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 · 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

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 · see citing works

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 · see citing works

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 · 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

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 · see citing works

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 · 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

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

A nuclear factor induced by hypoxia via de novo protein synthesis binds to the human erythropoietin gene enhancer at a site required for transcriptional activation

Semenza, G. L., & Wang, G. L. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.12.5447 · Cited by 2,617 · see citing works

A conserved family of prolyl-4-hydroxylases that modify HIF

Bruick, R. K., & McKnight, S. L. (2001) · Science · doi:10.1126/science.1066373 · Cited by 2,549 · see citing works

Dioxygen Activation at Mononuclear Nonheme Iron Active Sites: Enzymes, Models, and Intermediates

Costas, M., Mehn, M. P., Jensen, M. P., & QUE, L. J. (2004) · Chemical Reviews · doi:10.1021/cr020628n · Cited by 2,478 · see citing works

FIH-1 is an asparaginyl hydroxylase enzyme that regulates the transcriptional activity of hypoxia-inducible factor

Lando, D., Peet, D. J., Gorman, J. J., Whelan, D. A., Whitelaw, M. L., & Bruick, R. K. (2002) · Genes & Development · doi:10.1101/gad.991402 · Cited by 1,550 · see citing works

Biologically inspired oxidation catalysis

QUE, L. J., & Tolman, W. B. (2008) · Nature · doi:10.1038/nature07371 · Cited by 1,423 · see citing works

The genes of the Green Revolution

Hedden, P. (2002) · Trends in Genetics · doi:10.1016/s0168-9525(02)00009-4 · Cited by 1,332 · see citing works

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 · see citing works

Insulator dysfunction and oncogene activation in IDH mutant gliomas

Flavahan, W. A., Drier, Y., Liau, B. B., Gillespie, S. M., Venteicher, A. S., Stemmer-Rachamimov, A. O., Suvà, M. L., & Bernstein, B. E. (2016) · Nature · doi:10.1038/nature16490 · Cited by 1,288 · see citing works

Dimerization, DNA Binding, and Transactivation Properties of Hypoxia-inducible Factor 1

Jiang, B.-H., Rue, E., Wang, G. L., Roe, R., & Semenza, G. L. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.30.17771 · Cited by 1,106 · see citing works

G ROWTH R ETARDANTS : Effects on Gibberellin Biosynthesis and Other Metabolic Pathways

Rademacher, W. (2000) · Annual Review of Plant Physiology and Plant Molecular Biology · doi:10.1146/annurev.arplant.51.1.501 · Cited by 1,098 · 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

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 · 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

Transformation by the (R)-enantiomer of 2-hydroxyglutarate linked to EGLN activation

Koivunen, P., Lee, S., Duncan, C. G., Lopez, G., Lu, G., Ramkissoon, S., Losman, J. A., Joensuu, P., Bergmann, U., Gross, S., et al. (2012) · Nature · doi:10.1038/nature10898 · Cited by 727 · see citing works

Hypoxia-inducible factor (HIF) asparagine hydroxylase is identical to factor inhibiting HIF (FIH) and is related to the cupin structural family

Hewitson, K. S., McNeill, L. A., Riordan, M. V., Tian, Y.-M., Bullock, A. N., Welford, R. W., Elkins, J. M., Oldham, N. J., Bhattacharya, S., Gleadle, J. M., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.c200273200 · Cited by 719 · see citing works

Treatment of hereditary tyrosinaemia type I by inhibition of 4-hydroxyphenylpyruvate dioxygenase

LINDSTEDT, S. (1992) · The Lancet · doi:10.1016/0140-6736(92)92685-9 · Cited by 631 · see citing works

The metabolite α-ketoglutarate extends lifespan by inhibiting ATP synthase and TOR

Chin, R., Fu, X., Pai, M. Y., Vergnes, L., Hwang, H., Deng, G., Diep, S., Lomenick, B., Meli, V. S., Monsalve, G. C., et al. (2014) · Nature · doi:10.1038/nature13264 · Cited by 608 · see citing works

JARID2 regulates binding of the Polycomb repressive complex 2 to target genes in ES cells

Pasini, D., Cloos, P. A., Walfridsson, J., Olsson, L., Bukowski, J., Johansen, J. V., Bak, M., Tommerup, N., Rappsilber, J., & Helin, K. (2010) · Nature · doi:10.1038/nature08788 · Cited by 562 · see citing works

