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

Brändén, C.-I., & Tooze, J. (2012) · Garland Science eBooks · doi:10.1201/9781136969898 · Cited by 2,398

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

Klose, R. J., Kallin, E. M., & Zhang, Y. (2006) · Nature Reviews Genetics · doi:10.1038/nrg1945 · Cited by 1,290

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

Vaz, F. M., & Wanders, R. J. A. (2002) · Biochemical Journal · doi:10.1042/0264-6021:3610417 · Cited by 769

Dihydrolipoamide dehydrogenase from Leishmania donovani: New insights through biochemical characterization

Chiranjivi, A. K., & Dubey, V. K. (2018) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2018.02.112 · Cited by 10

Prolyl dihydroxylation of unassembled uS12/Rps23 regulates fungal hypoxic adaptation

Clasen, S. J., Shao, W., He, G., & Espenshade, P. J. (2017) · eLife · doi:10.7554/elife.28563 · Cited by 11

Tricarboxylic Acid Cycle Relationships with Non-Metabolic Processes: A Short Story with DNA Repair and Its Consequences on Cancer Therapy Resistance

Álvarez-González, E., & Sierra, L. M. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25169054 · Cited by 10

Oxidative C−F Cleavage in Metalloenzymes and Model Compounds

Costas, M. (2021) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.202100754 · Cited by 9

Functional classification of skeletal muscle networks. II. Applications to pathophysiology

Wang, Y., Winters, J. M., & Subramaniam, S. (2012) · Journal of Applied Physiology · doi:10.1152/japplphysiol.01515.2011 · Cited by 9

Non-heme iron enzyme-catalyzed complex transformations

Song, H., Naowarojna, N., Cheng, R., Lopez, J., & Liu, P. (2019) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2019.06.002 · Cited by 9

The Hydroxyproline Proteome of HeLa Cells with Emphasis on the Active Sites of Protein Disulfide Isomerases

Onisko, B. (2020) · Journal of Proteome Research · doi:10.1021/acs.jproteome.9b00625 · Cited by 9

Active site characterization and activity of the human aspartyl (asparaginyl) β-hydroxylase

Greve, J. M., Pinkham, A. M., Thompson, Z., & Cowan, J. A. (2021) · Metallomics · doi:10.1093/mtomcs/mfab056 · Cited by 9

Crystallographic and Selectivity Studies on the Approved HIF Prolyl Hydroxylase Inhibitors Desidustat and Enarodustat

Corner, T. P., Salah, E., Tumber, A., Kaur, S., Nakashima, Y., Allen, M. D., Schnaubelt, L. I., Fiorini, G., Brewitz, L., & Schofield, C. J. (2024) · ChemMedChem · doi:10.1002/cmdc.202400504 · Cited by 10

Crystal structure of the indole-3-acetic acid-catabolizing enzyme DAO1 from Arabidopsis thaliana

Jin, S.-H., Lee, H., Shin, Y., Kim, J., & Rhee, S. (2020) · Journal of Structural Biology · doi:10.1016/j.jsb.2020.107632 · Cited by 8

Alteration of Gene Expression Profile in Kidney of Spontaneously Hypertensive Rats Treated with Protein Hydrolysate of Blue Mussel (Mytilus edulis) by DNA Microarray Analysis

Feng, J., Dai, Z., Zhang, Y., Meng, L., Ye, J., & Ma, X. (2015) · PLoS ONE · doi:10.1371/journal.pone.0142016 · Cited by 8

Developing a colorimetric assay for Fe(II)/2-oxoglutarate-dependent dioxygenase

Guo, C., Hu, Y., Yang, C., Urs, A. N. N., & Zhang, Y. (2018) · Analytical Biochemistry · doi:10.1016/j.ab.2018.02.013 · Cited by 8

A non-canonical role of ELN protects from cellular senescence by limiting iron-dependent regulation of gene expression

Czarnecka‐Herok, J., Zhu, K., Flaman, J., Goehrig, D., Vernier, M., Makulyte, G., Lamboux, A., Dragic, H., Rhinn, M., Médard, J., et al. (2024) · Redox Biology · doi:10.1016/j.redox.2024.103204 · Cited by 7

