The TET enzymes

The TET enzymes During the past decade, we have learnt that the most common DNA modification, 5-methylcytosine (5mC), playing crucial roles in development and disease, is not stable but can be actively reversed to its unmodified form via enzymatic catalysis involving the TET enzymes. These ground-breaking discoveries have been achieved thanks to technological advances in the detection of the oxidized forms of 5mC and to the boldness of individual scientists. The TET enzymes require molecular oxygen for their catalysis, making them important targets for hypoxia research. They also require special cofactors which enable additional levels of regulation. Moreover, mutations and other genetic alterations in TETs are found, especially in myeloid malignances. This review focuses on the kinetic and inhibitory properties of the TET enzymes and the role of TETs in cellular differentiation and transformation and in cancer. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Cellular and Molecular Life Sciences Springer Journals

The TET enzymes

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Publisher
Springer Journals
Copyright
Copyright © 2017 by Springer International Publishing AG, part of Springer Nature
Subject
Life Sciences; Cell Biology; Biomedicine, general; Life Sciences, general; Biochemistry, general
ISSN
1420-682X
eISSN
1420-9071
D.O.I.
10.1007/s00018-017-2721-8
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Abstract

During the past decade, we have learnt that the most common DNA modification, 5-methylcytosine (5mC), playing crucial roles in development and disease, is not stable but can be actively reversed to its unmodified form via enzymatic catalysis involving the TET enzymes. These ground-breaking discoveries have been achieved thanks to technological advances in the detection of the oxidized forms of 5mC and to the boldness of individual scientists. The TET enzymes require molecular oxygen for their catalysis, making them important targets for hypoxia research. They also require special cofactors which enable additional levels of regulation. Moreover, mutations and other genetic alterations in TETs are found, especially in myeloid malignances. This review focuses on the kinetic and inhibitory properties of the TET enzymes and the role of TETs in cellular differentiation and transformation and in cancer.

Journal

Cellular and Molecular Life Sciences – Springer Journals

Published: Nov 28, 2017

References

  • Conversion of 5-methylcytosine to 5-hydroxymethylcytosine in mammalian DNA by MLL partner TET1
    Tahiliani, M; Koh, KP; Shen, Y; Pastor, WA; Bandukwala, H; Brudno, Y; Agarwal, S; Iyer, LM; Liu, DR; Aravind, L; Rao, A
  • LCX, leukemia-associated protein with a CXXC domain, is fused to MLL in acute myeloid leukemia with trilineage dysplasia having t(10;11)(q22;q23)
    Ono, R; Taki, T; Taketani, T; Taniwaki, M; Kobayashi, H; Hayashi, Y
