Structural studies on human 2-oxoglutarate dependent oxygenases
Abstract
2-Oxoglutarate and ferrous iron-dependent oxygenases have emerged as an important family of human enzymes that catalyse hydroxylations and related demethylation reactions. Their substrates in humans include proteins, nucleic acids, lipids and small molecules. They play roles in collagen biosynthesis, hypoxic sensing, regulation of gene expression and lipid biosynthesis/metabolism. Structural analyses, principally employing crystallography, have revealed that all of these oxygenases possess a double-stranded β-helix core fold that supports a highly conserved triad of iron binding residues and a less well conserved 2-oxoglutarate co-substrate binding site. The 2-oxoglutarate binds to the iron in a bidentate manner via its 1-carboxylate and 2-oxo groups. The primary substrate binding elements are more variable and can involve mobile elements.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The largest group of enzymes using vitamin C as a cofactor is the iron-dependent and 2-oxoglutarate-dependent dioxygenases superfamily (2OGO), representing about 80 enzymes in humans responsible for modification of important biological substances and processes.
“The largest group of enzymes using vitamin C as one of their cofactors is the iron-dependent and 2-oxoglutarate-dependent dioxygenases superfamily (2OGO, α-ketoglutarate-dependent hydroxylases). In humans, it represents about 80 enzymes responsible for the modification of important biological substances and processes (Table 2) [97,98,99].”
From Vitamin C-Sources, Physiological Role, Kinetics, Deficiency, Use, Toxicity, and Determination (2021) · cites this paper as [97]
Cites
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 · 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
Introduction to Protein Structure
Brändén, C.-I., & Tooze, J. (2012) · Garland Science eBooks · doi:10.1201/9781136969898 · Cited by 2,398 · see citing works
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 · see citing works
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 · see citing works
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 1,519 · 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
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 1,179 · 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
Carnitine biosynthesis in mammals
Vaz, F. M., & Wanders, R. J. A. (2002) · Biochemical Journal · doi:10.1042/0264-6021:3610417 · Cited by 769 · see citing works
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 · see citing works
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 · see citing works
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 · 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
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
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 · see citing works
Carnitine biosynthesis in mammals
Vaz, F. M., & Wanders, R. J. A. (2002) · Biochemical Journal · doi:10.1042/bj3610417 · Cited by 544 · see citing works
Hegg, E. L., & QUE, L. J. (1997) · European Journal of Biochemistry · doi:10.1111/j.1432-1033.1997.t01-1-00625.x · Cited by 528 · see citing works
Introduction to protein structure
Saffran, M. (1992) · Trends in Endocrinology and Metabolism · doi:10.1016/1043-2760(92)90006-m · Cited by 527 · see citing works
Expanding chemical biology of 2-oxoglutarate oxygenases
Loenarz, C., & Schofield, C. J. (2008) · Nature Chemical Biology · doi:10.1038/nchembio0308-152 · Cited by 498 · 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
Roach, P. L., Clifton, I. J., Hensgens, C. M. H., Shibata, N., Schofield, C. J., Hajdu, J., & Baldwin, J. E. (1997) · Nature · doi:10.1038/42990 · Cited by 437 · see citing works
Crystal structure of the FTO protein reveals basis for its substrate specificity
Han, Z., Niu, T., Chang, J., Lei, X., Zhao, M., Wang, Q., Cheng, W., Wang, J., Feng, Y., & Chai, J. (2010) · Nature · doi:10.1038/nature08921 · Cited by 426 · see citing works
Jmjd6 Catalyses Lysyl-Hydroxylation of U2AF65, a Protein Associated with RNA Splicing
Webby, C. J., Wolf, A., Gromak, N., Dreger, M., Kramer, H., Kessler, B. M., Nielsen, M. L., Schmitz, C., Butler, D. S., Yates, J. R., et al. (2009) · Science · doi:10.1126/science.1175865 · Cited by 423 · see citing works
Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes
Roach, P. L., Clifton, I. J., Fülöp, V., Harlos, K., Barton, G. J., Hajdu, J., Andersson, I., Schofield, C. J., & Baldwin, J. E. (1995) · Nature · doi:10.1038/375700a0 · Cited by 420 · see citing works
Structural Insights into Histone Demethylation by JMJD2 Family Members
Chen, Z., Zang, J., Whetstine, J. R., Hong, X., Davrazou, F., Kutateladze, T. G., Simpson, M., Mao, Q., Pan, C., Dai, S., et al. (2006) · Cell · doi:10.1016/j.cell.2006.04.024 · Cited by 396 · see citing works
Elkins, J. M., Hewitson, K. S., McNeill, L. A., Seibel, J. F., Schlemminger, I., Pugh, C. W., Ratcliffe, P. J., & Schofield, C. J. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.c200644200 · Cited by 391 · see citing works
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
Cellular oxygen sensing: Crystal structure of hypoxia-inducible factor prolyl hydroxylase (PHD2)
McDonough, M. A., Li, V., Flashman, E., Chowdhury, R., Mohr, C., Liénard, B. M. R., Zondlo, J., Oldham, N. J., Clifton, I. J., Lewis, J. K., et al. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0601283103 · Cited by 366 · 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
Direct spectroscopic detection of a C-H-cleaving high-spin Fe(IV) complex in a prolyl-4-hydroxylase
Hoffart, L. M., Barr, E. W., Guyer, R. B., Bollinger, J. M., Jr., & Krebs, C. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0604005103 · Cited by 324 · see citing works
Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase
Couture, J., Collazo, E., Ortiz-Tello, P. A., Brunzelle, J. S., & Trievel, R. C. (2007) · Nature Structural & Molecular Biology · doi:10.1038/nsmb1273 · Cited by 276 · see citing works
Loenarz, C., & Schofield, C. J. (2011) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2010.07.002 · Cited by 274 · 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
Crystal structures of DNA/RNA repair enzymes AlkB and ABH2 bound to dsDNA
Yang, C., Yi, C., Duguid, E. M., Sullivan, C. T., Jian, X., Rice, P. A., & He, C. (2008) · Nature · doi:10.1038/nature06889 · Cited by 260 · see citing works
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 · see citing works
Myllylä, R., Majamaa, K., Günzler, V., Hanauske-Abel, H. M., & Kivirikko, K. I. (1984) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)91023-9 · Cited by 243 · 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
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 · see citing works
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
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 · see citing works
Mutations in PHF8 are associated with X linked mental retardation and cleft lip/cleft palate
Laumonnier, F., Holbert, S., Ronce, N., Faravelli, F., Lenzner, S., Schwartz, C. E., Lespinasse, J., Esch, H. V., Lacombe, D., Goizet, C., et al. (2005) · Journal of Medical Genetics · doi:10.1136/jmg.2004.029439 · Cited by 213 · see citing works
Dann, C. E., Bruick, R. K., & Deisenhofer, J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.202614999 · Cited by 200 · see citing works
Human ABH3 structure and key residues for oxidative demethylation to reverse DNA/RNA damage
Sundheim, O., Vågbø, C. B., Bjørås, M., de Sousa, M. M. L., Monsen, V. T., Aas, P. A., Drabløs, F., Krokan, H. E., Tainer, J. A., & Slupphaug, G. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601219 · Cited by 174 · see citing works
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
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
Selective Inhibition of Factor Inhibiting Hypoxia-Inducible Factor
McDonough, M. A., McNeill, L. A., Tilliet, M., Papamicaël, C. A., Chen, Q., Banerji, B., Hewitson, K. S., & Schofield, C. J. (2005) · Journal of the American Chemical Society · doi:10.1021/ja050841b · Cited by 149 · see citing works
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 · see citing works
Structural basis of the recognition of a methylated histone tail by JMJD2A
Chen, Z., Zang, J., Kappler, J. W., Hong, X., Crawford, F., Wang, Q., Lan, F., Jiang, C., Whetstine, J. R., Dai, S., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0704525104 · Cited by 142 · see citing works
Flashman, E., Davies, S. L., Yeoh, K. K., & Schofield, C. J. (2010) · Biochemical Journal · doi:10.1042/bj20091609 · Cited by 129 · see citing works
Lee, C., Kim, S. J., Jeong, D. G., Lee, S. M., & Ryu, S. E. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210385200 · Cited by 121 · see citing works
