","first-page":"17803","DOI":"10.1016\/S0021-9258(17)46776-7","article-title":"Vaccinia virus ribonucleotide reductase expression and isolation of the recombinant large subunit.","volume":"268","author":"MB Slabaugh","year":"1993","journal-title":"J Biol Chem"},{"key":"ref94","doi-asserted-by":"crossref","first-page":"1710","DOI":"10.1038\/sj.bjc.6604344","article-title":"Ribonucleotide reductase subunits M1 and M2 mRNA expression levels and clinical outcome of lung adenocarcinoma patients treated with docetaxel\/gemcitabine.","volume":"98","author":"J Souglakos","year":"2008","journal-title":"Br J Cancer"},{"key":"ref95","doi-asserted-by":"crossref","first-page":"155","DOI":"10.1007\/BF01534695","article-title":"Altered expression of ribonucleotide reductase and role of M2 gene amplification in hydroxyurea-resistant hamster, mouse, rat, and human cell lines.","volume":"13","author":"JA Wright","year":"1987","journal-title":"Somat Cell Mol Genet"},{"key":"ref96","doi-asserted-by":"crossref","first-page":"4215s","DOI":"10.1158\/1078-0432.CCR-040006","article-title":"Gene expression as a predictive marker of outcome in stage IIB-IIIA-IIIB non-small cell lung cancer after induction gemcitabine-based chemotherapy followed by resectional surgery.","volume":"10","author":"R Rosell","year":"2004","journal-title":"Clin Cancer Res"},{"key":"ref97","doi-asserted-by":"crossref","first-page":"366","DOI":"10.1097\/00000658-199809000-00009","article-title":"Cancer gene therapy using a replication-competent herpes simplex virus type 1 vector.","volume":"228","author":"SS Yoon","year":"1998","journal-title":"Ann Surg"},{"key":"ref98","doi-asserted-by":"crossref","first-page":"1051","DOI":"10.1038\/sj.cgt.7700208","article-title":"Cytotoxicity, apoptosis, and viral replication in tumor cells treated with oncolytic ribonucleotide reductase-defective herpes simplex type 1 virus (hrR3) combined with ionizing radiation.","volume":"7","author":"MA Spear","year":"2000","journal-title":"Cancer Gene Ther"},{"key":"ref99","doi-asserted-by":"crossref","first-page":"1415","DOI":"10.1517\/14712598.7.9.1415","article-title":"Myxoma virus and oncolytic virotherapy: a new biologic weapon in the war against cancer.","volume":"7","author":"MM Stanford","year":"2007","journal-title":"Expert Opin Biol Ther"},{"key":"ref100","doi-asserted-by":"crossref","first-page":"2329","DOI":"10.1245\/s10434-008-9924-z","article-title":"Myxoma virus is oncolytic for human pancreatic adenocarcinoma cells.","volume":"15","author":"Y Woo","year":"2008","journal-title":"Ann Surg Oncol"},{"key":"ref101","doi-asserted-by":"crossref","first-page":"10300","DOI":"10.1128\/JVI.75.21.10300-10308.2001","article-title":"Yaba-like disease virus: an alternative replicating poxvirus vector for cancer gene therapy.","volume":"75","author":"Y Hu","year":"2001","journal-title":"J Virol"},{"key":"ref102","doi-asserted-by":"crossref","first-page":"19527","DOI":"10.1073\/pnas.0905893106","article-title":"Cell cycle deregulation by a poxvirus partial mimic of anaphase-promoting complex subunit 11.","volume":"106","author":"M Mo","year":"2009","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref103","doi-asserted-by":"crossref","first-page":"514","DOI":"10.1128\/MCB.24.2.514-526.2004","article-title":"Mitotic degradation of human thymidine kinase 1 is dependent on the anaphase-promoting complex\/cyclosome-CDH1-mediated pathway.","volume":"24","author":"PY Ke","year":"2004","journal-title":"Mol Cell