Enzymatic hydroxylation of L-pipecolic acid by L-proline cis-4-hydroxylases and isomers separation

Lu, F., Chen, J., Ye, H., Wu, H., Sha, F., Huang, F., Cao, F., & Wei, P. (2020) · Biotechnology Letters · doi:10.1007/s10529-020-03002-z · Cited by 7

Human phytanoyl‐CoA dioxygenase domain‐containing 1 (PHYHD1) is a putative oxygen sensor associated with RNA and carbohydrate metabolism

Ala‐Nisula, T., Sah‐Teli, S. K., Ronkainen, V., Dimova, E. Y., & Koivunen, P. (2023) · FEBS Letters · doi:10.1002/1873-3468.14666 · Cited by 5

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

Ren, R., Horton, J. R., Hong, S., & Cheng, X. (2022) · Advances in experimental medicine and biology · doi:10.1007/978-3-031-11454-0_12 · Cited by 6

Inhibition of HIF-prolyl 4-hydroxylases as a promising approach to the therapy of cardiometabolic diseases

Айтбаев, К. А., Murkamilov, I. T., & Fomin, V. V. (2018) · Terapevticheskii arkhiv · doi:10.26442/terarkh201890886-94 · Cited by 6

Functional Models for Oxygen Activating Nonheme Monoiron Enzymes

Ghosh, I., & Paine, T. K. (2021) · Elsevier eBooks · doi:10.1016/b978-0-08-102688-5.00019-2 · Cited by 6

NMR studies of the non-haem Fe(II) and 2-oxoglutarate-dependent oxygenases

Mbenza, N. M., Vadakkedath, P. G., McGillivray, D. J., & Leung, I. K. H. (2017) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2017.08.032 · Cited by 6

A scoping review regarding reproductive capacity modulation based on alpha-ketoglutarate supplementation

Doroftei, B., Ilie, O., Timofeiov, S., Dabuleanu, A., Scripcariu, I. S., Micu, R., & Tataranu, E. (2024) · Reproduction · doi:10.1530/rep-24-0137 · Cited by 4

Growing with the wind

Katz, M. J., Acevedo, J. M., & Wappner, P. (2014) · Fly · doi:10.4161/fly.29943 · Cited by 5

Structural Basis of Nucleic Acid Recognition and 6mA Demethylation by Caenorhabditis elegans NMAD-1A

Shang, G., Yang, M., Li, M., Ma, L., Liu, Y., Ma, J., Chen, Y., Wang, X., Fan, S., Xie, M., et al. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25020686 · Cited by 5

Mechanisms of Epigenetic Regulation by Nitric Oxide

Bovee, R. C., Hickok, J. R., Vasudevan, D., & Thomas, D. D. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-804273-1.00020-x · Cited by 5

Catalytic Function and Mechanism of Heme and Nonheme Iron(IV)–Oxo Complexes in Nature

Quesne, M. G., Faponle, A. S., Goldberg, D. P., & de Visser, S. P. (2015) · Wiley eBooks · doi:10.1002/9781118898277.ch9 · Cited by 5

Radical Ring Expansion Catalyzed by an α-Ketoglutarate-Dependent Dioxygenase in the Biosynthesis of Tropolones

Liu, M., Liu, J.-W., Bai, S., Chen, Z., Wu, Y., Du, D., Qi, X., He, X., & Hu, Y. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c11241 · Cited by 4

Enzyme Substrate Complex of the H200C Variant of Homoprotocatechuate 2,3-Dioxygenase: Mössbauer and Computational Studies

Meier, K. K., Rogers, M. S., Kovaleva, E. G., Lipscomb, J. D., Bominaar, E. L., & Münck, E. (2016) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.6b00148 · Cited by 4

Functional characterisation of Fe ( II ) and 2OG ‐dependent dioxygenase TcALKBH4 in the red flour beetle, Tribolium castaneum

Yu, R., Zhang, W., Li, Y., Tang, J., Kim, K.-C., & Li, B. (2023) · Insect Molecular Biology · doi:10.1111/imb.12865 · Cited by 4

