Vitamin C – A new player in regulation of the cancer epigenome

The cBio Cancer Genomics Portal: An Open Platform for Exploring Multidimensional Cancer Genomics Data

Cerami, E., Gao, J., Dogrusoz, U., Gross, B. E., Sumer, S. O., Aksoy, B. A., Jacobsen, A., Byrne, C. J., Heuer, M. L., Larsson, E., et al. (2012) · Cancer Discovery · doi:10.1158/2159-8290.cd-12-0095 · Cited by 17,455 · see citing works

Integrative Analysis of Complex Cancer Genomics and Clinical Profiles Using the cBioPortal

Gao, J., Aksoy, B. A., Dogrusoz, U., Dresdner, G., Gross, B., Sumer, S. O., Sun, Y., Jacobsen, A., Sinha, R., Larsson, E., et al. (2013) · Science Signaling · doi:10.1126/scisignal.2004088 · Cited by 15,160 · see citing works

Conversion of 5-Methylcytosine to 5-Hydroxymethylcytosine in Mammalian DNA by MLL Partner TET1

Tahiliani, M., Koh, K. P., Shen, Y., Pastor, W. A., Bandukwala, H., Brudno, Y., Agarwal, S., Iyer, L. M., Liu, D. R., Aravind, L., et al. (2009) · Science · doi:10.1126/science.1170116 · Cited by 5,836 · see citing works

Tet proteins can convert 5-methylcytosine to 5-formylcytosine and 5-carboxylcytosine

Ito, S., Shen, L., Dai, Q., Wu, S. C., Collins, L. B., Swenberg, J. A., He, C., & Zhang, Y. (2011) · Science · doi:10.1126/science.1210597 · Cited by 3,451 · see citing works

Epigenetics in human disease and prospects for epigenetic therapy

Egger, G., Liang, G., Aparicio, A., & Jones, P. A. (2004) · Nature · doi:10.1038/nature02625 · Cited by 3,232 · see citing works

Oncometabolite 2-Hydroxyglutarate Is a Competitive Inhibitor of α-Ketoglutarate-Dependent Dioxygenases

Xu, W., Yang, H., Liu, Y., Yang, Y., Wang, P., Kim, S.-H., Ito, S., Yang, C., Wang, P., Xiao, M.-T., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2010.12.014 · Cited by 2,875 · see citing works

A decade of exploring the cancer epigenome—biological and translational implications

Baylin, S. B., & Jones, P. A. (2011) · Nature Reviews Cancer · doi:10.1038/nrc3130 · Cited by 2,871 · see citing works

Tet-Mediated Formation of 5-Carboxylcytosine and Its Excision by TDG in Mammalian DNA

He, Y., Li, B.-Z., Li, Z., Liu, P., Wang, Y., Tang, Q., Ding, J., Jia, Y., Chen, Z., Li, L., et al. (2011) · Science · doi:10.1126/science.1210944 · Cited by 2,776 · see citing works

Leukemic IDH1 and IDH2 Mutations Result in a Hypermethylation Phenotype, Disrupt TET2 Function, and Impair Hematopoietic Differentiation

Figueroa, M. E., Abdel-Wahab, O., Lu, C., Ward, P. S., Patel, J., Shih, A., Li, Y., Bhagwat, N., Vasanthakumar, A., Fernandez, H. F., et al. (2010) · Cancer Cell · doi:10.1016/j.ccr.2010.11.015 · Cited by 2,766 · see citing works

The Nuclear DNA Base 5-Hydroxymethylcytosine Is Present in Purkinje Neurons and the Brain

Kriaucionis, S., & Heintz, N. (2009) · Science · doi:10.1126/science.1169786 · Cited by 2,700 · see citing works

Epigenetics in cancer

Sharma, S., Kelly, T. K., & Jones, P. A. (2010) · Carcinogenesis · doi:10.1093/carcin/bgp220 · Cited by 2,637 · see citing works

Histone demethylation by a family of JmjC domain-containing proteins

Tsukada, Y.-I., Fang, J., Erdjument‐Bromage, H., Warren, M., Borchers, C. H., Tempst, P., & Zhang, Y. (2005) · Nature · doi:10.1038/nature04433 · Cited by 2,171 · see citing works

Dietary Reference Intakes for Vitamin C, Vitamin E, Selenium, and Carotenoids

Compounds, P. O. D. A. A. R., Nutrients, S. O. U. R. L. O., Intakes, S. O. I. A. U. O. D. R., Standing Committee on the Scientific Evaluation of Dietary Reference Intakes, Food and Nutrition Board, & Institute of Medicine (2000) · doi:10.17226/9810 · Cited by 2,034 · see citing works

Inhibiting DNA Methylation Causes an Interferon Response in Cancer via dsRNA Including Endogenous Retroviruses

Chiappinelli, K. B., Strissel, P. L., Desrichard, A., Li, H., Henke, C., Akman, B., Hein, A., Rote, N. S., Cope, L. M., Snyder, A., et al. (2015) · Cell · doi:10.1016/j.cell.2015.07.011 · Cited by 2,022 · see citing works

Mutation in <i>TET2</i> in Myeloid Cancers

Delhommeau, F., Dupont, S., Valle, V. D., James, C., Trannoy, S., Massé, A., Kosmider, O., Le Couedic, J.-P., Robert, F., Alberdi, A., et al. (2009) · New England Journal of Medicine · doi:10.1056/nejmoa0810069 · Cited by 1,776 · see citing works

TET enzymes, TDG and the dynamics of DNA demethylation

Kohli, R. M., & Zhang, Y. (2013) · Nature · doi:10.1038/nature12750 · Cited by 1,623 · see citing works

DNA-Demethylating Agents Target Colorectal Cancer Cells by Inducing Viral Mimicry by Endogenous Transcripts

Roulois, D., Loo Yau, H., Singhania, R., Wang, Y., Danesh, A., Shen, S. Y., Han, H., Liang, G., Jones, P. A., Pugh, T. J., et al. (2015) · Cell · doi:10.1016/j.cell.2015.07.056 · Cited by 1,527 · see citing works

Impaired hydroxylation of 5-methylcytosine in myeloid cancers with mutant TET2

Ko, M., Huang, Y., Jankowska, A. M., Pape, U. J., Tahiliani, M., Bandukwala, H. S., An, J., Lamperti, E. D., Koh, K. P., Ganetzky, R. D., et al. (2010) · Nature · doi:10.1038/nature09586 · Cited by 1,294 · see citing works

Gene Body Methylation Can Alter Gene Expression and Is a Therapeutic Target in Cancer

Yang, X., Han, H., De Carvalho, D. D., Lay, F. D., Jones, P. A., & Liang, G. (2014) · Cancer Cell · doi:10.1016/j.ccr.2014.07.028 · Cited by 1,199 · see citing works

Inhibition of α-KG-dependent histone and DNA demethylases by fumarate and succinate that are accumulated in mutations of FH and SDH tumor suppressors

Xiao, M., Yang, H., Xu, W., Ma, S., Lin, H., Zhu, H., Liu, L., Liu, Y., Yang, C., Xu, Y., et al. (2012) · Genes &amp; Development · doi:10.1101/gad.191056.112 · Cited by 1,188 · see citing works

Transcription of IAP endogenous retroviruses is constrained by cytosine methylation

Walsh, C. P., Chaillet, J. R., & Bestor, T. H. (1998) · Nature Genetics · doi:10.1038/2413 · Cited by 1,105 · see citing works

Selective chemical labeling reveals the genome-wide distribution of 5-hydroxymethylcytosine

Song, C., Szulwach, K. E., Fu, Y., Dai, Q., Yi, C., Li, X., Li, Y., Chen, C.-H., Zhang, W., Jian, X., et al. (2010) · Nature Biotechnology · doi:10.1038/nbt.1732 · Cited by 1,089 · see citing works

Ascorbic acid: Chemistry, biology and the treatment of cancer

Du, J., Cullen, J. J., & Buettner, G. R. (2012) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2012.06.003 · Cited by 1,071 · see citing works

Active DNA demethylation: many roads lead to Rome

Wu, S. C., & Zhang, Y. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2950 · Cited by 1,054 · see citing works

Role of TET enzymes in DNA methylation, development, and cancer

Rasmussen, K. D., & Helin, K. (2016) · Genes &amp; Development · doi:10.1101/gad.276568.115 · Cited by 1,040 · see citing works

The oncometabolite 2-hydroxyglutarate inhibits histone lysine demethylases

Chowdhury, R., Yeoh, K. K., Tian, Y., Hillringhaus, L., Bagg, E. A., Rose, N. R., Leung, I. K. H., Li, X. S., Woon, E. C. Y., Yang, M., et al. (2011) · The EMBO Reports · doi:10.1038/embor.2011.43 · Cited by 1,035 · see citing works

The histone H3 lysine-27 demethylase Jmjd3 links inflammation to inhibition of polycomb-mediated gene silencing

De Santa, F., Totaro, M. G., Prosperini, E., Notarbartolo, S., Testa, G., & Natoli, G. (2007) · Cell · doi:10.1016/j.cell.2007.08.019 · Cited by 965 · see citing works

Vitamin C selectively kills <i>KRAS</i> and <i>BRAF</i> mutant colorectal cancer cells by targeting GAPDH

Yun, J., Mullarky, E., Lu, C., Bosch, K. N., Kavalier, A., Rivera, K., Roper, J., Chio, I. I. C., Giannopoulou, E. G., Rago, C., et al. (2015) · Science · doi:10.1126/science.aaa5004 · Cited by 913 · see citing works

A family of mammalian Na+-dependent L-ascorbic acid transporters

Tsukaguchi, H., Tokui, T., Mackenzie, B., Berger, U. V., Chen, X.-Z., Wang, Y., Brubaker, R. F., & Hediger, M. A. (1999) · Nature · doi:10.1038/19986 · Cited by 882 · see citing works