  • TET1, a member of a novel protein family, is fused to MLL in acute myeloid leukemia containing the t(10;11)(q22;q23)
    Lorsbach, RB; Moore, J; Mathew, S; Raimondi, SC; Mukatira, ST; Downing, JR
  • The nuclear DNA base 5-hydroxymethylcytosine is present in Purkinje neurons and the brain
    Kriaucionis, S; Heintz, N
  • Role of Tet proteins in 5mC to 5hmC conversion, ES-cell self-renewal and inner cell mass specification
    Ito, S; D’Alessio, AC; Taranova, OV; Hong, K; Sowers, LC; Zhang, Y
  • Inhibition of 2-oxoglutarate dependent oxygenases
    Rose, NR; McDonough, MA; King, ON; Kawamura, A; Schofield, CJ
  • Prolyl 4-hydroxylases, key enzymes in the synthesis of collagens and regulation of the response to hypoxia, and their roles as treatment targets
    Myllyharju, J
  • Tet-mediated formation of 5-carboxylcytosine and its excision by TDG in mammalian DNA
    He, Y; Li, B; Li, Z; Liu, P; Wang, Y; Tang, Q; Ding, J; Jia, Y; Chen, Z; Li, L; Sun, Y; Li, X; Dai, Q; Song, C; Zhang, K; He, C; Xu, G
  • Isoform switch of TET1 regulates DNA demethylation and mouse development
    Zhang, W; Xia, W; Wang, Q; Towers, AJ; Chen, J; Gao, R; Zhang, Y; Yen, CA; Lee, AY; Li, Y; Zhou, C; Liu, K; Zhang, J; Gu, TP; Chen, X; Chang, Z; Leung, D; Gao, S; Jiang, YH; Xie, W
  • Intrinsic and extrinsic connections of Tet3 dioxygenase with CXXC zinc finger modules
    Liu, N; Wang, M; Deng, W; Schmidt, CS; Qin, W; Leonhardt, H; Spada, F
  • Tet3 reads 5-carboxylcytosine through its CXXC domain and is a potential guardian against neurodegeneration
    Jin, SG; Zhang, ZM; Dunwell, TL; Harter, MR; Wu, X; Johnson, J; Li, Z; Liu, J; Szabo, PE; Lu, Q; Xu, GL; Song, J; Pfeifer, GP
  • Modulation of TET2 expression and 5-methylcytosine oxidation by the CXXC domain protein IDAX
    Ko, M; An, J; Bandukwala, HS; Chavez, L; Aijo, T; Pastor, WA; Segal, MF; Li, H; Koh, KP; Lahdesmaki, H; Hogan, PG; Aravind, L; Rao, A
  • Phosphoproteomic analysis of human embryonic stem cells
    Brill, LM; Xiong, W; Lee, KB; Ficarro, SB; Crain, A; Xu, Y; Terskikh, A; Snyder, EY; Ding, S
  • Phosphorylation of TET proteins is regulated via O-GlcNAcylation by the O-linked N-acetylglucosamine transferase (OGT)
    Bauer, C; Gobel, K; Nagaraj, N; Colantuoni, C; Wang, M; Muller, U; Kremmer, E; Rottach, A; Leonhardt, H
  • Fumarate and succinate regulate expression of hypoxia-inducible genes via TET enzymes
    Laukka, T; Mariani, CJ; Ihantola, T; Cao, JZ; Hokkanen, J; Kaelin, WG; Godley, LA; Koivunen, P
  • Collagen hydroxylases and the protein disulfide isomerase subunit of prolyl 4-hydroxylases
    Kivirikko, KI; Pihlajaniemi, T
  • Effect of desferrioxamine and metals on the hydroxylases in the oxygen sensing pathway
    Hirsila, M; Koivunen, P; Xu, L; Seeley, T; Kivirikko, KI; Myllyharju, J
  • Tumour hypoxia causes DNA hypermethylation by reducing TET activity
    Thienpont, B; Steinbacher, J; Zhao, H; D’Anna, F; Kuchnio, A; Ploumakis, A; Ghesquiere, B; Dyck, L; Boeckx, B; Schoonjans, L; Hermans, E; Amant, F; Kristensen, VN; Peng Koh, K; Mazzone, M; Coleman, M; Carell, T; Carmeliet, P; Lambrechts, D
