Udo Oppermann

Principal Investigator

University of Oxford
+44 (0)1865 227306

Professor Udo Oppermann obtained a Diploma in Human Biology in 1990 and PhD in Pharmacology and Toxicology in 1994, both with distinctions from Philipps University Marburg, Germany. He went on to become Associate Professor at Karolinska Institutet, Stockholm, in the Department of Medical Biochemistry and Biophysics where he stayed until 2004. After a sabbatical stay at Yale University, he has been a Principal Investigator of the Structural Genomics Consortium (SGC) in Oxford since its inception in 2003. In 2008 he became Professor in Molecular Biology at the Nuffield Department of Orthopaedics, Rheumatology and Musculoskeletal Sciences, and he is now Deputy Director of the Institute of Musculoskeletal Sciences, Botnar Research Centre, University of Oxford, as well as a Fellow of St Catherine's College.

Research Areas

Epigenetics describes inherited and acquired modifications of DNA, histones and proteins, which play critical roles in the regulation of gene expression, in chromosome stability, genomic imprinting, and differentiation. Alterations in epigenetic signaling are involved in major diseases including cancer, metabolic and neurodegenerative diseases. A dissection of the molecular mechanisms of epigenetic signaling will be facilitated by the availability of small molecule chemical probes that are selective for specific components of the epigenetic machinery. Our research focuses on the biology and structure-activity relationships of human metabolic protein families of all types but with emphasis on oxidoreductases such as short- or medium chain dehydrogenases / reductases (SDR, MDR), or oxidative enzymes such as the ketoglutarate dependent oxygenases. The use of chemical and structural biology to understand human biology is a major focus of the group and is currently applied to the field of epigenetic mechanisms in mesenchymal stem cell and bone biology, as well as chronic inflammatory, malignant and metabolic diseases (for further details visit the Botnar Research Centre website).

Publications

The roles of Jumonji-type oxygenases in human disease.
Johansson, C; Tumber, A; Che, K; Cain, P; Nowak, R; Gileadi, C; Oppermann, U;
Epigenomics. 2014 6:89-120. doi: 10.2217/epi.13.79
PMID: 24579949

Why is epigenetics important in understanding the pathogenesis of inflammatory musculoskeletal diseases?
O, U; p, ; p, ; e, ; r, ; m, ; a, ; n, ; n, ;
Arthritis Research and Therapy. 2013 15:209-. doi: 10.1186/ar4186
PMID: 23566317

A selective jumonji H3K27 demethylase inhibitor modulates the proinflammatory macrophage response.
Kruidenier, L; Chung, CW; Cheng, Z; Liddle, J; Che, K; Joberty, G; Bantscheff, M; Bountra, C; Bridges, A; Diallo, H; Eberhard, D; Hutchinson, S; Jones, E; Katso, R; Leveridge, M; Mander, PK; Mosley, J; Ramirez-Molina, C; Rowland, P; Schofield, CJ; Sheppard, RJ; Smith, JE; Swales, C; Tanner, R; Thomas, P; Tumber, A; Drewes, G; Oppermann, U; Patel, DJ; Lee, K; Wilson, DM;
Nature. 2012 488:404-408. doi: 10.1038/nature11262
PMID: 22842901

Structural and evolutionary basis for the dual substrate selectivity of human KDM4 histone demethylase family.
Hillringhaus, L; Yue, WW; Rose, NR; Ng, SS; Gileadi, C; Loenarz, C; Bello, SH; Bray, JE; Schofield, CJ; Oppermann, U;
Journal of Biological Chemistry. 2011 286:41616-41625. doi: 10.1074/jbc.M111.283689
PMID: 21914792

Crystal structures of the endoplasmic reticulum aminopeptidase-1 (ERAP1) reveal the molecular basis for N-terminal peptide trimming.
Kochan, G; Krojer, T; Harvey, D; Fischer, R; Chen, L; Vollmar, M; von Delft, F; Kavanagh, KL; Brown, MA; Bowness, P; Wordsworth, P; Kessler, BM; Oppermann, U;
Proceedings of the National Academy of Sciences of USA. 2011 108:7745-7750. doi: 10.1073/pnas.1101262108
PMID: 21508329

Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity.
Ng, SS; Kavanagh, KL; McDonough, MA; Butler, D; Pilka, ES; Lienard, BM; Bray, JE; Savitsky, P; Gileadi, O; von Delft, F; Rose, NR; Offer, J; Scheinost, JC; Borowski, T; Sundstrom, M; Schofield, CJ; Oppermann, U;
Nature. 2007 448:87-91. doi: 10.1038/nature05971
PMID: 17589501

2016

Advances and challenges in understanding histone demethylase biology.
Nowak, RP; Tumber, A; Johansson, C; Che, KH; Brennan, P; Owen, D; Oppermann, U;
Current Opinion in Chemical Biology. 2016 33:151-159. doi:
PMID: 27371875

Structural analysis of human KDM5B guides histone demethylase inhibitor development.
Johansson, C; Velupillai, S; Tumber, A; Szykowska, A; Hookway, ES; Nowak, RP; Strain-Damerell, C; Gileadi, C; Philpott, M; Burgess-Brown, N; Wu, N; Kopec, J; Nuzzi, A; Steuber, H; Egner, U; Badock, V; Munro, S; LaThangue, NB; Westaway, S; Brown, J; Athanasou, N; Prinjha, R; Brennan, PE; Oppermann, U;
Nature Chemical Biology. 2016 12:539-545. doi:
PMID: 27214403

The first international workshop on the epigenetics of osteoarthritis.
Meulenbelt, IM; Bhutani, N; den Hollander, W; Gay, S; Oppermann, U; Reynard, LN; Skelton, AJ; Young, DA; Beier, F; Loughlin, J;
Connective Tissue Research. 2016 :-. doi:
PMID: 27028588

Characterization of NK Cells in Endometriosis Associated Pain.
Soderstrom, K; Southcombe, J; Malzahn, J; Putsep, L; Oppermann, U; Shang, C; Becker, C; Zondervan, K; Martin-Fischer, O; Zollner, TM; Granne, I; Sacher, F;
Reproductive Sciences. 2016 23:161A-161A. doi:
PMID:

Sclerostin expression in bone tumours and tumour-like lesions.
Inagaki, Y; Hookway, ES; Kashima, TG; Munemoto, M; Tanaka, Y; Hassan, AB; Oppermann, U; Athanasou, NA;
Histopathology. 2016 69:470-478. doi:
PMID: 26896083

Identification of a small-molecule ligand of the epigenetic reader protein Spindlin1 via a versatile screening platform.
Wagner, T; Greschik, H; Burgahn, T; Schmidtkunz, K; Schott, AK; McMillan, J; Baranauskienė, L; Xiong, Y; Fedorov, O; Jin, J; Oppermann, U; Matulis, D; Schüle, R; Jung, M;
Nucleic Acids Research. 2016 44:e88-. doi:
PMID: 26893353

8-Substituted Pyrido[3,4-d]pyrimidin-4(3H)-one Derivatives As Potent, Cell Permeable, KDM4 (JMJD2) and KDM5 (JARID1) Histone Lysine Demethylase Inhibitors.
Bavetsias, V; Lanigan, RM; Ruda, GF; Atrash, B; McLaughlin, MG; Tumber, A; Mok, NY; Le Bihan, YV; Dempster, S; Boxall, KJ; Jeganathan, F; Hatch, SB; Savitsky, P; Velupillai, S; Krojer, T; England, KS; Sejberg, J; Thai, C; Donovan, A; Pal, A; Scozzafava, G; Bennett, JM; Kawamura, A; Johansson, C; Szykowska, A; Gileadi, C; Burgess-Brown, NA; von Delft, F; Oppermann, U; Walters, Z; Shipley, J; Raynaud, FI; Westaway, SM; Prinjha, RK; Fedorov, O; Burke, R; Schofield, CJ; Westwood, IM; Bountra, C; Müller, S; van Montfort, RL; Brennan, PE; Blagg, J;
Journal of Medicinal Chemistry. 2016 59:1388-1409. doi:
PMID: 26741168

H3K27me3 demethylases regulate in vitro chondrogenesis and chondrocyte activity in osteoarthritis.
Yapp, C; Carr, AJ; Price, A; Oppermann, U; Snelling, SJ;
Arthritis Research and Therapy. 2016 18:158-. doi:
PMID: 27388528

A germline mutation of CDKN2A and a novel RPLP1-C19MC fusion detected in a rare melanotic neuroectodermal tumor of infancy: a case report.
Barnes, DJ; Hookway, E; Athanasou, N; Kashima, T; Oppermann, U; Hughes, S; Swan, D; Lueerssen, D; Anson, J; Hassan, AB;
BMC Cancer. 2016 16:629-. doi:
PMID: 27519597

Dendritic and mast cell involvement in the inflammatory response to primary malignant bone tumours.
Inagaki, Y; Hookway, E; Williams, KA; Hassan, AB; Oppermann, U; Tanaka, Y; Soilleux, E; Athanasou, NA;
Clinical Sarcoma Research. 2016 6:13-. doi:
PMID: 27482375

Structures of Two Melanoma-Associated Antigens Suggest Allosteric Regulation of Effector Binding.
Newman, JA; Cooper, CD; Roos, AK; Aitkenhead, H; Oppermann, UC; Cho, HJ; Osman, R; Gileadi, O;
PLoS One. 2016 11:e0148762-. doi:
PMID: 26910052

Docking and Linking of Fragments To Discover Jumonji Histone Demethylase Inhibitors.
Korczynska, M; Le, DD; Younger, N; Gregori-Puigjané, E; Tumber, A; Krojer, T; Velupillai, S; Gileadi, C; Nowak, RP; Iwasa, E; Pollock, SB; Ortiz Torres, I; Oppermann, U; Shoichet, BK; Fujimori, DG;
Journal of Medicinal Chemistry. 2016 59:1580-1598. doi:
PMID: 26699912

2015

Inflammation activation and resolution in human tendon disease.
Dakin, SG; Martinez, FO; Yapp, C; Wells, G; Oppermann, U; Dean, BJ; Smith, RDJ; Wheway, K; Watkins, B; Roche, L; Carr, AJ;
Science Translational Medicine. 2015 7:-. doi: 10.1126/scitranslmed.aac4269.
PMID:

Towards an understanding of the role of DNA methylation in rheumatoid arthritis: therapeutic and diagnostic implications.
Cribbs, A; Feldmann, M; Oppermann, U;
Therapeutic Advances in Musculoskeletal Disease. 2015 7:206-219. doi:
PMID: 26425149

