CoChat
Sign Up
Cited by 28

The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.

Biochemical and Functional Interactions of Human Papillomavirus Proteins with Polycomb Group Proteins

McLaughlin-Drubin, Margaret, Munger, Karl·2013·Viruses
DOI 10.3390/v5051231PMC PMC3712305
Open this paper in CoChat — free account

Abstract

The role of enzymes involved in polycomb repression of gene transcription has been studied extensively in human cancer. Polycomb repressive complexes mediate oncogene-induced senescence, a principal innate cell-intrinsic tumor suppressor pathway that thwarts expansion of cells that have suffered oncogenic hits. Infections with human cancer viruses including human papillomaviruses (HPVs) and Epstein-Barr virus can trigger oncogene-induced senescence, and the viruses have evolved strategies to abrogate this response in order to establish an infection and reprogram their host cells to establish a long-term persistent infection. As a consequence of inhibiting polycomb repression and evading oncogene induced-senescence, HPV infected cells have an altered epigenetic program as evidenced by aberrant homeobox gene expression. Similar alterations are frequently observed in non-virus associated human cancers and may be harnessed for diagnosis and therapy.

Overview

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Integrity signals

Registry

Crossref · 10.3390/v5051231

Cites

6 of 6 references verified0 citation errors · 0 not checkable

Statistics

Figures

Figure 1 Cell division in a squamous epithelium. (A) Asymmetric cell division of a basal epithelial cell yields two unequal daughter cells. One remains an undifferentiated, DNA synthesis competent basal epithelial cell whereas the other daughter is a differentiating epithelial cell that will terminally withdraw from the cell division cycle. Human papillomaviruses (HPV) genomes segregated into such cells will retain these cells in a DNA replication competent state and complete their full replicative life cycle including viral progeny synthesis. (B) Symmetric cell division will yield two basal like cells. This mode of cell division is to replenish basal epithelial cell during wound healing. After the initial infection, HPVs establish a long-term persistent infection of these cells where the viral genome is maintained at a low copy number. The viral genome undergoes replication every time the cell replicates its genome. See text for details.
Figure 1 Cell division in a squamous epithelium. (A) Asymmetric cell division of a basal epithelial cell yields two unequal daughter cells. One remains an undifferentiated, DNA synthesis competent basal epithelial cell whereas the other daughter is a differentiating epithelial cell that will terminally withdraw from the cell division cycle. Human papillomaviruses (HPV) genomes segregated into such cells will retain these cells in a DNA replication competent state and complete their full replicative life cycle including viral progeny synthesis. (B) Symmetric cell division will yield two basal like cells. This mode of cell division is to replenish basal epithelial cell during wound healing. After the initial infection, HPVs establish a long-term persistent infection of these cells where the viral genome is maintained at a low copy number. The viral genome undergoes replication every time the cell replicates its genome. See text for details.CC BY · PubMed Central
Figure 2 Polycomb mediated silencing of gene expression. The polycomb repressive complex 2 (PRC2) silences chromatin by trimethylating lysine residue 27 (K27me3) of histone H3, causing chromatin compaction. H3K27me3 marked chromatin is bound by PRC1, which further silences gene expression by monoubiquitinating lysine residue 119 (K119Ub) of histone H2A.
Figure 2 Polycomb mediated silencing of gene expression. The polycomb repressive complex 2 (PRC2) silences chromatin by trimethylating lysine residue 27 (K27me3) of histone H3, causing chromatin compaction. H3K27me3 marked chromatin is bound by PRC1, which further silences gene expression by monoubiquitinating lysine residue 119 (K119Ub) of histone H2A.CC BY · PubMed Central