  • Structural insight into substrate preference for TET-mediated oxidation
    Hu, L; Lu, J; Cheng, J; Rao, Q; Li, Z; Hou, H; Lou, Z; Zhang, L; Li, W; Gong, W; Liu, M; Sun, C; Yin, X; Li, J; Tan, X; Wang, P; Wang, Y; Fang, D; Cui, Q; Yang, P; He, C; Jiang, H; Luo, C; Xu, Y
  • Analysis of TET expression/activity and 5mC oxidation during normal and malignant germ cell development
    Nettersheim, D; Heukamp, LC; Fronhoffs, F; Grewe, MJ; Haas, N; Waha, A; Honecker, F; Waha, A; Kristiansen, G; Schorle, H
  • Overexpression of TET dioxygenases in seminomas associates with low levels of DNA methylation and hydroxymethylation
    Benesova, M; Trejbalova, K; Kucerova, D; Vernerova, Z; Hron, T; Szabo, A; Amouroux, R; Klezl, P; Hajkova, P; Hejnar, J
  • 5-Hydroxymethylcytosine in cancer: significance in diagnosis and therapy
    Vasanthakumar, A; Godley, LA
  • Tet proteins can convert 5-methylcytosine to 5-formylcytosine and 5-carboxylcytosine
    Ito, Shinsuke; Shen, Li; Dai, Qing; Wu, Susan C; Collins, Leonard B; Swenberg, James A; He, Chuan; Zhang, Yi
  • A screen for hydroxymethylcytosine and formylcytosine binding proteins suggests functions in transcription and chromatin regulation
    Iurlaro, M; Ficz, G; Oxley, D; Raiber, E; Bachman, M; Booth, MJ; Andrews, S; Balasubramanian, S; Reik, W
  • In vivo genome-wide profiling reveals a tissue-specific role for 5-formylcytosine
    Iurlaro, M; McInroy, GR; Burgess, HE; Dean, W; Raiber, E; Bachman, M; Beraldi, D; Balasubramanian, S; Reik, W
  • Loss of 5-hydroxymethylcytosine is an epigenetic hallmark of melanoma
    Lian, CG; Xu, Y; Ceol, C; Wu, F; Larson, A; Dresser, K; Xu, W; Tan, L; Hu, Y; Zhan, Q; Lee, CW; Hu, D; Lian, BQ; Kleffel, S; Yang, Y; Neiswender, J; Khorasani, AJ; Fang, R; Lezcano, C; Duncan, LM; Scolyer, RA; Thompson, JF; Kakavand, H; Houvras, Y; Zon, LI; Mihm, MC; Kaiser, UB; Schatton, T; Woda, BA; Murphy, GF; Shi, YG
  • MicroRNA-antagonism regulates breast cancer stemness and metastasis via TET-family-dependent chromatin remodeling
    Song, SJ; Poliseno, L; Song, MS; Ala, U; Webster, K; Ng, C; Beringer, G; Brikbak, NJ; Yuan, X; Cantley, LC; Richardson, AL; Pandolfi, PP
  • CpG islands and the regulation of transcription
    Deaton, AM; Bird, A
  • The epigenomics of cancer
    Jones, PA; Baylin, SB
  • CpG island methylator phenotype in colorectal cancer
    Toyota, M; Ahuja, N; Ohe-Toyota, M; Herman, JG; Baylin, SB; Issa, JP
  • TET family dioxygenases and DNA demethylation in stem cells and cancers
    An, J; Rao, A; Ko, M
  • Loss of 5-hydroxymethylcytosine is an independent unfavorable prognostic factor for esophageal squamous cell carcinoma
    Shi, X; Yu, Y; Luo, M; Zhang, Z; Shi, S; Feng, X; Chen, Z; He, J
  • Decreased 5-hydroxymethylcytosine levels correlate with cancer progression and poor survival: a systematic review and meta-analysis
    Chen, Z; Shi, X; Guo, L; Li, Y; Luo, M; He, J