The inhibition of human farnesyl pyrophosphate synthase by nitrogen-containing bisphosphonates. Elucidating the role of active site threonine 201 and tyrosine 204 residues using enzyme mutants.
Tsoumpra, MK; Muniz, JR; Barnett, BL; Kwaasi, AA; Pilka, ES; Kavanagh, KL; Evdokimov, A; Walter, RL; Von Delft, F; Ebetino, FH; Oppermann, U; Russell, RG; Dunford, JE;
Bone. 2015 81:478-486. doi: 10.1016/j.bone.2015.08.020
PMID: 26318908

Discovery of NCT-501, a Potent and Selective Theophylline-Based Inhibitor of Aldehyde Dehydrogenase 1A1 (ALDH1A1).
Yang, SM; Yasgar, A; Miller, B; Lal-Nag, M; Brimacombe, K; Hu, X; Sun, H; Wang, A; Xu, X; Nguyen, K; Oppermann, U; Ferrer, M; Vasiliou, V; Simeonov, A; Jadhav, A; Maloney, DJ;
Journal of Medicinal Chemistry. 2015 58:5967-5978. doi: 10.1021/acs.jmedchem.5b00577
PMID: 26207746

Dentine matrix protein 1 (DMP-1) is a marker of bone formation and mineralisation in soft tissue tumours.
Inagaki, Y; Kashima, TG; Hookway, ES; Tanaka, Y; Hassan, AB; Oppermann, U; Athanasou, NA;
Virchows Archiv: an international journal of pathology. 2015 466:445-452. doi: 10.1007/s00428-014-1706-3
PMID: 25630512

Human prostaglandin reductase 1 (PGR1): Substrate specificity, inhibitor analysis and site-directed mutagenesis.
Mesa, J; Alsina, C; Oppermann, U; Parés, X; Farrés, J; Porté, S;
Chemico-Biological Interactions. 2015 234:105-113. doi: 10.1016/j.cbi.2015.01.021
PMID: 25619643

Inflammation activation and resolution in human tendon disease.
Dakin, SG; Martinez, FO; Yapp, C; Wells, G; Oppermann, U; Dean, BJ; Smith, RD; Wheway, K; Watkins, B; Roche, L; Carr, AJ;
Science Translational Medicine. 2015 7:311ra173-. doi:
PMID: 26511510

Towards a systematic analysis of human short-chain dehydrogenases/reductases (SDR): Ligand identification and structure-activity relationships.
Bhatia, C; Oerum, S; Bray, J; Kavanagh, KL; Shafqat, N; Yue, W; Oppermann, U;
Chemico-Biological Interactions. 2015 234:114-125. doi: 10.1016/j.cbi.2014.12.013
PMID: 25526675

The role of calcium and nicotinic acid adenine dinucleotide phosphate (NAADP) in human osteoclast formation and resorption.
Cheng, X; Hookway, ES; Kashima, T; Oppermann, U; Galione, A; Athanasou, NA;
Calcified Tissue International. 2015 96:73-79. doi: 10.1007/s00223-014-9939-3
PMID: 25433853

2014

Kruidenier et al. reply.
Kruidenier, L; Chung, CW; Cheng, Z; Liddle, J; Che, K; Joberty, G; Bantscheff, M; Bountra, C; Bridges, A; Diallo, H; Eberhard, D; Hutchinson, S; Jones, E; Katso, R; Leveridge, M; Mander, PK; Mosley, J; Ramirez-Molina, C; Rowland, P; Schofield, CJ; Sheppard, RJ; Smith, JE; Swales, C; Tanner, R; Thomas, P; Tumber, A; Drewes, G; Oppermann, U; Patel, DJ; Lee, K; Wilson, DM;
Nature. 2014 514:E2-. doi:
PMID: 25279927

Lysine methylation-dependent binding of 53BP1 to the pRb tumor suppressor.
Carr, SM; Munro, S; Zalmas, LP; Fedorov, O; Johansson, C; Krojer, T; Sagum, CA; Bedford, MT; Oppermann, U; La Thangue, NB;
Proceedings of the National Academy of Sciences of USA. 2014 111:11341-11346. doi:
PMID: 25049398

CHROMATIN MODIFYING MECHANISMS IN MACROPHAGES DIFFER BETWEEN HEALTHY CONTROLS AND PATIENTS WIH RHEUMATOID ARTHRITIS
Rooke, K; Kruidenier, L; Che, H; Mander, P; Swales, C; Prinjha, R; Oppermann, U;
Annals of the Rheumatic Diseases. 2014 73:823-824. doi: 10.1136/annrheumdis-2014-eular.4218
PMID:

Ribosomal oxygenases are structurally conserved from prokaryotes to humans.
Chowdhury, R; Sekirnik, R; Brissett, NC; Krojer, T; Ho, CH; Ng, SS; Clifton, IJ; Ge, W; Kershaw, NJ; Fox, GC; Muniz, JR; Vollmar, M; Phillips, C; Pilka, ES; Kavanagh, KL; von Delft, F; Oppermann, U; McDonough, MA; Doherty, AJ; Schofield, CJ;
Nature. 2014 510:422-426. doi: 10.1038/nature13263
PMID: 24814345

Human UTY(KDM6C) is a male-specific Nϵ-methyl lysyl demethylase.
Walport, LJ; Hopkinson, RJ; Vollmar, M; Madden, SK; Gileadi, C; Oppermann, U; Schofield, CJ; Johansson, C;
Journal of Biological Chemistry. 2014 289:18302-18313. doi:
PMID: 24798337

EPIGENETIC MODIFYING COMPOUNDS ALTER ACTIVITY OF PRIMARY HUMAN ARTICULAR CHONDROCYTES AND MESENCHYMAL STEM CELLS UNDERGOING CHONDROGENESIS
Snelling, S; Kramm, A; Yapp, C; Carr, A; Oppermann, U;
Osteoarthritis and Cartilage. 2014 22:S141-S141. doi:
PMID:

The roles of Jumonji-type oxygenases in human disease.
Johansson, C; Tumber, A; Che, K; Cain, P; Nowak, R; Gileadi, C; Oppermann, U;
Epigenomics. 2014 6:89-120. doi: 10.2217/epi.13.79
PMID: 24579949

Pleiotropic effect of somatic mutations in the E2F subunit DP-1 gene in human cancer.
Munro, S; Oppermann, U; La Thangue, NB;
Oncogene. 2014 33:3594-3603. doi: 10.1038/onc.2013.316
PMID: 23934193

2013

Identification of chromatin modifying mechanisms in human primary macrophages in an inflammatory model
Rooke, K; Kruidenier, L; Che, K; Mander, P; Swales, C; Prinjha, R; Oppermann, U;
International Journal of Experimental Pathology: mechanisms and models of disease. 2013 94:A17-A17. doi:
PMID:

Epigenetic modifying compounds alter activity of primary human articular chondrocytes and mesenchymal stem cells undergoing chondrogenesis
Snelling, SJB; Kramm, A; Cain, P; Yapp, C; Carr, AJ; Oppermann, U;
International Journal of Experimental Pathology: mechanisms and models of disease. 2013 94:A16-A16. doi:
PMID:

An epigenetic screen identifies bromodomain-containing protein 4 (BRD4) as a critical component for osteoblast differentiation
Kramm, A; Kubicek, S; Dunford, JE; Oppermann, U;
International Journal of Experimental Pathology: mechanisms and models of disease. 2013 94:A18-A18. doi:
PMID:

5-Carboxy-8-hydroxyquinoline is a broad spectrum 2-oxoglutarate oxygenase inhibitor which causes iron translocation
Hopkinson, RJ; Tumber, A; Yapp, C; Chowdhury, R; Aik, W; Che, KH; Li, XS; Kristensen, JBL; King, ONF; Chan, MC; Yeoh, KK; Choi, H; Walport, LJ; Thinnes, CC; Bush, JT; Lejeune, C; Rydzik, AM; Rose, NR; Bagg, EA; McDonough, MA; Krojer, TJ; Yue, WW; Ng, SS; Olsen, L; Brennan, PE; Oppermann, U; Müller, S; Klose, RJ; Ratcliffe, PJ; Schofield, CJ; Kawamura, A;
Chemical Science. 2013 4:3110-3117. doi: 10.1039/c3sc51122g
PMID: 26682036

Crystal structures of malonyl-coenzyme A decarboxylase provide insights into its catalytic mechanism and disease-causing mutations.
Froese, DS; Forouhar, F; Tran, TH; Vollmar, M; Kim, YS; Lew, S; Neely, H; Seetharaman, J; Shen, Y; Xiao, R; Acton, TB; Everett, JK; Cannone, G; Puranik, S; Savitsky, P; Krojer, T; Pilka, ES; Kiyani, W; Lee, WH; Marsden, BD; von Delft, F; Allerston, CK; Spagnolo, L; Gileadi, O; Montelione, GT; Oppermann, U; Yue, WW; Tong, L;
Structure. 2013 21:1182-1192. doi: 10.1016/j.str.2013.05.001
PMID: 23791943

Quantitative analysis of histone demethylase probes using fluorescence polarization.
Xu, W; Podoll, JD; Dong, X; Tumber, A; Oppermann, U; Wang, X;
Journal of Medicinal Chemistry. 2013 56:5198-5202. doi: 10.1021/jm3018628
PMID: 23725560

Dentine matrix protein 1 (DMP-1) is a marker of bone-forming tumours.
Kashima, TG; Dongre, A; Oppermann, U; Athanasou, NA;
Virchows Archiv: an international journal of pathology. 2013 462:583-591. doi: 10.1007/s00428-013-1399-z
PMID: 23559304

EPIGENETIC MODIFYING COMPOUNDS AFFECT THE ACTIVITY OF PRIMARY HUMAN ARTICULAR CHONDROCYTES AND MESENCHYMAL STEM CELLS UNDERGOING CHONDROGENESIS
Snelling, S; Kramm, A; Cain, P; Yapp, C; Carr, A; Price, A; Oppermann, U;
Osteoarthritis and Cartilage. 2013 21:S131-S131. doi:
PMID:

Insight into S-adenosylmethionine biosynthesis from the crystal structures of the human methionine adenosyltransferase catalytic and regulatory subunits.
Shafqat, N; Muniz, JR; Pilka, ES; Papagrigoriou, E; von Delft, F; Oppermann, U; Yue, WW;
Biochemical Journal. 2013 452:27-36. doi: 10.1042/BJ20121580
PMID: 23425511

