Structural studies on human 2-oxoglutarate dependent oxygenases

A Common Variant in the FTO Gene Is Associated with Body Mass Index and Predisposes to Childhood and Adult Obesity

Frayling, T. M., Timpson, N. J., Weedon, M. N., Zeggini, E., Freathy, R. M., Lindgren, C. M., Perry, J. R. B., Elliott, K. S., Lango, H., Rayner, N. W., et al. (2007) · Science · doi:10.1126/science.1141634 · Cited by 4,531

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

Kaelin, W. G., & Ratcliffe, P. J. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.04.009 · Cited by 3,251

Introduction to Protein Structure

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

Selak, M. A., Armour, S. M., MacKenzie, E. D., Boulahbel, H., Watson, D. G., Mansfield, K. D., Pan, Y., Simon, M. C., Thompson, C. B., & Gottlieb, E. (2005) · Cancer Cell · doi:10.1016/j.ccr.2004.11.022 · Cited by 2,108

Oxygen sensing by HIF hydroxylases

Schofield, C. J., & Ratcliffe, P. J. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1366 · Cited by 2,068

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

Gerken, T., Girard, C. A. J., Tung, Y. L., Webby, C. J., Saudek, V., Hewitson, K. S., Yeo, G. S. H., McDonough, M. A., Cunliffe, S. L., McNeill, L. A., et al. (2007) · Science · doi:10.1126/science.1151710 · Cited by 1,541

JmjC-domain-containing proteins and histone demethylation

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

Myllyharju, J. (2003) · Trends in Genetics · doi:10.1016/j.tig.2003.11.004 · Cited by 1,229

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

Hausinger, R. P. (2004) · Critical Reviews in Biochemistry and Molecular Biology · doi:10.1080/10409230490440541 · Cited by 937

Carnitine biosynthesis in mammals

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Metabolic reprogram associated with epithelial-mesenchymal transition in tumor progression and metastasis

Wang, Y., Dong, C., & Zhou, B. P. (2019) · Genes & Diseases · doi:10.1016/j.gendis.2019.09.012 · Cited by 48

Coordinated methyl-lysine erasure: structural and functional linkage of a Jumonji demethylase domain and a reader domain

Upadhyay, A. K., Horton, J. R., Zhang, X., & Cheng, X. (2011) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2011.08.003 · Cited by 46

DNA Base Flipping: A General Mechanism for Writing, Reading, and Erasing DNA Modifications

Hong, S., & Cheng, X. (2016) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-43624-1_14 · Cited by 46

The oncometabolite D-2-hydroxyglutarate induced by mutant IDH1 or -2 blocks osteoblast differentiation in vitro and in vivo

Suijker, J., Baelde, H. J., Roelofs, H., Cleton-Jansen, A., & Bovée, J. V. M. G. (2015) · Oncotarget · doi:10.18632/oncotarget.4024 · Cited by 47

Targeting histone demethylase KDM5B for cancer treatment

Fu, Y.-D., Huang, M.-J., Guo, J., You, Y.-Z., Liu, H., Huang, L., & Yu, B. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112760 · Cited by 45

Melatonin: A Potential Regulator of DNA Methylation

Linowiecka, K., Slominski, A. T., Reiter, R. J., Böhm, M., Steinbrink, K., Paus, R., & Kleszczyński, K. (2023) · Antioxidants · doi:10.3390/antiox12061155 · Cited by 48

Metabolic control of gene transcription in non-alcoholic fatty liver disease: the role of the epigenome

Sinton, M. C., Hay, D. C., & Drake, A. J. (2019) · Clinical Epigenetics · doi:10.1186/s13148-019-0702-5 · Cited by 44

Jumonji domain‐containing protein 6 protein and its role in cancer

Yang, J., Chen, S., Yang, Y., Ma, X., Shao, B., Yang, S., Wei, Y., & Wei, X. (2020) · Cell Proliferation · doi:10.1111/cpr.12747 · Cited by 45