Figure 3 PRC2 mediated gene silencing is reversible. The EZH2 histone methyl transferase in PRC2 silences gene expression by adding the trimethyl mark on lysine residue 27 of histone H3, and this mark can be removed by one of the two H3K27 specific demethylases, KDM6A or KDM6B. See text for details.
Figure 3 PRC2 mediated gene silencing is reversible. The EZH2 histone methyl transferase in PRC2 silences gene expression by adding the trimethyl mark on lysine residue 27 of histone H3, and this mark can be removed by one of the two H3K27 specific demethylases, KDM6A or KDM6B. See text for details.CC BY · PubMed Central
Figure 4 HPV16 E7 causes increased KDM6A and KDM6B expression. E7 mediated KDM6A and KDM6B induction affects multiple transcriptional programs, including keratinocyte differentiation and cell identity. KDM6B induction represents a cellular defense response to E7 oncogene expression that is to trigger cell cycle arrest and senescence. HPV16 E7 short-circuits this response by targeting the retinoblastoma tumor suppressor for degradation. Several other viruses including EBV have developed strategies to subvert such cellular defense responses. See text for details.
Figure 4 HPV16 E7 causes increased KDM6A and KDM6B expression. E7 mediated KDM6A and KDM6B induction affects multiple transcriptional programs, including keratinocyte differentiation and cell identity. KDM6B induction represents a cellular defense response to E7 oncogene expression that is to trigger cell cycle arrest and senescence. HPV16 E7 short-circuits this response by targeting the retinoblastoma tumor suppressor for degradation. Several other viruses including EBV have developed strategies to subvert such cellular defense responses. See text for details.CC BY · PubMed Central
Figure 5 Induction and abrogation of the Oncogene Induced Senescence (OIS) tumor suppressor response by HPV16 E7. (A) The retinoblastoma tumor suppressor (pRB) pathway regulates S-phase cell cycle entry. Activity of pRB is regulated by phosphorylation by cyclin dependent kinase 4 or 6 (CDK4/6). CDK4/6 activity is activated by association with a D-type cyclin (CCND) and negatively regulated by association with one of several small molecule inhibitors (p16INK4A, p18INK4C and p19INK4D), which are induced in response to different growth suppressive stimuli. CDK4/6 phosphorylation of pRB at the G1/S boundary inactivates the transcriptional repressor activity of the pRB/E2F complex and signals S-phase entry. (B) Oncogenic stimuli such as RAS/RAF signaling or HPV16 E7 expression causes KDM6B expression and de-repression of p16INK4A expression, which inhibits CDK4/6 activity and pRB phosphorylation, causing G1 cell cycle arrest and senescence (OIS). (C) HPV16 E7 has evolved to evade OIS by targeting pRB for ubiquitin mediated proteasomal degradation.
Figure 5 Induction and abrogation of the Oncogene Induced Senescence (OIS) tumor suppressor response by HPV16 E7. (A) The retinoblastoma tumor suppressor (pRB) pathway regulates S-phase cell cycle entry. Activity of pRB is regulated by phosphorylation by cyclin dependent kinase 4 or 6 (CDK4/6). CDK4/6 activity is activated by association with a D-type cyclin (CCND) and negatively regulated by association with one of several small molecule inhibitors (p16INK4A, p18INK4C and p19INK4D), which are induced in response to different growth suppressive stimuli. CDK4/6 phosphorylation of pRB at the G1/S boundary inactivates the transcriptional repressor activity of the pRB/E2F complex and signals S-phase entry. (B) Oncogenic stimuli such as RAS/RAF signaling or HPV16 E7 expression causes KDM6B expression and de-repression of p16INK4A expression, which inhibits CDK4/6 activity and pRB phosphorylation, causing G1 cell cycle arrest and senescence (OIS). (C) HPV16 E7 has evolved to evade OIS by targeting pRB for ubiquitin mediated proteasomal degradation.CC BY · PubMed Central

Verification

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

A few free checks a day · papers already verified open instantly · results are public