A structural mapping of mutations causing succinyl-CoA:3-ketoacid CoA transferase (SCOT) deficiency.
Shafqat, N; Kavanagh, KL; Sass, JO; Christensen, E; Fukao, T; Lee, WH; Oppermann, U; Yue, WW;
Journal of Inherited Metabolic Disease. 2013 36:983-987. doi: 10.1007/s10545-013-9589-z
PMID: 23420214

Why is epigenetics important in understanding the pathogenesis of inflammatory musculoskeletal diseases?
O, U; p, ; p, ; e, ; r, ; m, ; a, ; n, ; n, ;
Arthritis Research and Therapy. 2013 15:209-. doi: 10.1186/ar4186
PMID: 23566317

2012

Structure and mechanism of human UDP-xylose synthase: evidence for a promoting role of sugar ring distortion in a three-step catalytic conversion of UDP-glucuronic acid.
Eixelsberger, T; Sykora, S; Egger, S; Brunsteiner, M; Kavanagh, KL; Oppermann, U; Brecker, L; Nidetzky, B;
Journal of Biological Chemistry. 2012 287:31349-31358. doi: 10.1074/jbc.M112.386706
PMID: 22810237

Plant growth regulator daminozide is a selective inhibitor of human KDM2/7 histone demethylases.
Rose, NR; Woon, EC; Tumber, A; Walport, LJ; Chowdhury, R; Li, XS; King, ON; Lejeune, C; Ng, SS; Krojer, T; Chan, MC; Rydzik, AM; Hopkinson, RJ; Che, KH; Daniel, M; Strain-Damerell, C; Gileadi, C; Kochan, G; Leung, IK; Dunford, J; Yeoh, KK; Ratcliffe, PJ; Burgess-Brown, N; von Delft, F; Muller, S; Marsden, B; Brennan, PE; McDonough, MA; Oppermann, U; Klose, RJ; Schofield, CJ; Kawamura, A;
Journal of Medicinal Chemistry. 2012 55:6639-6643. doi: 10.1021/jm300677j
PMID: 22724510

Development and application of a fluoride-detection-based fluorescence assay for γ-butyrobetaine hydroxylase.
Rydzik, AM; Leung, IK; Kochan, GT; Thalhammer, A; Oppermann, U; Claridge, TD; Schofield, CJ;
ChemBioChem: a European journal of chemical biology. 2012 13:1559-1563. doi: 10.1002/cbic.201200256
PMID: 22730246

Structure of human aspartyl aminopeptidase complexed with substrate analogue: insight into catalytic mechanism, substrate specificity and M18 peptidase family.
Chaikuad, A; Pilka, ES; De Riso, A; von Delft, F; Kavanagh, KL; Vénien-Bryan, C; Oppermann, U; Yue, WW;
BMC Structural Biology. 2012 12:14-. doi: 10.1186/1472-6807-12-14
PMID: 22720794

Structure of MMACHC reveals an arginine-rich pocket and a domain-swapped dimer for its B12 processing function.
Froese, DS; Krojer, T; Wu, X; Shrestha, R; Kiyani, W; von Delft, F; Gravel, RA; Oppermann, U; Yue, WW;
Biochemistry. 2012 51:5083-5090. doi: 10.1021/bi300150y
PMID: 22642810

Linking of 2-oxoglutarate and substrate binding sites enables potent and highly selective inhibition of JmjC histone demethylases.
Woon, EC; Tumber, A; Kawamura, A; Hillringhaus, L; Ge, W; Rose, NR; Ma, JH; Chan, MC; Walport, LJ; Che, KH; Ng, SS; Marsden, BD; Oppermann, U; McDonough, MA; Schofield, CJ;
Angewandte Chemie International Edition. 2012 51:1631-1634. doi: 10.1002/anie.201107833
PMID: 22241642

Crystal structure of the secretory isozyme of mammalian carbonic anhydrases CA VI: implications for biological assembly and inhibitor development.
Pilka, ES; Kochan, G; Oppermann, U; Yue, WW;
Biochemical and Biophysical Research Communications. 2012 419:485-489. doi: 10.1016/j.bbrc.2012.02.038
PMID: 22366092

A selective jumonji H3K27 demethylase inhibitor modulates the proinflammatory macrophage response.
Kruidenier, L; Chung, CW; Cheng, Z; Liddle, J; Che, K; Joberty, G; Bantscheff, M; Bountra, C; Bridges, A; Diallo, H; Eberhard, D; Hutchinson, S; Jones, E; Katso, R; Leveridge, M; Mander, PK; Mosley, J; Ramirez-Molina, C; Rowland, P; Schofield, CJ; Sheppard, RJ; Smith, JE; Swales, C; Tanner, R; Thomas, P; Tumber, A; Drewes, G; Oppermann, U; Patel, DJ; Lee, K; Wilson, DM;
Nature. 2012 488:404-408. doi: 10.1038/nature11262
PMID: 22842901

Structural and kinetic evidence that catalytic reaction of human UDP-glucose 6-dehydrogenase involves covalent thiohemiacetal and thioester enzyme intermediates.
Egger, S; Chaikuad, A; Klimacek, M; Kavanagh, KL; Oppermann, U; Nidetzky, B;
Journal of Biological Chemistry. 2012 287:2119-2129. doi: 10.1074/jbc.M111.313015
PMID: 22123821

2011

Conformational plasticity of glycogenin and its maltosaccharide substrate during glycogen biogenesis.
Chaikuad, A; Froese, DS; Berridge, G; von Delft, F; Oppermann, U; Yue, WW;
Proceedings of the National Academy of Sciences of USA. 2011 108:21028-21033. doi: 10.1073/pnas.1113921108
PMID: 22160680

Directed differentiation of human induced pluripotent stem cells into chondrocytes
Hala, S; Yapp, C; Kramm, A; Carpenter, L; Watt, S; Carr, A; Dunford, J; Oppermann, U; Tirlapur, U;
International Journal of Experimental Pathology: mechanisms and models of disease. 2011 92:A21-A22. doi:
PMID:

Structural and evolutionary basis for the dual substrate selectivity of human KDM4 histone demethylase family.
Hillringhaus, L; Yue, WW; Rose, NR; Ng, SS; Gileadi, C; Loenarz, C; Bello, SH; Bray, JE; Schofield, CJ; Oppermann, U;
Journal of Biological Chemistry. 2011 286:41616-41625. doi: 10.1074/jbc.M111.283689
PMID: 21914792

A selective inhibitor and probe of the cellular functions of Jumonji C domain-containing histone demethylases.
Luo, X; Liu, Y; Kubicek, S; Myllyharju, J; Tumber, A; Ng, S; Che, KH; Podoll, J; Heightman, TD; Oppermann, U; Schreiber, SL; Wang, X;
Journal of the American Chemical Society. 2011 133:9451-9456. doi: 10.1021/ja201597b
PMID: 21585201

Interactive JIMD articles using the iSee concept: turning a new page on structural biology data
Lee, WH; Yue, WW; Raush, E; Totrov, M; Abagyan, R; Oppermann, U; Marsden, BD;
Journal of Inherited Metabolic Disease. 2011 :1-3. doi: 10.1007/s10545-011-9334-4
PMID: 21509537

Crystal structure of PHYHD1A, a 2OG oxygenase related to phytanoyl-CoA hydroxylase.
Zhang, Z; Kochan, GT; Ng, SS; Kavanagh, KL; Oppermann, U; Schofield, CJ; McDonough, MA;
Biochemical and Biophysical Research Communications. 2011 408:553-558. doi: 10.1016/j.bbrc.2011.04.059
PMID: 21530488

Crystal structures of the endoplasmic reticulum aminopeptidase-1 (ERAP1) reveal the molecular basis for N-terminal peptide trimming.
Kochan, G; Krojer, T; Harvey, D; Fischer, R; Chen, L; Vollmar, M; von Delft, F; Kavanagh, KL; Brown, MA; Bowness, P; Wordsworth, P; Kessler, BM; Oppermann, U;
Proceedings of the National Academy of Sciences of USA. 2011 108:7745-7750. doi: 10.1073/pnas.1101262108
PMID: 21508329

Structure and mechanism of human UDP-glucose 6-dehydrogenase.
Egger, S; Chaikuad, A; Kavanagh, KL; Oppermann, U; Nidetzky, B;
Journal of Biological Chemistry. 2011 286:23877-23887. doi: 10.1074/jbc.M111.234682
PMID: 21502315

The relationship between the chemistry and biological activity of the bisphosphonates.
Ebetino, FH; Hogan, AM; Sun, S; Tsoumpra, MK; Duan, X; Triffitt, JT; Kwaasi, AA; Dunford, JE; Barnett, BL; Oppermann, U; Lundy, MW; Boyde, A; Kashemirov, BA; McKenna, CE; Russell, RG;
Bone. 2011 49:20-33. doi: 10.1016/j.bone.2011.03.774
PMID: 21497677

Structural basis of fumarate hydratase deficiency.
Picaud, S; Kavanagh, KL; Yue, WW; Lee, WH; Muller-Knapp, S; Gileadi, O; Sacchettini, J; Oppermann, U;
Journal of Inherited Metabolic Disease. 2011 34:671-676. doi: 10.1007/s10545-011-9294-8
PMID: 21445611

Structure and kinetic characterization of human sperm-specific glyceraldehyde-3-phosphate dehydrogenase, GAPDS.
Chaikuad, A; Shafqat, N; Al-Mokhtar, R; Cameron, G; Clarke, AR; Brady, RL; Oppermann, U; Frayne, J; Yue, WW;
Biochemical Journal. 2011 435:401-409. doi: 10.1042/BJ20101442
PMID: 21269272

Animal models of epigenetic regulation in neuropsychiatric disorders.
Bountra, C; Oppermann, U; Heightman, TD;
Current Topics in Behavioral Neurosciences. 2011 7:281-322. doi: 10.1007/7854_2010_104
PMID: 21225415

INTERACTIVE 3D VISUALISATIONS OF PROTEIN STRUCTURES TO AID THE STUDY OF INBORN ERRORS OF METABOLISM
Lee, WH; Raush, E; Totrov, M; Abagyan, R; Marsden, BD; Oppermann, U; Yue, WW;
Journal of Inherited Metabolic Disease. 2011 34:S240-S240. doi:
PMID:

Interaction between ERAP1 and HLA-B27 in ankylosing spondylitis implicates peptide handling in the mechanism for HLA-B27 in disease susceptibility.
Evans, DM; Spencer, CC; Pointon, JJ; Su, Z; Harvey, D; Kochan, G; Oppermann, U; Dilthey, A; Pirinen, M; Stone, MA; Appleton, L; Moutsianas, L; Leslie, S; Wordsworth, T; Kenna, TJ; Karaderi, T; Thomas, GP; Ward, MM; Weisman, MH; Farrar, C; Bradbury, LA; Danoy, P; Inman, RD; Maksymowych, W; Gladman, D; Rahman, P; Spondyloarthritis Research Consortium of Canada (SPARCC), ; Morgan, A; Marzo-Ortega, H; Bowness, P; Gaffney, K; Gaston, JS; Smith, M; Bruges-Armas, J; Couto, AR; Sorrentino, R; Paladini, F; Ferreira, MA; Xu, H; Liu, Y; Jiang, L; Lopez-Larrea, C; Díaz-Peña, R; López-Vázquez, A; Zayats, T; Band, G; Bellenguez, C; Blackburn, H; Blackwell, JM; Bramon, E; Bumpstead, SJ; Casas, JP; Corvin, A; Craddock, N; Deloukas, P; Dronov, S; Duncanson, A; Edkins, S; Freeman, C; Gillman, M; Gray, E; Gwilliam, R; Hammond, N; Hunt, SE; Jankowski, J; Jayakumar, A; Langford, C; Liddle, J; Markus, HS; Mathew, CG; McCann, OT; McCarthy, MI; Palmer, CN; Peltonen, L; Plomin, R; Potter, SC; Rautanen, A; Ravindrarajah, R; Ricketts, M; Samani, N; Sawcer, SJ; Strange, A; Trembath, RC; Viswanathan, AC; Waller, M; Weston, P; Whittaker, P; Widaa, S; Wood, NW; McVean, G; Reveille, JD; Wordsworth, BP; Brown, MA; Donnelly, P; Australo-Anglo-American Spondyloarthritis Consortium (TASC), ; Wellcome Trust Case Control Consortium 2 (WTCCC2), ;
Nature Genetics. 2011 43:761-767. doi: 10.1038/ng.873
PMID: 21743469

DELINEATING THE MITOCHONDRIAL VITAMIN B12 PATHWAY THROUGH STRUCTURAL AND INTERACTION STUDIES
Froese, DS; Kochan, G; Muniz, JRC; Chaikuad, A; Wu, X; Gileadi, C; Ugochukwu, E; Krysztofinska, E; Gravel, RA; Oppermann, U; Yue, WW;
Journal of Inherited Metabolic Disease. 2011 34:S119-S119. doi:
PMID:

High-throughput structural biology of metabolic enzymes and its impact on human diseases.
Yue, WW; Oppermann, U;
Journal of Inherited Metabolic Disease. 2011 34:575-581. doi: 10.1007/s10545-011-9296-6
PMID: 21340633

Interplay between lysine methylation and Cdk phosphorylation in growth control by the retinoblastoma protein.
Carr, SM; Munro, S; Kessler, B; Oppermann, U; La Thangue, NB;
The EMBO Journal. 2011 30:317-327. doi: 10.1038/emboj.2010.311
PMID: 21119616

The crystal structure of human GLRX5: iron-sulfur cluster co-ordination, tetrameric assembly and monomer activity.
Johansson, C; Roos, AK; Montano, SJ; Sengupta, R; Filippakopoulos, P; Guo, K; von Delft, F; Holmgren, A; Oppermann, U; Kavanagh, KL;
Biochemical Journal. 2011 433:303-311. doi: 10.1042/BJ20101286
PMID: 21029046

Kinetic and structural evidence of the alkenal/one reductase specificity of human ζ-crystallin.
Porté, S; Moeini, A; Reche, I; Shafqat, N; Oppermann, U; Farrés, J; Parés, X;
Cellular and Molecular Life Sciences. 2011 68:1065-1077. doi: 10.1007/s00018-010-0508-2
PMID: 20835842

2010

Structural and mechanistic studies on γ-butyrobetaine hydroxylase.
Leung, IK; Krojer, TJ; Kochan, GT; Henry, L; von Delft, F; Claridge, TD; Oppermann, U; McDonough, MA; Schofield, CJ;
Chemistry and Biology. 2010 17:1316-1324. doi: 10.1016/j.chembiol.2010.09.016
PMID: 21168767

Structures of the human GTPase MMAA and vitamin B12-dependent methylmalonyl-CoA mutase and insight into their complex formation.
Froese, DS; Kochan, G; Muniz, JR; Wu, X; Gileadi, C; Ugochukwu, E; Krysztofinska, E; Gravel, RA; Oppermann, U; Yue, WW;
Journal of Biological Chemistry. 2010 285:38204-38213. doi: 10.1074/jbc.M110.177717
PMID: 20876572

UDP-glucose dehydrogenase: structure and function of a potential drug target.
Egger, S; Chaikuad, A; Kavanagh, KL; Oppermann, U; Nidetzky, B;
Biochemical Society Transactions. 2010 38:1378-1385. doi: 10.1042/BST0381378
PMID: 20863317

Quinone oxidoreductase-2-mediated prodrug cancer therapy.
Middleton, MR; Knox, R; Cattell, E; Oppermann, U; Midgley, R; Ali, R; Auton, T; Agarwal, R; Anderson, D; Sarker, D; Judson, I; Osawa, T; Spanswick, VJ; Davies, S; Hartley, JA; Kerr, DJ;
Science Translational Medicine. 2010 2:40ra50-. doi: 10.1126/scitranslmed.3000615
PMID: 20630857

IMPACT OF ANKYLOSING SPONDYLITIS-ASSOCIATED ERAP1 VARIANTS ON ITS AMINOPEPTIDASE ACTIVITY
Harvey, D; Kochan, G; Pointon, JJ; Oppermann, U; Wordsworth, BP;
Clinical and Experimental Rheumatology. 2010 28:607-607. doi:
PMID:

INVESTIGATING THE ROLE OF ENDOPLASMIC RETICULUM AMINOPEPTIDASE-1 (ERAP1) IN ANKYLOSING SPONDYLITIS
Chen, L; Fischer, R; Harvey, D; Kollnberger, S; Wordsworth, BP; Oppermann, U; Kessler, B; Bowness, P;
Clinical and Experimental Rheumatology. 2010 28:631-631. doi:
PMID:

THE GENETICS OF ERAP1 IN ANKYLOSING SPONDYLITIS
Wordsworth, BP; Harvey, D; Pointon, J; Oppermann, U;
Clinical and Experimental Rheumatology. 2010 28:603-603. doi:
PMID:

Aldehyde dehydrogenase 7A1 (ALDH7A1) is a novel enzyme involved in cellular defense against hyperosmotic stress.
Brocker, C; Lassen, N; Estey, T; Pappa, A; Cantore, M; Orlova, VV; Chavakis, T; Kavanagh, KL; Oppermann, U; Vasiliou, V;
Journal of Biological Chemistry. 2010 285:18452-18463. doi: 10.1074/jbc.M109.077925
PMID: 20207735

Structural impact of human and Escherichia coli biotin carboxyl carrier proteins on biotin attachment.
Healy, S; McDonald, MK; Wu, X; Yue, WW; Kochan, G; Oppermann, U; Gravel, RA;
Biochemistry. 2010 49:4687-4694. doi: 10.1021/bi901612y
PMID: 20443544

Crystal structure of the 2-oxoglutarate- and Fe(II)-dependent lysyl hydroxylase JMJD6.
Mantri, M; Krojer, T; Bagg, EA; Webby, CJ; Butler, DS; Kochan, G; Kavanagh, KL; Oppermann, U; McDonough, MA; Schofield, CJ;
Journal of Molecular Biology. 2010 401:211-222. doi:
PMID: 20684070

Superfamilies SDR and MDR: from early ancestry to present forms. Emergence of three lines, a Zn-metalloenzyme, and distinct variabilities.
Jörnvall, H; Hedlund, J; Bergman, T; Oppermann, U; Persson, B;
Biochemical and Biophysical Research Communications. 2010 396:125-130. doi: 10.1016/j.bbrc.2010.03.094
PMID: 20494124

Crystal structures of human HMG-CoA synthase isoforms provide insights into inherited ketogenesis disorders and inhibitor design.
Shafqat, N; Turnbull, A; Zschocke, J; Oppermann, U; Yue, WW;
Journal of Molecular Biology. 2010 398:497-506. doi: 10.1016/j.jmb.2010.03.034
PMID: 20346956

Classification of the short-chain dehydrogenase/reductase superfamily using hidden Markov models.
Kallberg, Y; Oppermann, U; Persson, B;
The Federation of European Biochemical Societies (FEBS) Journal. 2010 277:2375-2386. doi: 10.1111/j.1742-4658.2010.07656.x
PMID: 20423462

Thermolability of mutant MMACHC protein in the vitamin B12-responsive cblC disorder.
Froese, DS; Healy, S; McDonald, M; Kochan, G; Oppermann, U; Niesen, FH; Gravel, RA;
Molecular Genetics and Metabolism. 2010 100:29-36. doi: 10.1016/j.ymgme.2010.02.005
PMID: 20219402

Development of homogeneous luminescence assays for histone demethylase catalysis and binding.
Kawamura, A; Tumber, A; Rose, NR; King, ON; Daniel, M; Oppermann, U; Heightman, TD; Schofield, C;
Analytical Biochemistry. 2010 404:86-93. doi: 10.1016/j.ab.2010.04.030
PMID: 20435012

A non-enzymatic function of 17beta-hydroxysteroid dehydrogenase type 10 is required for mitochondrial integrity and cell survival.
Rauschenberger, K; Schöler, K; Sass, JO; Sauer, S; Djuric, Z; Rumig, C; Wolf, NI; Okun, JG; Kölker, S; Schwarz, H; Fischer, C; Grziwa, B; Runz, H; Nümann, A; Shafqat, N; Kavanagh, KL; Hämmerling, G; Wanders, RJ; Shield, JP; Wendel, U; Stern, D; Nawroth, P; Hoffmann, GF; Bartram, CR; Arnold, B; Bierhaus, A; Oppermann, U; Steinbeisser, H; Zschocke, J;
EMBO Molecular Medicine. 2010 2:51-62. doi: 10.1002/emmm.200900055
PMID: 20077426