Vitamin C induces Tet-dependent DNA demethylation and a blastocyst-like state in ES cells

Blaschke, K., Ebata, K. T., Karimi, M. M., Zepeda-Martínez, J. A., Goyal, P., Mahapatra, S., Tam, A., Laird, D. J., Hirst, M., Rao, A., et al. (2013) · Nature · doi:10.1038/nature12362 · Cited by 865 · see citing works

JHDM2A, a JmjC-Containing H3K9 Demethylase, Facilitates Transcription Activation by Androgen Receptor

Yamane, K., Toumazou, C., Tsukada, Y.-I., Erdjument‐Bromage, H., Tempst, P., Wong, J., & Zhang, Y. (2006) · Cell · doi:10.1016/j.cell.2006.03.027 · Cited by 840 · see citing works

A histone H3 lysine 27 demethylase regulates animal posterior development

Lan, F., Bayliss, P. E., Rinn, J. L., Whetstine, J. R., Wang, J. K., Chen, S., Iwase, S., Alpatov, R., Issaeva, I., Canaani, E., et al. (2007) · Nature · doi:10.1038/nature06192 · Cited by 782 · see citing works

Demethylation of H3K27 Regulates Polycomb Recruitment and H2A Ubiquitination

Lee, M. G., Villa, R., Trojer, P., Norman, J. A., Yan, K.-P., Reinberg, D., Croce, L. D., & Shiekhattar, R. (2007) · Science · doi:10.1126/science.1149042 · Cited by 772 · see citing works

JMJD6 Is a Histone Arginine Demethylase

Chang, B., Chen, Y., Zhao, Y., & Bruick, R. K. (2007) · Science · doi:10.1126/science.1145801 · Cited by 746 · see citing works

Restoration of TET2 Function Blocks Aberrant Self-Renewal and Leukemia Progression

Cimmino, L., Dolgalev, I., Wang, Y., Yoshimi, A., Martin, G. H., Wang, J., Ng, V., Xia, B., Witkowski, M. T., Mitchell-Flack, M., et al. (2017) · Cell · doi:10.1016/j.cell.2017.07.032 · Cited by 707 · see citing works

Identification of JmjC domain-containing UTX and JMJD3 as histone H3 lysine 27 demethylases

Hong, S., Cho, Y., Yu, L., Yu, H., Veenstra, T. D., & Ge, K. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0707292104 · Cited by 700 · see citing works

The X-Linked Mental Retardation Gene SMCX/JARID1C Defines a Family of Histone H3 Lysine 4 Demethylases

Iwase, S., Lan, F., Bayliss, P. E., de la Torre-Ubieta, L., Huarte, M., Qi, H. H., Whetstine, J. R., Bonni, A., Roberts, T. M., & Shi, Y. (2007) · Cell · doi:10.1016/j.cell.2007.02.017 · Cited by 695 · see citing works

Ascorbate in pharmacologic concentrations selectively generates ascorbate radical and hydrogen peroxide in extracellular fluid <i>in vivo</i>

Chen, Q., Espey, M. G., Sun, A. Y., Lee, J.-H., Krishna, M. C., Shacter, E., Choyke, P. L., Pooput, C., Kirk, K. L., Buettner, G. R., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702854104 · Cited by 676 · see citing works

Erasing the methyl mark: histone demethylases at the center of cellular differentiation and diseasePreprint

Cloos, P. A., Christensen, J., Agger, K., & Helin, K. (2008) · Genes & Development · doi:10.1101/gad.1652908 · Cited by 664 · see citing works

Tumour hypoxia causes DNA hypermethylation by reducing TET activity

Thienpont, B., Steinbacher, J., Zhao, H., D’Anna, F., Kuchnio, A., Ploumakis, A., Ghesquière, B., Van Dyck, L., Boeckx, B., Schoonjans, L., et al. (2016) · Nature · doi:10.1038/nature19081 · Cited by 635 · see citing works

The transcriptional repressor JHDM3A demethylates trimethyl histone H3 lysine 9 and lysine 36

Klose, R. J., Yamane, K., Bae, Y., Zhang, D., Erdjument‐Bromage, H., Tempst, P., Wong, J., & Zhang, Y. (2006) · Nature · doi:10.1038/nature04853 · Cited by 630 · see citing works

Ascorbic acid enhances Tet-mediated 5-methylcytosine oxidation and promotes DNA demethylation in mammals

Yin, R., Mao, S.-Q., Zhao, B., Chong, Z., Yang, Y., Zhao, C., Zhang, D., Huang, H., Gao, J., Li, Z., et al. (2013) · Journal of the American Chemical Society · doi:10.1021/ja4028346 · Cited by 609 · see citing works

Tumor development is associated with decrease of TET gene expression and 5-methylcytosine hydroxylation

Yang, H., Liu, Y., Bai, F., Zhang, J., Ma, S.-H., Liu, J., Xu, Z.-D., Zhu, H.-G., Ling, Z.-Q., Ye, D., et al. (2012) · Oncogene · doi:10.1038/onc.2012.67 · Cited by 575 · see citing works

Biophysical and biochemical characterization of five animal viruses with bisegmented double-stranded RNA genomes

Dobos, P., Hill, B. J., Hallett, R., Kells, D. T., Becht, H., & Teninges, D. (1979) · Journal of Virology · doi:10.1128/jvi.32.2.593-605.1979 · Cited by 572 · see citing works

The biochemical functions of ascorbic acid

Englard, S., & Seifter, S. (1986) · Annual Review of Nutrition · doi:10.1146/annurev.nu.06.070186.002053 · Cited by 564 · see citing works

RBP2 Belongs to a Family of Demethylases, Specific for Tri-and Dimethylated Lysine 4 on Histone 3

Christensen, J. F., Agger, K., Cloos, P. A., Pasini, D., Rose, S., Sennels, L., Rappsilber, J., Hansen, K. H., Salcini, A. E., & Helin, K. (2007) · Cell · doi:10.1016/j.cell.2007.02.003 · Cited by 554 · see citing works

Ascorbate regulates haematopoietic stem cell function and leukaemogenesis

Agathocleous, M., Meacham, C. E., Burgess, R. J., Piskounova, E., Zhao, Z., Crane, G. M., Cowin, B. L., Bruner, E., Murphy, M. M., Chen, W., et al. (2017) · Nature · doi:10.1038/nature23876 · Cited by 545 · see citing works

A new recommended dietary allowance of vitamin C for healthy young women

Levine, M., Wang, Y., Padayatty, S. J., & Morrow, J. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.171318198 · Cited by 496 · see citing works

Replication-Dependent Loss of 5-Hydroxymethylcytosine in Mouse Preimplantation Embryos

Inoue, A., & Zhang, Y. (2011) · Science · doi:10.1126/science.1212483 · Cited by 489 · see citing works

H3K9 methylation is a barrier during somatic cell reprogramming into iPSCs

Chen, J., He, L., Liu, J., Qi, J. Y., Wei, B., Yang, J., Liang, H., Chen, Y., Chen, J., Wu, Y., et al. (2012) · Nature Genetics · doi:10.1038/ng.2491 · Cited by 483 · see citing works

Protein methyltransferases as a target class for drug discovery

Copeland, R. A., Solomon, M. E., & Richon, V. M. (2009) · Nature Reviews Drug Discovery · doi:10.1038/nrd2974 · Cited by 467 · see citing works

The Histone Demethylases Jhdm1a/1b Enhance Somatic Cell Reprogramming in a Vitamin-C-Dependent Manner

Wang, T., Chen, K., Zeng, X., Yang, J., Wu, Y., Shi, X., Qin, B., Zeng, L., Esteban, M. A., Pan, G., et al. (2011) · Cell Stem Cell · doi:10.1016/j.stem.2011.10.005 · Cited by 458 · see citing works

The Retinoblastoma Binding Protein RBP2 Is an H3K4 Demethylase

Klose, R. J., Yan, Q., Tóthová, Z., Yamane, K., Erdjument‐Bromage, H., Tempst, P., Gilliland, D. G., Zhang, Y., & Kaelin, W. G. (2007) · Cell · doi:10.1016/j.cell.2007.02.013 · Cited by 446 · see citing works

O2⋅− and H2O2-Mediated Disruption of Fe Metabolism Causes the Differential Susceptibility of NSCLC and GBM Cancer Cells to Pharmacological Ascorbate

Schoenfeld, J. D., Sibenaller, Z. A., Mapuskar, K. A., Wagner, B. A., Cramer-Morales, K. L., Furqan, M., Sandhu, S., Carlisle, T. L., Smith, M. C., Abu Hejleh, T., et al. (2017) · Cancer Cell · doi:10.1016/j.ccell.2017.02.018 · Cited by 443 · see citing works

5-Hydroxymethylcytosine Is Strongly Depleted in Human Cancers but Its Levels Do Not Correlate with IDH1 Mutations

Jin, S., Jiang, Y., Qiu, R., Rauch, T. A., Wang, Y., Schackert, G., Krex, D., Lü, Q., & Pfeifer, G. P. (2011) · Cancer Research · doi:10.1158/0008-5472.can-11-2023 · Cited by 441 · see citing works

Jmjd6 Catalyses Lysyl-Hydroxylation of U2AF65, a Protein Associated with RNA Splicing

Webby, C. J., Wolf, A., Gromak, N., Dreger, M., Kramer, H., Kessler, B. M., Nielsen, M. L., Schmitz, C., Butler, D. S., Yates, J. R., et al. (2009) · Science · doi:10.1126/science.1175865 · Cited by 423 · see citing works

Global 5-hydroxymethylcytosine content is significantly reduced in tissue stem/progenitor cell compartments and in human cancers