Fe(2)OG: an integrated HMM profile-based web server to predict and analyze putative non-haem iron(II)- and 2-oxoglutarate-dependent dioxygenase function in protein sequences

Kundu, S. (2021) · BMC Research Notes · doi:10.1186/s13104-021-05477-z · Cited by 5

Binding Differences of the Peptide‐Substrate–Binding Domain of Collagen Prolyl 4‐Hydroxylases I and II for Proline‐ and Hydroxyproline‐Rich Peptides

Rahman, M. M., Sulu, R., Adediran, B., Tu, H., Salo, A. M., Murthy, S., Myllyharju, J., Wierenga, R. K., & Koski, M. K. (2025) · Proteins: Structure, Function, and Bioinformatics · doi:10.1002/prot.26839 · Cited by 3

A new family of bacterial DNA repair proteins annotated by the integration of non‐homology, distant homology and structural bioinformatic methods

Mello, L. V., & Rigden, D. J. (2012) · FEBS Letters · doi:10.1016/j.febslet.2012.09.023 · Cited by 3

Regulatory role of JMJD6 in placental development

Shen, X., Geyter, C. D., Zhang, H., & Huang, G. (2022) · Expert Reviews in Molecular Medicine · doi:10.1017/erm.2022.30 · Cited by 3

Purification, crystallization and preliminary crystallographic analysis of histone lysine demethylase NO66 fromHomo sapiens

Zhou, X., Tao, Y., Wu, M., Zhang, D., & Zang, J. (2012) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s174430911201740x · Cited by 3

Expression, purification, crystallization and preliminary X-ray analysis of a novel N-substituted branched-chain L -amino-acid dioxygenase fromBurkholderia ambifariaAMMD

Qin, H., Miyakawa, T., Nakamura, A., Xue, Y. Y., Kawashima, T., Kasahara, T., Hibi, M., Ogawa, J., & Tanokura, M. (2012) · Acta Crystallographica Section F Structural Biology and Crystallization Communications · doi:10.1107/s1744309112031508 · Cited by 3

The role of ascorbate in the regulation of HIF-1 in cancer cells

Kuiper, C. (2013) · Otago University Research Archive (University of Otago) · Cited by 2

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

Myllykoski, M., Sutinen, A., Koski, M. K., Kallio, J. P., Raasakka, A., Myllyharju, J., Wierenga, R. K., & Koivunen, P. (2020) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2020.10.25.354423 · Cited by 3

Methionine availability influences essential H3K36me3 dynamics during cell differentiationPreprint

Sun, Y., Ramesh, V., Wei, F., & Locasale, J. W. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.11.22.568331 · Cited by 4

Vitamin C is essential for proper myogenic differentiation

Kondo, Y., Sato, A., Osakabe, N., Minowa, T., Hung, Y.-L., Machida, S., & Ishigami, A. (2025) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2025.110704 · Cited by 2

Enzymatic formation of endoperoxide by Fe(II)/α-KG-dependent dioxygenase NvfI: Insight into substrate-assisted activation of the distant C–H bond and incorporation of two oxygen molecules

Yu, J., Fu, Y., Wang, B., & ZeXing, C. A. O. (2026) · CHINESE JOURNAL OF CATALYSIS (CHINESE VERSION) · doi:10.1016/s1872-2067(26)64954-6 · Cited by 2

Mechanistic Basis of Bifunctional Oxidation by a Non-Heme Fe(II)/2-Oxoglutarate-Dependent Enzyme CcTET toward N 6-Methyladenine and 5-Methylcytosine in Double-Stranded DNA

Varada, B., Rifayee, S. B. J. S., Thomas, M. G., Sommer, E., Davis, C., Waheed, S. O., Devadas, S., Kalita, S., Melayikandy, S., Karabencheva‐Christova, T. G., et al. (2026) · ACS Catalysis · doi:10.1021/acscatal.6c02591 · Cited by 4

Chemical Compounds Targeting DNA Methylation and Hydroxymethylation

Belle, R., Kawamura, A., & Arimondo, P. B. (2019) · Topics in medicinal chemistry · doi:10.1007/7355_2019_76 · Cited by 2

