2-Oxoglutarate-Dependent Oxygenases

Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2 tension.

Wang, G. L., Jiang, B. H., Rue, E. A., & Semenza, G. L. (1995) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.92.12.5510 · Cited by 6,212

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

Targeting of HIF-α to the von Hippel-Lindau Ubiquitylation Complex by O 2 -Regulated Prolyl Hydroxylation

Jaakkola, P., Mole, D. R., Tian, Y.-M., Wilson, M. I., Gielbert, J., Gaskell, S. J., Kriegsheim, A. V., Hebestreit, H. F., Mukherji, M., Schofield, C. J., et al. (2001) · Science · doi:10.1126/science.1059796 · Cited by 5,535

HIFα Targeted for VHL-Mediated Destruction by Proline Hydroxylation: Implications for O 2 Sensing

Ivan, M., Kondo, K., Yang, H., Kim, W., Valiando, J., Ohh, M., Salic, A., Asara, J. M., Lane, W. S., & Kaelin Jr., W. G. (2001) · Science · doi:10.1126/science.1059817 · Cited by 4,735

Collagen Structure and Stability

Shoulders, M. D., & Raines, R. T. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.77.032207.120833 · Cited by 3,923

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

C. elegans EGL-9 and mammalian homologs define a family of dioxygenases that regulate HIF by prolyl hydroxylation

Epstein, A. C. R., Gleadle, J. M., McNeill, L. A., Hewitson, K. S., O'Rourke, J., Mole, D. R., Mukherji, M., Metzen, E., Wilson, M. I., Dhanda, A., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00507-4 · Cited by 3,333

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

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

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

Proteolysis of a histone acetyl reader, ATAD2, induces chemoresistance of cancer cells under severe hypoxia by inhibiting cell cycle progression in S phase

Haitani, T., Kobayashi, M., Koyasu, S., Akamatsu, S., Suwa, T., Onodera, Y., Nam, J., Phuong, N. T. L., Menju, T., Date, H., et al. (2021) · Cancer Letters · doi:10.1016/j.canlet.2021.12.028 · Cited by 16

An Unusual Oxidative Rearrangement Catalyzed by a Divergent Member of the 2‐Oxoglutarate‐Dependent Dioxygenase Superfamily during Biosynthesis of Dehydrofosmidomycin

Parkinson, E. I., Lakkis, H. G., Alwali, A. A., Metcalf, M. E., Modi, R., & Metcalf, W. W. (2022) · Angewandte Chemie International Edition · doi:10.1002/anie.202206173 · Cited by 15

A comparative view on vitamin C effects on αβ- versus γδ T-cell activation and differentiation

Peters, C., Kouakanou, L., & Kabelitz, D. (2020) · Journal of Leukocyte Biology · doi:10.1002/jlb.1mr1219-245r · Cited by 16

TET-dioxygenase deficiency in oncogenesis and its targeting for tumor-selective therapeutics

Guan, Y., Hasipek, M., Tiwari, A. D., Maciejewski, J. P., & Jha, B. K. (2020) · Seminars in Hematology · doi:10.1053/j.seminhematol.2020.12.002 · Cited by 15

Micro but mighty—Micronutrients in the epigenetic regulation of adaptive immune responses*

Chen, H., Hsu, M., & Lio, C. J. (2021) · Immunological Reviews · doi:10.1111/imr.13045 · Cited by 17

Revealing the nature of the second branch point in the catalytic mechanism of the Fe( ii )/2OG-dependent ethylene forming enzyme

Rifayee, S. B. J. S., Thomas, M. G., & Christov, C. Z. (2025) · Chemical Science · doi:10.1039/d4sc08378d · Cited by 14

Structural bioinformatics enhances the interpretation of somatic mutations in KDM6A found in human cancers

Chi, Y., Stodola, T. J., de Assuncao, T. M., Leverence, E. N., Smith, B. C., Volkman, B. F., Mathison, A., Lomberk, G. A., Zimmermann, M. T., & Urrutia, R. A. (2022) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2022.04.028 · Cited by 15

MYC overrides HIF-1α to regulate proliferating primary cell metabolism in hypoxia