Structure of proline 3‐hydroxylase
Clifton, I. J., Hsueh, L., Baldwin, J. E., Harlos, K., & Schofield, C. J. (2001) · European Journal of Biochemistry · doi:10.1046/j.0014-2956.2001.02617.x · Cited by 113 · see citing works
Interaction of JMJD6 with single-stranded RNA
Hong, X., Zang, J., White, J., Wang, C., Pan, C., Zhao, R., Murphy, R. C., Dai, S., Henson, P. M., Kappler, J. W., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1008832107 · Cited by 111 · see citing works
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 · see citing works
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 92 · see citing works
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 · see citing works
Lancaster, D. E., McNeill, L. A., McDonough, M. A., Aplin, R. T., Hewitson, K. S., Pugh, C. W., Ratcliffe, P. J., & Schofield, C. J. (2004) · Biochemical Journal · doi:10.1042/bj20040735 · Cited by 83 · see citing works
Structural insights into a novel histone demethylase PHF8
Yu, L., Wang, Y., Huang, S., Wang, J., Deng, Z., Zhang, Q., Wu, W., Zhang, X., Liu, Z., Gong, W., et al. (2010) · Cell Research · doi:10.1038/cr.2010.8 · Cited by 80 · see citing works
Expanding Role of the Jumonji C Domain as an RNA Hydroxylase
Noma, A., Ishitani, R., Kato, M., Nagao, A., Nureki, O., & Suzuki, T. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.156398 · Cited by 73 · see citing works
Zhou, J., Gunsior, M., Bachmann, B. O., Townsend, C. A., & Solomon, E. I. (1998) · Journal of the American Chemical Society · doi:10.1021/ja983534x · Cited by 73 · see citing works
Evidence for a Stereoelectronic Effect in Human Oxygen Sensing
Loenarz, C., Mecinović, J., Chowdhury, R., McNeill, L. A., Flashman, E., & Schofield, C. J. (2009) · Angewandte Chemie International Edition · doi:10.1002/anie.200805427 · Cited by 68 · see citing works
The Active Site of an Algal Prolyl 4-Hydroxylase Has a Large Structural Plasticity
Koski, M. K., Hieta, R., Bollner, C., Kivirikko, K. I., Myllyharju, J., & Wierenga, R. K. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m706554200 · Cited by 65 · see citing works
Dynamic states of the DNA repair enzyme AlkB regulate product release
Bleijlevens, B., Shivarattan, T., Flashman, E., Yang, Y., Simpson, P. J., Koivisto, P., Sedgwick, B., Schofield, C. J., & Matthews, S. (2008) · EMBO Reports · doi:10.1038/embor.2008.120 · Cited by 60 · see citing works
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 59 · see citing works
Lu, L., Yi, C., Jian, X., Zheng, G., & He, C. (2010) · Nucleic Acids Research · doi:10.1093/nar/gkq129 · Cited by 58 · see citing works
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 · see citing works
The most versatile of all reactive intermediates?
Flashman, E., & Schofield, C. J. (2007) · Nature Chemical Biology · doi:10.1038/nchembio0207-86 · Cited by 48 · see citing works
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 · see citing works
Furusawa, H., Sato, Y., Tanaka, Y., Inai, Y., Amano, A., Iwama, M., Kondo, Y., Handa, S., Murata, A., Nishikimi, M., et al. (2008) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.31.1673 · Cited by 42 · see citing works
Crystal structure of human gamma-butyrobetaine hydroxylase
Tārs, K., Rumnieks, J., Zeltiņš, A., Kazāks, A., Koteloviča, S., Leonchiks, A., Sharipo, J., Vīksna, A., Kuka, J., Liepinsh, E., et al. (2010) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2010.06.121 · Cited by 41 · see citing works
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 · see citing works
Stuart, D. I. (1993) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(05)80148-4 · Cited by 21 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
An inhibitor of mutant IDH1 delays growth and promotes differentiation of glioma cells
Rohle, D., Popovici-Muller, J., Palaskas, N., Turcan, S., Grommes, C., Campos, C., Tsoi, J., Clark, O., Oldrini, B., Komisopoulou, E., et al. (2013) · Science · doi:10.1126/science.1236062 · Cited by 1,153 · see citing works
The role of mutations in epigenetic regulators in myeloid malignancies
Shih, A. H., Abdel-Wahab, O. I., Patel, J. P., & Levine, R. L. (2012) · Nature reviews. Cancer · doi:10.1038/nrc3343 · Cited by 671 · see citing works
Vitamin C-Sources, Physiological Role, Kinetics, Deficiency, Use, Toxicity, and Determination