A big picture of the mitochondria-mediated signals: From mitochondria to organism

Acar, N. V., & Özgül, R. K. (2023) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2023.08.032 · Cited by 2

A Focus on the Proximal Tubule Dysfunction in Dent Disease Type 1

de Combiens, E., Sakhi, I. B., & Lourdel, S. (2024) · Genes · doi:10.3390/genes15091175 · Cited by 2

The Molecular Basis of DNA Demethylation

Shi, M., & Shen, L. (2017) · Cancer drug discovery and develogment/Cancer drug discovery and development · doi:10.1007/978-3-319-59786-7_3 · Cited by 2

Properties, biosynthesis, and catalytic mechanisms of hydroxy-amino-acids

daoxuan, S. U. N., Cheng, X., Gao, D. K., Xu, P., Guo, Q., Zhu, Z., Zhu, M. L., Wang, X. Y., Qin, H., & Lu, F. (2018) · IOP Conference Series Earth and Environmental Science · doi:10.1088/1755-1315/188/1/012084 · Cited by 2

Rewriting the Script: The Story of Vitamin C and the Epigenome

Huff, T. C., & Wang, G. (2019) · Springer eBooks · doi:10.1007/978-3-319-55530-0_46 · Cited by 2

TemporalGSSA: A numerically robust R-wrapper to facilitate computation of a metabolite-specific and simulation time-dependent trajectory from stochastic simulation algorithm (SSA)-generated datasets

Kundu, S. (2022) · Journal of Bioinformatics and Computational Biology · doi:10.1142/s0219720022500184 · Cited by 2

Semi-Rational Design of L-Isoleucine Dioxygenase Generated Its Activity for Aromatic Amino Acid Hydroxylation

An, J., Guan, J., & Nie, Y. (2023) · Molecules · doi:10.3390/molecules28093750 · Cited by 1

L-Ascorbic Acid in the Epigenetic Regulation of Cancer Development and Stem Cell Reprogramming

Kovina, A. P., Petrova, N. V., Razin, S. V., & Kantidze, O. L. (2020) · Acta Naturae · doi:10.32607/actanaturae.11060 · Cited by 2

HIF1α controls somitogenesis and spine development by regulating levels of intracellular oxygen in the presomitic mesodermPreprint

Anderson, M. J., Yao, Q., Laslow, B., Schipani, E., & Lewandoski, M. B. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.19.694009 · Cited by 2

A Case-Control Study of the Associations between EGLN1 Gene Polymorphisms and COPD

Li, X., Zhang, P., Yu, J., Zhang, C., Shi, Y., Wei, X., Li, H., Zhang, X., Lin, A., Yang, Z., et al. (2024) · Frontiers in Bioscience-Landmark · doi:10.31083/j.fbl2901018 · Cited by 1

Structure-Guided Engineering of 2-Oxoglutarate-Dependent Oxygenases: Principles, Case Studies, and Emerging Opportunities

Nakashima, Y. (2025) · Chemical and Pharmaceutical Bulletin · doi:10.1248/cpb.c25-00652 · Cited by 1

Inhibitors of Jumonji C-Domain Histone Demethylases

Staller, P. (2015) · Elsevier eBooks · doi:10.1016/b978-0-12-800206-3.00020-3 · Cited by 1

2-Oxoglutarate-Dependent Oxygenases of Cephalosporin Synthesis

Andersson, I., & Valegard, K. (2015) · Royal Society of Chemistry eBooks · doi:10.1039/9781782621959-00385 · Cited by 1

Targeted Therapy of IDH1-Mutated Tumors

Clark, O., & Grommes, C. (2016) · Springer eBooks · doi:10.1007/978-3-319-49864-5_10 · Cited by 1

Molecular Insights of Compromised Female Reproduction in Ruminants Under Metabolic and Nutritional Stress

Nandi, S., Tripathi, S. K., Gupta, P. S. P., & Mondal, S. (2022) · Sustainable agriculture reviews · doi:10.1007/978-3-031-07496-7_7 · Cited by 1

Molecular aspects of 2OG-Fe (II) - dioxygenases and response to abiotic stress in rice