Copeland, C. A., Olenchock, B. A., Ziehr, D. R., McGarrity, S., Leahy, K., Young, J. D., Loscalzo, J., & Oldham, W. M. (2023) · eLife · doi:10.7554/elife.82597 · Cited by 12

Structural basis for binding of the renal carcinoma target hypoxia‐inducible factor 2α to prolyl hydroxylase domain 2

Figg, W. D., Fiorini, G., Chowdhury, R., Nakashima, Y., Tumber, A., McDonough, M. A., & Schofield, C. J. (2023) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.26541 · Cited by 15

Unraveling the role of cytochrome P450 enzymes in oleanane triterpenoid biosynthesis in arjuna tree

Srivastava, G., Vyas, P., Kumar, A., Singh, A., Bhargav, P., Dinday, S., & Ghosh, S. (2024) · The Plant Journal · doi:10.1111/tpj.16942 · Cited by 14

Chemical tools for probing histidine modifications

Bilgin, N., Hintzen, J. C. J., & Mecinović, J. (2025) · Chemical Communications · doi:10.1039/d4cc06586g · Cited by 16

Structural Insight into the Catalytic Mechanism of the Endoperoxide Synthase FtmOx1

Wu, L., Wang, Z., Cen, Y., Wang, B., & Zhou, J. (2021) · Angewandte Chemie · doi:10.1002/ange.202112063 · Cited by 14

Lysosome-targeted cyclometalated iridium(III) complexes: JMJD inhibition, dual induction of apoptosis, and autophagy

Lu, J., Ma, X.-R., Xie, K. M., Chen, M., Huang, B., Li, R., & Ye, R. (2022) · Metallomics · doi:10.1093/mtomcs/mfac068 · Cited by 14

Unraveling the Mechanism of the Oxidative C–C Bond Coupling Reaction Catalyzed by Deoxypodophyllotoxin Synthase

Su, Y., & Lai, W. (2024) · Inorganic Chemistry · doi:10.1021/acs.inorgchem.4c01263 · Cited by 13

Probing Ferryl Reactivity in a Nonheme Iron Oxygenase Using an Expanded Genetic Code

Hardy, F. J., Quesne, M. G., Gérard, E. F., Zhao, J., Ortmayer, M., Taylor, C. J., Ali, H. S., Slater, J. W., Levy, C., Heyes, D. J., et al. (2024) · ACS Catalysis · doi:10.1021/acscatal.4c02365 · Cited by 13

Establishing a coumarin production platform by protein and metabolic engineering

Xie, C., An, N., Zhou, L., Shen, X., Wang, J., Yan, Y., Sun, X., & Yuan, Q. (2024) · Metabolic Engineering · doi:10.1016/j.ymben.2024.09.009 · Cited by 13

Engineering the Reaction Pathway of a Non-heme Iron Oxygenase Using Ancestral Sequence Reconstruction

Yang, D., Chiang, C.-H., Wititsuwannakul, T., Brooks, C. L., Zimmerman, P. M., & Narayan, A. R. H. (2024) · Journal of the American Chemical Society · doi:10.1021/jacs.4c08420 · Cited by 13

Comparison of a Nonheme Iron Cyclopropanase with a Homologous Hydroxylase Reveals Mechanistic Features Associated with Distinct Reaction Outcomes

Zheng, Y., Li, X., Cha, L., Paris, J. C., Michael, C., Ushimaru, R., Ogasawara, Y., Abe, I., Guo, Y., & Chang, W. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.4c17741 · Cited by 13

Aboral cell types of Clytia and coral larvae have shared features and link taurine to the regulation of settlement

Ramon-Mateu, J., Ferraioli, A., Teixidó, N., Domart-Coulon, I. J., Houliston, E., & Copley, R. R. (2025) · Science Advances · doi:10.1126/sciadv.adv1159 · Cited by 15

Skp1 isoforms are differentially modified by a dual function prolyl 4-hydroxylase/N-acety lglucosaminyltransferase in a plant pathogen

van der Wel, H., Gas‐Pascual, E., & West, C. M. (2019) · Glycobiology · doi:10.1093/glycob/cwz049 · Cited by 13