Jarid2/Jumonji Coordinates Control of PRC2 Enzymatic Activity and Target Gene Occupancy in Pluripotent Cells

Peng, J. C., Valouev, A., Swigut, T., Zhang, J., Zhao, Y., Sidow, A., & Wysocka, J. (2009) · Cell · doi:10.1016/j.cell.2009.12.002 · Cited by 533 · see citing works

The Discovery of 5‐Formylcytosine in Embryonic Stem Cell DNA

Pfaffeneder, T., Hackner, B., Truß, M., Münzel, M., Müller, M., Deiml, C. A., Hagemeier, C., & Carell, T. (2011) · Angewandte Chemie International Edition · doi:10.1002/anie.201103899 · Cited by 483 · see citing works

Crystal Structure of TET2-DNA Complex: Insight into TET-Mediated 5mC Oxidation

Hu, L., Li, Z., Cheng, J., Rao, Q., Gong, W., Liu, M., Shi, Y. G., Zhu, J., Wang, P., & Xu, Y. (2013) · Cell · doi:10.1016/j.cell.2013.11.020 · Cited by 448 · see citing works

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 · see citing works

An E3 ligase possessing an iron-responsive hemerythrin domain is a regulator of iron homeostasis

Salahudeen, A. A., Thompson, J. W., Ruiz, J. C., Ma, H.-W., Kinch, L. N., Li, Q., Grishin, N. V., & Bruick, R. K. (2009) · Science · doi:10.1126/science.1176326 · Cited by 432 · see citing works

Reversal of DNA alkylation damage by two human dioxygenases

Duncan, T., Trewick, S. C., Koivisto, P., Bates, P. A., Lindahl, T. L., & Sedgwick, B. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.262589799 · Cited by 414 · see citing works

Evidence for Hydrogen Abstraction from C1 of Taurine by the High-Spin Fe(IV) Intermediate Detected during Oxygen Activation by Taurine:α-Ketoglutarate Dioxygenase (TauD)

Price, J. C., Barr, E. W., Glass, T. E., Krebs, C., & Bollinger, J. M., Jr. (2003) · Journal of the American Chemical Society · doi:10.1021/ja037400h · Cited by 403 · see citing works

Inhibition of 2-oxoglutarate dependent oxygenases

Rose, N. R., McDonough, M. A., King, O. N. F., Kawamura, A., & Schofield, C. J. (2011) · Chemical Society Reviews · doi:10.1039/c0cs00203h · Cited by 395 · 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 & Molecular Biology · doi:10.1038/nsmb.1753 · Cited by 389 · see citing works

Crystal structure of the non-haem iron halogenase SyrB2 in syringomycin biosynthesis

Blasiak, L. C., Vaillancourt, F. H., Walsh, C. T., & Drennan, C. L. (2006) · Nature · doi:10.1038/nature04544 · Cited by 385 · see citing works

An inhibitor of KDM5 demethylases reduces survival of drug-tolerant cancer cells

Vinogradova, M. V., Gehling, V. S., Gustafson, A. E., Arora, S., Tindell, C., WILSON, C. A., Williamson, K. E., Guler, G. D., Gangurde, P., Manieri, W., et al. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2085 · Cited by 358 · see citing works

Signalling hypoxia by HIF hydroxylases

Schofield, C. J., & Ratcliffe, P. J. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.08.111 · Cited by 343 · see citing works

Structure of a cephalosporin synthase

Valegard, K., van Scheltinga, A. C. T., Lloyd, M. D., Hara, T., Ramaswamy, S., Anastassis Perrakis, A., Thompson, A., Lee, H., Baldwin, J. E., Schofield, C. J., et al. (1998) · Nature · doi:10.1038/29575 · Cited by 337 · see citing works

Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity

Ng, S. S., Kavanagh, K. L., McDonough, M. A., Butler, D. S., Pilka, E. S., Liénard, B. M. R., Bray, J. E., Savitsky, P. A., Gileadi, O., von Delft, F., et al. (2007) · Nature · doi:10.1038/nature05971 · Cited by 329 · see citing works