Wamaedeesa, R. (2016) · CentAUR (University of Reading) · Cited by 1

JmjC ‐domain‐Containing Histone Demethylases

Højrup, C., Coleman, O. D., Bukowski, J., Clausen, R. P., & Kawamura, A. (2019) · Methods and principles in medicinal chemistry · doi:10.1002/9783527809257.ch11 · Cited by 1

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

Cassiano, L. M. G., Oliveira, M. S., Pioline, J., Salim, A. C. M., & Coimbra, R. S. (2022) · Research Square · doi:10.21203/rs.3.rs-1363569/v1 · Cited by 1

Mitochondrial Complex II in Cancer

Kľučková, K., Neužil, J., & Rohlena, J. (2014) · Springer eBooks · doi:10.1007/978-94-017-8984-4_4

Bio-chemical study of Nitric oxide and its effect on TET enzymes activity

Arvind, A. (2012) · Figshare

Development and Evaluation of Chemical Probes for the Study of Histone Demethylases

Marholz, L. J. (2015) · CU Scholar (University of Colorado Boulder)

Investigating Novel Biological Mechanisms of Head and Neck Cancers

Lenarduzzi, M. (2014) · TSpace (University of Toronto)

Rewriting the Script: The Story of Vitamin C and the Epigenome

Huff, T. C., & Wang, G. (2017) · Springer eBooks · doi:10.1007/978-3-319-31143-2_46-1

Mammalian O2 Sensing and Signalling

Chaplin, V. D., Barlow, A. N., & Knapp, M. J. (2017) · Royal Society of Chemistry eBooks · doi:10.1039/9781788012836-00219

Characterisation of the cellular response to defective translational termination

Ploumakis, A. (2018) · University of Birmingham Institutional Research Archive (University of Birmingham)

Nonheme mono- and dioxygenases

Ferraroni, M. (2023) · Elsevier eBooks · doi:10.1016/b978-0-12-823974-2.00028-0

Inhibition of KDM6A Decreased the Reactive Astrocytes Proliferation Induced by Hypoxic and IschemicPreprint

Feng, C., Xu, L., Liu, Q., Li, M., & Feng, X. (2023) · Research Square · doi:10.21203/rs.3.rs-3455406/v1

Functional analysis of an α-ketoglutarate-dependent non-heme iron oxygenase in fungal meroterpenoid biosynthesis

Tao, H., & Abe, I. (2024) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/bs.mie.2024.05.005

Structure of an Fe 2+ -binding-deficient mimiviral collagen lysyl hydroxylase

Chen, T., Buhlheller, C., & Guo, H. (2025) · Acta Crystallographica Section F Structural Biology Communications · doi:10.1107/s2053230x25003735

Inhibitors and degraders of epigenetic regulation in cancer

Gao, P., Kanıskan, H. Ü., & Jin, J. (2025) · Elsevier eBooks · doi:10.1016/b978-0-443-29808-0.00037-6

Redox-controlled dimerisation regulates ethylene biosynthesisPreprint

Gunawardana, D. M., Kuang, F., Kaur, S., McIvor, J. A. P., Chen, X., Yosaatmadja, Y., Sethi, A., Tang, H. Y. H., Middleditch, M., Mercadante, D., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2025.12.04.692314

Structural and Functional Validation of Pseudomonas Savastanoi Ethylene Forming Enzymes Reveals Flexibility in 2‐Oxoglutarate Binding Mode and Conformation

Sun, Y., Dhingra, S., Allen, M. D., Cheng, E. S. Z., Zhang, Z., Schofield, C. J., & Brewitz, L. (2026) · ChemBioChem · doi:10.1002/cbic.202500702

Non-classic deubiquitinase USP13 inhibits bladder cancer metastasis through destabilizing cytoplasmic KDM3A

Hu, H., Zhan, X., Xiong, Y., Yuan, R., Du, Y., Dong, Q., Li, S., Guo, B., Li, Z., Feng, J., et al. (2026) · Oncogene · doi:10.1038/s41388-026-03730-y

Implication de la protéine ClC-5 dans la physiopathologie de la maladie de Dent : analyse de mutants pathogènes et caractérisation d’un modèle de souris transgéniques