A human protein hydroxylase that accepts D-residues

Choi, H., Hardy, A., Leissing, T. M., Chowdhury, R., Nakashima, Y., Ge, W., Markoulides, M. S., Scotti, J. S., Gerken, P. A., Thorbjørnsrud, H. V., et al. (2020) · Communications Chemistry · doi:10.1038/s42004-020-0290-5 · Cited by 13

Human aspartyl (asparaginyl) hydroxylase. A multifaceted enzyme with broad intra- and extra-cellular activity

Greve, J. M., Pinkham, A. M., & Cowan, J. A. (2021) · Metallomics · doi:10.1093/mtomcs/mfab044 · Cited by 13

Functional Characterization of a 2OGD Involved in Abietane-Type Diterpenoids Biosynthetic Pathway in Salvia miltiorrhiza

Hu, Z. M., Ren, L., Bu, J., Liu, X., Li, Q., Guo, W., Ma, Y., Wang, J., Chen, T., Wang, L., et al. (2022) · Frontiers in Plant Science · doi:10.3389/fpls.2022.947674 · Cited by 13

Oxygen-dependent regulation of E3(SCF)ubiquitin ligases and a Skp1-associated JmjD6 homolog in development of the social amoeba Dictyostelium

Boland, A. W., Gas‐Pascual, E., Nottingham, B. L., van der Wel, H., Daniel, N. G., Sheikh, M. O., Schafer, C. M., & West, C. M. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102305 · Cited by 11

Dynamic metal coordination controls chemoselectivity in a radical halogenase

Kissman, E., Kipouros, I., Slater, J., Stone, E., Yang, A. Y., Braun, A., Ensberg, A. R., Whitten, A. M., Chatterjee, K., Bogacz, I., et al. (2025) · Nature Chemical Biology · doi:10.1038/s41589-025-02077-x · Cited by 9

Exploring links between 2‐oxoglutarate‐dependent oxygenases and Alzheimer's disease

Liu, H., Xie, Y., Wang, X., Abboud, M. I., Ma, C., Ge, W., & Schofield, C. J. (2022) · Alzheimer s & Dementia · doi:10.1002/alz.12733 · Cited by 14

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

Sánchez-Eguía, B. N., Serrano‐Plana, J., Anna Company, & Costas, M. (2020) · Chemical Communications · doi:10.1039/d0cc05942k · Cited by 12

Impaired protein hydroxylase activity causes replication stress and developmental abnormalities in humans

Fletcher, S. C., Hall, C., Kennedy, T. J., Pajusalu, S., Wojcik, M. H., Boora, U., Li, C., Oja, K. T., Hendrix, E., Westrip, C. A. E., et al. (2023) · Journal of Clinical Investigation · doi:10.1172/jci152784 · Cited by 11

Substrate-Dependent Mechanism Switch in the Desaturation Reactions of the Mononuclear Nonheme Iron Enzyme PtlD

Chen, L., Deng, Q., Ma, T., Gu, J., Yang, J., Zhang, X., Zou, Y., Deng, Z., Chen, L., & Zhao, C. (2024) · ACS Catalysis · doi:10.1021/acscatal.4c00757 · Cited by 11

α-Ketoglutarate-Dependent Dioxygenase-Catalyzed Macrocyclization in RiPPs

Xia, Y., Shi, Y., Xiao, Z., Xie, X., Wang, B., Yao, H., & Wang, H. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c07332 · Cited by 11

A three-component monooxygenase from Rhodococcus wratislaviensis may expand industrial applications of bacterial enzymes

Hibi, M., Fukuda, D., Kenchu, C., Nojiri, M., Hara, R., Takeuchi, M., Aburaya, S., Aoki, W., Mizutani, K., Yasohara, Y., et al. (2021) · Communications Biology · doi:10.1038/s42003-020-01555-3 · Cited by 11

Epigenetic and metabolic interplay in cutaneous squamous cell carcinoma

Pacella, G., & Capell, B. C. (2021) · Experimental Dermatology · doi:10.1111/exd.14354 · Cited by 11