Human 2-oxoglutarate-dependent oxygenases: nutrient sensors, stress responders, and disease mediators

Fletcher, S. C., & Coleman, M. L. (2020) · Biochemical Society Transactions · doi:10.1042/bst20190333 · Cited by 44

Properties of the Reactants and Their Interactions within and with the Enzyme Binding Cavity Determine Reaction Selectivities. The Case of Fe(II)/2‐Oxoglutarate Dependent Enzymes

Wojdyła, Z., & Borowski, T. (2022) · Chemistry - A European Journal · doi:10.1002/chem.202104106 · Cited by 41

The Novel Roles of Connexin Channels and Tunneling Nanotubes in Cancer Pathogenesis

Valdebenito, S., Lou, E., Baldoni, J., Okafo, G. N., & Eugenín, E. A. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19051270 · Cited by 41

A human pluripotent stem cell model for the analysis of metabolic dysfunction in hepatic steatosis

Sinton, M. C., Meseguer-Ripolles, J., Lucendo‐Villarin, B., Wernig-Zorc, S., Thomson, J. P., Carter, R. N., Lyall, M. J., Walker, P. D., Thakker, A., Meehan, R. R., et al. (2020) · iScience · doi:10.1016/j.isci.2020.101931 · Cited by 39

Structural Insight into the Catalytic Mechanism of the Endoperoxide Synthase FtmOx1

Wu, L., Wang, Z., Cen, Y., Wang, B., & Zhou, J. (2021) · Angewandte Chemie International Edition · doi:10.1002/anie.202112063 · Cited by 40

Growing concerns about using hypoxia-inducible factor prolyl hydroxylase inhibitors for the treatment of renal anemia

Nakanishi, T., & Kuragano, T. (2024) · Clinical Kidney Journal · doi:10.1093/ckj/sfae051 · Cited by 39

Glutamine metabolite α-ketoglutarate acts as an epigenetic co-factor to interfere with osteoclast differentiation

Lee, S.-Y., Kim, H. S., Kim, M. J., Min, K. Y., Choi, W. S., & You, J. S. (2020) · Bone · doi:10.1016/j.bone.2020.115836 · Cited by 39

The Structural Motifs for Substrate Binding and Dimerization of the α Subunit of Collagen Prolyl 4-Hydroxylase

Anantharajan, J., Koski, M. K., Kursula, P., Hieta, R., Bergmann, U., Myllyharju, J., & Wierenga, R. K. (2013) · Structure · doi:10.1016/j.str.2013.09.005 · Cited by 37

Biochemical and structural investigations clarify the substrate selectivity of the 2-oxoglutarate oxygenase JMJD6

Islam, M. S., McDonough, M. A., Chowdhury, R., Gault, J., Khan, A. P., Pires, E., & Schofield, C. J. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.008693 · Cited by 37

Dysregulated Iron Homeostasis as Common Disease Etiology and Promising Therapeutic Target

Holbein, B. E., & Lehmann, C. (2023) · Antioxidants · doi:10.3390/antiox12030671 · Cited by 37

The role of metabolic enzymes in mesenchymal tumors and tumor syndromes: genetics, pathology, and molecular mechanisms

Schaefer, I., Hornick, J. L., & Bovée, J. V. M. G. (2018) · Laboratory Investigation · doi:10.1038/s41374-017-0003-6 · Cited by 36

Circles of Life: linking metabolic and epigenetic cycles to immunity

Lio, C. J., & Huang, S. C. (2020) · Immunology · doi:10.1111/imm.13207 · Cited by 36

Mechanistic analysis of carbon–carbon bond formation by deoxypodophyllotoxin synthase

Tang, H., Wu, M.-H., Lin, H.-Y., Han, M.-R., Tu, Y.-H., Yang, Z., Chien, T., Chan, N., & Chang, W. (2021) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2113770119 · Cited by 34