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

Citations

Cites

Research works printed but not linked: 87

  1. Bernard, 2010, Classification of papillomaviruses (PVs) based on 189 PV types and proposal of taxonomic amendments, Virology, 401, 70, 10.1016/j.virol.2010.02.002 · DOI
  2. Moody, 2010, Human papillomavirus oncoproteins: Pathways to transformation, Nat. Rev. Cancer, 10, 550, 10.1038/nrc2886 · DOI
  3. Munoz, 2003, Epidemiologic classification of human papillomavirus types associated with cervical cancer, N. Engl. J. Med., 348, 518, 10.1056/NEJMoa021641 · DOI · Paper page
  4. Jemal, 2013, Annual report to the nation on the status of cancer, 1975–2009, Featuring the burden and trends in human papillomavirus(HPV)-associated cancers and HPV vaccination coverage levels, J. Nat. Cancer Inst., 105, 175, 10.1093/jnci/djs491 · DOI
  5. Kane, 2012, Implementation of human papillomavirus immunization in the developing world, Vaccine, 30, F192, 10.1016/j.vaccine.2012.06.075 · DOI
  6. Frazer, 2004, Prevention of cervical cancer through papillomavirus vaccination, Nat. Rev. Immunol., 4, 46, 10.1038/nri1260 · DOI
  7. Hebner, 2006, Human papillomaviruses: Basic mechanisms of pathogenesis and oncogenicity, Rev. Med. Virol., 16, 83, 10.1002/rmv.488 · DOI
  8. Bodily, 2011, Persistence of human papillomavirus infection: Keys to malignant progression, Trends Microbiol., 19, 33, 10.1016/j.tim.2010.10.002 · DOI
  9. Baker, 1987, Structural and translational analysis of human papillomavirus type 16 sequences in cervical carcinoma cell lines, J. Virol., 61, 962, 10.1128/jvi.61.4.962-971.1987 · DOI
  10. Schwarz, 1985, Structure and transcription of human papillomavirus sequences in cervical carcinoma cells, Nature, 314, 111, 10.1038/314111a0 · DOI
  11. Munger, 2009, Oncogenic activities of human papillomaviruses, Virus Res., 143, 195, 10.1016/j.virusres.2009.06.008 · DOI
  12. Riley, 2003, Dissection of human papillomavirus E6 and E7 function in transgenic mouse models of cervical carcinogenesis, Cancer Res., 63, 4862
  13. Francis, 2000, Repression of the integrated papillomavirus E6/E7 promoter is required for growth suppression of cervical cancer cells, J. Virol., 74, 2679, 10.1128/JVI.74.6.2679-2686.2000 · DOI
  14. Goodwin, 2000, Repression of human papillomavirus oncogenes in HeLa cervical carcinoma cells causes the orderly reactivation of dormant tumor suppressor pathways, Proc. Natl. Acad. Sci. USA, 97, 12513, 10.1073/pnas.97.23.12513 · DOI · Paper page
  15. Thierry, 1987, The BPV-1 E2 trans-acting protein can be either an activator or repressor of the HPV-18 regulatory region, EMBO, 6, 3391, 10.1002/j.1460-2075.1987.tb02662.x · DOI
  16. Bracken, 2009, Polycomb group proteins: Navigators of lineage pathways led astray in cancer, Nat. Rev. Cancer, 9, 773, 10.1038/nrc2736 · DOI · Paper page
  17. Trojer, 2011, L3MBTL2 protein acts in concert with PcG protein-mediated monoubiquitination of H2A to establish a repressive chromatin structure, Mol. Cell, 42, 438, 10.1016/j.molcel.2011.04.004 · DOI
  18. Qin, 2012, The polycomb group protein L3mbtl2 assembles an atypical PRC1-family complex that is essential in pluripotent stem cells and early development, Cell Stem Cell, 11, 319, 10.1016/j.stem.2012.06.002 · DOI
