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

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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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Structure of an HIF-1α-pVHL Complex: Hydroxyproline Recognition in Signaling

Min, J.-H., Yang, H., Ivan, M., Gertler, F., Kaelin, W. G., & Pavletich, N. P. (2002) · Science · doi:10.1126/science.1073440 · Cited by 765

Oxidative demethylation by Escherichia coli AlkB directly reverts DNA base damage

Trewick, S. C., Henshaw, T. F., Hausinger, R. P., Lindahl, T. L., & Sedgwick, B. (2002) · Nature · doi:10.1038/nature00908 · Cited by 762

Structural basis for the recognition of hydroxyproline in HIF-1α by pVHL

Hon, W.-C., Wilson, M. I., Harlos, K., Claridge, T. D. W., Schofield, C. J., Pugh, C. W., Maxwell, P. H., Ratcliffe, P. J., Stuart, D. I., & Jones, E. Y. (2002) · Nature · doi:10.1038/nature00767 · Cited by 751

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

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

AlkB-mediated oxidative demethylation reverses DNA damage in Escherichia coli

Falnes, P. Ø., Johansen, R., & Seeberg, E. C. (2002) · Nature · doi:10.1038/nature01048 · Cited by 617

Carnitine biosynthesis in mammals

Vaz, F. M., & Wanders, R. J. A. (2002) · Biochemical Journal · doi:10.1042/bj3610417 · Cited by 544

The 2‐His‐1‐Carboxylate Facial Triad — An Emerging Structural Motif in Mononuclear Non‐Heme Iron(II) Enzymes

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Introduction to protein structure

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Expanding chemical biology of 2-oxoglutarate oxygenases

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

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Structure of isopenicillinN synthase complexed with substrate and the mechanism ofpenicillin formation

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Crystal structure of the FTO protein reveals basis for its substrate specificity

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Jmjd6 Catalyses Lysyl-Hydroxylation of U2AF65, a Protein Associated with RNA Splicing

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Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes

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Structural Insights into Histone Demethylation by JMJD2 Family Members

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Structure of Factor-inhibiting Hypoxia-inducible Factor (HIF) Reveals Mechanism of Oxidative Modification of HIF-1α

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Enzymatic and structural insights for substrate specificity of a family of jumonji histone lysine demethylases

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Cellular oxygen sensing: Crystal structure of hypoxia-inducible factor prolyl hydroxylase (PHD2)

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Structure of a cephalosporin synthase

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Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity

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Direct spectroscopic detection of a C-H-cleaving high-spin Fe(IV) complex in a prolyl-4-hydroxylase

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Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase

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

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A stereochemical concept for the catalytic mechanism of prolylhydroxylase

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Crystal structures of DNA/RNA repair enzymes AlkB and ABH2 bound to dsDNA

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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

Inhibitor Scaffolds for 2-Oxoglutarate-Dependent Histone Lysine Demethylases

Rose, N. R., Ng, S. S., Mecinović, J., Liénard, B. M. R., Bello, S. H., Sun, Z., McDonough, M. A., Oppermann, U. C. T., & Schofield, C. J. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm800936s · Cited by 255

Ascorbate is consumed stoichiometrically in the uncoupled reactions catalyzed by prolyl 4-hydroxylase and lysyl hydroxylase.

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

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Structural and mechanistic studies on the inhibition of the hypoxia-inducible transcription factor hydroxylases by tricarboxylic acid cycle intermediates

Hewitson, K. S., Liénard, B. M. R., McDonough, M. A., Clifton, I. J., Butler, D., Soares, A. S., Oldham, N. J., McNeill, L. A., & Schofield, C. J. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m608337200 · Cited by 235

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

Asparaginyl Hydroxylation of the Notch Ankyrin Repeat Domain by Factor Inhibiting Hypoxia-inducible Factor

Coleman, M. L., McDonough, M. A., Hewitson, K. S., Coles, C., Mecinovicí, J., Edelmann, M., Cook, K. M., Cockman, M. E., Lancaster, D. E., Kessler, B. M., et al. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m704102200 · Cited by 222

Mutations in PHF8 are associated with X linked mental retardation and cleft lip/cleft palate

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Structure of factor-inhibiting hypoxia-inducible factor 1: an asparaginyl hydroxylase involved in the hypoxic response pathway

Dann, C. E., Bruick, R. K., & Deisenhofer, J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.202614999 · Cited by 200

Human ABH3 structure and key residues for oxidative demethylation to reverse DNA/RNA damage

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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

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

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Selective Inhibition of Factor Inhibiting Hypoxia-Inducible Factor

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Selective Inhibitors of the JMJD2 Histone Demethylases: Combined Nondenaturing Mass Spectrometric Screening and Crystallographic Approaches