Regulatory Role of N6-methyladenosine (m6A) Modification in Osteosarcoma

Zhang, Y., Wang, Y., Ying, L., Tao, S., Shi, M., Lin, P., Wang, Y., & Han, B. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2021.683768 · Cited by 10

Structural analysis of the 2-oxoglutarate binding site of the circadian rhythm linked oxygenase JMJD5

Islam, M. S., Markoulides, M. S., Chowdhury, R., & Schofield, C. J. (2022) · Scientific Reports · doi:10.1038/s41598-022-24154-0 · Cited by 11

New tricks for an old drug

Nelson, B. S., Kremer, D. M., & Lyssiotis, C. A. (2018) · Nature Chemical Biology · doi:10.1038/s41589-018-0137-x · Cited by 11

The functional importance of bacterial oxidative phosphonate pathways

Pallitsch, K., & Zechel, D. L. (2023) · Biochemical Society Transactions · doi:10.1042/bst20220479 · Cited by 10

Study and design of amino acid-based radical enzymes using unnatural amino acids

Yuan, F., Su, B., Yu, Y., & Wang, J. (2023) · RSC Chemical Biology · doi:10.1039/d2cb00250g · Cited by 10

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 11

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

Corner, T. P., Tumber, A., Salah, E., Jabbary, M., Nakashima, Y., Schnaubelt, L. I., Basak, S., Alshref, F. M., Brewitz, L., & Schofield, C. J. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c00586 · Cited by 10

Enzymatic Characterization of In Vitro Activity of RNA Methyltransferase PCIF1 on DNA

Yu, D., Zhou, J., Chen, Q., Wu, T., Blumenthal, R., Zhang, X., & Cheng, X. (2022) · Biochemistry · doi:10.1021/acs.biochem.2c00134 · Cited by 10

Functional Repercussions of Hypoxia-Inducible Factor-2α in Idiopathic Pulmonary Fibrosis

Torres-Soria, A. K., Romero, Y., Balderas-Martínez, Y. I., Velázquez‐Cruz, R., Espíndola, L. M. T., Camarena, Á., Flores‐Soto, E., Solís‐Chagoyán, H., Ruiz, V., Carlos‐Reyes, Á., et al. (2022) · Cells · doi:10.3390/cells11192938 · Cited by 11

Functional characterization of 2-oxoglutarate-dependent dioxygenase gene family in chickpea

Saxena, S., Pal, G., & Pandey, A. K. (2023) · Plant Science · doi:10.1016/j.plantsci.2023.111836 · Cited by 10

Using NMR to Monitor TET-Dependent Methylcytosine Dioxygenase Activity and Regulation

Treadway, C. J., Boyer, J. A., Yang, S., Yang, H., Liu, M., Li, Z., Cheng, M., Marzluff, W. F., Ye, D., Xiong, Y., et al. (2024) · ACS Chemical Biology · doi:10.1021/acschembio.3c00619 · Cited by 10

Elucidating the Role of O 2 Uncoupling for the Adaptation of Bacterial Biodegradation Reactions Catalyzed by Rieske Oxygenases

Bopp, C. E., Bernet, N. M., Meyer, F., Khan, R. A., Robinson, S. L., Kohler, H. E., Buller, R., & Hofstetter, T. B. (2024) · ACS Environmental Au · doi:10.1021/acsenvironau.4c00016 · Cited by 8

A Nonheme FeII/2-Oxoglutarate-Dependent Oxygenase Catalyzes a Double Bond Migration within a Dimethylallyl Moiety Accompanied by Hydroxylation

Ran, H., Wohlgemuth, V., Xie, X., & Li, S. (2018) · ACS Chemical Biology · doi:10.1021/acschembio.8b00588 · Cited by 10

Isolation and characterization of collagen type I crosslink from skin: high-resolution NMR reveals diastereomers of hydroxylysinonorleucine crosslink

Naffa, R., Edwards, P. J. B., & Norris, G. E. (2019) · Amino Acids · doi:10.1007/s00726-019-02708-3 · Cited by 10

A chromatin perspective on metabolic and genotoxic impacts on hematopoietic stem and progenitor cells