  19. Zhang, 2012, Epigenetic regulation of skin: Focus on the Polycomb complex, Cell Mol. Life Sci., 69, 2161, 10.1007/s00018-012-0920-x · DOI
  20. Eckert, 2011, Polycomb group proteins are key regulators of keratinocyte function, J. Invest. Dermatol., 131, 295, 10.1038/jid.2010.318 · DOI
  21. Shaw, 2009, Epigenetic reprogramming during wound healing: Loss of polycomb-mediated silencing may enable upregulation of repair genes, EMBO Rep., 10, 881, 10.1038/embor.2009.102 · DOI · Paper page
  22. Eklund, 2011, The role of Hox proteins in leukemogenesis: Insights into key regulatory events in hematopoiesis, Crit. Rev. Oncog., 16, 65, 10.1615/CritRevOncog.v16.i1-2.70 · DOI
  23. Kelly, 2011, HOX genes in ovarian cancer, J. Ovarian. Res., 4, e16, 10.1186/1757-2215-4-16 · DOI
  24. Ewing, 2012, Germline mutations in HOXB13 and prostate-cancer risk, N. Engl. J. Med., 366, 141, 10.1056/NEJMoa1110000 · DOI
  25. Martin, 2013, Interplay between homeobox proteins and polycomb repressive complexes in p16 regulation, EMBO, 32, 982, 10.1038/emboj.2013.37 · DOI
  26. Hung, 2003, Homeobox gene expression and mutation in cervical carcinoma cells, Cancer Sci., 94, 437, 10.1111/j.1349-7006.2003.tb01461.x · DOI
  27. Alami, 1999, HOXC5 and HOXC8 expression are selectively turned on in human cervical cancer cells compared to normal keratinocytes, Biochem. Biophys. Res. Commun., 257, 738, 10.1006/bbrc.1999.0516 · DOI
  28. Santos, 2012, Hox B4 as potential marker of non-differentiated cells in human cervical cancer cells, J. Cancer Res. Clin. Oncol., 138, 293, 10.1007/s00432-011-1081-2 · DOI
  29. Zhai, 2007, Gene expression analysis of preinvasive and invasive cervical squamous cell carcinomas identifies HOXC10 as a key mediator of invasion, Cancer Res., 67, 10163, 10.1158/0008-5472.CAN-07-2056 · DOI
  30. White, 2013, Proteomic approaches to the study of papillomavirus-host interactions, Virology, 435, 57, 10.1016/j.virol.2012.09.046 · DOI · Paper page
  31. Huh, 2005, Association of the human papillomavirus type 16 E7 oncoprotein with the 600-kDa retinoblastoma protein-associated factor, p600, Proc. Natl. Acad. Sci. USA, 102, 11492, 10.1073/pnas.0505337102 · DOI · Paper page
  32. Huh, 2008, Human papillomavirus type 16 E7 oncoprotein associates with E2F6, J. Virol., 82, 8695, 10.1128/JVI.00579-08 · DOI · Paper page
  33. Cartwright, 1998, E2F-6: A novel member of the E2F family is an inhibitor of E2F-dependent transcription, Oncogene, 17, 611, 10.1038/sj.onc.1201975 · DOI
  34. Gaubatz, 1998, Unusual proliferation arrest and transcriptional control properties of a newly discovered E2F family member, E2F-6, Proc. Natl. Acad. Sci. USA, 95, 9190, 10.1073/pnas.95.16.9190 · DOI
  35. Trimarchi, 2001, The E2F6 transcription factor is a component of the mammalian Bmi1-containing polycomb complex, Proc. Natl. Acad. Sci. USA, 98, 1519, 10.1073/pnas.98.4.1519 · DOI
  36. Ogawa, 2002, A complex with chromatin modifiers that occupies E2F- and Myc-responsive genes in G0 cells, Science, 296, 1132, 10.1126/science.1069861 · DOI
  37. Attwooll, 2005, A novel repressive E2F6 complex containing the polycomb group protein, EPC1, that interacts with EZH2 in a proliferation-specific manner, J. Biol. Chem., 280, 1199, 10.1074/jbc.M412509200 · DOI