  • Low level of 5-hydroxymethylcytosine predicts poor prognosis in non-small cell lung cancer
    Liao, Y; Gu, J; Wu, Y; Long, X; Ge, DI; Xu, J; Ding, J
  • Decreased 5-hydroxymethylcytosine is associated with neural progenitor phenotype in normal brain and shorter survival in malignant glioma
    Orr, BA; Haffner, MC; Nelson, WG; Yegnasubramanian, S; Eberhart, CG
  • Characterization of TET and IDH gene expression in chronic lymphocytic leukemia: comparison with normal B cells and prognostic significance
    Damme, M; Crompot, E; Meuleman, N; Maerevoet, M; Mineur, P; Bron, D; Lagneaux, L; Stamatopoulos, B
  • Tet and TDG mediate DNA demethylation essential for mesenchymal-to-epithelial transition in somatic cell reprogramming
    Hu, X; Zhang, L; Mao, SQ; Li, Z; Chen, J; Zhang, RR; Wu, HP; Gao, J; Guo, F; Liu, W; Xu, GF; Dai, HQ; Shi, YG; Li, X; Hu, B; Tang, F; Pei, D; Xu, GL
  • Genetic characterization of TET1, TET2, and TET3 alterations in myeloid malignancies
    Abdel-Wahab, O; Mullally, A; Hedvat, C; Garcia-Manero, G; Patel, J; Wadleigh, M; Malinge, S; Yao, J; Kilpivaara, O; Bhat, R; Huberman, K; Thomas, S; Dolgalev, I; Heguy, A; Paietta, E; Beau, MM; Beran, M; Tallman, MS; Ebert, BL; Kantarjian, HM; Stone, RM; Gilliland, DG; Crispino, JD; Levine, RL
  • Mutation in TET2 in myeloid cancers
    Delhommeau, F; Dupont, S; Della Valle, V; James, C; Trannoy, S; Masse, A; Kosmider, O; Couedic, JP; Robert, F; Alberdi, A; Lecluse, Y; Plo, I; Dreyfus, FJ; Marzac, C; Casadevall, N; Lacombe, C; Romana, SP; Dessen, P; Soulier, J; Viguie, F; Fontenay, M; Vainchenker, W; Bernard, OA
  • The Ten-Eleven Translocation-2 (TET2) gene in hematopoiesis and hematopoietic diseases
    Solary, E; Bernard, OA; Tefferi, A; Fuks, F; Vainchenker, W
  • TET2 and DNMT3A mutations in human T-cell lymphoma
    Couronne, L; Bastard, C; Bernard, OA
  • Impaired hydroxylation of 5-methylcytosine in myeloid cancers with mutant TET2
    Ko, M; Huang, Y; Jankowska, AM; Pape, UJ; Tahiliani, M; Bandukwala, HS; An, J; Lamperti, ED; Koh, KP; Ganetzky, R; Liu, XS; Aravind, L; Agarwal, S; Maciejewski, JP; Rao, A
  • TET1 plays an essential oncogenic role in MLL-rearranged leukemia
    Huang, H; Jiang, X; Li, Z; Li, Y; Song, CX; He, C; Sun, M; Chen, P; Gurbuxani, S; Wang, J; Hong, GM; Elkahloun, AG; Arnovitz, S; Wang, J; Szulwach, K; Lin, L; Street, C; Wunderlich, M; Dawlaty, M; Neilly, MB; Jaenisch, R; Yang, FC; Mulloy, JC; Jin, P; Liu, PP; Rowley, JD; Xu, M; He, C; Chen, J
  • Exome sequencing identifies mutation in CNOT3 and ribosomal genes RPL5 and RPL10 in T-cell acute lymphoblastic leukemia
    Keersmaecker, K; Atak, ZK; Li, N; Vicente, C; Patchett, S; Girardi, T; Gianfelici, V; Geerdens, E; Clappier, E; Porcu, M; Lahortiga, I; Luca, R; Yan, J; Hulselmans, G; Vranckx, H; Vandepoel, R; Sweron, B; Jacobs, K; Mentens, N; Wlodarska, I; Cauwelier, B; Cloos, J; Soulier, J; Uyttebroeck, A; Bagni, C; Hassan, BA; Vandenberghe, P; Johnson, AW; Aerts, S; Cools, J