Biol"},{"key":"ref104","doi-asserted-by":"crossref","first-page":"201","DOI":"10.1038\/nrmicro1099","article-title":"Poxvirus tropism.","volume":"3","author":"G McFadden","year":"2005","journal-title":"Nat Rev Microbiol"},{"key":"ref105","doi-asserted-by":"crossref","first-page":"9391","DOI":"10.1128\/JVI.00605-06","article-title":"Cidofovir resistance in vaccinia virus is linked to diminished virulence in mice.","volume":"80","author":"G Andrei","year":"2006","journal-title":"J Virol"},{"key":"ref106","doi-asserted-by":"crossref","first-page":"2393","DOI":"10.1128\/JVI.74.5.2393-2405.2000","article-title":"Clustered charge-to-alanine mutagenesis of the vaccinia virus H5 gene: isolation of a dominant, temperature-sensitive mutant with a profound defect in morphogenesis.","volume":"74","author":"J DeMasi","year":"2000","journal-title":"J Virol"},{"key":"ref107","doi-asserted-by":"crossref","first-page":"1849","DOI":"10.1128\/JVI.62.6.1849-1854.1988","article-title":"Escherichia coli gpt gene provides dominant selection for vaccinia virus open reading frame expression vectors.","volume":"62","author":"FG Falkner","year":"1988","journal-title":"J Virol"},{"key":"ref108","doi-asserted-by":"crossref","first-page":"14345","DOI":"10.1073\/pnas.2235583100","article-title":"Vaccinia virus encodes a previously uncharacterized mitochondrial-associated inhibitor of apoptosis.","volume":"100","author":"ST Wasilenko","year":"2003","journal-title":"Proc Natl Acad Sci U S A"},{"key":"ref109","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1016\/S0147-619X(02)00154-3","article-title":"Construction of a novel set of transfer vectors to study vaccinia virus replication and foreign gene expression.","volume":"49","author":"B Dvoracek","year":"2003","journal-title":"Plasmid"},{"key":"ref110","doi-asserted-by":"crossref","first-page":"1094","DOI":"10.2144\/97236st07","article-title":"Compact, synthetic, vaccinia virus early\/late promoter for protein expression.","volume":"23","author":"S Chakrabarti","year":"1997","journal-title":"Biotechniques"},{"key":"ref111","doi-asserted-by":"crossref","first-page":"353","DOI":"10.1128\/JVI.78.1.353-366.2004","article-title":"The genome of canarypox virus.","volume":"78","author":"ER Tulman","year":"2004","journal-title":"J Virol"},{"key":"ref112","doi-asserted-by":"crossref","first-page":"55","DOI":"10.1016\/S0168-1702(00)00210-0","article-title":"Viral genome organizer: a system for analyzing complete viral genomes.","volume":"70","author":"C Upton","year":"2000","journal-title":"Virus Res"}],"container-title":["PLoS Pathogens"],"original-title":[],"language":"en","link":[{"URL":"http:\/\/dx.plos.org\/10.1371\/journal.ppat.1000984","content-type":"unspecified","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,2,22]],"date-time":"2025-02-22T14:46:41Z","timestamp":1740235601000},"score":1,"resource":{"primary":{"URL":"https:\/\/dx.plos.org\/10.1371\/journal.ppat.1000984"}},"subtitle":[],"editor":[{"given":"Grant","family":"McFadden","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"editor"}]}],"short-title":[],"issued":{"date-parts":[[2010,7,8]]},"references-count":112,"journal-issue":{"issue":"7","published-online":{"date-parts":[[2010,7,8]]}},"URL":"https:\/\/doi.org\/10.1371\/journal.ppat.1000984","relation":{"has-review":[{"id-type":"doi","id":"10.3410\/f.4916975.4847079","asserted-by":"object"}]},"ISSN":["1553-7374"],"issn-type":[{"value":"1553-7374","type":"electronic"}],"subject":[],"published":{"date-parts":[[2010,7,8]]}}}