Nucleic Acid Modifications in Regulation of Gene Expression

Chen, K., Zhao, B. S., & He, C. (2016) · Cell chemical biology · doi:10.1016/j.chembiol.2015.11.007 · Cited by 285 · see citing works

Structural studies on human 2-oxoglutarate dependent oxygenases

McDonough, M. A., Loenarz, C., Chowdhury, R., Clifton, I. J., & Schofield, C. J. (2010) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2010.08.006 · Cited by 280 · see citing works

Physiological and biochemical aspects of hydroxylations and demethylations catalyzed by human 2-oxoglutarate oxygenases

Loenarz, C., & Schofield, C. J. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.07.002 · Cited by 274 · see citing works

Formation of cyanide from carbon 1 of 1-aminocyclopropane-1-carboxylic acid during its conversion to ethylene

Peiser, G. D., Wang, T.-T., Hoffman, N. E., Yang, S. F., Liu, H., & Walsh, C. T. (1984) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.81.10.3059 · Cited by 270 · see citing works

A stereochemical concept for the catalytic mechanism of prolylhydroxylase

Hanauske-Abel, H. M., & Günzler, V. (1982) · Journal of Theoretical Biology · doi:10.1016/0022-5193(82)90320-4 · Cited by 267 · see citing works

Structural origins of the selectivity of the trifunctional oxygenase clavaminic acid synthase.

Harlos, K., Schofield, C. J., Zhang, Z., Ren, J., STAMMERS, D. K., & Baldwin, J. E. (2000) · Nature Structural Biology · doi:10.1038/72398 · Cited by 260 · see citing works

Structural Basis for Binding of Hypoxia-Inducible Factor to the Oxygen-Sensing Prolyl Hydroxylases

Chowdhury, R., McDonough, M. A., Mecinović, J., Loenarz, C., Flashman, E., Hewitson, K. S., Domene, C., & Schofield, C. J. (2009) · Structure · doi:10.1016/j.str.2009.06.002 · Cited by 241 · see citing works

Arginine demethylation is catalysed by a subset of JmjC histone lysine demethylases

Walport, L. J., Hopkinson, R. J., Chowdhury, R., Schiller, R., Ge, W., Kawamura, A., & Schofield, C. J. (2016) · Nature Communications · doi:10.1038/ncomms11974 · Cited by 236 · see citing works

The hypoxia‐inducible transcription factor pathway regulates oxygen sensing in the simplest animal, Trichoplax adhaerens

Loenarz, C., Coleman, M. L., Boleininger, A., Schierwater, B., Holland, P. W. H., Ratcliffe, P. J., & Schofield, C. J. (2010) · EMBO Reports · doi:10.1038/embor.2010.170 · Cited by 235 · see citing works

X-ray Crystal Structure of Escherichia coli Taurine/α-Ketoglutarate Dioxygenase Complexed to Ferrous Iron and Substrates,

Elkins, J. M., Ryle, M. J., Clifton, I. J., Hotopp, J. C. D., Lloyd, J. S., Burzlaff, N. I., Baldwin, J. E., Hausinger, R. P., & Roach, P. L. (2002) · Biochemistry · doi:10.1021/bi016014e · Cited by 225 · see citing works

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 214 · see citing works

The enzymes of β-lactam biosynthesis

Hamed, R. B., Castellanos, J. R. G., Henry, L., Ducho, C., McDonough, M. A., & Schofield, C. J. (2012) · Natural Product Reports · doi:10.1039/c2np20065a · Cited by 208 · see citing works

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

Thinnes, C. C., England, K. S., Kawamura, A., Chowdhury, R., Schofield, C. J., & Hopkinson, R. J. (2014) · Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms · doi:10.1016/j.bbagrm.2014.05.009 · Cited by 195 · see citing works

Halogenation of Unactivated Carbon Centers in Natural Product Biosynthesis: Trichlorination of Leucine during Barbamide Biosynthesis

Galonić, D. P., Vaillancourt, F. H., & Walsh, C. T. (2006) · Journal of the American Chemical Society · doi:10.1021/ja060151n · Cited by 194 · see citing works

Mechanisms of human histone and nucleic acid demethylases

Walport, L. J., Hopkinson, R. J., & Schofield, C. J. (2012) · Current Opinion in Chemical Biology · doi:10.1016/j.cbpa.2012.09.015 · Cited by 194 · see citing works