Haffner, M. C., Chaux, A., Meeker, A. K., Esopi, D., Gerber, J. M., Pellakuru, L. G., Toubaji, A., Argani, P., Iacobuzio–Donahue, C. A., Nelson, W. G., et al. (2011) · Oncotarget · doi:10.18632/oncotarget.316 · Cited by 419 · see citing works

Ascorbate induces ten-eleven translocation (Tet) methylcytosine dioxygenase-mediated generation of 5-hydroxymethylcytosine

Minor, E. A., Court, B. L., Young, J. I., & Wang, G. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.c113.464800 · Cited by 413 · see citing works

Tissue type is a major modifier of the 5-hydroxymethylcytosine content of human genesPreprint

Nestor, C. E., Ottaviano, R., Reddington, J. P., Sproul, D., Reinhardt, D., Dunican, D. S., Katz, E., Dixon, J. M., Harrison, D. J., & Meehan, R. R. (2011) · Genome Research · doi:10.1101/gr.126417.111 · Cited by 403 · see citing works

Enzymatic and structural insights for substrate specificity of a family of jumonji histone lysine demethylases

Horton, J. R., Upadhyay, A. K., Qi, H. H., Zhang, X., Shi, Y., & Cheng, X. (2010) · Nature Structural &amp; Molecular Biology · doi:10.1038/nsmb.1753 · Cited by 389 · see citing works

Inhibition of DNA methylation by 5-aza-2'-deoxycytidine suppresses the growth of human tumor cell lines.

Bender, C. M., Pao, M. M., & Jones, P. A. (1998) · PubMed · Cited by 386 · see citing works

REGULATION OF VITAMIN C TRANSPORT

Wilson, J. X. (2005) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.25.050304.092647 · Cited by 376 · see citing works

Genomic mapping of 5-hydroxymethylcytosine in the human brain

Jin, S.-G., Wu, X., Li, A. X., & Pfeifer, G. P. (2011) · Nucleic Acids Research · doi:10.1093/nar/gkr120 · Cited by 375 · see citing works

The Interplay of Reactive Oxygen Species, Hypoxia, Inflammation, and Sirtuins in Cancer Initiation and Progression

Tafani, M., Sansone, L., Limana, F., Arcangeli, T., Santis, E. D., Polese, M., Fini, M., & Russo, M. A. (2015) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2016/3907147 · Cited by 371 · see citing works

Epigenetic changes in cancer

Grønbæk, K., Hother, C., & Jones, P. A. (2007) · Apmis · doi:10.1111/j.1600-0463.2007.apm_636.xml.x · Cited by 368 · see citing works

Ascorbic-acid transporter Slc23a1 is essential for vitamin C transport into the brain and for perinatal survival

Sotiriou, S., Gispert, S., Cheng, J., Wang, Y., Chen, A., Hoogstraten-Miller, S., Miller, G. F., Kwon, O., Levine, M., Guttentag, S. H., et al. (2002) · Nature Medicine · doi:10.1038/0502-514 · Cited by 367 · see citing works

DNMT and HDAC inhibitors induce cryptic transcription start sites encoded in long terminal repeats

Brocks, D., Schmidt, C. R., Daskalakis, M., Jang, H. S., Shah, N. M., Li, D., Li, J., Zhang, B., Hou, Y., Laudato, S., et al. (2017) · Nature Genetics · doi:10.1038/ng.3889 · Cited by 339 · see citing works

Loss of Tet Enzymes Compromises Proper Differentiation of Embryonic Stem Cells

Dawlaty, M. M., Breiling, A., Le, T., Barrasa, M. I., Raddatz, G., Gao, Q., Powell, B. E., Cheng, A. W., Faull, K. F., Lyko, F., et al. (2014) · Developmental Cell · doi:10.1016/j.devcel.2014.03.003 · Cited by 338 · see citing works

BloodSpot: a database of gene expression profiles and transcriptional programs for healthy and malignant haematopoiesis

Bagger, F. O., Sasivarevic, D., Sohi, S. H., Laursen, L. G., Pundhir, S., Sønderby, C. K., Winther, O., Rapin, N., & Porse, B. T. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv1101 · Cited by 330 · see citing works

Oncogenic cancer/testis antigens: prime candidates for immunotherapy

Gjerstorff, M. F., Andersen, M. H., & Ditzel, H. J. (2015) · Oncotarget · doi:10.18632/oncotarget.4694 · Cited by 320 · see citing works

Creation of genomic methylation patterns

Bestor, T. H., & Tycko, B. (1996) · Nature Genetics · doi:10.1038/ng0496-363 · Cited by 310 · see citing works

WT1 Recruits TET2 to Regulate Its Target Gene Expression and Suppress Leukemia Cell Proliferation

Wang, Y., Xiao, M., Chen, X., Chen, L., Xu, Y., Lv, L., Wang, P., Yang, H., Ma, S., Lin, H., et al. (2015) · Molecular Cell · doi:10.1016/j.molcel.2014.12.023 · Cited by 304 · see citing works

Histone H4K20/H3K9 demethylase PHF8 regulates zebrafish brain and craniofacial development

Qi, H. H., Sarkissian, M., Hu, G., Wang, Z., Bhattacharjee, A., Gordon, D. B., Gonzales, M., Lan, F., Ongusaha, P. P., Huarte, M., et al. (2010) · Nature · doi:10.1038/nature09261 · Cited by 303 · see citing works

JMJD3 is a histone H3K27 demethylase

Xiang, Y., Zhu, Z., Han, G., Lin, H., Xu, L., & Chen, C. D. (2007) · Cell Research · doi:10.1038/cr.2007.83 · Cited by 301 · see citing works

JHDM1B/FBXL10 is a nucleolar protein that represses transcription of ribosomal RNA genes

Frescas, D., Guardavaccaro, D., Bassermann, F., Koyama-Nasu, R., & Pagano, M. (2007) · Nature · doi:10.1038/nature06255 · Cited by 284 · see citing works

Regulation of NF-κB by NSD1/FBXL11-dependent reversible lysine methylation of p65

Lu, T., Jackson, M. W., Wang, B., Yang, M., Chance, M. R., Miyagi, M., Gudkov, A. V., & Stark, G. R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0912493107 · Cited by 281 · see citing works

Expression of GLUT1 and GLUT3 Glucose Transporters in Endometrial and Breast Cancers

Krześlak, A., Wójcik‐Krowiranda, K., Forma, E., Jóźwiak, P., Romanowicz, H., Bieńkiewicz, A., & Bryś, M. (2012) · Pathology & Oncology Research · doi:10.1007/s12253-012-9500-5 · Cited by 280 · see citing works

Loss of 5‐hydroxymethylcytosine is accompanied with malignant cellular transformation

Kudo, Y., Tateishi, K., Yamamoto, K., Yamamoto, S., Asaoka, Y., Ijichi, H., Nagae, G., Yoshida, H., Aburatani, H., & Koike, K. (2012) · Cancer Science · doi:10.1111/j.1349-7006.2012.02213.x · Cited by 278 · see citing works

The active role of vitamin C in mammalian iron metabolism: Much more than just enhanced iron absorption!

Lane, D. J. R., & Richardson, D. R. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.07.007 · Cited by 264 · see citing works

Physical and Functional Association of a Trimethyl H3K4 Demethylase and Ring6a/MBLR, a Polycomb-like Protein

Lee, M. G., Norman, J. A., Shilatifard, A., & Shiekhattar, R. (2007) · Cell · doi:10.1016/j.cell.2007.02.004 · Cited by 254 · see citing works

Scientific Opinion on Dietary Reference Values for vitamin A

EFSA Panel on Dietetic Products, N. (2015) · EFSA Journal · doi:10.2903/j.efsa.2015.4028 · Cited by 240 · see citing works

Vitamin C increases viral mimicry induced by 5-aza-2′-deoxycytidine

Liu, M., Ohtani, H., Zhou, W., Ørskov, A. D., Charlet, J., Zhang, Y. W., Shen, H., Baylin, S. B., Liang, G., Grønbæk, K., et al. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1612262113 · Cited by 225 · see citing works

Human UTY(KDM6C) Is a Male-specific Nϵ-Methyl Lysyl Demethylase

Walport, L. J., Hopkinson, R. J., Vollmar, M., Madden, S. K., Gileadi, C., Oppermann, U. C. T., Schofield, C. J., & Johansson, C. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.555052 · Cited by 220 · see citing works

Effect of the inflammatory response on trace element and vitamin status

Galloway, S. P., McMillan, D. C., & Sattar, N. (2000) · Annals of Clinical Biochemistry International Journal of Laboratory Medicine · doi:10.1258/0004563001899429 · Cited by 202 · see citing works

Dynamic Histone H1 Isotype 4 Methylation and Demethylation by Histone Lysine Methyltransferase G9a/KMT1C and the Jumonji Domain-containing JMJD2/KDM4 Proteins

Trojer, P., Zhang, J., Yonezawa, M., Schmidt, A., Zheng, H., Jenuwein, T., & Reinberg, D. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m807818200 · Cited by 201 · see citing works

Vitamin C deficiency in cancer patients

Mayland, C. R., Bennett, M. I., & Allan, K. (2005) · Palliative Medicine · doi:10.1191/0269216305pm970oa · Cited by 199 · see citing works

KDM8, a H3K36me2 histone demethylase that acts in the cyclin A1 coding region to regulate cancer cell proliferation

Hsia, D. A., Tepper, C. G., Pochampalli, M. R., Hsia, E. Y. C., Izumiya, C., Huerta, S. B., Wright, M. E., Chen, H.-W., Kung, H.-J., & Izumiya, Y. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1000401107 · Cited by 197 · see citing works