Yang, Z., & Jiang, H. (2020) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-020-03522-x · Cited by 10

Inhibition of JMJD6 by 2‐Oxoglutarate Mimics

Islam, M. S., Thinnes, C. C., Holt‐Martyn, J. P., Chowdhury, R., McDonough, M. A., & Schofield, C. J. (2021) · ChemMedChem · doi:10.1002/cmdc.202100398 · Cited by 9

Psychology and Pathophysiological Outcomes of Eating

Takada, A., & Himmerich, H. (2021) · IntechOpen eBooks · doi:10.5772/intechopen.92917 · Cited by 10

BBOX1 promotes triple-negative breast cancer progression by controlling IP3R3 stability

Liao, C., & Zhang, Q. (2020) · Molecular & Cellular Oncology · doi:10.1080/23723556.2020.1813526 · Cited by 10

The archaeal non-heme iron-containing Sulfur Oxygenase Reductase

Ferreira, P., Fernandes, P. A., & Ramos, M. J. (2021) · Coordination Chemistry Reviews · doi:10.1016/j.ccr.2021.214358 · Cited by 9

XMECP: Reaching State-of-the-Art MECP Optimization in Multiscale Complex Systems

Xu, J., Hao, J., Bu, C., Meng, Y., Han, X., Zhang, M., & Li, C. (2024) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.4c00033 · Cited by 9

The metabolic baton: conducting the dance of N6-methyladenosine writing and erasing

Rabelo-Fernández, R. J., Yuen, M., & Batista, P. J. (2024) · Current Opinion in Genetics & Development · doi:10.1016/j.gde.2024.102206 · Cited by 9

Mechanistic insights into the role of RNA demethylase ALKBH5 in malignant tumor therapy

An, R., Shao, Y., & Gu, W. (2025) · Journal of Translational Medicine · doi:10.1186/s12967-025-06938-w · Cited by 10

Revealing the catalytic mechanism of the Fe(II)/2-oxoglutarate-dependent human epigenetic modifying enzyme ALKBH5

Cherilakkudy, F. H., Thomas, M. G., Varghese, A., Waheed, S. O., Krishnan, A., Venditti, V., Schofield, C. J., Li, D., Christov, C. Z., & Karabencheva‐Christova, T. G. (2025) · Cell Reports Physical Science · doi:10.1016/j.xcrp.2025.102779 · Cited by 9

Role of prolyl hydroxylase domain proteins in bone metabolism

Wolf, D., Muralidharan, A., & Mohan, S. (2022) · Osteoporosis and Sarcopenia · doi:10.1016/j.afos.2022.03.001 · Cited by 10

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

Non-Heme Mono-Iron Enzymes: Co-Substrate-Dependent Dioxygen Activation

Guo, Y., Chang, W., Li, J., & Davidson, M. (2020) · Elsevier eBooks · doi:10.1016/b978-0-12-409547-2.14820-6 · Cited by 9

Carbon Monoxide is an Inhibitor of HIF Prolyl Hydroxylase Domain 2

Mbenza, N. M., Nasarudin, N., Vadakkedath, P. G., Patel, K. D., Ismail, A. Z., Hanif, M., Wright, L. J., Sarojini, V., Hartinger, C. G., & Leung, I. K. H. (2021) · ChemBioChem · doi:10.1002/cbic.202100181 · Cited by 9

Factor inhibiting HIF can catalyze two asparaginyl hydroxylations in VNVN motifs of ankyrin fold proteins

Leissing, T. M., Hardy, A., Chan, H. F., Wang, Y., Tumber, A., Chowdhury, R., Feng, T., Coleman, M. L., Cockman, M. E., Kramer, H., et al. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102020 · Cited by 10

Kinetic Studies on the 2-Oxoglutarate/Fe(II)-Dependent Nucleic Acid Modifying Enzymes from the AlkB and TET Families

Peng, Z., Ma, J., Christov, C. Z., Karabencheva‐Christova, T. G., Lehnert, N., & Li, D. (2023) · DNA · doi:10.3390/dna3020005 · Cited by 9

Nickel Toxicity, Regulation, and Resistance in Bacteria

Macomber, L., & Hausinger, R. P. (2016) · doi:10.1002/9781119004813.ch110 · 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