Selective inhibitors of the JMJD2 histone demethylases: combined nondenaturing mass spectrometric screening and crystallographic approaches.
Rose, NR; Woon, EC; Kingham, GL; King, ON; Mecinović, J; Clifton, IJ; Ng, SS; Talib-Hardy, J; Oppermann, U; McDonough, MA; Schofield, CJ;
Journal of Medicinal Chemistry. 2010 53:1810-1818. doi: 10.1021/jm901680b
PMID: 20088513

Crystal structure of the PHF8 Jumonji domain, an Nepsilon-methyl lysine demethylase.
Yue, WW; Hozjan, V; Ge, W; Loenarz, C; Cooper, CD; Schofield, CJ; Kavanagh, KL; Oppermann, U; McDonough, MA;
FEBS Letters. 2010 584:825-830. doi: 10.1016/j.febslet.2009.12.055
PMID: 20067792

A miniaturized screen for inhibitors of Jumonji histone demethylases.
Sakurai, M; Rose, NR; Schultz, L; Quinn, AM; Jadhav, A; Ng, SS; Oppermann, U; Schofield, CJ; Simeonov, A;
Molecular Biosystems. 2010 6:357-364. doi: 10.1039/b912993f
PMID: 20094655

High-affinity inhibitors of human NAD-dependent 15-hydroxyprostaglandin dehydrogenase: mechanisms of inhibition and structure-activity relationships.
Niesen, FH; Schultz, L; Jadhav, A; Bhatia, C; Guo, K; Maloney, DJ; Pilka, ES; Wang, M; Oppermann, U; Heightman, TD; Simeonov, A;
PLoS One. 2010 5:e13719-. doi: 10.1371/journal.pone.0013719
PMID: 21072165

Quantitative high-throughput screening identifies 8-hydroxyquinolines as cell-active histone demethylase inhibitors.
King, ON; Li, XS; Sakurai, M; Kawamura, A; Rose, NR; Ng, SS; Quinn, AM; Rai, G; Mott, BT; Beswick, P; Klose, RJ; Oppermann, U; Jadhav, A; Heightman, TD; Maloney, DJ; Schofield, CJ; Simeonov, A;
PLoS One. 2010 5:e15535-. doi: 10.1371/journal.pone.0015535
PMID: 21124847

A homogeneous method for investigation of methylation-dependent protein-protein interactions in epigenetics.
Quinn, AM; Bedford, MT; Espejo, A; Spannhoff, A; Austin, CP; Oppermann, U; Simeonov, A;
Nucleic Acids Research. 2010 38:e11-. doi: 10.1093/nar/gkp899
PMID: 19897549

2009

Investigating the genetic association between ERAP1 and ankylosing spondylitis.
Harvey, D; Pointon, JJ; Evans, DM; Karaderi, T; Farrar, C; Appleton, LH; Sturrock, RD; Stone, MA; Oppermann, U; Brown, MA; Wordsworth, BP;
Human Molecular Genetics. 2009 18:4204-4212. doi: 10.1093/hmg/ddp371
PMID: 19692350

Crystal structure of human carbonic anhydrase-related protein VIII reveals the basis for catalytic silencing.
Picaud, SS; Muniz, JR; Kramm, A; Pilka, ES; Kochan, G; Oppermann, U; Yue, WW;
Proteins: Structure, Function, and Bioinformatics. 2009 76:507-511. doi: 10.1002/prot.22411
PMID: 19360879

Structural basis for different specificities of acyltransferases associated with the human cytosolic and mitochondrial fatty acid synthases.
Bunkoczi, G; Misquitta, S; Wu, X; Lee, WH; Rojkova, A; Kochan, G; Kavanagh, KL; Oppermann, U; Smith, S;
Chemistry and Biology. 2009 16:667-675. doi: 10.1016/j.chembiol.2009.04.011
PMID: 19549604

Three-dimensional structure and enzymatic function of proapoptotic human p53-inducible quinone oxidoreductase PIG3.
Porté, S; Valencia, E; Yakovtseva, EA; Borràs, E; Shafqat, N; Debreczeny, JE; Pike, AC; Oppermann, U; Farrés, J; Fita, I; Parés, X;
Journal of Biological Chemistry. 2009 284:17194-17205. doi: 10.1074/jbc.M109.001800
PMID: 19349281

Evidence for the involvement of the threonine 201 side-chain in the interaction of nitrogen-containing bisphosphonates with farnesyl pyrophosphate synthase
Kwassi, AAA; Pilka, ES; Evdokimov, A; Barnett, BL; Ebetino, FH; Russell, RGG; Kavanagh, KL; Oppermann, U; Dunford, JE;
Bone. 2009 44:S323-S323. doi: 10.1016/j.bone.2009.03.611
PMID:

Structural snapshots for the conformation-dependent catalysis by human medium-chain acyl-coenzyme A synthetase ACSM2A.
Kochan, G; Pilka, ES; von Delft, F; Oppermann, U; Yue, WW;
Journal of Molecular Biology. 2009 388:997-1008. doi: 10.1016/j.jmb.2009.03.064
PMID: 19345228

REFINING THE GENETIC ASSOCIATION BETWEEN ANKYLOSING SPODYLITIS AND ERAP1
Harvey, D; Pointon, JJ; Farrar, C; Appleton, LA; Oppermann, U; Brown, MA; Wordsworth, BP;
Rheumatology. 2009 48:I52-I52. doi:
PMID:

Short-term glucocorticoid treatment increases insulin secretion in islets derived from lean mice through multiple pathways and mechanisms.
Hult, M; Ortsäter, H; Schuster, G; Graedler, F; Beckers, J; Adamski, J; Ploner, A; Jörnvall, H; Bergsten, P; Oppermann, U;
Molecular and Cellular Endocrinology. 2009 301:109-116. doi: 10.1016/j.mce.2008.09.038
PMID: 18984029

Structure-activity relationships of human AKR-type oxidoreductases involved in bile acid synthesis: AKR1D1 and AKR1C4.
Lee, WH; Lukacik, P; Guo, K; Ugochukwu, E; Kavanagh, KL; Marsden, B; Oppermann, U;
Molecular and Cellular Endocrinology. 2009 301:199-204. doi: 10.1016/j.mce.2008.09.042
PMID: 19013211

Analysis of the substrate-binding site of human carbonyl reductases CBR1 and CBR3 by site-directed mutagenesis.
El-Hawari, Y; Favia, AD; Pilka, ES; Kisiela, M; Oppermann, U; Martin, HJ; Maser, E;
Chemico-Biological Interactions. 2009 178:234-241. doi: 10.1016/j.cbi.2008.11.004
PMID: 19061875

The human short-chain dehydrogenase/reductase (SDR) superfamily: a bioinformatics summary.
Bray, JE; Marsden, BD; Oppermann, U;
Chemico-Biological Interactions. 2009 178:99-109. doi: 10.1016/j.cbi.2008.10.058
PMID: 19061874

The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative.
Persson, B; Kallberg, Y; Bray, JE; Bruford, E; Dellaporta, SL; Favia, AD; Duarte, RG; Jörnvall, H; Kavanagh, KL; Kedishvili, N; Kisiela, M; Maser, E; Mindnich, R; Orchard, S; Penning, TM; Thornton, JM; Adamski, J; Oppermann, U;
Chemico-Biological Interactions. 2009 178:94-98. doi: 10.1016/j.cbi.2008.10.040
PMID: 19027726

Dynamic protein methylation in chromatin biology.
Ng, SS; Yue, WW; Oppermann, U; Klose, RJ;
Cellular and Molecular Life Sciences. 2009 66:407-422. doi: 10.1007/s00018-008-8303-z
PMID: 18923809

Discovery of a potent and selective inhibitor for human carbonyl reductase 1 from propionate scanning applied to the macrolide zearalenone.
Zimmermann, TJ; Niesen, FH; Pilka, ES; Knapp, S; Oppermann, U; Maier, ME;
Bioorganic and Medicinal Chemistry. 2009 17:530-536. doi: 10.1016/j.bmc.2008.11.076
PMID: 19097799

Structural basis for substrate specificity in human monomeric carbonyl reductases.
Pilka, ES; Niesen, FH; Lee, WH; El-Hawari, Y; Dunford, JE; Kochan, G; Wsol, V; Martin, HJ; Maser, E; Oppermann, U;
PLoS One. 2009 4:e7113-. doi: 10.1371/journal.pone.0007113
PMID: 19841672

2008

Inhibitor scaffolds for 2-oxoglutarate-dependent histone lysine demethylases.
Rose, NR; Ng, SS; Mecinović, J; Liénard, BM; Bello, SH; Sun, Z; McDonough, MA; Oppermann, U; Schofield, CJ;
Journal of Medicinal Chemistry. 2008 51:7053-7056. doi: 10.1021/jm800936s
PMID: 18942826

The Role of Active Site Threonine 201 in the Inhibition of Farnesyl Pyrophosphate Synthase by Nitrogen Containing Bisphosphonates
Dunford, JE; Pilka, E; Kwaasi, A; Evdokimov, A; Barnett, BL; Oppermann, U; Ebetino, FH; Russell, RGG; Kavanagh, KL;
Journal of Bone and Mineral Research. 2008 23:S122-S122. doi:
PMID:

CARB 4-Elucidating the mechanism of human UDP-glucose dehydrogenase using kinetic, mutational and structural studies
Egger, S; Guo, K; Kavanagh, KL; Oppermann, U; Klimacek, M; Nidetzky, B;
ACS National Meeting Book of Abstracts. 2008 236:-. doi:
PMID:

Codon optimization can improve expression of human genes in Escherichia coli: A multi-gene study.
Burgess-Brown, NA; Sharma, S; Sobott, F; Loenarz, C; Oppermann, U; Gileadi, O;
Protein Expression and Purification. 2008 59:94-102. doi: 10.1016/j.pep.2008.01.008
PMID: 18289875

Structure-activity relationships among the nitrogen containing bisphosphonates in clinical use and other analogues: time-dependent inhibition of human farnesyl pyrophosphate synthase.
Dunford, JE; Kwaasi, AA; Rogers, MJ; Barnett, BL; Ebetino, FH; Russell, RG; Oppermann, U; Kavanagh, KL;
Journal of Medicinal Chemistry. 2008 51:2187-2195. doi: 10.1021/jm7015733
PMID: 18327899