The chemical nature of vitamin C

Svirbely, J. L., & Szent‐Györgyi, A. (1932) · Biochemical Journal · doi:10.1042/bj0260865 · Cited by 196 · see citing works

Dehydroascorbic Acid Transport by GLUT4 in XenopusOocytes and Isolated Rat Adipocytes

Rumsey, S. C., Daruwala, R., Al‐Hasani, H., Zarnowski, M. J., Simpson, I. A., & Levine, M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000988200 · Cited by 196 · see citing works

Demethylation of trimethylated histone H3 Lys4 in vivo by JARID1 JmjC proteins

Seward, D. J., Cubberley, G., Kim, S., Schonewald, M., Zhang, L., Tripet, B., & Bentley, D. L. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1200 · Cited by 185 · see citing works

Inhibition of TET2-mediated conversion of 5-methylcytosine to 5-hydroxymethylcytosine disturbs erythroid and granulomonocytic differentiation of human hematopoietic progenitors

Pronier, E., Almire, C., Mokrani, H., Vasanthakumar, A., Simon, A., Monte-Mór, B. D. C. R., Massé, A., Couedic, J. P. L., Pendino, F., Carbonne, B., et al. (2011) · Blood · doi:10.1182/blood-2010-12-324707 · Cited by 184 · see citing works

Vitamin C Promotes Widespread Yet Specific DNA Demethylation of the Epigenome in Human Embryonic Stem Cells

Chung, T.-L., Brena, R. M., Kolle, G., Grimmond, S. M., Berman, B. P., Laird, P. W., Pera, M. F., & Wolvetang, E. J. (2010) · Stem Cells · doi:10.1002/stem.493 · Cited by 182 · see citing works

Structural and Evolutionary Basis for the Dual Substrate Selectivity of Human KDM4 Histone Demethylase Family

Hillringhaus, L., Yue, W. W., Rose, N. R., Ng, S. S., Gileadi, C., Loenarz, C., Bello, S. H., Bray, J. E., Schofield, C. J., & Oppermann, U. C. T. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.283689 · Cited by 175 · see citing works

Scientific Opinion on Dietary Reference Values for vitamin C

EFSA Panel on Dietetic Products, N. A. A. (. (2013) · EFSA Journal · doi:10.2903/j.efsa.2013.3418 · Cited by 173 · see citing works

Stromal cell oxidation: a mechanism by which tumors obtain vitamin C.

Agus, D. B., Vera, J. C., & Golde, D. W. (1999) · PubMed · Cited by 168 · see citing works

Glut1 and Glut3 as Potential Prognostic Markers for Oral Squamous Cell Carcinoma

Ayala, F. R. R., Rocha, R. M., Carvalho, K. C., Carvalho, A. L., da Cunha, I. W., Lourenço, S. V., & Soares, F. A. (2010) · Molecules · doi:10.3390/molecules15042374 · Cited by 165 · see citing works

Retinol and ascorbate drive erasure of epigenetic memory and enhance reprogramming to naïve pluripotency by complementary mechanisms

Hore, T. A., von Meyenn, F., Ravichandran, M., Bachman, M., Ficz, G., Oxley, D., Santos, F., Balasubramanian, S., Jurkowski, T. P., & Reik, W. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1608679113 · Cited by 164 · see citing works

Regulation of the osteoblast‐specific transcription factor Osterix by NO66, a Jumonji family histone demethylase

Sinha, K. M., Yasuda, H., Coombes, M. M., Dent, S., & Crombrugghe, B. D. (2009) · The EMBO Journal · doi:10.1038/emboj.2009.332 · Cited by 160 · see citing works

Inhibition of succinate dehydrogenase dysregulates histone modification in mammalian cells

Cervera, A. M., Bayley, J.-P., Devilee, P., & McCreath, K. J. (2009) · Molecular Cancer · doi:10.1186/1476-4598-8-89 · Cited by 156 · see citing works

Oxygenase-catalyzed ribosome hydroxylation occurs in prokaryotes and humans

Ge, W., Wolf, A., Feng, T., Ho, C.-H., Sekirnik, R., Zayer, A., Granatino, N., Cockman, M. E., Loenarz, C., Loik, N. D., et al. (2012) · Nature Chemical Biology · doi:10.1038/nchembio.1093 · Cited by 154 · see citing works

Duodenal Cytochrome b (DCYTB) in Iron Metabolism: An Update on Function and Regulation

Lane, D. J. R., Bae, D.-H., Merlot, A. M., Sahni, S., & Richardson, D. R. (2015) · Nutrients · doi:10.3390/nu7042274 · Cited by 153 · see citing works

Recognition of Histone H3K4 Trimethylation by the Plant Homeodomain of PHF2 Modulates Histone Demethylation

Wen, H., Li, J., Song, T., Lu, M., Kan, P., Lee, M. G., Sha, B., & Shi, X. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.c109.097667 · Cited by 153 · see citing works

Tumor suppressor gene identification using retroviral insertional mutagenesis in Blm‐deficient mice

Suzuki, T., Minehata, K., Akagi, K., Jenkins, N. A., & Copeland, N. G. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601215 · Cited by 148 · see citing works

Low values of 5‐hydroxymethylcytosine (5hmC), the “sixth base,” are associated with anaplasia in human brain tumors

Kraus, T. F. J., Globisch, D., Wagner, M., Eigenbrod, S., Widmann, D., Münzel, M., Müller, M., Pfaffeneder, T., Hackner, B., Feiden, W., et al. (2012) · International Journal of Cancer · doi:10.1002/ijc.27429 · Cited by 146 · see citing works

Lysyl 5-Hydroxylation, a Novel Histone Modification, by Jumonji Domain Containing 6 (JMJD6)*

Unoki, M., Masuda, A., Dohmae, N., Arita, K., Yoshimatsu, M., Iwai, Y., Fukui, Y., Ueda, K., Hamamoto, R., Shirakawa, M., et al. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.433284 · Cited by 140 · see citing works

Intestinal Dehydroascorbic Acid (DHA) Transport Mediated by the Facilitative Sugar Transporters, GLUT2 and GLUT8

Corpe, C. P., Eck, P., Wang, J., Al‐Hasani, H., & Levine, M. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.436790 · Cited by 140 · see citing works

Breathing-in epigenetic change with vitamin C

Monfort, A., & Wutz, A. (2013) · The EMBO Reports · doi:10.1038/embor.2013.29 · Cited by 140 · see citing works

Glucose Modulates Vitamin C Transport in Adult Human Small Intestinal Brush Border Membrane Vesicles

Malo, C., & Wilson, J. X. (2000) · Journal of Nutrition · doi:10.1093/jn/130.1.63 · Cited by 135 · see citing works

Biochemical indices of human vitamin C status

Jacob, R. A., Skala, J. H., & Omaye, S. T. (1987) · American Journal of Clinical Nutrition · doi:10.1093/ajcn/46.5.818 · Cited by 130 · see citing works

Is There a Role for Oral or Intravenous Ascorbate (Vitamin C) in Treating Patients With Cancer? A Systematic Review

Jacobs, C. M., Hutton, B., Ng, T. L., Shorr, R., & Clemons, M. J. (2015) · The Oncologist · doi:10.1634/theoncologist.2014-0381 · Cited by 114 · see citing works

Severe hypovitaminosis C in lung-cancer patients: the utilization of vitamin C in surgical repair and lymphocyte-related host resistance

Anthony, H. M., & Schorah, C. J. (1982) · British Journal of Cancer · doi:10.1038/bjc.1982.211 · Cited by 112 · see citing works

Genetic variation at the SLC23A1 locus is associated with circulating concentrations of l-ascorbic acid (vitamin C): evidence from 5 independent studies with &gt;15,000 participants

Timpson, N. J., Forouhi, N. G., Brion, M.-J., Harbord, R. M., Cook, D. G., Johnson, P., McConnachie, A., Morris, R. W., Rodriguez, S., Luan, J., et al. (2010) · The American Journal of Clinical Nutrition · doi:10.3945/ajcn.2010.29438 · Cited by 107 · see citing works

Molecular functions of human endogenous retroviruses in health and disease

Suntsova, M., Garazha, A., Ivanova, A., Kaminsky, D., Zhavoronkov, A. A., & Buzdin, A. A. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-1947-6 · Cited by 99 · see citing works

Lung cancer-associated JmjC domain protein mdig suppresses formation of tri-methyl lysine 9 of histone H3

Lu, Y., Beezhold, K., Chang, Q., Zhang, Y., Rojanasakul, Y., Zhao, H., Castranova, V., Shi, X., & Chen, F. (2009) · Cell Cycle · doi:10.4161/cc.8.13.8927 · Cited by 94 · see citing works

Exploring the emerging complexity in transcriptional regulation of energy homeostasis

Lempradl, A. M., Pospisilik, J. A., & Penninger, J. M. (2015) · Nature Reviews Genetics · doi:10.1038/nrg3941 · Cited by 94 · see citing works

Vitamin C-induced epigenomic remodelling in IDH1 mutant acute myeloid leukaemia

Mingay, M., Chaturvedi, A., Bilenky, M., Cao, Q., Jackson, L., Hui, T., Moksa, M., Heravi-Moussavi, A., Humphries, R. K., Heuser, M., et al. (2018) · Leukemia · doi:10.1038/leu.2017.171 · Cited by 94 · see citing works

PHF8 is a histone H3K9me2 demethylase regulating rRNA synthesis

Zhu, Z., Wang, Y., Li, X., Wang, Y., Xu, L., Wang, X., Sun, T., Dong, X., Chen, L., Mao, H., et al. (2010) · Cell Research · doi:10.1038/cr.2010.75 · Cited by 92 · see citing works

Glutathione, ascorbic acid and antioxidant enzymes in the tumor tissue and blood of patients with oral squamous cell carcinoma.