Dual-action inhibitors of HIF prolyl hydroxylases that induce binding of a second iron ion

Yeoh, K. K., Chan, M. C., Thalhammer, A., Demetriades, M., Chowdhury, R., Tian, Y., Stolze, I. P., McNeill, L. A., Lee, M. K., Woon, E. C. Y., et al. (2012) · Organic & Biomolecular Chemistry · doi:10.1039/c2ob26648b · Cited by 34

Optimisation of a triazolopyridine based histone demethylase inhibitor yields a potent and selective KDM2A (FBXL11) inhibitor

England, K. S., Tumber, A., Krojer, T. J., Scozzafava, G., Ng, S. S., Daniel, M., Szykowska, A., Che, K., von Delft, F., Burgess-Brown, N., et al. (2014) · MedChemComm · doi:10.1039/c4md00291a · Cited by 33

Diet-induced weight loss decreases adipose tissue oxygen tension with parallel changes in adipose tissue phenotype and insulin sensitivity in overweight humans

Vink, R., Roumans, N. J. T., Čajlaković, M., Cleutjens, J. P. M., Boekschoten, M. V., Fazelzadeh, P., Vogel, M., Blaak, E. E., Mariman, E. C. M., van Baak, M. A., et al. (2017) · International Journal of Obesity · doi:10.1038/ijo.2017.38 · Cited by 33

Regulation of the 2-oxoglutarate-dependent dioxygenases and implications for cancer

Vissers, M. C. M., Kuiper, C., & Dachs, G. U. (2014) · Biochemical Society Transactions · doi:10.1042/bst20140118 · Cited by 32

Advances and challenges in understanding histone demethylase biology

Nowak, R. P., Tumber, A., Johansson, C., Che, K. H., Brennan, P. E., Owen, D. R., & Oppermann, U. C. T. (2016) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2016.06.021 · Cited by 32

Supplementation with uric and ascorbic acid protects stored red blood cells through enhancement of non-enzymatic antioxidant activity and metabolic rewiring

Tzounakas, V. L., Anastasiadi, A. T., Arvaniti, V.-Z., Lelli, V., Fanelli, G., Paronis, E., Apostolidou, A. C., Balafas, E., Kostomitsopoulos, N. G., Papageorgiou, E. G., et al. (2022) · Redox Biology · doi:10.1016/j.redox.2022.102477 · Cited by 38

Development and Application of a Fluoride‐Detection‐Based Fluorescence Assay for γ‐Butyrobetaine Hydroxylase

Rydzik, A. M., Leung, I. K. H., Kochan, G. T., Thalhammer, A., Oppermann, U. C. T., Claridge, T. D. W., & Schofield, C. J. (2012) · ChemBioChem · doi:10.1002/cbic.201200256 · Cited by 32

The role and prospect of lysine‐specific demethylases in cancer chemoresistance

Song, Y., Yang, G., Ma, D., Wang, W., & Leung, C. (2023) · Medicinal Research Reviews · doi:10.1002/med.21955 · Cited by 32

α‐ketoglutarate is associated with delayed wound healing in diabetes

Tan, Q., Wang, W., Yang, C., Zhang, J., Sun, K., Luo, H., Mai, L., Lao, Y., Yan, L., & Ren, M. (2016) · Clinical Endocrinology · doi:10.1111/cen.13047 · Cited by 31

Large-scale examination of functional and sequence diversity of 2-oxoglutarate/Fe(II)-dependent oxygenases in Metazoa

Jia, B., Tang, K., Chun, B. H., & Jeon, C. O. (2017) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2017.08.019 · Cited by 30

IDH1 Targeting as a New Potential Option for Intrahepatic Cholangiocarcinoma Treatment—Current State and Future Perspectives