  • The role of Tet3 DNA dioxygenase in epigenetic reprogramming by oocytes
    Gu, TP; Guo, F; Yang, H; Wu, HP; Xu, GF; Liu, W; Xie, ZG; Shi, L; He, X; Jin, SG; Iqbal, K; Shi, YG; Deng, Z; Szabo, PE; Pfeifer, GP; Li, J; Xu, GL
  • Tet1 is dispensable for maintaining pluripotency and its loss is compatible with embryonic and postnatal development
    Dawlaty, MM; Ganz, K; Powell, BE; Hu, YC; Markoulaki, S; Cheng, AW; Gao, Q; Kim, J; Choi, SW; Page, DC; Jaenisch, R
  • Tet2 loss leads to increased hematopoietic stem cell self-renewal and myeloid transformation
    Moran-Crusio, K; Reavie, L; Shih, A; Abdel-Wahab, O; Ndiaye-Lobry, D; Lobry, C; Figueroa, ME; Vasanthakumar, A; Patel, J; Zhao, X; Perna, F; Pandey, S; Madzo, J; Song, C; Dai, Q; He, C; Ibrahim, S; Beran, M; Zavadil, J; Nimer, SD; Melnick, A; Godley, LA; Aifantis, I; Levine, RL
  • TET2 inactivation results in pleiotropic hematopoietic abnormalities in mouse and is a recurrent event during human lymphomagenesis
    Quivoron, C; Couronne, L; Della Valle, V; Lopez, CK; Plo, I; Wagner-Ballon, O; Do Cruzeiro, M; Delhommeau, F; Arnulf, B; Stern, MH; Godley, L; Opolon, P; Tilly, H; Solary, E; Duffourd, Y; Dessen, P; Merle-Beral, H; Nguyen-Khac, F; Fontenay, M; Vainchenker, W; Bastard, C; Mercher, T; Bernard, OA
  • Combined deficiency of Tet1 and Tet2 causes epigenetic abnormalities but is compatible with postnatal development
    Dawlaty, MM; Breiling, A; Le, T; Raddatz, G; Barrasa, MI; Cheng, AW; Gao, Q; Powell, BE; Li, Z; Xu, M; Faull, KF; Lyko, F; Jaenisch, R
  • Hypoxia-inducible factors: master regulators of cancer progression
    Schito, L; Semenza, GL
  • TET1-mediated hydroxymethylation facilitates hypoxic gene induction in neuroblastoma
    Mariani, CJ; Vasanthakumar, A; Madzo, J; Yesilkanal, A; Bhagat, T; Yu, Y; Bhattacharyya, S; Wenger, RH; Cohn, SL; Nanduri, J; Verma, A; Prabhakar, NR; Godley, LA
  • Novel epigenetic controlling of hypoxia pathway related to overexpression and promoter hypomethylation of TET1 and TET2 in RPE cells
    Alivand, MR; Soheili, ZS; Pornour, M; Solali, S; Sabouni, F
  • Accumulation of Krebs cycle intermediates and over-expression of HIF1alpha in tumours which result from germline FH and SDH mutations
    Pollard, PJ; Briere, JJ; Alam, NA; Barwell, J; Barclay, E; Wortham, NC; Hunt, T; Mitchell, M; Olpin, S; Moat, SJ; Hargreaves, IP; Heales, SJ; Chung, YL; Griffiths, JR; Dalgleish, A; McGrath, JA; Gleeson, MJ; Hodgson, SV; Poulsom, R; Rustin, P; Tomlinson, IP
  • Inhibition of alpha-KG-dependent histone and DNA demethylases by fumarate and succinate that are accumulated in mutations of FH and SDH tumor suppressors
    Xiao, M; Yang, H; Xu, W; Ma, S; Lin, H; Zhu, H; Liu, L; Liu, Y; Yang, C; Xu, Y; Zhao, S; Ye, D; Xiong, Y; Guan, KL
  • SDH mutations establish a hypermethylator phenotype in paraganglioma
    Letouze, E; Martinelli, C; Loriot, C; Burnichon, N; Abermil, N; Ottolenghi, C; Janin, M; Menara, M; Nguyen, AT; Benit, P; Buffet, A; Marcaillou, C; Bertherat, J; Amar, L; Rustin, P; Reynies, A; Gimenez-Roqueplo, AP; Favier, J