Fiaschi, A. I., Cozzolino, A., Ruggiero, G., & Giorgi, G. (2005) · PubMed · Cited by 87 · see citing works

Molecular Mechanisms and Regulation of Iron Transport

Chung, J., & Wessling‐Resnick, M. (2003) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/713609332 · Cited by 85 · see citing works

Ascorbate-induced generation of 5-hydroxymethylcytosine is unaffected by varying levels of iron and 2-oxoglutarate

Dickson, K. M., Gustafson, C. B., Young, J. I., Zuchner, S. L., & Wang, G. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.09.010 · Cited by 81 · see citing works

Polymorphisms in the Estrogen Receptor 1 and Vitamin C and Matrix Metalloproteinase Gene Families Are Associated with Susceptibility to Lymphoma

Skibola, C. F., Bracci, P. M., Halperin, E., Nieters, A., Hubbard, A., Paynter, R. A., Skibola, D. R., Agana, L., Becker, N., Tressler, P., et al. (2008) · PLoS ONE · doi:10.1371/journal.pone.0002816 · Cited by 80 · see citing works

Protein Complex Interactor Analysis and Differential Activity of KDM3 Subfamily Members Towards H3K9 Methylation

Brauchle, M., Yao, Z., Arora, R., Thigale, S., Clay, I., Inverardi, B., Fletcher, J., Taslimi, P., Acker, M. G., Gerrits, B., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0060549 · Cited by 79 · see citing works

JMJD5, a Jumonji C (JmjC) Domain-containing Protein, Negatively Regulates Osteoclastogenesis by Facilitating NFATc1 Protein Degradation

Youn, M., Yokoyama, A., Fujiyama, S., Ohtake, F., Minehata, K., Yasuda, H., Suzuki, T., Kato, S., & Imai, Y. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.323105 · Cited by 70 · see citing works

DNA methylation and hydroxymethylation in hematologic differentiation and transformation

Ko, M., An, J., & Rao, A. (2015) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2015.10.009 · Cited by 70 · see citing works

Vitamin C induces specific demethylation of H3K9me2 in mouse embryonic stem cells via Kdm3a/b

Ebata, K. T., Mesh, K., Liu, S., Bilenky, M., Fekete, A., Acker, M. G., Hirst, M., Garcia, B. A., & Ramalho‐Santos, M. (2017) · Epigenetics & Chromatin · doi:10.1186/s13072-017-0143-3 · Cited by 70 · see citing works

Cancer: a collagen disease, secondary to a nutritional deficiency.

McCORMICK, W. J. (1959) · PubMed · Cited by 68 · see citing works

Inhibition of chemically induced morphological transformation and reversion of the transformed phenotype of ascorbic acid in C3H/10T 1/2 cells.

Benedict, W. F., Wheatley, W. L., & Jones, P. A. (1980) · PubMed · Cited by 67 · see citing works

Increased facilitated transport of dehydroascorbic acid without changes in sodium-dependent ascorbate transport in human melanoma cells.

Spielholz, C., Golde, D. W., Houghton, A. N., Nualart, F., & Vera, J. C. (1997) · PubMed · Cited by 67 · see citing works

Azacitidine: A Review in Myelodysplastic Syndromes and Acute Myeloid Leukaemia

Scott, L. J. (2016) · Drugs · doi:10.1007/s40265-016-0585-0 · Cited by 66 · see citing works

Differential expression of facilitative glucose transporters in normal and tumour kidney tissues

Suganuma, N., Segade, F., Matsuzu, K., & Bowden, D. W. (2007) · British Journal of Urology · doi:10.1111/j.1464-410x.2007.06765.x · Cited by 63 · see citing works

Serum antioxidative vitamin levels and lipid peroxidation in gastric carcinoma patients

Choi, M., Kim, B.-S., & Yu, R. (1999) · Cancer Letters · doi:10.1016/s0304-3835(98)00312-7 · Cited by 62 · see citing works

Genetic variation in sodium-dependent ascorbic acid transporters and risk of gastric cancer in Poland

Wright, M. E., Andreotti, G., Lissowska, J., Yeager, M., Zatonski, W., Chanock, S. J., Chow, W.-H., & Hou, L. (2009) · European Journal of Cancer · doi:10.1016/j.ejca.2009.01.027 · Cited by 62 · see citing works

Identification of non-histone substrates for JMJD2A–C histone demethylases

Ponnaluri, V. K. C., Vavilala, D. T., Putty, S., Gutheil, W. G., & Mukherji, M. (2009) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2009.09.107 · Cited by 57 · see citing works

Hyperpolarized [1-13C]Dehydroascorbate MR Spectroscopy in a Murine Model of Prostate Cancer: Comparison with 18F-FDG PET

Keshari, K. R., Sai, V., Wang, Z. J., VanBrocklin, H. F., Kurhanewicz, J. V., & Wilson, D. M. (2013) · Journal of Nuclear Medicine · doi:10.2967/jnumed.112.115402 · Cited by 57 · see citing works

The 2‐Oxoglutarate‐Dependent Oxygenase JMJD6 Catalyses Oxidation of Lysine Residues to give 5S‐Hydroxylysine Residues

Mantri, M., Loik, N. D., Hamed, R. B., Claridge, T. D. W., McCullagh, J., & Schofield, C. J. (2011) · ChemBioChem · doi:10.1002/cbic.201000641 · Cited by 55 · see citing works

Vitamin C enhances the expression of IL17 in a Jmjd2-dependent manner

Song, M. H., Nair, V. S., & Oh, K. I. (2017) · BMB Reports · doi:10.5483/bmbrep.2017.50.1.193 · Cited by 55 · see citing works

Folate Deficiency and Plasma Homocysteine during Increased Oxidative Stress

Rogers, E. J., Chen, S., & Chan, A. (2007) · New England Journal of Medicine · doi:10.1056/nejmc066569 · Cited by 49 · see citing works

Serial Profile of Vitamins and Trace Elements during the Acute Phase of Allogeneic Stem Cell Transplantation

Nannya, Y., Shinohara, A., Ichikawa, M., & Kurokawa, M. (2013) · Transplantation and Cellular Therapy · doi:10.1016/j.bbmt.2013.12.554 · Cited by 40 · see citing works

Crystal structure of the PHF8 Jumonji domain, an Nε‐methyl lysine demethylase

Yue, W. W., Hozjan, V., Ge, W., Loenarz, C., Cooper, C. D. O., Schofield, C. J., Kavanagh, K. L., Oppermann, U. C. T., & McDonough, M. A. (2010) · FEBS Letters · doi:10.1016/j.febslet.2009.12.055 · Cited by 37 · see citing works

Hydroxymethylcytosine and demethylation of theγ-globingene promoter during erythroid differentiation

Ruiz, M. A., Rivers, A. E., Ibañez, V., Vaitkus, K., Mahmud, N., DeSimone, J., & Lavelle, D. (2015) · Epigenetics · doi:10.1080/15592294.2015.1039220 · Cited by 27 · see citing works

Effect of ascorbic acid on the resistance of the extracellular matrix to hydrolysis by tumor cells.

DeClerck, Y. A., & Jones, P. A. (1980) · PubMed · Cited by 15 · see citing works

Effect of ascorbic acid on the resistance of the extracellular matrix to hydrolysis by tumor cells

Bingham, H. G. (1981) · Plastic & Reconstructive Surgery · doi:10.1097/00006534-198103000-00131 · Cited by 7 · see citing works

Targeting cancer vulnerabilities with high-dose vitamin C

Ngo, B., Van Riper, J. M., Cantley, L. C., & Yun, J. (2019) · Nature Reviews Cancer · doi:10.1038/s41568-019-0135-7 · Cited by 423 · see citing works

Biomarkers of Nutrition and Health: New Tools for New Approaches

Picó, C., Serra, F., Rodríguez, A. M., Keijer, J., & Palou, A. (2019) · Nutrients · doi:10.3390/nu11051092 · Cited by 287 · see citing works

Recent trends in cancer therapy: A review on the current state of gene delivery

Yahya, E. B., & Alqadhi, A. M. (2021) · Life Sciences · doi:10.1016/j.lfs.2021.119087 · Cited by 240 · see citing works

Vitamin C and immune cell function in inflammation and cancer

Ang, A., Pullar, J. M., Currie, M. J., & Vissers, M. C. M. (2018) · Biochemical Society Transactions · doi:10.1042/bst20180169 · Cited by 191 · see citing works

Potential Mechanisms of Action for Vitamin C in Cancer: Reviewing the Evidence

Vissers, M. C. M., & Das, A. B. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00809 · Cited by 188 · see citing works

Intravenous Vitamin C for Cancer Therapy – Identifying the Current Gaps in Our Knowledge

Carr, A. C., & Cook, J. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.01182 · Cited by 133 · see citing works

Discrepancies in global vitamin C recommendations: a review of RDA criteria and underlying health perspectives

Carr, A. C., & Lykkesfeldt, J. (2020) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2020.1744513 · Cited by 127 · see citing works

Vitamin C as a Modulator of the Response to Cancer Therapy

Błaszczak, W., Barczak, W., Masternak, J., Kopczyński, P., Zhitkovich, A., & Rubiś, B. (2019) · Molecules · doi:10.3390/molecules24030453 · Cited by 104 · see citing works

TET family dioxygenases and the TET activator vitamin C in immune responses and cancer

Yue, X., & Rao, A. (2020) · Blood · doi:10.1182/blood.2019004158 · Cited by 105 · see citing works

The Burden of Cancer, Government Strategic Policies, and Challenges in Pakistan: A Comprehensive Review