Doseděl, M., Jirkovský, E., Macáková, K., Krčmová, L., Javorská, L., Pourová, J., Mercolini, L., Remião, F., Nováková, L., Mladěnka, P., et al. (2021) · Nutrients · doi:10.3390/nu13020615 · Cited by 553 · see citing works
2-Oxoglutarate-Dependent Oxygenases
Islam, M. S., Leissing, T. M., Chowdhury, R., Hopkinson, R. J., & Schofield, C. J. (2018) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-061516-044724 · Cited by 472 · see citing works
Histone lysine demethylases as targets for anticancer therapy
Højfeldt, J. W., Agger, K., & Helin, K. (2013) · Nature Reviews Drug Discovery · doi:10.1038/nrd4154 · Cited by 461 · see citing works
Histone demethylase KDM6A directly senses oxygen to control chromatin and cell fate
Chakraborty, A. A., Laukka, T., Myllykoski, M., Ringel, A. E., Booker, M. A., Tolstorukov, M. Y., Meng, Y. J., Meier, S. R., Jennings, R. B., Creech, A. L., et al. (2019) · Science · doi:10.1126/science.aaw1026 · Cited by 432 · 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
Mechanism and Function of Oxidative Reversal of DNA and RNA Methylation
Shen, L., Song, C., He, C., & Zhang, Y. (2014) · Annual Review of Biochemistry · doi:10.1146/annurev-biochem-060713-035513 · Cited by 359 · see citing works
Human high-altitude adaptation: forward genetics meets the HIF pathwayPreprint
Bigham, A. W., & Lee, F. S. (2014) · Genes & Development · doi:10.1101/gad.250167.114 · Cited by 350 · see citing works
DNA Methylation, Its Mediators and Genome Integrity
Meng, H., Cao, Y., Qin, J., Song, X., Zhang, Q., Shi, Y. S., & Cao, L. (2015) · International Journal of Biological Sciences · doi:10.7150/ijbs.11218 · Cited by 327 · see citing works
Regulation of the epigenome by vitamin C
Young, J. I., Züchner, S., & Wang, G. (2015) · Annual Review of Nutrition · doi:10.1146/annurev-nutr-071714-034228 · Cited by 319 · see citing works
Fumarate and Succinate Regulate Expression of Hypoxia-inducible Genes via TET Enzymes
Laukka, T., Mariani, C. J., Ihantola, T., Cao, J. Z., Hokkanen, J., Kaelin, W. G., Godley, L. A., & Koivunen, P. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.688762 · Cited by 307 · see citing works
Glutamine Metabolism Regulates Proliferation and Lineage Allocation in Skeletal Stem Cells
Yu, Y., Newman, H., Shen, L., Sharma, D., Hu, G., Mirando, A. J., Zhang, H., Knudsen, E., Zhang, G.-F., Hilton, M. J., et al. (2019) · Cell Metabolism · doi:10.1016/j.cmet.2019.01.016 · Cited by 253 · see citing works
Aik, W. S., Scotti, J. S., Choi, H., Gong, L., Demetriades, M., Schofield, C. J., & McDonough, M. A. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku085 · Cited by 246 · see citing works
Zdzisińska, B., Żurek, A., & Kandefer-Szerszeń, M. (2017) · Archivum Immunologiae et Therapiae Experimentalis · doi:10.1007/s00005-016-0406-x · Cited by 221 · 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
Gao, S., Naowarojna, N., Cheng, R., Liu, X., & Liu, P. (2018) · Natural Product Reports · doi:10.1039/c7np00067g · Cited by 203 · see citing works
Structural analysis of human KDM5B guides histone demethylase inhibitor development
Johansson, C., Velupillai, S., Tumber, A., Szykowska, A., Hookway, E. S., Nowak, R. P., Strain-Damerell, C. M., Gileadi, C., Philpott, M., Burgess-Brown, N., et al. (2016) · Nature Chemical Biology · doi:10.1038/nchembio.2087 · Cited by 200 · see citing works
Crystal Structures of the Human RNA Demethylase Alkbh5 Reveal Basis for Substrate Recognition
Feng, C., Liu, Y., Wang, G., Deng, Z., Zhang, Q., Wu, W., Tong, Y., Cheng, C., & Chen, Z. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.546168 · Cited by 199 · 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
Targeting Histone Demethylases: A New Avenue for the Fight against Cancer
Rotili, D., & Mai, A. (2011) · Genes & Cancer · doi:10.1177/1947601911417976 · Cited by 192 · see citing works
The Roles of Jumonji-Type Oxygenases in Human Disease
Johansson, C., Tumber, A., Che, K., Cain, P., Nowak, R. P., Gileadi, C., & Oppermann, U. C. T. (2014) · Epigenomics · doi:10.2217/epi.13.79 · Cited by 163 · see citing works
Epigenetic Regulation by Histone Demethylases in Hypoxia
Hancock, R. L., Dunne, K., Walport, L. J., Flashman, E., & Kawamura, A. (2015) · Epigenomics · doi:10.2217/epi.15.24 · Cited by 162 · see citing works
Cussó, O., Ribas, X., & Costas, M. (2015) · Chemical Communications · doi:10.1039/c5cc05576h · Cited by 151 · see citing works