JmjC catalysed histone H2a N-methyl arginine demethylation and C4-arginine hydroxylation reveals importance of sequence-reactivity relationships

Bonnici, J., Oueini, R., Salah, E., Johansson, C., Pires, E., Abboud, M. I., Dawber, R. S., Tumber, A., Rabe, P., Saraç, H., et al. (2024) · Communications Biology · doi:10.1038/s42003-024-07183-5 · Cited by 8

Copper-Dependent Hydroxylation Catalyzed by the DUF3328 Enzyme CctR

Seshadri, K., Chiang, C.-Y., Nagasawa, K. K., & Tang, Y. (2025) · Organic Letters · doi:10.1021/acs.orglett.5c02280 · Cited by 8

Diverging Reaction Pathways and Key Intermediates in Ethylene Forming Enzyme

Wang, C., & Sayfutyarova, E. R. (2025) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.5c02007 · Cited by 8

Manipulating Gibberellin Control Over Growth and Fertility as a Possible Target for Managing Wild Radish Weed Populations in Cropping Systems

Groszmann, M., Chandler, P. M., Ross, J. J., & Swain, S. M. (2020) · Frontiers in Plant Science · doi:10.3389/fpls.2020.00190 · Cited by 9

Formate dehydrogenase contributes to the early Arabidopsis thaliana responses against Xanthomonas campestris pv campestris infection

Marzorati, F., Vigani, G., Morandini, P. A., & Murgia, I. (2021) · Physiological and Molecular Plant Pathology · doi:10.1016/j.pmpp.2021.101633 · Cited by 8

Identification of Disease-Related 2-Oxoglutarate/Fe (II)-Dependent Oxygenase Based on Reduced Amino Acid Cluster Strategy

Zhou, J., Bo, S., Wang, H., Zheng, L., Liang, P., & Zuo, Y. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.707938 · Cited by 8

Nitric oxide-based regulation of metabolism: Hints from TRAP1 and SIRT3 crosstalk

Faienza, F., Rasola, A., & Filomeni, G. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2022.942729 · Cited by 7

A survey of C–C bond formation strategies and mechanism deployed by iron-containing enzymes in natural products

Michael, C., & Chang, W. (2024) · Tetrahedron · doi:10.1016/j.tet.2024.134084 · Cited by 7

Effects of Clinical Mutations in the Second Coordination Sphere and Remote Regions on the Catalytic Mechanism of Non‐Heme Fe(II)/2‐Oxoglutarate‐Dependent Aspartyl Hydroxylase AspH

Krishnan, A., Waheed, S. O., Melayikandy, S., LaRouche, C., Paik, M., Schofield, C. J., & Karabencheva‐Christova, T. G. (2024) · ChemPhysChem · doi:10.1002/cphc.202400303 · Cited by 7

Evidence human FTO catalyses hydroxylation of N6-methyladenosine without direct formation of a demethylated product contrasting with ALKBH5/2/3 and bacterial AlkB

Kaur, S., Maheswaran, P., Kaur, S., Lai, Y., Salah, E., Zhang, D., Shishodia, S., Schofield, C. J., & Aik, W. S. (2025) · Nucleic Acids Research · doi:10.1093/nar/gkaf813 · Cited by 7

α-Ketoglutaric acid as a promising platform chemical for sustainable bio-based industries

Opsommer, L.-T. J. D., Schalck, T., Yogiswara, S., Verstrepen, K. J., Michiels, J. J., & Sels, B. F. (2025) · Chemical Society Reviews · doi:10.1039/d4cs01125b · Cited by 9

Refining the Substrate-Cofactor Disposition Model of Hyoscyamine 6β-Hydroxylase Catalysis Using Hyoscyamine Analogs

Ushimaru, R., Chen, R., Fan, P., Liu, X., Ruszczycky, M. W., & Liu, H. (2025) · Journal of the American Chemical Society · doi:10.1021/jacs.5c17484 · Cited by 7

Glutamine Homeostasis and Its Role in the Adaptive Strategies of the Blind Mole Rat, Spalax

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