  38. Deshpande, 2007, PHC3, a component of the hPRC-H complex, associates with E2F6 during G0 and is lost in osteosarcoma tumors, Oncogene, 26, 1714, 10.1038/sj.onc.1209988 · DOI
  39. Crum, 2011, Human papillomavirus E7 oncoprotein induces KDM6A and KDM6B histone demethylase expression and causes epigenetic reprogramming, Proc. Natl. Acad. Sci. USA, 108, 2130, 10.1073/pnas.1009933108 · DOI · Paper page
  40. Hyland, 2011, Evidence for alteration of EZH2, BMI1, and KDM6A and epigenetic reprogramming in human papillomavirus type 16 E6/E7-expressing keratinocytes, J. Virol., 85, 10999, 10.1128/JVI.00160-11 · DOI
  41. Morin, 2010, Somatic mutations altering EZH2 (Tyr641) in follicular and diffuse large B-cell lymphomas of germinal-center origin, Nat. Genet., 42, 181, 10.1038/ng.518 · DOI · Paper page
  42. Chase, 2011, Aberrations of EZH2 in cancer, Clin. Cancer Res., 17, 2613, 10.1158/1078-0432.CCR-10-2156 · DOI
  43. Holland, 2008, Activation of the enhancer of zeste homologue 2 gene by the human papillomavirus E7 oncoprotein, Cancer Res., 68, 9964, 10.1158/0008-5472.CAN-08-1134 · DOI · Paper page
  44. Cha, 2005, Akt-mediated phosphorylation of EZH2 suppresses methylation of lysine 27 in histone H3, Science, 310, 306, 10.1126/science.1118947 · DOI
  45. Menges, 2006, Human papillomavirus type 16 E7 up-regulates AKT activity through the retinoblastoma protein, Cancer Res., 66, 5555, 10.1158/0008-5472.CAN-06-0499 · DOI · Paper page
  46. Spangle, 2010, The human papillomavirus type 16 E6 oncoprotein activates mTORC1 signaling and increases protein synthesis, J. Virol., 84, 9398, 10.1128/JVI.00974-10 · DOI · Paper page
  47. Xu, 2012, EZH2 oncogenic activity in castration-resistant prostate cancer cells is Polycomb-independent, Science, 338, 1465, 10.1126/science.1227604 · DOI
  48. Kuzmichev, 2005, Composition and histone substrates of polycomb repressive group complexes change during cellular differentiation, Proc. Natl. Acad. Sci. USA, 102, 1859, 10.1073/pnas.0409875102 · DOI · Paper page
  49. Honig, 2010, Overexpression of polycomb protein BMI-1 in human specimens of breast, Ovarian, endometrial and cervical cancer, Anticancer Res., 30, 1559
  50. Min, 2011, Clinicopathological and prognostic significance of Bmi-1 expression in human cervical cancer, Acta Obstet. Gynecol. Scand., 90, 737, 10.1111/j.1600-0412.2011.01102.x · DOI
  51. Zhang, 2010, Overexpression of Bmi-1 in uterine cervical cancer: Correlation with clinicopathology and prognosis, Int. J. Gynecol. Cancer, 20, 1597
  52. Zhang, 2012, Detection of circulating Bmi-1 mRNA in plasma and its potential diagnostic and prognostic value for uterine cervical cancer, Int. J. Cancer, 131, 165, 10.1002/ijc.26360 · DOI
  53. Tong, 2011, BMI-1 autoantibody as a new potential biomarker for cervical carcinoma, PLoS One, 6, e27804, 10.1371/journal.pone.0027804 · DOI
  54. Miller, 2013, HPV16 E7 Protein and hTERT proteins defective for telomere maintenance cooperate to immortalize human keratinocytes, PLoS Pathog., 9, e1003284, 10.1371/journal.ppat.1003284 · DOI
  55. Chen, 2011, Knockdown of BMI-1 causes cell-cycle arrest and derepresses p16INK4a, HOXA9 and HOXC13 mRNA expression in HeLa cells, Med. Oncol., 28, 1201, 10.1007/s12032-010-9634-9 · DOI
  56. Greenfield, 1998, The UTX gene escapes X inactivation in mice and humans, Hum. Mol. Genet., 7, 737, 10.1093/hmg/7.4.737 · DOI