  • Intracellular alpha-ketoglutarate maintains the pluripotency of embryonic stem cells
    Carey, BW; Finley, LW; Cross, JR; Allis, CD; Thompson, CB
  • Multiple sclerosis: immunopathology and treatment update
    Dargahi, N; Katsara, M; Tselios, T; Androutsou, ME; Courten, M; Matsoukas, J; Apostolopoulos, V
  • Oncometabolite 2-hydroxyglutarate is a competitive inhibitor of alpha-ketoglutarate-dependent dioxygenases
    Xu, W; Yang, H; Liu, Y; Yang, Y; Wang, P; Kim, SH; Ito, S; Yang, C; Wang, P; Xiao, MT; Liu, LX; Jiang, WQ; Liu, J; Zhang, JY; Wang, B; Frye, S; Zhang, Y; Xu, YH; Lei, QY; Guan, KL; Zhao, SM; Xiong, Y
  • The oncometabolite 2-hydroxyglutarate inhibits histone lysine demethylases
    Chowdhury, R; Yeoh, KK; Tian, YM; Hillringhaus, L; Bagg, EA; Rose, NR; Leung, IK; Li, XS; Woon, EC; Yang, M; McDonough, MA; King, ON; Clifton, IJ; Klose, RJ; Claridge, TD; Ratcliffe, PJ; Schofield, CJ; Kawamura, A
  • Transformation by the (R)-enantiomer of 2-hydroxyglutarate linked to EGLN activation
    Koivunen, P; Lee, S; Duncan, CG; Lopez, G; Lu, G; Ramkissoon, S; Losman, JA; Joensuu, P; Bergmann, U; Gross, S; Travins, J; Weiss, S; Looper, R; Ligon, KL; Verhaak, RG; Yan, H; Kaelin, WG
  • Detection of 2-hydroxyglutarate in IDH-mutated glioma patients by in vivo spectral-editing and 2D correlation magnetic resonance spectroscopy
    Andronesi, OC; Kim, GS; Gerstner, E; Batchelor, T; Tzika, AA; Fantin, VR; Vander Heiden, MG; Sorensen, AG
  • A gene encoding a putative FAD-dependent l-2-hydroxyglutarate dehydrogenase is mutated in l-2-hydroxyglutaric aciduria
    Rzem, R; Veiga-da-Cunha, M; Noel, G; Goffette, S; Nassogne, MC; Tabarki, B; Scholler, C; Marquardt, T; Vikkula, M; Schaftingen, E
  • l-2-Hydroxyglutaric aciduria: identification of a mutant gene C14orf160, localized on chromosome 14q22.1
    Topcu, M; Jobard, F; Halliez, S; Coskun, T; Yalcinkayal, C; Gerceker, FO; Wanders, RJ; Prud’homme, JF; Lathrop, M; Ozguc, M; Fischer, J
  • De novo DNA methylation drives 5hmC accumulation in mouse zygotes
    Amouroux, R; Nashun, B; Shirane, K; Nakagawa, S; Hill, PW; D’Souza, Z; Nakayama, M; Matsuda, M; Turp, A; Ndjetehe, E; Encheva, V; Kudo, NR; Koseki, H; Sasaki, H; Hajkova, P
  • Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor
    Hirsila, M; Koivunen, P; Gunzler, V; Kivirikko, KI; Myllyharju, J
  • The hydroxylase inhibitor dimethyloxalylglycine is protective in a murine model of colitis
    Cummins, EP; Seeballuck, F; Keely, SJ; Mangan, NE; Callanan, JJ; Fallon, PG; Taylor, CT
  • HIF-1 activation attenuates postischemic myocardial injury: role for heme oxygenase-1 in modulating microvascular chemokine generation
    Ockaili, R; Natarajan, R; Salloum, F; Fisher, BJ; Jones, D; Fowler, AA; Kukreja, RC
  • Inhibition of hypoxia inducible factor hydroxylases protects against renal ischemia-reperfusion injury
    Hill, P; Shukla, D; Tran, MG; Aragones, J; Cook, HT; Carmeliet, P; Maxwell, PH