Crispo, F., Pietrafesa, M., Condelli, V., Maddalena, F., Bruno, G., Piscazzi, A., Sgambato, A., Esposito, F., & Landriscina, M. (2020) · Molecules · doi:10.3390/molecules25163754 · Cited by 32

Control of Histone H3 Lysine 9 (H3K9) Methylation State via Cooperative Two-step Demethylation by Jumonji Domain Containing 1A (JMJD1A) Homodimer

Goda, S., Isagawa, T., Chikaoka, Y., Kawamura, T., & Aburatani, H. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.492595 · Cited by 32

Small Molecule Models for Nonporphyrinic Iron and Manganese Oxygenases

Anna Company, Lloret‐Fillol, J., & Costas, M. (2013) · Elsevier eBooks · doi:10.1016/b978-0-08-097774-4.00323-5 · Cited by 31

Vitamin C enhances substantially formation of 5-hydroxymethyluracil in cellular DNA

Modrzejewska, M., Gawroński, M., Skonieczna, M., Zarakowska, E., Starczak, M., Foksiński, M., Rzeszowska‐Wolny, J., Gackowski, D., & Oliński, R. (2016) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2016.10.535 · Cited by 30

Quantum chemical modelling in the research of molecular mechanisms of enzymatic catalysis

Nemukhin, A. V., Grigorenko, B. L., Lushchekina, S. V., & Varfolomeev, S. D. (2012) · Russian Chemical Reviews · doi:10.1070/rc2012v081n11abeh004311 · Cited by 30

Hypoxia-inducible factor prolyl 4-hydroxylase inhibition in cardiometabolic diseases

Koivunen, P., Serpi, R., & Dimova, E. Y. (2016) · Pharmacological Research · doi:10.1016/j.phrs.2016.11.003 · Cited by 33

Mechanism of Molecular Oxygen Diffusion in a Hypoxia-Sensing Prolyl Hydroxylase Using Multiscale Simulation

Domene, C., Jorgensen, C., & Schofield, C. J. (2020) · Journal of the American Chemical Society · doi:10.1021/jacs.9b09236 · Cited by 29

Dissecting the Mechanism of the Nonheme Iron Endoperoxidase FtmOx1 Using Substrate Analogues

Zhu, G., Yan, W., Wang, X., Cheng, R., Naowarojna, N., Wang, K., Wang, J., Song, H., Wang, Y., Liu, H., et al. (2022) · JACS Au · doi:10.1021/jacsau.2c00248 · Cited by 29

Targeting 2-oxoglutarate dehydrogenase for cancer treatment.

Chang, L., Chiang, S.-K., Chen, S., & Hung, M. (2022) · PubMed Central · Cited by 29

Mechanisms of Vitamins Inhibiting Ferroptosis

Zhang, M., Chen, X., & Zhang, Y. (2024) · Antioxidants · doi:10.3390/antiox13121571 · Cited by 32

From the proteomic point of view: Integration of adaptive changes to iron deficiency in plants

Mai, H., & Bauer, P. (2016) · Current Plant Biology · doi:10.1016/j.cpb.2016.02.001 · Cited by 27

Crystal structure of PHYHD1A, a 2OG oxygenase related to phytanoyl-CoA hydroxylase

Zhang, Z., Kochan, G. T., Ng, S. S., Kavanagh, K. L., Oppermann, U. C. T., Schofield, C. J., & McDonough, M. A. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.04.059 · Cited by 26

The Unique Role of the Second Coordination Sphere to Unlock and Control Catalysis in Nonheme Fe(II)/2-Oxoglutarate Histone Demethylase KDM2A

Thomas, M. G., Rifayee, S. B. J. S., Chaturvedi, S. S., Gorantla, K. R., White, W., Wildey, J., Schofield, C. J., & Christov, C. Z. (2024) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.4c01365 · Cited by 25

Efficient Biosynthesis of High-Value Succinic Acid and 5-Hydroxyleucine Using a Multienzyme Cascade and Whole-Cell Catalysis