Ali, A., Manzoor, M. F., Aḥmad, N., Aadil, R. M., Qin, H., Siddique, R., Riaz, S., Ahmad, A., Korma, S. A., Khalid, W., et al. (2022) · Frontiers in Nutrition · doi:10.3389/fnut.2022.940514 · Cited by 123 · see citing works

Protection and controlled release of vitamin C by different micro/nanocarriers

Comunian, T. A., Babazadeh, A., Rehman, A., Shaddel, R., Akbari‐Alavijeh, S., Boostani, S., & Jafari, S. M. (2020) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2020.1865258 · Cited by 100 · see citing works

Oral vitamin C supplementation to patients with myeloid cancer on azacitidine treatment: Normalization of plasma vitamin C induces epigenetic changes

Gillberg, L., Ørskov, A. D., Nasif, A., Ohtani, H., Madaj, Z., Hansen, J. W., Rapin, N., Mogensen, J. B., Liu, M., Dufva, I. H., et al. (2019) · Clinical Epigenetics · doi:10.1186/s13148-019-0739-5 · Cited by 89 · see citing works

Novel Strategies for Cancer Treatment: Highlights from the 55th IACR Annual Conference

Charmsaz, S., Collins, D. M., Perry, A. S., & Prencipe, M. (2019) · Cancers · doi:10.3390/cancers11081125 · Cited by 77 · see citing works

The potential role of vitamin C in empowering cancer immunotherapy

Bedhiafi, T., Inchakalody, V. P., Fernandes, Q., Mestiri, S., Billa, N., Shahab Uddin, M. S., Merhi, M., & Dermime, S. (2021) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2021.112553 · Cited by 77 · see citing works

Maize bHLH55 functions positively in salt tolerance through modulation of AsA biosynthesis by directly regulating GDP-mannose pathway genes

Yu, C., Yan, M., Dong, H., Luo, J., Ke, Y., Guo, A., Chen, Y., Zhang, J., & Huang, X. (2020) · Plant Science · doi:10.1016/j.plantsci.2020.110676 · Cited by 65 · see citing works

Vitamin C and the Immune System

Jafari, D., Esmaeilzadeh, A., Mohammadi-Kordkhayli, M., & Rezaei, N. (2019) · Springer eBooks · doi:10.1007/978-3-030-16073-9_5 · Cited by 62 · see citing works

The role of vitamin C in epigenetic cancer therapy

Mikkelsen, S. U., Gillberg, L., Lykkesfeldt, J., & Grønbæk, K. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.03.017 · Cited by 61 · see citing works

Context dependent effects of ascorbic acid treatment in TET2 mutant myeloid neoplasia

Guan, Y., Greenberg, E. F., Hasipek, M., Shi, C., Liu, X., Kerr, C. M., Gackowski, D., Zarakowska, E., Radivoyevitch, T., Gu, X., et al. (2020) · Communications Biology · doi:10.1038/s42003-020-01220-9 · Cited by 57 · see citing works

The Epigenetic Role of Vitamin C in Neurodevelopment

Coker, S. J., Smith-Díaz, C. C., Dyson, R. M., Vissers, M. C. M., & Berry, M. J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031208 · Cited by 56 · see citing works

High-Dose Vitamin C: Preclinical Evidence for Tailoring Treatment in Cancer Patients

Giansanti, M., Karimi, T., Faraoni, I., & Graziani, G. (2021) · Cancers · doi:10.3390/cancers13061428 · Cited by 50 · see citing works

Combination Therapy with Vitamin C Could Eradicate Cancer Stem Cells

Satheesh, N. J., Samuel, S. M., & Büsselberg, D. (2020) · Biomolecules · doi:10.3390/biom10010079 · Cited by 48 · see citing works

Prognostic Ability of Enhancer RNAs in Metastasis of Non-Small Cell Lung Cancer

Liu, J., Jia, J., Wang, S., Zhang, J., Xian, S., Zheng, Z., Deng, L., Deng, L., Zhang, Y., & Zhang, Y. (2022) · Molecules · doi:10.3390/molecules27134108 · Cited by 46 · see citing works

Ascorbic Acid Chemosensitizes Colorectal Cancer Cells and Synergistically Inhibits Tumor Growth

Pires, A. S., Marques, C. R., Encarnação, J. C., Abrantes, A. M., Marques, I. A., Laranjo, M., Oliveira, R. C., Casalta‐Lopes, J., Gonçalves, A. C., Sarmento‐Ribeiro, A. B., et al. (2018) · Frontiers in Physiology · doi:10.3389/fphys.2018.00911 · Cited by 45 · see citing works

Mechanisms and Applications of the Anti-cancer Effect of Pharmacological Ascorbic Acid in Cervical Cancer Cells

Wu, T.-M., Liu, S., Chen, S.-Y., Chen, G., Wu, C., & Huang, S. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.01483 · Cited by 43 · see citing works

Cracking the Code of Oocyte Quality: The Oxidative Stress Link to IVF Success

Voros, C., Athanasiou, D., Papapanagiotou, I., Mavrogianni, D., Varthaliti, A., Bananis, K., Athanasiou, A. I., Athanasiou, A. V., Papadimas, G. K., Gkirgkinoudis, A., et al. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26136377 · Cited by 38 · see citing works

Pharmacoepigenetic Processors: Epigenetic Drugs, Drug Resistance, Toxicoepigenetics, and Nutriepigenetics

Cacabelos, R., Carril, J. C., Sanmartín, A., & Cacabelos, P. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-813939-4.00006-1 · Cited by 35 · see citing works

Enhanced Anticancer Effect of Adding Magnesium to Vitamin C Therapy: Inhibition of Hormetic Response by SVCT-2 Activation

Cho, S., Chae, J. S., Shin, H. C., Shin, Y., Kim, Y.-W., Kil, E., Byun, H., Cho, S.-H., Park, S., Lee, S., et al. (2019) · Translational Oncology · doi:10.1016/j.tranon.2019.10.017 · Cited by 32 · see citing works

Cell signaling pathways based on vitamin C and their application in cancer therapy

Fan, D., Liu, X., Shen, Z., Wu, P., Zhong, L., & Lin, F. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.114695 · Cited by 30 · see citing works

Rinsing with L-Ascorbic Acid Exhibits Concentration-Dependent Effects on Human Gingival Fibroblast In Vitro Wound Healing Behavior

Chaitrakoonthong, T., Ampornaramveth, R. S., & Kamolratanakul, P. (2020) · International Journal of Dentistry · doi:10.1155/2020/4706418 · Cited by 30 · see citing works

Methylomic Signatures of High Grade Serous Ovarian Cancer

Cárdenas, H., Fang, F., Jiang, G., Perkins, S. M., Zhang, C., Emerson, R. E., Hutchins, G., Keer, H. N., Liu, Y., Matei, D. E., et al. (2020) · Epigenetics · doi:10.1080/15592294.2020.1853402 · Cited by 29 · see citing works

Metabolo-epigenetic interplay provides targeted nutritional interventions in chronic diseases and ageing

de Cedrón, M. G., Palomares, R. M., & de Molina, A. R. (2023) · Frontiers in Oncology · doi:10.3389/fonc.2023.1169168 · Cited by 31 · see citing works

Vitamin C: A stem cell promoter in cancer metastasis and immunotherapy

Fu, J., Wu, Z., Liu, J., & Wu, T. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110588 · Cited by 28 · see citing works

An integrated spectroscopic strategy to trace the geographical origins of emblic medicines: Application for the quality assessment of natural medicines

Qi, L., Zhong, F., Chen, Y., Mao, S., Yan, Z., & Ma, Y. (2020) · Journal of Pharmaceutical Analysis · doi:10.1016/j.jpha.2019.12.004 · Cited by 26 · see citing works

Vitamin C Suppresses Pancreatic Carcinogenesis through the Inhibition of Both Glucose Metabolism and Wnt Signaling

Kim, J. H., Hwang, S., Lee, J., Im, S. S., & Son, J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232012249 · Cited by 26 · see citing works

Emerging epigenetic therapeutics for myeloid leukemia: modulating demethylase activity with ascorbate

Das, A. B., Smith-Díaz, C. C., & Vissers, M. C. M. (2020) · Haematologica · doi:10.3324/haematol.2020.259283 · Cited by 25 · see citing works

Functional benefit and molecular mechanism of vitamin C against perfluorooctanesulfonate-associated leukemia

Li, R., Guo, C., Yu, H., Xiao, L., & Su, M. (2020) · Chemosphere · doi:10.1016/j.chemosphere.2020.128242 · Cited by 24 · see citing works

Multiple vitamin co-exposure and mortality risk: A prospective study

Cui, Y., Zhou, H., Wei, M., Song, W., Di, D., Zhang, R., Wei, S., Liu, J., & Wang, Q. (2021) · Clinical Nutrition · doi:10.1016/j.clnu.2021.12.010 · Cited by 24 · see citing works

Vitamin C supplementation expands the therapeutic window of BETi for triple negative breast cancer

Mustafi, S., Camarena, V., Qureshi, R., Yoon, H., Volmar, C., Huff, T. C., Sant, D., Zheng, L., Brothers, S. P., Wahlestedt, C., et al. (2019) · EBioMedicine · doi:10.1016/j.ebiom.2019.04.006 · Cited by 24 · see citing works

Vitamin C Inhibits Metastasis of Peritoneal Tumors By Preventing Spheroid Formation in ID8 Murine Epithelial Peritoneal Cancer Model

Xu, Y., Guo, X., Wang, G., & Zhou, C. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.00645 · Cited by 23 · see citing works

Loss of 5-Hydroxymethylcytosine Is an Epigenetic Biomarker in Cutaneous T-Cell Lymphoma

Qiu, L., Liu, F., Yi, S., Li, X., Liu, X., Xiao, C., Lian, C. G., Tu, P., & Wang, Y. (2018) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2018.05.007 · Cited by 23 · see citing works