  • Global 5-hydroxymethylcytosine levels are profoundly reduced in multiple genitourinary malignancies
    Munari, E; Chaux, A; Vaghasia, AM; Taheri, D; Karram, S; Bezerra, SM; Gonzalez Roibon, N; Nelson, WG; Yegnasubramanian, S; Netto, GJ; Haffner, MC
  • Global 5-hydroxymethylcytosine content is significantly reduced in tissue stem/progenitor cell compartments and in human cancers
    Haffner, MC; Chaux, A; Meeker, AK; Esopi, DM; Gerber, J; Pellakuru, LG; Toubaji, A; Argani, P; Iacobuzio-Donahue, C; Nelson, WG; Netto, GJ; Marzo, AM; Yegnasubramanian, S
  • TET1 suppresses cancer invasion by activating the tissue inhibitors of metalloproteinases
    Hsu, CH; Peng, KL; Kang, ML; Chen, YR; Yang, YC; Tsai, CH; Chu, CS; Jeng, YM; Chen, YT; Lin, FM; Huang, HD; Lu, YY; Teng, YC; Lin, ST; Lin, RK; Tang, FM; Lee, SB; Hsu, HM; Yu, JC; Hsiao, PW; Juan, LJ
  • Loss of 5-hydroxymethylcytosine is linked to gene body hypermethylation in kidney cancer
    Chen, K; Zhang, J; Guo, Z; Ma, Q; Xu, Z; Zhou, Y; Xu, Z; Li, Z; Liu, Y; Ye, X; Li, X; Yuan, B; Ke, Y; He, C; Zhou, L; Liu, J; Ci, W
  • Loss of the epigenetic mark, 5-hydroxymethylcytosine, correlates with small cell/nevoid subpopulations and assists in microstaging of human melanoma
    Lee, JJ; Cook, M; Mihm, MC; Xu, S; Zhan, Q; Wang, TJ; Murphy, GF; Lian, CG
  • Epigenetic silencing of TET2 and TET3 induces an EMT-like process in melanoma
    Gong, F; Guo, Y; Niu, Y; Jin, J; Zhang, X; Shi, X; Zhang, L; Li, R; Chen, L; Ma, RZ
  • Combined loss of Tet1 and Tet2 promotes B cell, but not myeloid malignancies, in mice
    Zhao, Z; Chen, L; Dawlaty, MM; Pan, F; Weeks, O; Zhou, Y; Cao, Z; Shi, H; Wang, J; Lin, L; Chen, S; Yuan, W; Qin, Z; Ni, H; Nimer, SD; Yang, FC; Jaenisch, R; Jin, P; Xu, M
  • Fumarate is an epigenetic modifier that elicits epithelial-to-mesenchymal transition
    Sciacovelli, M; Gonçalves, E; Johnson, TI; Zecchini, VR; Costa, Ana; Henriques, Sofia; Gaude, E; Drubbel, AV; Theobald, SJ; Abbo, SR; Tran, MGB; Rajeeve, V; Cardaci, S; Foster, S; Yun, H; Cutillas, P; Warren, A; Gnanapragasam, V; Gottlieb, E; Franze, K; Huntly, B; Maher, ER; Maxwell, PH; Saez-Rodriguez, J; Frezza, C
  • 5-Hydroxymethylcytosine expression in proliferative nodules arising within congenital nevi allows differentiation from malignant melanoma
    Pavlova, O; Fraitag, S; Hohl, D
  • TET family proteins and 5-hydroxymethylcytosine in esophageal squamous cell carcinoma
    Murata, A; Baba, Y; Ishimoto, T; Miyake, K; Kosumi, K; Harada, K; Kurashige, J; Iwagami, S; Sakamoto, Y; Miyamoto, Y; Yoshida, N; Yamamoto, M; Oda, S; Watanabe, M; Nakao, M; Baba, H
  • Decreased 5-Hydroxymethylcytosine (5-hmC) predicts poor prognosis in early-stage laryngeal squamous cell carcinoma
    Zhang, Y; Wu, K; Shao, Y; Sui, F; Yang, Q; Shi, B; Hou, P; Ji, M
  • Adult T cell leukemia aggressivenness correlates with loss of both 5-hydroxymethylcytosine and TET2 expression