Sun, D., Liu, X., Zhu, M., Chen, Y., Li, C., Cheng, X., Zhu, Z., Lu, F., & Qin, H. (2019) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.9b05529 · Cited by 25

Chemical Inhibitors Targeting the Histone Lysine Demethylase Families with Potential for Drug Discovery

Das, N. D., Niwa, H., & Umehara, T. (2023) · Epigenomes · doi:10.3390/epigenomes7010007 · Cited by 26

Wild-Type IDH1 and Mutant IDH1 Opposingly Regulate Podoplanin Expression in Glioma

Sun, C., Xiao, L., Zhao, Y., Shi, J., Yuan, Y., Gu, Y., Zhang, F., Gao, X., Yang, Y., Yang, R., et al. (2020) · Translational Oncology · doi:10.1016/j.tranon.2020.100758 · Cited by 25

Structural Insights Into m6A-Erasers: A Step Toward Understanding Molecule Specificity and Potential Antiviral Targeting

Bayoumi, M. M., & Munir, M. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2020.587108 · Cited by 24

The Role of 2-Oxoglutarate Dependent Dioxygenases in Gliomas and Glioblastomas: A Review of Epigenetic Reprogramming and Hypoxic Response

Crake, R., Burgess, E. R., Royds, J. A., Phillips, E., Vissers, M. C. M., & Dachs, G. U. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.619300 · Cited by 25

Comparison of the substrate selectivity and biochemical properties of human and bacterial γ-butyrobetaine hydroxylase

Rydzik, A. M., Leung, I. K. H., Kochan, G. T., Loik, N. D., Henry, L., McDonough, M. A., Claridge, T. D. W., & Schofield, C. J. (2014) · Organic & Biomolecular Chemistry · doi:10.1039/c4ob01167h · Cited by 24

Assembly of the elongated collagen prolyl 4-hydroxylase α2β2 heterotetramer around a central α2 dimer

Koski, M. K., Anantharajan, J., Kursula, P., Dhavala, P., Murthy, A. V., Bergmann, U., Myllyharju, J., & Wierenga, R. K. (2017) · Biochemical Journal · doi:10.1042/bcj20161000 · Cited by 24

The impact of mitochondria on cancer treatment resistance

van der Merwe, M., van Niekerk, G., Fourie, C., du Plessis, M., & Engelbrecht, A. (2021) · Cellular Oncology · doi:10.1007/s13402-021-00623-y · Cited by 24

Structural insights into the interactions and epigenetic functions of human nucleic acid repair protein ALKBH6

Ma, L., Lu, H., Tian, Z., Yang, M., Ma, J., Shang, G., Liu, Y., Xie, M., Wang, G., Wu, W., et al. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.101671 · Cited by 23

Structure and Function of TET Enzymes

Yin, X., Hu, L., & Xu, Y. (2022) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-11454-0_10 · Cited by 24

Oxidative modification of free-standing amino acids by Fe(II)/αKG-dependent oxygenases

Tao, H., & Abe, I. (2022) · Engineering Microbiology · doi:10.1016/j.engmic.2022.100062 · Cited by 22

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

The broad spectrum 2-oxoglutarate oxygenase inhibitor N-oxalylglycine is present in rhubarb and spinach leaves

Al‐Qahtani, K., Jabeen, B., Sekirnik, R., Riaz, N., Claridge, T. D. W., Schofield, C. J., & McCullagh, J. (2015) · Phytochemistry · doi:10.1016/j.phytochem.2015.06.028 · Cited by 23

Crystal Structure of a Novel N-Substituted L-Amino Acid Dioxygenase from Burkholderia ambifaria AMMD

Qin, H., Miyakawa, T., Jia, M. Z., Nakamura, A., Ohtsuka, J., Xue, Y. Y., Kawashima, T., Kasahara, T., Hibi, M., Ogawa, J., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0063996 · Cited by 22