Epigenetic Regulators of DNA Cytosine Modification: Promising Targets for Cancer Therapy

Jung, I., An, J., & Ko, M. (2023) · Biomedicines · doi:10.3390/biomedicines11030654 · Cited by 22 · see citing works

Molecular mechanism for vitamin C-derived C5-glyceryl-methylcytosine DNA modification catalyzed by algal TET homologue CMD1

Li, W., Zhang, T., Sun, M., Shi, Y., Zhang, X., Xu, G., & Ding, J. (2021) · Nature Communications · doi:10.1038/s41467-021-21061-2 · Cited by 21 · see citing works

Micronutrients and Breast Cancer Progression: A Systematic Review

Cuenca-Micó, O., & Aceves, C. (2020) · Nutrients · doi:10.3390/nu12123613 · Cited by 20 · see citing works

Impact of Diets on Response to Immune Checkpoint Inhibitors (ICIs) Therapy against Tumors

Zhang, X., Li, H., Lv, X., Hu, L., Li, W., Zi, M., & He, Y. (2022) · Life · doi:10.3390/life12030409 · Cited by 18 · see citing works

Nutrientes e compostos bioativos na modulação epigenética associada à prevenção e combate ao câncer

Fernandes, D. P., Coutinho, V. E. A., Medeiros, L. D. B., & Pereira, N. L. V. (2020) · Mudra Jurnal Seni Budaya · doi:10.31091/mudra.v40i3.2914 · Cited by 19 · see citing works

Ascorbate is a multifunctional micronutrient whose synthesis is lacking in primates

Fujii, J. (2021) · Journal of Clinical Biochemistry and Nutrition · doi:10.3164/jcbn.20-181 · Cited by 19 · see citing works

Exploring the Role of Metabolites in Cancer and the Associated Nerve Crosstalk

Gu, I., Gregory, E., Atwood, C., Lee, S., & Song, Y. H. (2022) · Nutrients · doi:10.3390/nu14091722 · Cited by 20 · see citing works

Vitamin C Deficiency in Patients With Acute Myeloid Leukemia

Ottone, T., Faraoni, I., Fucci, G., Divona, M., Travaglini, S., Bellis, E. D., Marchesi, F., Angelini, D. F., Palmieri, R., Gurnari, C., et al. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.890344 · Cited by 20 · see citing works

VITAMINA C EN LA SALUD Y EN LA ENFERMEDAD

Velarde, E. R. C. (2019) · Revista de la Facultad de Medicina Humana · doi:10.25176/rfmh.v19i4.2351 · Cited by 19 · see citing works

Vitamin C and epigenetics: A short physiological overview

Pavlović, V., Ćirić, M., Petković, M., & Golubović, M. (2023) · Open Medicine · doi:10.1515/med-2023-0688 · Cited by 18 · see citing works

The Anti-Leukemia Effect of Ascorbic Acid: From the Pro-Oxidant Potential to the Epigenetic Role in Acute Myeloid Leukemia

Travaglini, S., Gurnari, C., Antonelli, S., Silvestrini, G., Noguera, N. I., Ottone, T., & Voso, M. T. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.930205 · Cited by 17 · see citing works

Application of Electrolyzed Water in Fruits and Vegetables Industry

Hao, J., & Wang, Q. (2019) · Springer eBooks · doi:10.1007/978-981-13-3807-6_4 · Cited by 16 · see citing works

IDENTIFICATION OF ASCORBIC ACID CONTENT IN Carica papaya L. USING IODIMETRY AND UV-VIS SPECTROPHOTOMETRY

Riscahyani, N. M., Ekawati, E. R., & Ngibad, K. (2019) · INDONESIAN JOURNAL OF MEDICAL LABORATORY SCIENCE AND TECHNOLOGY · doi:10.33086/ijmlst.v1i2.1291 · Cited by 14 · see citing works

Labile iron affects pharmacological ascorbate-induced toxicity in osteosarcoma cell lines

Zhou, L., Zhang, L., Wang, S., Zhao, B., Lv, H., & Shang, P. (2020) · Free Radical Research · doi:10.1080/10715762.2020.1744577 · Cited by 14 · see citing works

The dual role of vitamin C in cancer: from antioxidant prevention to prooxidant therapeutic applications

Cao, X., Yi, Y., Ji, M., Liu, Y., Wang, D., & Zhu, H. (2025) · Frontiers in Medicine · doi:10.3389/fmed.2025.1633447 · Cited by 13 · see citing works

Empowering γδ T‐cell functionality with vitamin C

Kabelitz, D., Cierna, L., Juraske, C., Zarobkiewicz, M. K., Schamel, W. W. A., & Peters, C. (2024) · European Journal of Immunology · doi:10.1002/eji.202451028 · Cited by 12 · see citing works

Immunotherapy With Human Gamma Delta T Cells—Synergistic Potential of Epigenetic Drugs?

Bhat, J., Kouakanou, L., Peters, C., Yin, Z., & Kabelitz, D. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.00512 · Cited by 11 · see citing works

Poly(ADP-Ribose) Polymerase Inhibitors for Arsenic Trioxide–Resistant Acute Promyelocytic Leukemia: Synergistic In Vitro Antitumor Effects with Hypomethylating Agents or High-Dose Vitamin C

Giansanti, M., Gabrieli, A. D., Prete, S. P., Ottone, T., Divona, M. D., Karimi, T., Ciccarone, F., Voso, M. T., Graziani, G., & Faraoni, I. (2021) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.121.000537 · Cited by 11 · see citing works

Metabolic Classification and Intervention Opportunities for Tumor Energy Dysfunction

Monferrer, E., Vieco-Martí, I., López-Carrasco, A., Fariñas, F., Abanades, S., de la Cruz‐Merino, L., Noguera, R., & Naranjo, T. Á. (2021) · Metabolites · doi:10.3390/metabo11050264 · Cited by 11 · see citing works

Exploring the Ascorbate Requirement of the 2-Oxoglutarate-Dependent Dioxygenases

Smith-Díaz, C. C., Das, A. B., Jurkowski, T. P., Hore, T. A., & Vissers, M. C. M. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c02342 · Cited by 10 · see citing works

Nano-engineered vitamins as a potential epigenetic modifier against environmental air pollutants

Ratre, P., Chauhan, P., Bhargava, A., Tiwari, R. R., Thareja, S., Srivastava, R. K., & Mishra, P. K. (2022) · Reviews on Environmental Health · doi:10.1515/reveh-2022-0027 · Cited by 9 · see citing works

The role of nutrition in harnessing the immune system: a potential approach to prevent cancer

Xiaogang, H., Sharma, M., Saif, I., Ali, G., Li, X., & Salama, E. (2022) · Medical Oncology · doi:10.1007/s12032-022-01850-5 · Cited by 11 · see citing works

PHLPP2 is a novel biomarker and epigenetic target for the treatment of vitamin C in pancreatic cancer

Chen, L., Song, H., Luo, Z., Cui, H., Zheng, W., Liu, Y., Li, W., Luo, F., & Liu, J. (2020) · International Journal of Oncology · doi:10.3892/ijo.2020.5001 · Cited by 9 · see citing works

Oxidative Stress and Mitochondrial Dysfunction in Myelodysplastic Syndrome: Roles in Development, Diagnosis, Prognosis, and Treatment

Pierro, F., Fazio, M., Murdaca, G., Stagno, F., Gangemi, S., & Allegra, A. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26136415 · Cited by 8 · see citing works

Redox Signaling Modulates Activity of Immune Checkpoint Inhibitors in Cancer Patients

Allegra, A., Murdaca, G., Mirabile, G., & Gangemi, S. (2023) · Biomedicines · doi:10.3390/biomedicines11051325 · Cited by 8 · see citing works

An overview of vitamins as epidrugs for colorectal cancer prevention

Boughanem, H., Kompella, P., Tinahones, F. J., & Macías‐González, M. (2022) · Nutrition Reviews · doi:10.1093/nutrit/nuac065 · Cited by 8 · see citing works

Introduction: Epigenetics in cancer

Rosenquist, R., Esteller, M., & Plass, C. (2018) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2018.07.002 · Cited by 8 · see citing works

Impact of polymorphisms within genes involved in regulating DNA methylation in patients with metastatic colorectal cancer enrolled in three independent, randomised, open-label clinical trials: a meta-analysis from TRIBE, MAVERICC and FIRE-3

Puccini, A., Loupakis, F., Stintzing, S., Cao, S., Battaglin, F., Tokunaga, R., Naseem, M., Berger, M. D., Soni, S., Zhang, W., et al. (2019) · European Journal of Cancer · doi:10.1016/j.ejca.2019.01.105 · Cited by 7 · see citing works

The Potential Role of Epigenetics in Aquaculture

Wang, H., & Shen, Z. (2023) · Wiley eBooks · doi:10.1002/9781119821946.ch1 · Cited by 7 · see citing works

Vitamin C enhances co-localization of novel TET1 nuclear bodies with both Cajal and PML bodies in colorectal cancer cells

Osmani, N. E., Prévostel, C., Lasorsa, L., El-Harakeh, M., Radwan, Z., Mawlawi, H., El-Sabban, M. E., Shirinian, M., & Dassouki, Z. (2024) · Epigenetics · doi:10.1080/15592294.2024.2337142 · Cited by 6 · see citing works

Vitamin C Inhibits Lipopolysaccharide-Induced Hyperinflammatory State of Chronic Myeloid Leukemia Cells through Purinergic Signaling and Autophagy

Pires, D. A., Brandão-Rangel, M. A. R., Silva-Reis, A., Olimpio, F. R. D. S., Aimbire, F., Oliveira, C. R., da Silva, J. R. M., Zamarioli, L. D. S., Bachi, A. L. L., Bella, Y. F., et al. (2024) · Nutrients · doi:10.3390/nu16030383 · Cited by 6 · see citing works

Efecto nefroprotector del Camu Camu (Myrciaria dubia) en un modelo de nefrotoxicidad inducida por gentamicina en ratas

Katherine Becerra, B., Josh García, D., Becerra-Bravo, M. A., Ruiz-Ramírez, E., & Lesly Chávez, R. (2019) · Revista chilena de nutrición · doi:10.4067/s0717-75182019000300303 · Cited by 6 · see citing works

Are the oxidative stress levels in the tumor center and tumor boundary different from those in healthy tissue?

