Structural studies on human 2-oxoglutarate dependent oxygenases

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Oxygen sensing by metazoans: the central role of the HIF hydroxylase pathway.

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Succinate links TCA cycle dysfunction to oncogenesis by inhibiting HIF-α prolyl hydroxylase

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Oxygen sensing by HIF hydroxylases

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The Obesity-Associated FTO Gene Encodes a 2-Oxoglutarate-Dependent Nucleic Acid Demethylase

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Collagens, modifying enzymes and their mutations in humans, flies and worms

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Fe(II)/α-Ketoglutarate-Dependent Hydroxylases and Related Enzymes

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Carnitine biosynthesis in mammals

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An inhibitor of mutant IDH1 delays growth and promotes differentiation of glioma cells

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The role of mutations in epigenetic regulators in myeloid malignancies

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Vitamin C-Sources, Physiological Role, Kinetics, Deficiency, Use, Toxicity, and Determination

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2-Oxoglutarate-Dependent Oxygenases

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Histone lysine demethylases as targets for anticancer therapy

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Histone demethylase KDM6A directly senses oxygen to control chromatin and cell fate

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Inhibition of 2-oxoglutarate dependent oxygenases

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Mechanism and Function of Oxidative Reversal of DNA and RNA Methylation

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Human high-altitude adaptation: forward genetics meets the HIF pathwayPreprint

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DNA Methylation, Its Mediators and Genome Integrity

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Regulation of the epigenome by vitamin C

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Fumarate and Succinate Regulate Expression of Hypoxia-inducible Genes via TET Enzymes

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Glutamine Metabolism Regulates Proliferation and Lineage Allocation in Skeletal Stem Cells

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Structure of human RNA N6-methyladenine demethylase ALKBH5 provides insights into its mechanisms of nucleic acid recognition and demethylation

Aik, W. S., Scotti, J. S., Choi, H., Gong, L., Demetriades, M., Schofield, C. J., & McDonough, M. A. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku085 · Cited by 250

Alpha-Ketoglutarate as a Molecule with Pleiotropic Activity: Well-Known and Novel Possibilities of Therapeutic Use

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Role of the jelly-roll fold in substrate binding by 2-oxoglutarate oxygenases

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The enzymes of β-lactam biosynthesis

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Recent examples of α-ketoglutarate-dependent mononuclear non-haem iron enzymes in natural product biosyntheses

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Structural analysis of human KDM5B guides histone demethylase inhibitor development

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Crystal Structures of the Human RNA Demethylase Alkbh5 Reveal Basis for Substrate Recognition

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Targeting histone lysine demethylases — Progress, challenges, and the future

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Targeting Histone Demethylases: A New Avenue for the Fight against Cancer

Rotili, D., & Mai, A. (2011) · Genes & Cancer · doi:10.1177/1947601911417976 · Cited by 201

The Roles of Jumonji-Type Oxygenases in Human Disease

Johansson, C., Tumber, A., Che, K., Cain, P., Nowak, R. P., Gileadi, C., & Oppermann, U. C. T. (2014) · Epigenomics · doi:10.2217/epi.13.79 · Cited by 167

Epigenetic Regulation by Histone Demethylases in Hypoxia

Hancock, R. L., Dunne, K., Walport, L. J., Flashman, E., & Kawamura, A. (2015) · Epigenomics · doi:10.2217/epi.15.24 · Cited by 162

Biologically inspired non-heme iron-catalysts for asymmetric epoxidation; design principles and perspectives

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Oncometabolites‐driven tumorigenesis: From genetics to targeted therapy

Morin, A., Letouzé, É., Gimenez‐Roqueplo, A., & Favier, J. (2014) · International Journal of Cancer · doi:10.1002/ijc.29080 · Cited by 162

Krebs cycle intermediates regulate DNA and histone methylation: Epigenetic impact on the aging process

Salminen, A., Kauppinen, A., Hiltunen, M. O., & Kaarniranta, K. (2014) · Ageing Research Reviews · doi:10.1016/j.arr.2014.05.004 · Cited by 145

Structure of a Naegleria Tet-like dioxygenase in complex with 5-methylcytosine DNA