Therapeutic potential of ALKB homologs for cardiovascular disease

Xiao, M., Liu, J., Xian, C.-L., Chen, K.-Y., Liu, Z., & Cheng, Y. (2020) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2020.110645 · Cited by 21

The metabolite alpha-ketoglutarate inhibits vascular calcification partially through modulation of the TET2/NLRP3 inflammasome signaling pathway

Fu, M., Lan, Z., Ye, Y., Gong, Y., Liang, Q., Li, M., Feng, L., Chen, A., Dong, Q., Li, Y., et al. (2025) · Kidney International · doi:10.1016/j.kint.2025.04.016 · Cited by 24

Neuroinflammation regulates the balance between hippocampal neuron death and neurogenesis in an ex vivo model of thiamine deficiency

Cassiano, L. M. G., Oliveira, M. D. S., Pioline, J., Salim, A. C. M., & Coimbra, R. S. (2022) · Journal of Neuroinflammation · doi:10.1186/s12974-022-02624-6 · Cited by 21

Biocatalytic Production of Chemical Building Blocks in Technical Scale with α‐Ketoglutarate‐Dependent Dioxygenases

Hüttel, W. (2013) · Chemie Ingenieur Technik · doi:10.1002/cite.201300008 · Cited by 21

The Krebs Cycle Connection: Reciprocal Influence Between Alternative Splicing Programs and Cell Metabolism

Biamonti, G., Maita, L., & Montecucco, A. (2018) · Frontiers in Oncology · doi:10.3389/fonc.2018.00408 · Cited by 22

Iron and FER‐LIKE IRON DEFICIENCY‐INDUCED TRANSCRIPTION FACTOR‐dependent regulation of proteins and genes in Arabidopsis thaliana roots

Mai, H., Lindermayr, C., von Toerne, C., Fink‐Straube, C., Durner, J., & Bauer, P. (2015) · PROTEOMICS · doi:10.1002/pmic.201400351 · Cited by 20

Targeting lysine specific demethylase 4A (KDM4A) tandem TUDOR domain – A fragment based approach

Upadhyay, A. K., Judge, R. A., Li, L., Pithawalla, R. B., Simanis, J. A., Bodelle, P. M., Marin, V. L., Henry, R. F., Petros, A. M., & Sun, C. C. (2018) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2018.04.050 · Cited by 20

Collagen Hydroxylases

Myllyharju, J. (2015) · Royal Society of Chemistry eBooks · doi:10.1039/9781782621959-00149 · Cited by 17

Redesign and engineering of a dioxygenase targeting biocatalytic synthesis of 5-hydroxyl leucine

Sun, D., Gao, D., Liu, X., Zhu, M., Li, C., Chen, Y., Zhu, Z., Lu, F., & Qin, H. (2019) · Catalysis Science & Technology · doi:10.1039/c9cy00110g · Cited by 19

Synergistic inhibitory effects of deferasirox in combination with decitabine on leukemia cell lines SKM-1, THP-1, and K-562

Li, N., Chen, Q., Gu, J., Li, S., Zhao, G., Wang, W., Wang, Z., & Wang, X. (2017) · Oncotarget · doi:10.18632/oncotarget.16583 · Cited by 18

Novel Scaffolds of Cell-Active Histone Demethylase Inhibitors Identified from High-Throughput Screening

Wang, W., Marholz, L. J., & Wang, X. (2015) · SLAS DISCOVERY · doi:10.1177/1087057115579637 · Cited by 18

Biochemical and biophysical analyses of hypoxia sensing prolyl hydroxylases from Dictyostelium discoideum and Toxoplasma gondii

Liu, T., Abboud, M. I., Chowdhury, R., Tumber, A., Hardy, A., Lippl, K., Lohans, C. T., Pires, E., Wickens, J. R., McDonough, M. A., et al. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.013998 · Cited by 18