Recent Progress in Histone Demethylase Inhibitors

McAllister, T. E., England, K. S., Hopkinson, R. J., Brennan, P. E., Kawamura, A., & Schofield, C. J. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01758 · Cited by 191 · see citing works

Repair deficient mice reveal mABH2 as the primary oxidative demethylase for repairing 1meA and 3meC lesions in DNA

Ringvoll, J., Nordstrand, L. M., Vågbø, C. B., Monsen, V. T., Reite, K., Aas, P. A., Lauritzen, K. H., Liabakk, N., Bjørk, A., Doughty, R. W., et al. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601109 · Cited by 187 · see citing works

Differential Sensitivity of Hypoxia Inducible Factor Hydroxylation Sites to Hypoxia and Hydroxylase Inhibitors

Tian, Y., Yeoh, K. K., Lee, M. K., Eriksson, T., Kessler, B. M., Kramer, H., Edelmann, M. J., Willam, C., Pugh, C. W., Schofield, C. J., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.211110 · Cited by 186 · see citing works

ALKBH8-mediated formation of a novel diastereomeric pair of wobble nucleosides in mammalian tRNA

van den Born, E., Vågbø, C. B., Songe-Møller, L., Leihne, V., Lien, G. F., Leszczyńska, G., Małkiewicz, A. J., Krokan, H. E., Kirpekar, F., Klungland, A., et al. (2011) · Nature Communications · doi:10.1038/ncomms1173 · Cited by 174 · see citing works

Stimulation of erythropoietin gene transcription during hypoxia and cobalt exposure

Schuster, S. J., Badiavas, E. V., Costa-Giomi, P., Weinmann, R. S., Erslev, A. J., & Caro, J. (1989) · Blood · doi:10.1182/blood.v73.1.13.13 · Cited by 174 · see citing works

PHF8, a gene associated with cleft lip/palate and mental retardation, encodes for an Nε-dimethyl lysine demethylase

Loenarz, C., Ge, W., Coleman, M. L., Rose, N. R., Cooper, C. D. O., Klose, R. J., Ratcliffe, P. J., & Schofield, C. J. (2009) · Human Molecular Genetics · doi:10.1093/hmg/ddp480 · Cited by 171 · see citing works

Structural basis for halogenation by iron- and 2-oxo-glutarate-dependent enzyme WelO5

Mitchell, A. J., Zhu, Q., Maggiolo, A. O., Ananth, N. R., Hillwig, M. L., Liu, X., & Boal, A. K. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2112 · Cited by 169 · see citing works

5-Carboxy-8-hydroxyquinoline is a broad spectrum 2-oxoglutarate oxygenase inhibitor which causes iron translocation

Hopkinson, R. J., Tumber, A., Yapp, C., Chowdhury, R., Aik, W. S., Che, K. H., Li, X. S., Kristensen, J. B. L., King, O. N. F., Chan, M. C., et al. (2013) · Chemical Science · doi:10.1039/c3sc51122g · Cited by 168 · see citing works

2-Oxoglutarate-Dependent Oxygenases

Hausinger, R. P., & Schofield, C. J. (2015) · Royal Society of Chemistry eBooks · doi:10.1039/9781782621959 · Cited by 167 · see citing works

Alcaligenes eutrophus JMP134 "2,4-dichlorophenoxyacetate monooxygenase" is an alpha-ketoglutarate-dependent dioxygenase

Fukumori, F., & Hausinger, R. P. (1993) · Journal of Bacteriology · doi:10.1128/jb.175.7.2083-2086.1993 · Cited by 166 · see citing works

Inhibition of Hypoxia-Inducible Factor Prolyl Hydroxylase Domain Oxygen Sensors: Tricking the Body into Mounting Orchestrated Survival and Repair Responses

Rabinowitz, M. H. (2013) · Journal of Medicinal Chemistry · doi:10.1021/jm400386j · Cited by 165 · see citing works

Osmotically Induced Synthesis of the Compatible Solute Hydroxyectoine Is Mediated by an Evolutionarily Conserved Ectoine Hydroxylase

Bursy, J., Pierik, A. J., Pica, N., & Bremer, E. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704023200 · Cited by 161 · see citing works