Hashimoto, H., Pais, J. E., Zhang, X., Saleh, L., Fu, Z.-Q., Dai, N., Junior, I. R. C., Zheng, Y., & Cheng, X. (2013) · Nature · doi:10.1038/nature12905 · Cited by 138

A Comprehensive Review of Lysine-Specific Demethylase 1 and its Roles in Cancer

Hosseini, A., & Minucci, S. (2017) · Epigenomics · doi:10.2217/epi-2017-0022 · Cited by 139

Advances in histone demethylase KDM4 as cancer therapeutic targets

Lee, D. H., Kim, G. W., Jeon, Y. H., Yoo, J. H., Lee, S. W., & Kwon, S. H. (2020) · The FASEB Journal · doi:10.1096/fj.201902584r · Cited by 137

The α-ketoglutarate dehydrogenase complex in cancer metabolic plasticity

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Pharmacological targeting of the HIF hydroxylases – A new field in medicine development

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Intestinal hypoxia and hypoxia-induced signalling as therapeutic targets for IBD

Welden, S. V., Selfridge, A. C., & Hindryckx, P. (2017) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/nrgastro.2017.101 · Cited by 128

Carbon–fluorine bond cleavage mediated by metalloenzymes

Wang, Y., & Liu, A. (2020) · Chemical Society Reviews · doi:10.1039/c9cs00740g · Cited by 130

Structure–function relationships of human JmjC oxygenases—demethylases versus hydroxylases

Markolovic, S., Leissing, T. M., Chowdhury, R., Wilkins, S. E., Lü, X., & Schofield, C. J. (2016) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2016.05.013 · Cited by 125

KDM5B is a master regulator of the H3K4-methylome in stem cells, development and cancer

Xhabija, B., & Kidder, B. L. (2018) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2018.11.001 · Cited by 120

Prolyl 4‐hydroxylases, master regulators of the hypoxia response

Myllyharju, J. (2013) · Acta Physiologica · doi:10.1111/apha.12096 · Cited by 123

Structural and Functional Coordination of DNA and Histone MethylationPreprint

Cheng, X. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a018747 · Cited by 125

Nitric Oxide Modifies Global Histone Methylation by Inhibiting Jumonji C Domain-containing Demethylases

Hickok, J. R., Vasudevan, D., Antholine, W. E., & Thomas, D. D. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.432294 · Cited by 120

Intracellular ascorbate enhances hypoxia-inducible factor (HIF)-hydroxylase activity and preferentially suppresses the HIF-1 transcriptional response

Kuiper, C., Dachs, G. U., Currie, M. J., & Vissers, M. C. M. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.01.033 · Cited by 117

A rice gene that confers broad-spectrum resistance to β-triketone herbicides

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Targeting the histone orthography of cancer: drugs for writers, erasers and readers

Simó‐Riudalbas, L., & Esteller, M. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12844 · Cited by 111

Ribosomal oxygenases are structurally conserved from prokaryotes to humans

Chowdhury, R., Sekirnik, R., Brissett, N. C., Krojer, T., Ho, C.-H., Ng, S. S., Clifton, I. J., Ge, W., Kershaw, N. J., Fox, G. C., et al. (2014) · Nature · doi:10.1038/nature13263 · Cited by 105

Impaired mitochondrial energy metabolism in Alzheimer's disease: Impact on pathogenesis via disturbed epigenetic regulation of chromatin landscape

Salminen, A., Haapasalo, A., Kauppinen, A., Kaarniranta, K., Soininen, H. S., & Hiltunen, M. O. (2015) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.05.001 · Cited by 107

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

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Distinct RNA N- demethylation pathways catalyzed by nonheme iron ALKBH5 and FTO enzymes enable regulation of formaldehyde release rates

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2-Oxoglutarate-dependent dioxygenases are sensors of energy metabolism, oxygen availability, and iron homeostasis: potential role in the regulation of aging process

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The oxygenase Jmjd6–a case study in conflicting assignments

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Krebs cycle dysfunction shapes epigenetic landscape of chromatin: Novel insights into mitochondrial regulation of aging process

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A molecular threading mechanism underlies Jumonji lysine demethylase KDM2A regulation of methylated H3K36Preprint

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Hypoxia-Inducible Histone Lysine Demethylases: Impact on the Aging Process and Age-Related Diseases