  57. Shpargel, 2012, UTX and UTY demonstrate histone demethylase-independent function in mouse embryonic development, PLoS Genet., 8, e1002964, 10.1371/journal.pgen.1002964 · DOI
  58. Lee, 2012, UTX, a histone H3-lysine 27 demethylase, acts as a critical switch to activate the cardiac developmental program, Dev. Cell, 22, 25, 10.1016/j.devcel.2011.11.009 · DOI
  59. Wang, 2012, UTX regulates mesoderm differentiation of embryonic stem cells independent of H3K27 demethylase activity, Proc. Natl. Acad. Sci. USA, 109, 15324, 10.1073/pnas.1204166109 · DOI
  60. Burgold, 2012, The H3K27 demethylase JMJD3 is required for maintenance of the embryonic respiratory neuronal network, Neonatal breathing, and survival, Cell Rep., 2, 1244, 10.1016/j.celrep.2012.09.013 · DOI
  61. Narang, 2009, Jmjd3 contributes to the control of gene expression in LPS-activated macrophages, EMBO, 28, 3341, 10.1038/emboj.2009.271 · DOI
  62. Lee, 2007, Demethylation of H3K27 regulates polycomb recruitment and H2A ubiquitination, Science, 318, 447, 10.1126/science.1149042 · DOI
  63. Issaeva, 2007, Knockdown of ALR (MLL2) reveals ALR target genes and leads to alterations in cell adhesion and growth, Mol. Cell Biol., 27, 1889, 10.1128/MCB.01506-06 · DOI
  64. Dalgliesh, 2009, Somatic mutations of the histone H3K27 demethylase gene UTX in human cancer, Nat. Genet., 41, 521, 10.1038/ng.349 · DOI · Paper page
  65. Xiang, 2007, JMJD3 is a histone H3K27 demethylase, Cell Res., 17, 850, 10.1038/cr.2007.83 · DOI
  66. Sen, 2008, Control of differentiation in a self-renewing mammalian tissue by the histone demethylase JMJD3, Gene. Develop., 22, 1865, 10.1101/gad.1673508 · DOI
  67. Agger, 2009, The H3K27me3 demethylase JMJD3 contributes to the activation of the INK4A-ARF locus in response to oncogene- and stress-induced senescence, Gene. Develop., 23, 1171, 10.1101/gad.510809 · DOI · Paper page
  68. Sano, 1998, Expression status of p16 protein is associated with human papillomavirus oncogenic potential in cervical and genital lesions, Amer. J. Pathol., 153, 1741, 10.1016/S0002-9440(10)65689-1 · DOI
  69. Klaes, 2001, Overexpression of p16(INK4A) as a specific marker for dysplastic and neoplastic epithelial cells of the cervix uteri, Int. J. Cancer, 92, 276, 10.1002/ijc.1174 · DOI
  70. Khleif, 1996, Inhibition of cyclin D-CDK4/CDK6 activity is associated with an E2F-mediated induction of cyclin kinase inhibitor activity, Proc. Natl. Acad. Sci. USA, 93, 4350, 10.1073/pnas.93.9.4350 · DOI
  71. Gonzalez, 2001, Degradation of the retinoblastoma tumor suppressor by the human papillomavirus type 16 E7 oncoprotein is important for functional inactivation and is separable from proteasomal degradation of E7, J. Virol., 75, 7583, 10.1128/JVI.75.16.7583-7591.2001 · DOI · Paper page
  72. Skalska, 2013, Induction of p16(INK4a) is the major barrier to proliferation when Epstein-Barr Virus (EBV) transforms primary B cells into lymphoblastoid cell lines, PLoS Pathog., 9, e1003187, 10.1371/journal.ppat.1003187 · DOI
  73. Skalska, 2010, Epigenetic repression of p16(INK4A) by latent Epstein-Barr virus requires the interaction of EBNA3A and EBNA3C with CtBP, PLoS Pathog., 6, e1000951, 10.1371/journal.ppat.1000951 · DOI