    Marçais, A; Waast, L; Bruneau, J; Hanssens, K; Asnafi, V; Gaulard, P; Suarez, F; Dubreuil, P; Gessain, A; Hermine, O; Pique, C
  • Impact of TET2 mutations on response rate to azacitidine in myelodysplastic syndromes and low blast count acute myeloid leukemias
    Itzykson, R; Kosmider, O; Cluzeau, T; Mansat-De Mas, V; Dreyfus, F; Beyne-Rauzy, O; Quesnel, B; Vey, N; Gelsi-Boyer, V; Raynaud, S; Preudhomme, C; Ades, L; Fenaux, P; Fontenay, M
  • TET2 mutations predict response to hypomethylating agents in myelodysplastic syndrome patients
    Bejar, R; Lord, A; Stevenson, K; Bar-Natan, M; Perez-Ladaga, A; Zaneveld, J; Wang, H; Caughey, B; Stojanov, P; Getz, G; Garcia-Manero, G; Kantarjian, H; Chen, R; Stone, RM; Neuberg, D; Steensma, DP; Ebert, BL
  • Inhibition of hypoxia-inducible factor (HIF) hydroxylases by citric acid cycle intermediates: possible links between cell metabolism and stabilization of HIF
    Koivunen, P; Hirsila, M; Remes, AM; Hassinen, IE; Kivirikko, KI; Myllyharju, J
  • The length of peptide substrates has a marked effect on hydroxylation by the hypoxia-inducible factor prolyl 4-hydroxylases
    Koivunen, P; Hirsila, M; Kivirikko, KI; Myllyharju, J
  • Studies on the activity of the hypoxia-inducible-factor hydroxylases using an oxygen consumption assay
    Ehrismann, D; Flashman, E; Genn, DN; Mathioudakis, N; Hewitson, KS; Ratcliffe, PJ; Schofield, CJ
  • Characterization of the iron- and 2-oxoglutarate-binding sites of human prolyl 4-hydroxylase
    Myllyharju, J; Kivirikko, KI
  • Hydroxylation of (Pro-Pro-Gly)5 and (Pro-Pro-Gly)10 by prolyl hydroxylase. Evidence for an asymmetric active site in the enzyme
    Berg, RA; Kishida, Y; Sakakibara, S; Prockop, DJ
  • Catalytic properties of the asparaginyl hydroxylase (FIH) in the oxygen sensing pathway are distinct from those of its prolyl 4-hydroxylases
    Koivunen, P; Hirsila, M; Gunzler, V; Kivirikko, KI; Myllyharju, J
  • The activity of JmjC histone lysine demethylase KDM4A is highly sensitive to oxygen concentrations
    Hancock, RL; Masson, N; Dunne, K; Flashman, E; Kawamura, A
  • Studies on the catalytic domains of multiple JmjC oxygenases using peptide substrates
    Williams, ST; Walport, LJ; Hopkinson, RJ; Madden, SK; Chowdhury, R; Schofield, CJ; Kawamura, A
  • Repair of methylation damage in DNA and RNA by mammalian AlkB homologues
    Lee, DH; Jin, SG; Cai, S; Chen, Y; Pfeifer, GP; O’Connor, TR
  • The 2-oxoglutarate binding site of prolyl 4-hydroxylase. Identification of distinct subsites and evidence for 2-oxoglutarate decarboxylation in a ligand reaction at the enzyme-bound ferrous ion
    Majamaa, K; Hanauske-Abel, HM; Gunzler, V; Kivirikko, KI
  • Mechanism of the prolyl hydroxylase reaction. 1. Role of co-substrates
    Tuderman, L; Myllyla, R; Kivirikko, KI
  • Inhibitor scaffolds for 2-oxoglutarate-dependent histone lysine demethylases
    Rose, NR; Ng, SS; Mecinovic, J; Lienard, BM; Bello, SH; Sun, Z; McDonough, MA; Oppermann, U; Schofield, CJ

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