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Ascorbic acid induces global epigenetic reprogramming to promote meiotic maturation and developmental competence of porcine oocytes

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Perspectives on the interactions between metabolism, redox, and epigenetics in plants

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Aberrant DNA methylation reprogramming in bovine SCNT preimplantation embryos

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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

Studies on the catalytic domains of multiple JmjC oxygenases using peptide substrates

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Epigenetics: The third pillar of nitric oxide signaling

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Emulsion PCR Significantly Improves Nonequilibrium Capillary Electrophoresis of Equilibrium Mixtures-Based Aptamer Selection: Allowing for Efficient and Rapid Selection of Aptamer to Unmodified ABH2 Protein

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Mutations in the Isocitrate Dehydrogenase Genes IDH1 and IDH2 in Tumors

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Molecular architecture of the multifunctional collagen lysyl hydroxylase and glycosyltransferase LH3

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Hydroxylation of methylated CpG dinucleotides reverses stabilisation of DNA duplexes by cytosine 5-methylation

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OH, the Places You’ll Go! Hydroxylation, Gene Expression, and Cancer

Ploumakis, A., & Coleman, M. L. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.05.026 · Cited by 77

Advances in Histone Demethylase KDM3A as a Cancer Therapeutic Target

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Biochemical Diversity of 2-Oxoglutarate-Dependent Oxygenases

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Crystal Structure and Functional Analysis of JMJD5 Indicate an Alternate Specificity and Function

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New themes in the biological functions of 5‐methylcytosine and 5‐hydroxymethylcytosine

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Jumonji domain containing protein 6 (Jmjd6) modulates splicing and specifically interacts with arginine–serine-rich (RS) domains of SR- and SR-like proteins

Heim, A., Grimm, C., Müller, U., Häußler, S., Mackeen, M. M., Merl‐Pham, J., Hauck, S. M., Kessler, B. M., Schofield, C. J., Wolf, A., et al. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku488 · Cited by 65

Molecular Pathogenesis and Diagnostic, Prognostic and Predictive Molecular Markers in Sarcoma

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Autocatalysed oxidative modifications to 2‐oxoglutarate dependent oxygenases

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Reshaping the Binding Pocket of Lysine Hydroxylase for Enhanced Activity

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Metabolic Dysregulations and Epigenetics: A Bidirectional Interplay that Drives Tumor Progression

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IDH Mutations in Tumorigenesis and Their Potential Role As Novel Therapeutic Targets

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Vitamin C Transporters and Their Implications in Carcinogenesis

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Reporter Ligand NMR Screening Method for 2-Oxoglutarate Oxygenase Inhibitors

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Genetics of Myeloproliferative Neoplasms

Viny, A. D., & Levine, R. L. (2014) · The Cancer Journal · doi:10.1097/ppo.0000000000000013 · Cited by 60

Mitochondria and Hypoxia: Metabolic Crosstalk in Cell-Fate Decisions

Bargiela, D., Burr, S. P., & Chinnery, P. F. (2018) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2018.02.002 · Cited by 60

Comparative Biology of Oxygen Sensing in Plants and Animals

Holdsworth, M. J., & Gibbs, D. J. (2020) · Current Biology · doi:10.1016/j.cub.2020.03.021 · Cited by 56

Trimethyllysine: From Carnitine Biosynthesis to Epigenetics

Maas, M. N., Hintzen, J. C. J., Porzberg, M. R. B., & Mecinović, J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249451 · Cited by 58

Modulation of intracellular iron metabolism by iron chelation affects chromatin remodeling proteins and corresponding epigenetic modifications in breast cancer cells and increases their sensitivity to chemotherapeutic agents

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The histone methyltransferase DOT1L: regulatory functions and a cancer therapy target.

Wong, M., Polly, P., & Liu, T. (2015) · Europe PMC (PubMed Central) · Cited by 57

Mutant IDH in Gliomas: Role in Cancer and Treatment Options

Solomou, G., Finch, A., Asghar, A., & Bardella, C. (2023) · Cancers · doi:10.3390/cancers15112883 · Cited by 62

Now a Nobel gas: oxygen

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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 57

Epigenetic drugs against cancer: an evolving landscape

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Aspartate/asparagine-β-hydroxylase crystal structures reveal an unexpected epidermal growth factor-like domain substrate disulfide pattern

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