Oncometabolites‐driven tumorigenesis: From genetics to targeted therapy
Morin, A., Letouzé, É., Gimenez‐Roqueplo, A., & Favier, J. (2014) · International Journal of Cancer · doi:10.1002/ijc.29080 · Cited by 150 · see citing works
Salminen, A., Kauppinen, A., Hiltunen, M. O., & Kaarniranta, K. (2014) · Ageing Research Reviews · doi:10.1016/j.arr.2014.05.004 · Cited by 142 · see citing works
Structure of a Naegleria Tet-like dioxygenase in complex with 5-methylcytosine DNA
Hashimoto, H., Pais, J. E., Zhang, X., Saleh, L., Fu, Z.-Q., Dai, N., Junior, I. R. C., Zheng, Y., & Cheng, X. (2013) · Nature · doi:10.1038/nature12905 · Cited by 138 · see citing works
A Comprehensive Review of Lysine-Specific Demethylase 1 and its Roles in Cancer
Hosseini, A., & Minucci, S. (2017) · Epigenomics · doi:10.2217/epi-2017-0022 · Cited by 137 · see citing works
Advances in histone demethylase KDM4 as cancer therapeutic targets
Lee, D. H., Kim, G. W., Jeon, Y. H., Yoo, J. H., Lee, S. W., & Kwon, S. H. (2020) · The FASEB Journal · doi:10.1096/fj.201902584r · Cited by 136 · see citing works
The α-ketoglutarate dehydrogenase complex in cancer metabolic plasticity
Vatrinet, R., Leone, G., Luise, M. D., Girolimetti, G., Vidone, M., Gasparre, G., & Porcelli, A. M. (2017) · Cancer & Metabolism · doi:10.1186/s40170-017-0165-0 · Cited by 130 · see citing works
Pharmacological targeting of the HIF hydroxylases – A new field in medicine development
Chan, M. C., Holt‐Martyn, J. P., Schofield, C. J., & Ratcliffe, P. J. (2016) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2016.01.001 · Cited by 126 · see citing works
Intestinal hypoxia and hypoxia-induced signalling as therapeutic targets for IBD
Welden, S. V., Selfridge, A. C., & Hindryckx, P. (2017) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/nrgastro.2017.101 · Cited by 124 · see citing works
Carbon–fluorine bond cleavage mediated by metalloenzymes
Wang, Y., & Liu, A.-M. (2020) · Chemical Society Reviews · doi:10.1039/c9cs00740g · Cited by 64 · see citing works
Structure–function relationships of human JmjC oxygenases—demethylases versus hydroxylases
Markolovic, S., Leissing, T. M., Chowdhury, R., Wilkins, S. E., Lü, X., & Schofield, C. J. (2016) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2016.05.013 · Cited by 123 · see citing works
KDM5B is a master regulator of the H3K4-methylome in stem cells, development and cancer
Xhabija, B., & Kidder, B. L. (2018) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2018.11.001 · Cited by 120 · see citing works
Prolyl 4‐hydroxylases, master regulators of the hypoxia response
Myllyharju, J. (2013) · Acta Physiologica · doi:10.1111/apha.12096 · Cited by 118 · see citing works
Structural and Functional Coordination of DNA and Histone MethylationPreprint
Cheng, X. (2014) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a018747 · Cited by 119 · see citing works
Hickok, J. R., Vasudevan, D., Antholine, W. E., & Thomas, D. D. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.432294 · Cited by 120 · see citing works
Kuiper, C., Dachs, G. U., Currie, M. J., & Vissers, M. C. M. (2014) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2014.01.033 · Cited by 117 · see citing works
A rice gene that confers broad-spectrum resistance to β-triketone herbicides
Maeda, H., Murata, K., Sakuma, N., Takei, S., Yamazaki, A., Karim, M. R., KAWATA, M., Hirose, S., Kawagishi-Kobayashi, M., Taniguchi, Y., et al. (2019) · Science · doi:10.1126/science.aax0379 · Cited by 109 · see citing works
Targeting the histone orthography of cancer: drugs for writers, erasers and readers
Simó‐Riudalbas, L., & Esteller, M. (2014) · British Journal of Pharmacology · doi:10.1111/bph.12844 · Cited by 108 · see citing works
Ribosomal oxygenases are structurally conserved from prokaryotes to humans
Chowdhury, R., Sekirnik, R., Brissett, N. C., Krojer, T., Ho, C.-H., Ng, S. S., Clifton, I. J., Ge, W., Kershaw, N. J., Fox, G. C., et al. (2014) · Nature · doi:10.1038/nature13263 · Cited by 105 · see citing works
Self-citationSalminen, A., Haapasalo, A., Kauppinen, A., Kaarniranta, K., Soininen, H. S., & Hiltunen, M. O. (2015) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2015.05.001 · Cited by 105 · see citing works
TET family dioxygenases and the TET activator vitamin C in immune responses and cancer