Crystal structures of the acyl transferases involved in the human cytosolic and mitochondrial fatty acid synthase
Misquitta, SA; Bunkoczi, G; Wu, X; Kavanagh, KL; Hozjan, V; Oppermann, U; Smith, S;
The FASEB Journal. 2008 22:-. doi:
PMID:

Role of short-chain hydroxyacyl CoA dehydrogenases in SCHAD deficiency.
Filling, C; Keller, B; Hirschberg, D; Marschall, HU; Jörnvall, H; Bennett, MJ; Oppermann, U;
Biochemical and Biophysical Research Communications. 2008 368:6-11. doi: 10.1016/j.bbrc.2007.10.188
PMID: 18036338

Characterization of the human carbonyl reductase 3 (CBR3) by site-directed mutagenesis
El-Hawari, Y; Pilka, E; Martin, H-J; Oppermann, U; Maser, E;
Naunyn-Schmiedebergs Archives of Pharmacology. 2008 377:67-67. doi:
PMID:

Structure activity relationships of nitrogen containing bisphosphonates which induce conformational changes in farnesyl pyrophosphate synthase
Dunford, JE; Kwaasi, AA; Kavanagh, KL; Rogers, MJ; Oppermann, U; Barnett, BB; Ebetino, FH; Graham, R; Russell, G;
Bone. 2008 42:S71-S71. doi: 10.1016/j.bone.2007.12.129
PMID:

The interaction of sidechain nitrogen with active site threonine is not essential for inhibition of farnesyl pyrophosphate synthase by nitrogen containing bisphosphonates
Dunford, JE; Pilka, E; Kwaasi, AA; Evdokimov, A; Barnett, BL; Oppermann, U; Ebetino, FH; Graham, R; Russell, G; Kavanagh, KL;
Bone. 2008 42:S70-S71. doi: 10.1016/j.bone.2007.12.128
PMID:

Ligand supplementation as a method to increase soluble heterologous protein production.
Hozjan, V; Guo, K; Wu, X; Oppermann, U;
Expert Review of Proteomics. 2008 5:137-143. doi: 10.1586/14789450.5.1.137
PMID: 18282129

SALMON: solvent accessibility, ligand binding, and mapping of ligand orientation by NMR spectroscopy.
Ludwig, C; Michiels, PJ; Wu, X; Kavanagh, KL; Pilka, E; Jansson, A; Oppermann, U; Günther, UL;
Journal of Medicinal Chemistry. 2008 51:1-3. doi: 10.1021/jm701020f
PMID: 18062662

Thermal unfolding of the archaeal DNA and RNA binding protein Ssh10.
Wu, X; Oppermann, M; Berndt, KD; Bergman, T; Jörnvall, H; Knapp, S; Oppermann, U;
Biochemical and Biophysical Research Communications. 2008 373:482-487. doi: 10.1016/j.bbrc.2008.06.030
PMID: 18571501

Interaction of the active site threonine 201 sidechain with the nitrogen of nttrogen-containing bisphosphonates is not essential for slow tight inhibition to farnesyl pyrophosphate synthase
Dunford, JE; Pilka, E; Kwaasi, AA; Evdokimov, A; Barnett, BL; Oppermann, U; Ebetino, FH; Russell, RG; Kavanagh, KL;
Calcified Tissue International. 2008 82:S223-S223. doi:
PMID:

2007

Evaluation of micro-parallel liquid chromatography as a method for HTS-coupled actives verification.
Simeonov, A; Yasgar, A; Klumpp, C; Zheng, W; Shafqat, N; Oppermann, U; Austin, CP; Inglese, J;
Assay and Drug Development Technologies. 2007 5:815-824. doi: 10.1089/adt.2007.097
PMID: 18078381

Bisphosphonates: an update on mechanisms of action and how these relate to clinical efficacy.
Russell, RG; Xia, Z; Dunford, JE; Oppermann, U; Kwaasi, A; Hulley, PA; Kavanagh, KL; Triffitt, JT; Lundy, MW; Phipps, RJ; Barnett, BL; Coxon, FP; Rogers, MJ; Watts, NB; Ebetino, FH;
Annals of the New York Academy of Sciences. 2007 1117:209-257. doi: 10.1196/annals.1402.089
PMID: 18056045

Mechanism and substrate recognition of human holo ACP synthase.
Bunkoczi, G; Pasta, S; Joshi, A; Wu, X; Kavanagh, KL; Smith, S; Oppermann, U;
Chemistry and Biology. 2007 14:1243-1253. doi: 10.1016/j.chembiol.2007.10.013
PMID: 18022563

The scientific impact of the Structural Genomics Consortium: a protein family and ligand-centered approach to medically-relevant human proteins.
Gileadi, O; Knapp, S; Lee, WH; Marsden, BD; Müller, S; Niesen, FH; Kavanagh, KL; Ball, LJ; von Delft, F; Doyle, DA; Oppermann, UC; Sundström, M;
Journal of Structural and Functional Genomics. 2007 8:107-119. doi: 10.1007/s10969-007-9027-2
PMID: 17932789

Crystal structures of histone demethylase JMJD2A reveal basis for substrate specificity.
Ng, SS; Kavanagh, KL; McDonough, MA; Butler, D; Pilka, ES; Lienard, BM; Bray, JE; Savitsky, P; Gileadi, O; von Delft, F; Rose, NR; Offer, J; Scheinost, JC; Borowski, T; Sundstrom, M; Schofield, CJ; Oppermann, U;
Nature. 2007 448:87-91. doi: 10.1038/nature05971
PMID: 17589501

Nitrogen-containing bisphosphonates and prediction of their clinical potencies: Dissociation of target enzyme- and hydroxyapatite-binding affinities
Xia, Z; Dunford, J; Lawson, MA; Triffitt, JT; Kavanagh, K; Oppermann, U; Barnett, BL; Ebetino, FH; Russell, RGG;
Journal of Bone and Mineral Research. 2007 22:1125-1125. doi:
PMID:

Predicting pharmacological potencies of nitrogen-containing bisphosphonates; novel methods dissociate enzyme- and hydroxyapatite-binding affinities
Xia, Z; Dunford, J; Lawson, MA; Triffitt, JT; Kavanagh, K; Oppermann, U; Roze, C; Kashemirov, B; McKenna, CE; Ebetino, FH; Russell, RG;
Bone. 2007 40:S301-S302. doi:
PMID:

Structural and biochemical characterization of human orphan DHRS10 reveals a novel cytosolic enzyme with steroid dehydrogenase activity.
Lukacik, P; Keller, B; Bunkoczi, G; Kavanagh, KL; Lee, WH; Adamski, J; Oppermann, U;
Biochemical Journal. 2007 402:419-427. doi: 10.1042/BJ20061319
PMID: 17067289

Biochemical characterization of TASSELSEED 2, an essential plant short-chain dehydrogenase/reductase with broad spectrum activities.
Wu, X; Knapp, S; Stamp, A; Stammers, DK; Jörnvall, H; Dellaporta, SL; Oppermann, U;
The Federation of European Biochemical Societies (FEBS) Journal. 2007 274:1172-1182. doi: 10.1111/j.1742-4658.2007.05642.x
PMID: 17298439

Structural genomics and drug discovery: Case studies on human metabolic enzymes
Oppermann, U; Kavanagh, KL; Guo, K; Ng, S; Shafqat, N; Danford, J; Rojkova, A; Pilka, E; Hozjan, V; Kochan, G; Wu, X; Lukacik, P;
Naunyn-Schmiedebergs Archives of Pharmacology. 2007 375:69-69. doi:
PMID:

Reversible sequestration of active site cysteines in a 2Fe-2S-bridged dimer provides a mechanism for glutaredoxin 2 regulation in human mitochondria.
Johansson, C; Kavanagh, KL; Gileadi, O; Oppermann, U;
Journal of Biological Chemistry. 2007 282:3077-3082. doi: 10.1074/jbc.M608179200
PMID: 17121859

SDR-type human hydroxysteroid dehydrogenases involved in steroid hormone activation.
Wu, X; Lukacik, P; Kavanagh, KL; Oppermann, U;
Molecular and Cellular Endocrinology. 2007 265-266:71-76. doi: 10.1016/j.mce.2006.12.006
PMID: 17234335

Kinetic analysis of conformational changes in farnesyl pyrophosphate synthase induced by nitrogen containing bisphosphonates
Dunford, JE; Kavanagh, KL; Rogers, MJ; Oppermann, U; Ebetin, FH; Russell, G;
Calcified Tissue International. 2007 80:S41-S42. doi:
PMID:

Carbonyl reductases: the complex relationships of mammalian carbonyl- and quinone-reducing enzymes and their role in physiology.
O, U; p, ; p, ; e, ; r, ; m, ; a, ; n, ; n, ;
Annual Review of Pharmacology and Toxicology. 2007 47:293-322. doi: 10.1146/annurev.pharmtox.47.120505.105316
PMID: 17009925

2006

Analysis of the kinetic mechanism of inhibition of Farnesyl Pyrophosphate Synthase by nitrogen containing bisphosphonates.
Dunford, JE; Kavanagh, K; Oppermann, U; Ebetino, EH; Russell, RGG; Rogers, MJ;
Journal of Bone and Mineral Research. 2006 21:S396-S397. doi:
PMID:

Type 1 11beta-hydroxysteroid dehydrogenase as universal drug target in metabolic diseases?
O, U; p, ; p, ; e, ; r, ; m, ; a, ; n, ; n, ;
Endocrine, Metabolic and Immune Disorders - Drug Targets. 2006 6:259-269. doi:
PMID: 17017977

The crystal structure of human geranylgeranyl pyrophosphate synthase reveals a novel hexameric arrangement and inhibitory product binding.
Kavanagh, KL; Dunford, JE; Bunkoczi, G; Russell, RG; Oppermann, U;
Journal of Biological Chemistry. 2006 281:22004-22012. doi: 10.1074/jbc.M602603200
PMID: 16698791

The molecular mechanism of nitrogen-containing bisphosphonates as antiosteoporosis drugs.
Kavanagh, KL; Guo, K; Dunford, JE; Wu, X; Knapp, S; Ebetino, FH; Rogers, MJ; Russell, RG; Oppermann, U;
Proceedings of the National Academy of Sciences of USA. 2006 103:7829-7834. doi: 10.1073/pnas.0601643103
PMID: 16684881