Sakhi, I. B. (2021) · doi:10.70675/e60d4b71za6a2z46f3z8d6dzaddf97c7d918

Targeting collagen biosynthesis by small molecules inhibiting the function of the peptide-substrate-binding domain of collagen prolyl 4-hydroxylases

Adediran, B., Vela‐Rodríguez, C., Murthy, S., Rahman, M. M., Wierenga, R. K., Lehtiö, L., & Koski, M. K. (2026) · Scientific Reports · doi:10.1038/s41598-026-53109-y

KDM6A loss enhances oxidative phosphorylation uncovering tissue-level convergent evolution

Cartalemi, A. A., Rosano, D., Ferrari, C., Crupi, G., Cassina, L., Gatti, G., Corigliano, F., Punzi, S., VILLANTI, I., Dupéré-Richer, D., et al. (2026) · The EMBO Journal · doi:10.1038/s44318-026-00891-0

BindingDB Entry 50002355: Targeting lysine specific demethylase 4A (KDM4A) tandem TUDOR domain - A fragment based approach.

BindingDB (2020) · UC San Diego · doi:10.7270/q2wm1h1x

BindingDB Entry 50023353: Derivatives of the Clinically Used HIF Prolyl Hydroxylase Inhibitor Desidustat Are Efficient Inhibitors of Human γ-Butyrobetaine Hydroxylase.

BindingDB (2026) · UC San Diego · doi:10.7270/q2tq66gb

BindingDB Entry 50006314: Optimisation of a triazolopyridine based histone demethylase inhibitor yields a potent and selective KDM2A (FBXL11) inhibitor.

BindingDB (2020) · UC San Diego · doi:10.7270/q2kh0rbn

BindingDB Entry 50042359: Reporter ligand NMR screening method for 2-oxoglutarate oxygenase inhibitors.

BindingDB (2013) · UC San Diego · doi:10.7270/q26q1zjv

BindingDB Entry 50044761: Ejection of structural zinc leads to inhibition of¿-butyrobetaine hydroxylase.

BindingDB (2016) · UC San Diego · doi:10.7270/q2d2207x

BindingDB Entry 50018355: Targeting histone demethylase KDM5B for cancer treatment.

BindingDB (2024) · UC San Diego · doi:10.7270/q2nk3k7p

BindingDB Entry 50047161: Docking and Linking of Fragments To Discover Jumonji Histone Demethylase Inhibitors.

BindingDB (2017) · UC San Diego · doi:10.7270/q2p84drx

BindingDB Entry 7450: Structural analysis of human KDM5B guides histone demethylase inhibitor development.

BindingDB (2016) · UC San Diego · doi:10.7270/q27p8x6k

The Dual Role of HIF Hydroxylase PHD3 in Cancer Cell Survival

Rantanen, K. (2012) · UTUPub (University of Turku)

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

Aik, W. S., Chowdhury, R., Clifton, I. J., Hopkinson, R. J., Leissing, T. M., McDonough, M. A., Nowak, R. P., Schofield, C. J., & Walport, L. J. (2015) · Royal Society of Chemistry eBooks · doi:10.1039/9781782621959-00059 · Cited by 52

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

Hewitson, K. S., Granatino, N., Welford, R. W. D., McDonough, M. A., & Schofield, C. J. (2005) · Philosophical Transactions of the Royal Society A Mathematical Physical and Engineering Sciences · doi:10.1098/rsta.2004.1540 · Cited by 63

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

Clifton, I. J., McDonough, M. A., Ehrismann, D., Kershaw, N. J., Granatino, N., & Schofield, C. J. (2006) · Journal of Inorganic Biochemistry · doi:10.1016/j.jinorgbio.2006.01.024 · Cited by 444

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

Aik, W. S., McDonough, M. A., Thalhammer, A., Chowdhury, R., & Schofield, C. J. (2012) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2012.10.001 · Cited by 219

Structural Basis for Divergent Reaction Outcomes in Iron(II)/2OG‐dependent Oxygenases

Boal, A. K. (2016) · The FASEB Journal · doi:10.1096/fasebj.30.1_supplement.501.3