Crystal Structure and Mechanistic Implications of 1-Aminocyclopropane-1-Carboxylic Acid Oxidase—The Ethylene-Forming Enzyme

Zhang, Z., Ren, J., Clifton, I. J., & Schofield, C. J. (2004) · Chemistry & Biology · doi:10.1016/j.chembiol.2004.08.012 · Cited by 160 · see citing works

Plant Growth Regulator Daminozide Is a Selective Inhibitor of Human KDM2/7 Histone Demethylases

Rose, N. R., Woon, E. C. Y., Tumber, A., Walport, L. J., Chowdhury, R., Li, X. S., King, O. N. F., Lejeune, C., Ng, S. S., Krojer, T. J., et al. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm300677j · Cited by 160 · see citing works

KDM7 is a dual demethylase for histone H3 Lys 9 and Lys 27 and functions in brain development

Tsukada, Y.-I., Ishitani, T., & Nakayama, K. I. (2010) · Genes & Development · doi:10.1101/gad.1864410 · Cited by 158 · see citing works

The AlkB Domain of Mammalian ABH8 Catalyzes Hydroxylation of 5‐Methoxycarbonylmethyluridine at the Wobble Position of tRNA

Fu, Y., Dai, Q., Zhang, W., Jin, R., Pan, T., & He, C. (2010) · Angewandte Chemie International Edition · doi:10.1002/anie.201001242 · Cited by 155 · 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

Highly selective inhibition of histone demethylases by de novo macrocyclic peptides

Kawamura, A., Münzel, M., Kojima, T., Yapp, C., Bhushan, B., Goto, Y., Tumber, A., Katoh, T., King, O. N. F., Passioura, T., et al. (2017) · Nature Communications · doi:10.1038/ncomms14773 · Cited by 150 · see citing works

Oncometabolites: tailoring our genes

Nowicki, S., & Gottlieb, E. (2015) · FEBS Journal · doi:10.1111/febs.13295 · Cited by 145 · see citing works

Structural basis for oxygen degradation domain selectivity of the HIF prolyl hydroxylases

Chowdhury, R., Leung, I. K. H., Tian, Y.-M., Abboud, M. I., Ge, W., Domene, C., Cantrelle, F.-X., Landrieu, I., Hardy, A. P., Pugh, C. W., et al. (2016) · Nature Communications · doi:10.1038/ncomms12673 · Cited by 145 · see citing works

Proteomics-based Identification of Novel Factor Inhibiting Hypoxia-inducible Factor (FIH) Substrates Indicates Widespread Asparaginyl Hydroxylation of Ankyrin Repeat Domain-containing Proteins

Cockman, M. E., Webb, J. D., Kramer, H., Kessler, B. M., & Ratcliffe, P. J. (2008) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m800340-mcp200 · Cited by 139 · see citing works

Mechanism of the C5 Stereoinversion Reaction in the Biosynthesis of Carbapenem Antibiotics

Chang, W., Guo, Y., Wang, C., Butch, S. E., Rosenzweig, A. C., Boal, A. K., Krebs, C., & Bollinger, J. M., Jr. (2014) · Science · doi:10.1126/science.1248000 · Cited by 138 · see citing works

Visualizing the Reaction Cycle in an Iron(II)- and 2-(Oxo)-glutarate-Dependent Hydroxylase

Mitchell, A. J., Dunham, N. P., Martinie, R. J., Bergman, J. A., Pollock, C. J., Hu, K., Allen, B. D., Chang, W., Silakov, A., Bollinger, J. M., Jr., et al. (2017) · Journal of the American Chemical Society · doi:10.1021/jacs.7b07374 · Cited by 137 · see citing works

Hydroxylation of the eukaryotic ribosomal decoding center affects translational accuracy

Loenarz, C., Sekirnik, R., Thalhammer, A., Ge, W., Spivakovsky, E., Mackeen, M. M., McDonough, M. A., Cockman, M. E., Kessler, B. M., Ratcliffe, P. J., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1311750111 · Cited by 127 · see citing works

VioC is a Non‐Heme Iron, α‐Ketoglutarate‐Dependent Oxygenase that Catalyzes the Formation of 3S‐Hydroxy‐ L ‐Arginine during Viomycin Biosynthesis

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

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