Reprogramming Carbohydrate Metabolism in Cancer and Its Role in Regulating the Tumor Microenvironment

Adhikari, S., Guha, D., Mohan, C., Mukherjee, S., Tyler, J. K., & Das, C. (2022) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-3-031-07634-3_1 · Cited by 19

Molecular basis for the substrate specificity and catalytic mechanism of thymine-7-hydroxylase in fungi

Li, W., Zhang, T., & Ding, J. (2015) · Nucleic Acids Research · doi:10.1093/nar/gkv979 · Cited by 17

Epigenetic Metalloenzymes

Blanquart, C., Linot, C., Cartron, P., Tomaselli, D., Mai, A., & Bertrand, P. (2018) · Current Medicinal Chemistry · doi:10.2174/0929867325666180706105903 · Cited by 17

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 18

Hypoxia research, where to now?

Ortmann, B. M., Taylor, C. T., & Rocha, S. (2024) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2024.03.008 · Cited by 18

Structural optimization of SadA, an Fe(II)- and α-ketoglutarate-dependent dioxygenase targeting biocatalytic synthesis of N-succinyl-l-threo-3,4-dimethoxyphenylserine

Qin, H., Miyakawa, T., Nakamura, A., Hibi, M., Ogawa, J., & Tanokura, M. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.07.008 · Cited by 16

A simple but effective modeling strategy for structural properties of non‐heme Fe(II) sites in proteins: Test of force field models and application to proteins in the AlkB family

Pang, X., Han, K., & Cui, Q. (2013) · Journal of Computational Chemistry · doi:10.1002/jcc.23305 · Cited by 16

Harnessing Fe(II)/α-ketoglutarate-dependent oxygenases for structural diversification of fungal meroterpenoids

Tao, H., & Abe, I. (2022) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2022.102763 · Cited by 14

Hypoxia inducible factor prolyl hydroxylases in inflammatory bowel disease

Lun, J., Zhang, H., Guo, J., Yu, M., & Fang, J. S. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1045997 · Cited by 15

Oxidative Demethylation of DNA and RNA Mediated by Non‐Heme Iron‐Dependent Dioxygenases

Lu, L., Zhu, C., Xia, B., & Yi, C. (2014) · Chemistry - An Asian Journal · doi:10.1002/asia.201402148 · Cited by 15

Human carnitine biosynthesis proceeds via (2S,3S)-3-hydroxy-N ε -trimethyllysine

Leśniak, R. K., Markolovic, S., Tārs, K., & Schofield, C. J. (2016) · Chemical Communications · doi:10.1039/c6cc08381a · Cited by 14

Selective Inhibitors of a Human Prolyl Hydroxylase (OGFOD1) Involved in Ribosomal Decoding

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Structure of the JmjC domain-containing protein NO66 complexed with ribosomal protein Rpl8

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Catalytic O 2 activation with synthetic models of α-ketoglutarate dependent oxygenases

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Structure of transmembrane prolyl 4-hydroxylase reveals unique organization of EF and dioxygenase domains

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Alpha-ketoglutarate supplementation ameliorates ovarian reserve and oocyte quality decline with aging in mice

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2-oxoglutarate-dependent dioxygenases: A renaissance in attention for ascorbic acid in plants

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

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Derivatives of the Clinically Used HIF Prolyl Hydroxylase Inhibitor Desidustat Are Efficient Inhibitors of Human γ-Butyrobetaine Hydroxylase

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The Role of 2-Oxoglutarate-Dependent Oxygenases in Hypoxia Sensing

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Ejection of structural zinc leads to inhibition of γ-butyrobetaine hydroxylase

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Introduction to Structural Studies on 2-Oxoglutarate-Dependent Oxygenases and Related Enzymes

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Oxidation by 2-oxoglutarate oxygenases: non-haem iron systems in catalysis and signalling

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Structural studies on 2-oxoglutarate oxygenases and related double-stranded β-helix fold proteins

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

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