Doğan, R., Güler, E. M., Koçyiğit, A., Çelik, İ., Şentürk, E., Yenigün, A., Tuğrul, S., & Özturan, O. (2021) · European Archives of Oto-Rhino-Laryngology · doi:10.1007/s00405-021-06749-x · Cited by 6 · see citing works

Types of Cancers, Epidemiology, and Molecular Insights

Sobti, R. C., Gosipatala, S. B., Sharma, M., Reddy, P., Khalko, R. K., Kaur, T., & Thakur, M. (2023) · Springer eBooks · doi:10.1007/978-981-99-2196-6_1-1 · Cited by 5 · see citing works

Beyond genetics: integrative oncology and the metabolic perspective on cancer treatment

Nair, P. M. K., Silwal, K., Ramalakshmi, R., Devibala, M., Saranya, M., Sivaranjani, S., Ramasamy, T., Palanisamy, A., & Mahalingam, M. (2024) · Frontiers in Oncology · doi:10.3389/fonc.2024.1455022 · Cited by 5 · see citing works

Association of Leukemia Target Genes Tet2, Bcl2, and Slc23a2 in Vitamin C Pathways

Li, J., Zhang, W., Liu, W., RONG, J., Chen, Y., Gu, W., & Zhang, W. (2019) · Cancer Genomics & Proteomics · doi:10.21873/cgp.20138 · Cited by 5 · see citing works

A Study on the Effect of Vitamins A and C to Modulate the Expression of NKG2D Ligands in Hepatic and Colon Cancer Cells

Zamzami, M. A., Nasrullah, M., Choudhry, H., & Khan, M. I. (2020) · Nutrition and Cancer · doi:10.1080/01635581.2020.1860240 · Cited by 5 · see citing works

Optimization of the Process for Production of Enriched Ketchup

Basika, E., Kigozi, J. B., & Tumuhimbise, G. (2021) · Journal of Food Studies · doi:10.5296/jfs.v10i1.18567 · Cited by 4 · see citing works

Introduction to cancer biology and current research trends

Tyagi, L., Kumar, U., Simran, S., Mishra, S., Singh, H., Rathi, G., & Parashar, D. (2025) · Methods in cell biology · doi:10.1016/bs.mcb.2025.05.003 · Cited by 3 · see citing works

Vitamin C’s essential role in DNA and histone demethylation and a preclinical rationale for its therapeutic high-dose potential in renal cell carcinoma

Huang, C.-H., & Chang, C. (2019) · Annals of Translational Medicine · doi:10.21037/atm.2019.05.49 · Cited by 3 · see citing works

Lifestyle and preventive medical epigenetics

Sanusi, K. O., Uthman, Y. A., Ooi, D. J., Ismail, M., & Imam, M. U. (2021) · Elsevier eBooks · doi:10.1016/b978-0-12-823928-5.00024-4 · Cited by 3 · see citing works

A Luminescence Resonance Energy Transfer (LRET)‐Based Nanoprobe for Ascorbic Acid Detection in Living Cells and Real Samples

Pan, S., Hong, Y., Jian, Y., Shen, P., Lu, X., Chen, Y., Lin, Y., Zha, S., Jiang, L., & Fang, X. (2025) · Chemistry - An Asian Journal · doi:10.1002/asia.202500124 · Cited by 2 · see citing works

Epigenetics of Metabolic Diseases

Gillberg, L., & Hjort, L. (2022) · Elsevier eBooks · doi:10.1016/b978-0-323-91909-8.00026-8 · Cited by 2 · see citing works

The Protective Effect of Propolis Compared to Vitamins C and E Antioxidant Mixture in Cyclophosphamide-Induced Lung Toxicity In Mice

MAHROUS, A. H. (2018) · The Medical Journal of Cairo University/The Medical Journal of Cairo University · doi:10.21608/mjcu.2018.64913 · Cited by 2 · see citing works

The Role of Nutrition in Cancer: From Cellular and Molecular Perspective

Rasaei, N., Ildarabadi, A., Rahmani, F., Shiravi, F., Shoaibinobarian, N., & Tahvildari, A. (2024) · Interdisciplinary cancer research · doi:10.1007/16833_2024_354 · Cited by 1 · see citing works

Types of Cancers, Epidemiology, and Molecular Insights

Sobti, R. C., Gosipatala, S. B., Sharma, M., Reddy, P., Khalko, R. K., Kaur, T., & Thakur, M. (2024) · Springer eBooks · doi:10.1007/978-981-99-6263-1_1 · Cited by 1 · see citing works

Vitamin C: An Epigenetic Regulator

Pehlivan, F. E. (2019) · IntechOpen eBooks · doi:10.5772/intechopen.82563 · Cited by 1 · see citing works

Plant Kingdom as Source of Vitamins

Rivière, C., & Hennebelle, T. (2020) · Springer eBooks · doi:10.1007/978-981-13-1745-3_27-1 · Cited by 1 · see citing works

Decreased promoter methylation of E-cadherin gene due to overexpression of TET enzyme by vitamin C in MCF-7 cell line

Miandoab, S. S., Haghi, M., Salehi, M., & Feizi, M. A. H. (2021) · Gene Reports · doi:10.1016/j.genrep.2021.101188

Plant Kingdom as Source of Vitamins

Rivière, C., & Hennebelle, T. (2021) · Springer eBooks · doi:10.1007/978-981-15-4148-3_27

Nutrição e compostos essenciais e não essenciais na degradação epigenética associada à prevenção e combate ao câncer

da Luz, R., Júnior, E. L., & Boldt, A. B. W. (2022) · Research Society and Development · doi:10.33448/rsd-v11i3.26455

Hematopoietic Stem Cells (HSC) and Granulocyte Macrophage Progenitors (GMP) are the Oxidative Stress Targets in Low/Intermediate-1 Risk Myelodysplastic Syndromes

Giai, V., Bensi, T., Bertassello, C., Savio, M., Ferrero, D., Ciriello, M. M., & Ladetto, M. (2022) · Journal of Biotechnology and Biomedicine · doi:10.26502/jbb.2642-91280063

Modulatory Effect of Vitamin C on Hypoxia Induced Breast Cancer Stem Cells

Kazemi, M., Montazersaheb, S., Noroozpour, M., Farajnia, S., & Charoudeh, H. N. (2023) · Advanced Pharmaceutical Bulletin · doi:10.34172/apb.2023.073

In?vitro?Effect?of?L-ascorbic?acid?on?gingival?fibroblast?to?regulate?wound?healing.

Chaitrakoonthong, T., & Kamolratanakul, P. (2017) · doi:10.58837/chula.the.2017.388

DNA methylation in T cell leukaemia

Bensberg, M. (2024) · Linköping University medical dissertations · doi:10.3384/9789180755405

THE INVOLVEMENT OF DIFFERENT VITAMIN TYPES IN ASSISTING THE ACTIVATION OF STEM CELLS: A REVIEW

Hapsari, T. P. (2024) · Journal of Stem Cell Research and Tissue Engineering · doi:10.20473/jscrte.v8i1.57473

Food Bioactives as Natural Anticancer Therapeutic Agents

Lima, T. P. B., Coimbra, P. P. S., Araújo-Lima, C. F., & Teodoro, A. J. (2025) · Springer eBooks · doi:10.1007/978-981-97-9723-3_12

Nutriepigenetics

Cacabelos, R., Martínez-Iglesias, O. A., Corzo, L., Carrera, I., Cacabelos, N., & Naidoo, V. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-18722-3.00008-6

Harnessing Oxidative Stress to Kill Hepatocellular Carcinoma Cancer Cells: The Power of Methylselenic Acid and/or Pharmacological Ascorbate Combination—An In Vitro Study

Rataan, A. O., Alrosan, A. Z., Amawi, H. A., Rababah, L. K., Alrob, O. A., & Fazaa, A. T. (2026) · Advances in Pharmacological and Pharmaceutical Sciences · doi:10.1155/adpp/9901780

Identification of TET1-positive nuclear bodies in colorectal cancer cells : how Vitamin C and herbicides could both impact DNA demethylation in solid tumors

Osmani, N. E. (2022) · doi:10.70675/44703178z2ad1z4ebcza891z61cf9febffe8

The role of vitamin C in epigenetic cancer therapy

Mikkelsen, S. U., Gillberg, L., Lykkesfeldt, J., & Grønbæk, K. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.03.017 · Cited by 61 · see citing works

Vitamin C : An Epigenetic Regulator

Eryƒ±lmaz Pehlivan, F. (2018) · BiblioBoard Library Catalog (Open Research Library)

Vitamin C: epigenetic roles and cancer

Mustafi, S., & Wang, G. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-811907-5.00003-8 · Cited by 3 · see citing works

Reprogramming the epigenome with vitamin C

Lee Chong, T., Ahearn, E. L., & Cimmino, L. (2019) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2019.00128 · Cited by 120 · see citing works

Beyond redox: vitamin C in signaling, epigenetic regulation and protein modification—relevance to cancer therapy

H, A. S., Nixon, S., Ananda, H., Nune, M., & Rao, V. K. (2026) · Clinical Epigenetics · doi:10.1186/s13148-026-02211-z