Hep27, a member of the short-chain dehydrogenase/reductase family, is an NADPH-dependent dicarbonyl reductase expressed in vascular endothelial tissue.
Shafqat, N; Shafqat, J; Eissner, G; Marschall, HU; Tryggvason, K; Eriksson, U; Gabrielli, F; Lardy, H; Jörnvall, H; Oppermann, U;
Cellular and Molecular Life Sciences. 2006 63:1205-1213. doi: 10.1007/s00018-006-6013-y
PMID: 16685466

Characterization of human DHRS6, an orphan short chain dehydrogenase/reductase enzyme: a novel, cytosolic type 2 R-beta-hydroxybutyrate dehydrogenase.
Guo, K; Lukacik, P; Papagrigoriou, E; Meier, M; Lee, WH; Adamski, J; Oppermann, U;
Journal of Biological Chemistry. 2006 281:10291-10297. doi: 10.1074/jbc.M511346200
PMID: 16380372

Active site variability of type 1 11beta-hydroxysteroid dehydrogenase revealed by selective inhibitors and cross-species comparisons.
Hult, M; Shafqat, N; Elleby, B; Mitschke, D; Svensson, S; Forsgren, M; Barf, T; Vallgårda, J; Abrahmsen, L; Oppermann, U;
Molecular and Cellular Endocrinology. 2006 248:26-33. doi: 10.1016/j.mce.2005.11.043
PMID: 16431016

Structure and function of human 17beta-hydroxysteroid dehydrogenases.
Lukacik, P; Kavanagh, KL; Oppermann, U;
Molecular and Cellular Endocrinology. 2006 248:61-71. doi: 10.1016/j.mce.2005.12.007
PMID: 16414178

Human farnesyl diphosphate synthase crystal structures with active and inactive bisphosphonates
Evdokimov, A; Pokross, M; Barnett, BL; Kavanagh, K; Oppermann, U; Russell, RGG; McKenna, CE; Ebetino, FH;
Bone. 2006 38:S49-S49. doi: 10.1016/j.bone.2005.12.041
PMID:

Crystal structures and molecular interactions of risedronate and zoledronate with human farnesyl diphosphate synthase
Kavanagh, KL; Guo, K; Wu, X; Knapp, S; Ebetino, FH; Dunford, JE; Rogers, MJ; Russell, RGG; Oppermann, U;
Bone. 2006 38:53-53. doi: 10.1016/j.bone.2005.12.050
PMID:

Investigations into the kinetic mechanism of inhibition of farnesyl diphosphate synthase by nitrogen containing bisphosphonates
Dunford, JE; Kavanagh, K; Oppermann, U; Ebetino, FH; Russell, RGG; Rogers, MJ;
Bone. 2006 38:S47-S48. doi: 10.1016/j.bone.2005.12.037
PMID:

Molecular modeling comparison of nitrogen-containing bisphosphonates of varying potency co-crystalized in farnesyl diphosphate synthase
Ebetino, FH; Kashemirov, B; McKenna, CE; Evdokimov, A; Pokross, M; Barnett, BL; Dunford, J; Kavanagh, K; Rogers, MJ; Lundy, MW; Oppermann, U; Russell, RGG;
Bone. 2006 38:S49-S50. doi: 10.1016/j.bone.2005.12.042
PMID:

SDR goes SGC: A structural genomics initiative
Oppermann, U; Kavanagh, K; Guo, KD; Ng, S; Lukacik, P; Wu, XQ; Dubinina, E; Shafqat, N; Bray, J; Marsden, B; Sharma, S; Vedadi, M; von Delft, F; Sundstrom, M;
. 2006 12:235-241. doi:
PMID:

2005

Structure of human phytanoyl-CoA 2-hydroxylase identifies molecular mechanisms of Refsum disease.
McDonough, MA; Kavanagh, KL; Butler, D; Searls, T; Oppermann, U; Schofield, CJ;
Journal of Biological Chemistry. 2005 280:41101-41110. doi: 10.1074/jbc.M507528200
PMID: 16186124

Human farnesyl diphosphate synthase (FDFS): Crystal structure and molecular interactions with Nnitrogen-containing bisphosphonates.
Kavanagh, K; Guo, K; Wu, X; Knapp, S; Ebetino, FH; Dunford, JE; Rogers, MJ; Russell, RGG; Oppermann, U;
Journal of Bone and Mineral Research. 2005 20:S95-S96. doi:
PMID:

The crystal structure of guinea pig 11beta-hydroxysteroid dehydrogenase type 1 provides a model for enzyme-lipid bilayer interactions.
Ogg, D; Elleby, B; Norström, C; Stefansson, K; Abrahmsén, L; Oppermann, U; Svensson, S;
Journal of Biological Chemistry. 2005 280:3789-3794. doi: 10.1074/jbc.M412463200
PMID: 15542590

2004

Tic32, an essential component in chloroplast biogenesis.
Hörmann, F; Küchler, M; Sveshnikov, D; Oppermann, U; Li, Y; Soll, J;
Journal of Biological Chemistry. 2004 279:34756-34762. doi: 10.1074/jbc.M402817200
PMID: 15180984

High-level production and optimization of monodispersity of 11beta-hydroxysteroid dehydrogenase type 1.
Elleby, B; Svensson, S; Wu, X; Stefansson, K; Nilsson, J; Hallén, D; Oppermann, U; Abrahmsén, L;
Biochimica et Biophysica Acta: international journal of biochemistry and biophysics. 2004 1700:199-207. doi: 10.1016/j.bbapap.2004.05.003
PMID: 15262229

Crystal structure and biophysical characterization of human GDP-D-mannose 4, 6-dehydratase
Vedadi, M; Walker, JR; Sharma, S; Houston, SA; Wasney, GA; Loppnau, P; Oppermann, U;
Protein Science. 2004 13:81-82. doi:
PMID:

Membrane protein isolation by in situ solubilization, partitioning and affinity adsorption in aqueous two-phase systems. Purification of the human type 1 11beta-hydroxysteroid dehydrogenase.
Roobol-Bóza, M; Dolby, V; Doverskog, M; Barrefelt, A; Lindqvist, F; Oppermann, UC; Köhler Van Alstine, K; Tjerneld, F;
Journal of Chromatography A. 2004 1043:217-223. doi:
PMID: 15330095

Human and rodent type 1 11beta-hydroxysteroid dehydrogenases are 7beta-hydroxycholesterol dehydrogenases involved in oxysterol metabolism.
Hult, M; Elleby, B; Shafqat, N; Svensson, S; Rane, A; Jörnvall, H; Abrahmsen, L; Oppermann, U;
Cellular and Molecular Life Sciences. 2004 61:992-999. doi: 10.1007/s00018-003-3476-y
PMID: 15095019

Codon optimization reveals critical factors for high level expression of two rare codon genes in Escherichia coli: RNA stability and secondary structure but not tRNA abundance.
Wu, X; Jörnvall, H; Berndt, KD; Oppermann, U;
Biochemical and Biophysical Research Communications. 2004 313:89-96. doi:
PMID: 14672702

2003

Expanded substrate screenings of human and Drosophila type 10 17beta-hydroxysteroid dehydrogenases (HSDs) reveal multiple specificities in bile acid and steroid hormone metabolism: characterization of multifunctional 3alpha/7alpha/7beta/17beta/20beta
Shafqat, N; Marschall, HU; Filling, C; Nordling, E; Wu, XQ; Björk, L; Thyberg, J; Mårtensson, E; Salim, S; Jörnvall, H; Oppermann, U;
Biochemical Journal. 2003 376:49-60. doi: 10.1042/BJ20030877
PMID: 12917011

Molecular mechanisms underlying WOX1 activation during apoptotic and stress responses.
Chang, NS; Doherty, J; Ensign, A; Lewis, J; Heath, J; Schultz, L; Chen, ST; Oppermann, U;
Biochemical Pharmacology. 2003 66:1347-1354. doi:
PMID: 14555208

Hot spots in Tcf4 for the interaction with beta-catenin.
Fasolini, M; Wu, X; Flocco, M; Trosset, JY; Oppermann, U; Knapp, S;
Journal of Biological Chemistry. 2003 278:21092-21098. doi: 10.1074/jbc.M301781200
PMID: 12657632

High-level expression and rapid purification of rare-codon genes from hyperthermophilic archaea by the GST gene fusion system.
Wu, X; Oppermann, U;
Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences. 2003 786:177-185. doi:
PMID: 12651013

Glucocorticoid activation by 11beta-hydroxysteroid dehydrogenase type 1: A novel pharmacological target in the metabolic syndrome
Oppermann, U; Hult, M; Shafqat, N; Elleby, B; Svensson, S; Vallgarda, J; Abrahmsen, L;
Naunyn-Schmiedebergs Archives of Pharmacology. 2003 367:R13-R13. doi:
PMID:

Coenzyme-based functional assignments of short-chain dehydrogenases/reductases (SDRs).
Persson, B; Kallberg, Y; Oppermann, U; Jörnvall, H;
Chemico-Biological Interactions. 2003 143-144:271-278. doi:
PMID: 12604213

Short-chain dehydrogenases/reductases (SDR): the 2002 update.
Oppermann, U; Filling, C; Hult, M; Shafqat, N; Wu, X; Lindh, M; Shafqat, J; Nordling, E; Kallberg, Y; Persson, B; Jörnvall, H;
Chemico-Biological Interactions. 2003 143-144:247-253. doi:
PMID: 12604210

Comparative enzymology of 11 beta -hydroxysteroid dehydrogenase type 1 from glucocorticoid resistant (Guinea pig) versus sensitive (human) species.
Shafqat, N; Elleby, B; Svensson, S; Shafqat, J; Jörnvall, H; Abrahmsen, L; Oppermann, U;
Journal of Biological Chemistry. 2003 278:2030-2035. doi: 10.1074/jbc.M210135200
PMID: 12397058

2002

Structure of bacterial 3beta/17beta-hydroxysteroid dehydrogenase at 1.2 A resolution: a model for multiple steroid recognition.
Benach, J; Filling, C; Oppermann, UC; Roversi, P; Bricogne, G; Berndt, KD; Jörnvall, H; Ladenstein, R;
Biochemistry. 2002 41:14659-14668. doi:
PMID: 12475215

Short-chain dehydrogenases/reductases (SDRs).
Kallberg, Y; Oppermann, U; Jörnvall, H; Persson, B;
The Federation of European Biochemical Societies (FEBS) Journal. 2002 269:4409-4417. doi:
PMID: 12230552