Rose, N. R., Woon, E. C. Y., Kingham, G. L., King, O. N. F., Mecinović, J., Clifton, I. J., Ng, S. S., Talib-Hardy, J., Oppermann, U. C. T., McDonough, M. A., et al. (2010) · Journal of Medicinal Chemistry · doi:10.1021/jm901680b · Cited by 148

Structural basis of the recognition of a methylated histone tail by JMJD2A

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Investigating the dependence of the hypoxia-inducible factor hydroxylases (factor inhibiting HIF and prolyl hydroxylase domain 2) on ascorbate and other reducing agents

Flashman, E., Davies, S. L., Yeoh, K. K., & Schofield, C. J. (2010) · Biochemical Journal · doi:10.1042/bj20091609 · Cited by 133

Structure of Human FIH-1 Reveals a Unique Active Site Pocket and Interaction Sites for HIF-1 and von Hippel-Lindau

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Structure of proline 3‐hydroxylase

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Interaction of JMJD6 with single-stranded RNA

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Structural and Mechanistic Studies on γ-Butyrobetaine Hydroxylase

Leung, I. K. H., Krojer, T. J., Kochan, G. T., Henry, L., von Delft, F., Claridge, T. D. W., Oppermann, U. C. T., McDonough, M. A., & Schofield, C. J. (2010) · Chemistry & Biology · doi:10.1016/j.chembiol.2010.09.016 · Cited by 103

Crystal Structure of the 2-Oxoglutarate- and Fe(II)-Dependent Lysyl Hydroxylase JMJD6

Mantri, M., Krojer, T. J., Bagg, E. A. L., Webby, C. J., Butler, D. S., Kochan, G. T., Kavanagh, K. L., Oppermann, U. C. T., McDonough, M. A., & Schofield, C. J. (2010) · Journal of Molecular Biology · doi:10.1016/j.jmb.2010.05.054 · Cited by 94

Disruption of dimerization and substrate phosphorylation inhibit factor inhibiting hypoxia-inducible factor (FIH) activity

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Structure of Human Phytanoyl-CoA 2-Hydroxylase Identifies Molecular Mechanisms of Refsum Disease*

McDonough, M. A., Kavanagh, K. L., Butler, D. S., Searls, T., Oppermann, U. C. T., & Schofield, C. J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m507528200 · Cited by 84

Structural insights into a novel histone demethylase PHF8

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Expanding Role of the Jumonji C Domain as an RNA Hydroxylase

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Substrate Binding to the α-Ketoglutarate-Dependent Non-Heme Iron Enzyme Clavaminate Synthase 2: Coupling Mechanism of Oxidative Decarboxylation and Hydroxylation

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Evidence for a Stereoelectronic Effect in Human Oxygen Sensing

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The Active Site of an Algal Prolyl 4-Hydroxylase Has a Large Structural Plasticity

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Asparagine β-hydroxylation stabilizes the ankyrin repeat domain fold

Kelly, L., McDonough, M. A., Coleman, M. L., Ratcliffe, P. J., & Schofield, C. J. (2008) · Molecular BioSystems · doi:10.1039/b815271c · Cited by 61

Dynamic states of the DNA repair enzyme AlkB regulate product release

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Structure determination of DNA methylation lesions N 1 -meA and N 3 -meC in duplex DNA using a cross-linked protein–DNA system

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Evidence That Two Enzyme-derived Histidine Ligands Are Sufficient for Iron Binding and Catalysis by Factor Inhibiting HIF (FIH)

Hewitson, K. S., Holmes, S. L., Ehrismann, D., Hardy, A., Chowdhury, R., Schofield, C. J., & McDonough, M. A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804999200 · Cited by 57

The most versatile of all reactive intermediates?

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Application of a Proteolysis/Mass Spectrometry Method for Investigating the Effects of Inhibitors on Hydroxylase Structure

Stubbs, C. J., Loenarz, C., Mecinović, J., Yeoh, K. K., Hindley, N., Liénard, B. M. R., Sobott, F., Schofield, C. J., & Flashman, E. (2009) · Journal of Medicinal Chemistry · doi:10.1021/jm900285r · Cited by 46

Vitamin C Is Not Essential for Carnitine Biosynthesis in Vivo: Verification in Vitamin C-Depleted Senescence Marker Protein-30/Gluconolactonase Knockout Mice

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Crystal structure of human gamma-butyrobetaine hydroxylase

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Crystal structure of the PHF8 Jumonji domain, an Nε‐methyl lysine demethylase

Yue, W. W., Hozjan, V., Ge, W., Loenarz, C., Cooper, C. D. O., Schofield, C. J., Kavanagh, K. L., Oppermann, U. C. T., & McDonough, M. A. (2010) · FEBS Letters · doi:10.1016/j.febslet.2009.12.055 · Cited by 37

Viruses

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

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The role of mutations in epigenetic regulators in myeloid malignancies

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

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2-Oxoglutarate-Dependent Oxygenases

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Histone lysine demethylases as targets for anticancer therapy

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

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