Yue, X., & Rao, A. (2020) · Blood · doi:10.1182/blood.2019004158 · Cited by 105 · see citing works
Toh, J. D. W., Crossley, S. W. M., Bruemmer, K. J., Ge, E. J., He, D., Iovan, D. A., & Chang, C. J. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2007349117 · Cited by 103 · see citing works
Salminen, A., Kauppinen, A., & Kaarniranta, K. (2015) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-015-1978-z · Cited by 99 · see citing works
The oxygenase Jmjd6–a case study in conflicting assignments
Böttger, A., Islam, M. S., Chowdhury, R., Schofield, C. J., & Wolf, A. (2015) · Biochemical Journal · doi:10.1042/bj20150278 · Cited by 99 · see citing works
Salminen, A., Kaarniranta, K., Hiltunen, M. O., & Kauppinen, A. (2014) · Cellular Signalling · doi:10.1016/j.cellsig.2014.03.030 · Cited by 96 · see citing works
Cheng, Z., Cheung, P., Kuo, A. J., Yukl, E. T., Wilmot, C. M., Gozani, O., & Patel, D. J. (2014) · Genes & Development · doi:10.1101/gad.246561.114 · Cited by 90 · see citing works
Hypoxia-Inducible Histone Lysine Demethylases: Impact on the Aging Process and Age-Related Diseases
Salminen, A., Kai, K., & Kauppinen, A. (2016) · Aging and Disease · doi:10.14336/ad.2015.0929 · Cited by 90 · see citing works
Yu, X., Liu, Y., Liu, X., Wang, P., Liu, S., Miao, J., Du, Z., & Yang, C. (2018) · Scientific Reports · doi:10.1038/s41598-018-24395-y · Cited by 86 · see citing works
Perspectives on the interactions between metabolism, redox, and epigenetics in plants
Shen, Y., Issakidis‐Bourguet, E., & Zhou, D. (2016) · Journal of Experimental Botany · doi:10.1093/jxb/erw310 · Cited by 85 · see citing works
Aberrant DNA methylation reprogramming in bovine SCNT preimplantation embryos
Zhang, S., Chen, X., Wang, F., An, X., Tang, B., Zhang, X., Sun, L., & Li, Z. (2016) · Scientific Reports · doi:10.1038/srep30345 · Cited by 84 · see citing works
Dickson, K. M., Gustafson, C. B., Young, J. I., Zuchner, S. L., & Wang, G. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.09.010 · Cited by 81 · see citing works
Studies on the catalytic domains of multiple JmjC oxygenases using peptide substrates
Williams, S. T., Walport, L. J., Hopkinson, R. J., Madden, S. K., Chowdhury, R., Schofield, C. J., & Kawamura, A. (2014) · Epigenetics · doi:10.4161/15592294.2014.983381 · Cited by 82 · see citing works
Epigenetics: The third pillar of nitric oxide signaling
Socco, S., Bovee, R. C., Palczewski, M. B., Hickok, J. R., & Thomas, D. D. (2017) · Pharmacological Research · doi:10.1016/j.phrs.2017.04.011 · Cited by 80 · see citing works
Yufa, R., Krylova, S. M., Bruce, C., Bagg, E. A. L., Schofield, C. J., & Krylov, S. N. (2014) · Analytical Chemistry · doi:10.1021/ac5044187 · Cited by 79 · see citing works
Mutations in the Isocitrate Dehydrogenase Genes IDH1 and IDH2 in Tumors
Schaap, F. G., French, P. J., & Bovée, J. V. M. G. (2012) · Advances in Anatomic Pathology · doi:10.1097/pap.0b013e31827b654d · Cited by 78 · see citing works
Molecular architecture of the multifunctional collagen lysyl hydroxylase and glycosyltransferase LH3
Scietti, L., Chiapparino, A., Giorgi, F. D., Fumagalli, M., Khoriauli, L., Nergadze, S. G., Basu, S., Oliéric, V., Cucca, L., Banushi, B., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-05631-5 · Cited by 76 · see citing works
Thalhammer, A., Hansen, A. S., El-Sagheer, A. H., Brown, T. P., & Schofield, C. J. (2011) · Chemical Communications · doi:10.1039/c0cc05671e · Cited by 75 · see citing works
OH, the Places You’ll Go! Hydroxylation, Gene Expression, and Cancer
Ploumakis, A., & Coleman, M. L. (2015) · Molecular Cell · doi:10.1016/j.molcel.2015.05.026 · Cited by 74 · see citing works
Advances in Histone Demethylase KDM3A as a Cancer Therapeutic Target
Yoo, J. H., Jeon, Y. H., Cho, H. Y., Lee, S. W., Kim, G. W., Lee, D. H., & Kwon, S. H. (2020) · Cancers · doi:10.3390/cancers12051098 · Cited by 73 · see citing works
Biochemical Diversity of 2-Oxoglutarate-Dependent Oxygenases
Hausinger, R. P. (2015) · Royal Society of Chemistry eBooks · doi:10.1039/9781782621959-00001 · Cited by 71 · see citing works
Crystal Structure and Functional Analysis of JMJD5 Indicate an Alternate Specificity and Function
Rizzo, P. A. D., Krishnan, S., & Trievel, R. C. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.00513-12 · Cited by 71 · see citing works
New themes in the biological functions of 5‐methylcytosine and 5‐hydroxymethylcytosine