Liver X receptors downregulate 11beta-hydroxysteroid dehydrogenase type 1 expression and activity.
Stulnig, TM; Oppermann, U; Steffensen, KR; Schuster, GU; Gustafsson, JA;
Diabetes. 2002 51:2426-2433. doi:
PMID: 12145154

Critical residues for structure and catalysis in short-chain dehydrogenases/reductases.
Filling, C; Berndt, KD; Benach, J; Knapp, S; Prozorovski, T; Nordling, E; Ladenstein, R; Jörnvall, H; Oppermann, U;
Journal of Biological Chemistry. 2002 277:25677-25684. doi: 10.1074/jbc.M202160200
PMID: 11976334

2001

Structural role of conserved Asn179 in the short-chain dehydrogenase/reductase scaffold.
Filling, C; Nordling, E; Benach, J; Berndt, KD; Ladenstein, R; Jörnvall, H; Oppermann, U;
Biochemical and Biophysical Research Communications. 2001 289:712-717. doi: 10.1006/bbrc.2001.6032
PMID: 11726206

Metabolic conversion as a pre-receptor control mechanism for lipophilic hormones.
Nobel, S; Abrahmsen, L; Oppermann, U;
The Federation of European Biochemical Societies (FEBS) Journal. 2001 268:4113-4125. doi:
PMID: 11488903

Forms and functions of human SDR enzymes.
Oppermann, UC; Filling, C; Jörnvall, H;
Chemico-Biological Interactions. 2001 130-132:699-705. doi:
PMID: 11306087

Novel enzymological profiles of human 11beta-hydroxysteroid dehydrogenase type 1.
Hult, M; Nobel, CS; Abrahmsen, L; Nicoll-Griffith, DA; Jörnvall, H; Oppermann, UC;
Chemico-Biological Interactions. 2001 130-132:805-814. doi:
PMID: 11306096

Subcellular targeting analysis of SDR-type hydroxysteroid dehydrogenases.
Filling, C; Wu, X; Shafqat, N; Hult, M; Mårtensson, E; Shafqat, J; Oppermann, UC;
Molecular and Cellular Endocrinology. 2001 171:99-101. doi:
PMID: 11165017

Human type 10 17 beta-hydroxysteroid dehydrogenase: molecular modelling and substrate docking.
Nordling, E; Oppermann, UC; Jörnvall, H; Persson, B;
Journal of Molecular Graphics and Modelling. 2001 19:514-593. doi:
PMID: 11552679

2000

Type 1 11beta -hydroxysteroid dehydrogenase mediates glucocorticoid activation and insulin release in pancreatic islets.
Davani, B; Khan, A; Hult, M; Mårtensson, E; Okret, S; Efendic, S; Jörnvall, H; Oppermann, UC;
Journal of Biological Chemistry. 2000 275:34841-34844. doi: 10.1074/jbc.C000600200
PMID: 10973946

Human liver class I alcohol dehydrogenase gammagamma isozyme: the sole cytosolic 3beta-hydroxysteroid dehydrogenase of iso bile acids.
Marschall, HU; Oppermann, UC; Svensson, S; Nordling, E; Persson, B; Höög, JO; Jörnvall, H;
Hepatology. 2000 31:990-996. doi: 10.1053/he.2000.5720
PMID: 10733557

Characterization of gel separated proteins
Bergman, AC; Oppermann, M; Oppermann, U; Jornvall, H; Bergman, T;
. 2000 :81-87. doi:
PMID:

1999

An ethanol-inducible MDR ethanol dehydrogenase/acetaldehyde reductase in Escherichia coli: structural and enzymatic relationships to the eukaryotic protein forms.
Shafqat, J; Höög, JO; Hjelmqvist, L; Oppermann, UC; Ibáñez, C; Jörnvall, H;
The Federation of European Biochemical Societies (FEBS) Journal. 1999 263:305-311. doi:
PMID: 10406936

Studies on variants of alcohol dehydrogenases and its domains.
Shafqat, J; Höög, JO; Hjelmqvist, L; Oppermann, U; Ibanez, C; Jörnvall, H;
Advances in Experimental Medicine and Biology. 1999 463:285-293. doi:
PMID: 10352697

Bioinformatics in studies of SDR and MDR enzymes.
Persson, B; Nordling, E; Kallberg, Y; Lundh, D; Oppermann, UC; Marschall, HU; Jörnvall, H;
Advances in Experimental Medicine and Biology. 1999 463:373-377. doi:
PMID: 10352708

Regulatory factors and motifs in SDR enzymes.
Oppermann, U; Salim, S; Hult, M; Eissner, G; Jörnvall, H;
Advances in Experimental Medicine and Biology. 1999 463:365-371. doi:
PMID: 10352707

Structure-function relationships of 3 beta-hydroxysteroid dehydrogenases involved in bile acid metabolism.
Filling, C; Marschall, HU; Prozorovski, T; Nordling, E; Persson, B; Jörnvall, H; Oppermann, UC;
Advances in Experimental Medicine and Biology. 1999 463:389-394. doi:
PMID: 10352710

1998

Selective inhibition of human type 1 11beta-hydroxysteroid dehydrogenase by synthetic steroids and xenobiotics.
Hult, M; Jörnvall, H; Oppermann, UC;
FEBS Letters. 1998 441:25-28. doi:
PMID: 9877158

Isolation and structure of repressor-like proteins from the archaeon Sulfolobus solfataricus. Co-purification of RNase A with Sso7c.
Oppermann, UC; Knapp, S; Bonetto, V; Ladenstein, R; Jörnvall, H;
FEBS Letters. 1998 432:141-144. doi:
PMID: 9720912

Carbonyl reduction of an anti-insect agent imidazole analogue of metyrapone in soil bacteria, invertebrate and vertebrate species.
Oppermann, UC; Nagel, G; Belai, I; Bueld, JE; Genti-Raimondi, S; Koolman, J; Netter, KJ; Maser, E;
Chemico-Biological Interactions. 1998 114:211-224. doi:
PMID: 9839632

1997

Function, gene organization and protein structures of 11beta-hydroxysteroid dehydrogenase isoforms.
Oppermann, UC; Persson, B; Jörnvall, H;
The Federation of European Biochemical Societies (FEBS) Journal. 1997 249:355-360. doi:
PMID: 9370340

Role of type-1 11beta-hydroxysteroid dehydrogenase in detoxification processes.
Maser, E; Oppermann, UC;
The Federation of European Biochemical Societies (FEBS) Journal. 1997 249:365-369. doi:
PMID: 9370342

Active site directed mutagenesis of 3 beta/17 beta-hydroxysteroid dehydrogenase establishes differential effects on short-chain dehydrogenase/reductase reactions.
Oppermann, UC; Filling, C; Berndt, KD; Persson, B; Benach, J; Ladenstein, R; Jörnvall, H;
Biochemistry. 1997 36:34-40. doi: 10.1021/bi961803v
PMID: 8993315

Structure-function relationships of SDR hydroxysteroid dehydrogenases.
Oppermann, UC; Persson, B; Filling, C; Jörnvall, H;
Advances in Experimental Medicine and Biology. 1997 414:403-415. doi:
PMID: 9059645

The 11β-hydroxysteroid dehydrogenase system, a determinant of glucocorticoid and mineralocorticoid action
Oppermann, UCT; Persson, B; Jörnvall, H;
The Federation of European Biochemical Societies (FEBS) Journal. 1997 249:355-360. doi:
PMID:

1996

Characterization of a 3 alpha-hydroxysteroid dehydrogenase/carbonyl reductase from the gram-negative bacterium Comamonas testosteroni.
Oppermann, UC; Maser, E;
The Federation of European Biochemical Societies (FEBS) Journal. 1996 241:744-749. doi:
PMID: 8944761

Leukotriene A4 hydrolase: protection from mechanism-based inactivation by mutation of tyrosine-378.
Mueller, MJ; Blomster, M; Oppermann, UC; Jörnvall, H; Samuelsson, B; Haeggström, JZ;
Proceedings of the National Academy of Sciences of USA. 1996 93:5931-5935. doi:
PMID: 8650196

Antibiotic resistance and enhanced insecticide catabolism as consequences of steroid induction in the gram-negative bacterium Comamonas testosteroni.
Oppermann, UC; Belai, I; Maser, E;
The Journal of Steroid Biochemistry and Molecular Biology. 1996 58:217-223. doi:
PMID: 8809204

Crystallization and crystal packing of recombinant 3 (or 17) beta-hydroxysteroid dehydrogenase from Comamonas testosteroni ATTC 11996.
Benach, J; Knapp, S; Oppermann, UC; Hägglund, O; Jörnvall, H; Ladenstein, R;
The Federation of European Biochemical Societies (FEBS) Journal. 1996 236:144-148. doi:
PMID: 8617258

1995

Cloning and primary structure of murine 11 beta-hydroxysteroid dehydrogenase/microsomal carbonyl reductase.
Oppermann, UC; Netter, KJ; Maser, E;
The Federation of European Biochemical Societies (FEBS) Journal. 1995 227:202-208. doi:
PMID: 7851387

1993

Carbonyl reduction by 3α-HSD from Comamonas testosteroni - New properties and its relationship to the SCAD family
Oppermann, UCT; Netter, KJ; Maser, E;
Advances in Experimental Medicine and Biology. 1993 328:379-390. doi:
PMID: 8493916

1992

Homologies between enzymes involved in steroid and xenobiotic carbonyl reduction in vertebrates, invertebrates and procaryonts.
Oppermann, UC; Maser, E; Hermans, JJ; Koolman, J; Netter, KJ;
The Journal of Steroid Biochemistry and Molecular Biology. 1992 43:665-675. doi:
PMID: 1472459

1991

Heterogeneity of carbonyl reduction in subcellular fractions and different organs in rodents.
Oppermann, UC; Maser, E; Mangoura, SA; Netter, KJ;
Biochemical Pharmacology. 1991 42 Suppl:S189-S195. doi:
PMID: 1768277

The influence of cytochrome P-450 inducers on carbonyl reduction in mouse liver.
Maser, E; Hahnemann, B; Legrum, W; Oppermann, U; Netter, KJ;
Archives of toxicology. Supplement. Archiv f�r Toxikologie. Supplement. 1991 14:188-192. doi:
PMID: 1805730

1990

Immunological homologies between carbonyl reducing enzymes from prokaryonts and mammalian liver microsomes
Maser, E; Oppermann, U; Netter, KJ;
European Journal of Pharmacology. 1990 183:1366-1366. doi: 10.1016/0014-2999(90)94490-O
PMID:

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