  74. White, 2010, Extensive co-operation between the Epstein-Barr virus EBNA3 proteins in the manipulation of host gene expression and epigenetic chromatin modification, PLoS One, 5, e13979, 10.1371/journal.pone.0013979 · DOI
  75. Paschos, 2012, BIM promoter directly targeted by EBNA3C in polycomb-mediated repression by EBV, Nucleic Acids Res., 40, 7233, 10.1093/nar/gks391 · DOI
  76. Andrisani, 2013, Deregulation of epigenetic mechanisms by the hepatitis B virus x protein in hepatocarcinogenesis, Viruses, 5, 858, 10.3390/v5030858 · DOI
  77. Herschkowitz, 2008, The functional loss of the retinoblastoma tumour suppressor is a common event in basal-like and luminal B breast carcinomas, Breast Cancer Res., 10, R75, 10.1186/bcr2142 · DOI
  78. Jarrard, 2002, Alterations in the p16/pRb cell cycle checkpoint occur commonly in primary and metastatic human prostate cancer, Cancer Lett., 185, 191, 10.1016/S0304-3835(02)00282-3 · DOI
  79. Kommoss, 2007, Independent prognostic significance of cell cycle regulator proteins p16(INK4a) and pRb in advanced-stage ovarian carcinoma including optimally debulked patients: a translational research subprotocol of a randomised study of the Arbeitsgemeinschaft Gynaekologische Onkologie Ovarian Cancer Study Group, Br. J. Cancer, 96, 306, 10.1038/sj.bjc.6603531 · DOI
  80. Andujar, 2010, p16INK4A inactivation mechanisms in non-small-cell lung cancer patients occupationally exposed to asbestos, Lung Cancer, 67, 23, 10.1016/j.lungcan.2009.03.018 · DOI
  81. Malumbres, 2001, To cycle or not to cycle: a critical decision in cancer, Nat. Rev. Cancer, 1, 222, 10.1038/35106065 · DOI
  82. Horner, 2004, Repression of the human papillomavirus E6 gene initiates p53-dependent, Telomerase-independent senescence and apoptosis in HeLa cervical carcinoma cells, J. Virol., 78, 4063, 10.1128/JVI.78.8.4063-4073.2004 · DOI
  83. Psyrri, 2004, Role of the retinoblastoma pathway in senescence triggered by repression of the human papillomavirus E7 protein in cervical carcinoma cells, Cancer Res., 64, 3079, 10.1158/0008-5472.CAN-03-3739 · DOI
  84. DeFilippis, 2003, Endogenous human papillomavirus E6 and E7 proteins differentially regulate proliferation, senescence, and apoptosis in HeLa cervical carcinoma cells, J. Virol., 77, 1551, 10.1128/JVI.77.2.1551-1563.2003 · DOI
  85. Westbrook, 2005, A genetic screen for candidate tumor suppressors identifies REST, Cell, 121, 837, 10.1016/j.cell.2005.03.033 · DOI
  86. Coulson, 2000, A splice variant of the neuron-restrictive silencer factor repressor is expressed in small cell lung cancer: A potential role in derepression of neuroendocrine genes and a useful clinical marker, Cancer Res., 60, 1840
  87. Westbrook, 2008, SCFbeta-TRCP controls oncogenic transformation and neural differentiation through REST degradation, Nature, 452, 370, 10.1038/nature06780 · DOI · Paper page

Cited by

See all 28

Metadata

Authors
McLaughlin-Drubin, M., & Munger, K.
Affiliations
Division of Infectious Diseases, Brigham and Women's Hospital and Department of Medicine, Harvard Medical School, 181 Longwood Avenue, MCP 861, Boston, MA 02115, USA
Venue
Viruses
Publisher
MDPI AG
Published
2013-05-14
Volume
5
Issue
5
Pages
1231-1249
ISSN
1999-4915
DOI
10.3390/v5051231
PMC
PMC3712305
Cited by
28
References
6
Language
en
Licence
creativecommons.org/licenses/by/3.0/ (vor)

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review