Moen, E. L., Mariani, C. J., Zullow, H. J., Jeff‐Eke, M., Litwin, E., Nikitas, J. N., & Godley, L. A. (2014) · Immunological Reviews · doi:10.1111/imr.12242 · Cited by 66 · see citing works
Heim, A., Grimm, C., Müller, U., Häußler, S., Mackeen, M. M., Merl‐Pham, J., Hauck, S. M., Kessler, B. M., Schofield, C. J., Wolf, A., et al. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku488 · Cited by 66 · see citing works
Molecular Pathogenesis and Diagnostic, Prognostic and Predictive Molecular Markers in Sarcoma
Mariño‐Enríquez, A., & Bovée, J. V. M. G. (2016) · Surgical pathology clinics · doi:10.1016/j.path.2016.04.009 · Cited by 65 · see citing works
Autocatalysed oxidative modifications to 2‐oxoglutarate dependent oxygenases
Mantri, M., Zhang, Z., McDonough, M. A., & Schofield, C. J. (2012) · FEBS Journal · doi:10.1111/j.1742-4658.2012.08496.x · Cited by 64 · see citing works
Reshaping the Binding Pocket of Lysine Hydroxylase for Enhanced Activity
Wang, F., Zhu, M., Song, Z. Q., Li, C., Wang, Y., Zhu, Z., Sun, D., Lu, F., & Qin, H. (2020) · ACS Catalysis · doi:10.1021/acscatal.0c03841 · Cited by 64 · see citing works
Metabolic Dysregulations and Epigenetics: A Bidirectional Interplay that Drives Tumor Progression
Crispo, F., Condelli, V., Lepore, S., Notarangelo, T., Sgambato, A., Esposito, F., Maddalena, F., & Landriscina, M. (2019) · Cells · doi:10.3390/cells8080798 · Cited by 61 · see citing works
IDH Mutations in Tumorigenesis and Their Potential Role As Novel Therapeutic Targets
Krell, D., Mulholland, P. J., Frampton, A. E., Krell, J., Stebbing, J., & Bardella, C. (2013) · Future Oncology · doi:10.2217/fon.13.143 · Cited by 62 · see citing works
Vitamin C Transporters and Their Implications in Carcinogenesis
Linowiecka, K., Foksiński, M., & Brożyna, A. A. (2020) · Nutrients · doi:10.3390/nu12123869 · Cited by 60 · see citing works
Reporter Ligand NMR Screening Method for 2-Oxoglutarate Oxygenase Inhibitors
Leung, I. K. H., Demetriades, M., Hardy, A., Lejeune, C., Smart, T. J., Szöllössi, A., Kawamura, A., Schofield, C. J., & Claridge, T. D. W. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm301583m · Cited by 62 · see citing works
Genetics of Myeloproliferative Neoplasms
Viny, A. D., & Levine, R. L. (2014) · The Cancer Journal · doi:10.1097/ppo.0000000000000013 · Cited by 59 · see citing works
Mitochondria and Hypoxia: Metabolic Crosstalk in Cell-Fate Decisions
Bargiela, D., Burr, S. P., & Chinnery, P. F. (2018) · Trends in Endocrinology & Metabolism · doi:10.1016/j.tem.2018.02.002 · Cited by 60 · see citing works
Comparative Biology of Oxygen Sensing in Plants and Animals
Holdsworth, M. J., & Gibbs, D. J. (2020) · Current Biology · doi:10.1016/j.cub.2020.03.021 · Cited by 57 · see citing works
Trimethyllysine: From Carnitine Biosynthesis to Epigenetics
Maas, M. N., Hintzen, J. C. J., Porzberg, M. R. B., & Mecinović, J. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21249451 · Cited by 58 · see citing works
Pogribny, I. P., Tryndyak, V., Pogribna, M., Shpyleva, S., Surratt, G., da Costa, G. G., & Beland, F. A. (2013) · International Journal of Oncology · doi:10.3892/ijo.2013.1855 · Cited by 57 · see citing works
The histone methyltransferase DOT1L: regulatory functions and a cancer therapy target.
Wong, M., Polly, P., & Liu, T. (2015) · Europe PMC (PubMed Central) · Cited by 57 · see citing works
Mutant IDH in Gliomas: Role in Cancer and Treatment Options
Solomou, G., Finch, A., Asghar, A., & Bardella, C. (2023) · Cancers · doi:10.3390/cancers15112883 · Cited by 57 · see citing works
Fandrey, J., Schödel, J., Eckardt, K., Katschinski, D. M., & Wenger, R. H. (2019) · Pflügers Archiv - European Journal of Physiology · doi:10.1007/s00424-019-02334-8 · Cited by 54 · see citing works
The Epigenetic Role of Vitamin C in Neurodevelopment
Coker, S. J., Smith-Díaz, C. C., Dyson, R. M., Vissers, M. C. M., & Berry, M. J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23031208 · Cited by 56 · see citing works
Epigenetic drugs against cancer: an evolving landscape
Costanzo, A. D., Gaudio, N. D., Migliaccio, A., & Altucci, L. (2014) · Archives of Toxicology · doi:10.1007/s00204-014-1315-6 · Cited by 54 · see citing works
Pfeffer, I., Brewitz, L., Krojer, T. J., Jensen, S. A., Kochan, G. T., Kershaw, N. J., Hewitson, K. S., McNeill, L. A., Kramer, H., Münzel, M., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-12711-7 · Cited by 55 · see citing works
Tao, H., Mori, T., Chen, H., Lyu, S., Nonoyama, A., Lee, S., 张惠平, Hayashi, F., & Abe, I. (2022) · Nature Communications · doi:10.1038/s41467-021-27636-3 · Cited by 55 · see citing works
Targeting Tumor Hypoxia With Hypoxia-Activated Prodrugs
Yeh, J. J., & Kim, W. Y. (2015) · Journal of Clinical Oncology · doi:10.1200/jco.2014.60.0759 · Cited by 54 · see citing works
Wang, G., He, Q., Feng, C., Liu, Y., Deng, Z., Qi, X., Wu, W., Mei, P., & Chen, Z. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.590505 · Cited by 53 · see citing works
Huang, X., Lan, Y., Shen, J., Zhao, X., Zhou, Y., Wu, W., Mao, J., Wu, Y., Xie, Z., & Chen, Z. (2024) · Molecular Therapy · doi:10.1016/j.ymthe.2024.02.005 · Cited by 56 · see citing works
Tarhonskaya, H., Szöllössi, A., Leung, I. K. H., Bush, J. T., Henry, L., Chowdhury, R., Iqbal, A., Claridge, T. D. W., Schofield, C. J., & Flashman, E. (2014) · Biochemistry · doi:10.1021/bi500086p · Cited by 53 · see citing works
Ratcliffe, P. P., & Bishop, T. (2014) · Hypoxia · doi:10.2147/hp.s47598 · Cited by 52 · see citing works
Pro-metastatic collagen lysyl hydroxylase dimer assemblies stabilized by Fe2+-binding
Guo, H., Tsai, C.-L., Terajima, M., Tan, X., Banerjee, P., Miller, M. D., Liu, X., Jiang, Y. L., Byemerwa, J. K., Alvarado, S. K., et al. (2018) · Nature Communications · doi:10.1038/s41467-018-02859-z · Cited by 51 · see citing works
Docking and Linking of Fragments To Discover Jumonji Histone Demethylase Inhibitors
Korczynska, M., Le, D. D., Younger, N. S., Gregori‐Puigjané, E., Tumber, A., Krojer, T. J., Velupillai, S., Gileadi, C., Nowak, R. P., Iwasa, E., et al. (2015) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5b01527 · Cited by 51 · see citing works
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 51 · see citing works
TET enzymatic oxidation of 5-methylcytosine, 5-hydroxymethylcytosine and 5-formylcytosine
Cadet, J., & Wagner, J. R. (2013) · Mutation Research/Genetic Toxicology and Environmental Mutagenesis · doi:10.1016/j.mrgentox.2013.09.001 · Cited by 50 · see citing works
Katz, M. J., Acevedo, J. M., Loenarz, C., Galagovsky, D., Liu-Yi, P., Pérez-Pepe, M., Thalhammer, A., Sekirnik, R., Ge, W., Melani, M., et al. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1314485111 · Cited by 50 · see citing works
Mitochondrial metabolites extend lifespan
Mishur, R. J., Khan, M. H., Munkácsy, E., Sharma, L. K., Bokov, A. F., Beam, H., Radetskaya, O., Borror, M. B., Lane, R. K., Bai, Y., et al. (2016) · Aging Cell · doi:10.1111/acel.12439 · Cited by 50 · see citing works
Wenger, R. H., & Kurtz, A. (2011) · Comprehensive physiology · doi:10.1002/cphy.c100075 · Cited by 53 · see citing works
Zhao, S., Wu, L., Xu, Y., & Nie, Y. (2024) · Natural Product Reports · doi:10.1039/d4np00030g · Cited by 48 · see citing works
Structure and Function of TET Enzymes
Yin, X., & Xu, Y. (2016) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-43624-1_12 · Cited by 47 · see citing works
- Authors
- McDonough, M. A., Loenarz, C., Chowdhury, R., Clifton, I. J., & Schofield, C. J.
- Affiliations
- University of Oxford (GB)
- Corresponding author
- Schofield, Christopher J
- ORCID
- Venue
- Current Opinion in Structural Biology
- Publisher
- Elsevier BV
- Published
- 2010-12
- Volume
- 20
- Issue
- 6
- Pages
- 659-672
- ISSN
- 0959-440X (ISSN-L)
- OpenAlex
- W2069351864
- Cited by
- 280
- References
- 73
- Citations by year
- 2026: 7 · 2025: 12 · 2024: 16 · 2023: 15 · 2022: 20 · 2021: 13 · 2020: 27 · 2019: 16 · 2018: 18 · 2017: 15 · 2016: 20 · 2015: 29 · 2014: 33 · 2013: 16 · 2012: 16
- FWCI
- 0.56
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Current Opinion in Structural Biology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Wellcome Trust
- European Commission
- Biotechnology and Biological Sciences Research Council (BB/D011523/1, BB/F006349/1)
- Topics
- Physical Sciences › Chemistry › Inorganic Chemistry › Metal-Catalyzed Oxygenation Mechanisms
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- 2-oxoglutarate-dependent dioxygenase, substrate binding, collagen synthesis, gene expression regulation, lipid metabolism, crystal structure
- MeSH terms
- Animals, Fatty Acids, Humans, Hydroxylation, Ketoglutaric Acids, Nucleic Acids, Oxygenases, Biocatalysis
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
