Articles

Search Articles

Advanced search
Help

Catalogue

Articles

Databases

X
Search Filters
Format Format
Format Format
X
Sort by Item Count (A-Z)
Filter by Count
Journal Article (14362) 14362
Publication (2304) 2304
Book Chapter (203) 203
Book Review (86) 86
Dissertation (66) 66
Conference Proceeding (52) 52
Magazine Article (4) 4
Trade Publication Article (4) 4
Government Document (3) 3
Newspaper Article (3) 3
Book / eBook (2) 2
Data Set (2) 2
Paper (1) 1
more...
Subjects Subjects
Subjects Subjects
X
Sort by Item Count (A-Z)
Filter by Count
index medicus (6211) 6211
humans (4901) 4901
animals (3893) 3893
biochemistry & molecular biology (2916) 2916
male (2280) 2280
female (2126) 2126
dioxygenase (2098) 2098
enzymes (1875) 1875
mice (1714) 1714
analysis (1598) 1598
microbiology (1576) 1576
dioxygenases (1556) 1556
research (1494) 1494
expression (1443) 1443
molecular sequence data (1438) 1438
genes (1276) 1276
biotechnology & applied microbiology (1268) 1268
indoleamine-pyrrole 2,3,-dioxygenase - metabolism (1258) 1258
procollagen-proline dioxygenase - metabolism (1249) 1249
physiological aspects (1231) 1231
gene expression (1219) 1219
dioxygenases - metabolism (1196) 1196
amino acid sequence (1132) 1132
metabolism (1091) 1091
oxygenases - metabolism (1064) 1064
cell biology (1060) 1060
degradation (1043) 1043
biodegradation (1034) 1034
indoleamine 2,3-dioxygenase (1023) 1023
adult (976) 976
kinetics (954) 954
middle aged (950) 950
rats (945) 945
proteins (942) 942
genetic aspects (938) 938
article (916) 916
immunology (911) 911
research article (910) 910
escherichia-coli (904) 904
plant sciences (893) 893
dioxygenases - genetics (882) 882
oxygenases - genetics (842) 842
biosynthesis (837) 837
bacteria (800) 800
cells, cultured (793) 793
substrate specificity (784) 784
dendritic cells (773) 773
biodegradation, environmental (759) 759
tryptophan (756) 756
models, molecular (700) 700
life sciences (695) 695
cancer (688) 688
multidisciplinary sciences (687) 687
oxidation-reduction (680) 680
base sequence (677) 677
alpha-ketoglutarate-dependent dioxygenase fto (669) 669
hydroxylation (664) 664
catalysis (647) 647
cloning, molecular (640) 640
indoleamine-pyrrole 2,3,-dioxygenase - genetics (633) 633
proteins - genetics (626) 626
obesity (607) 607
mutation (604) 604
identification (603) 603
hypoxia (593) 593
gene (591) 591
inhibition (582) 582
aged (581) 581
tryptophan catabolism (581) 581
chemistry, multidisciplinary (572) 572
oxidation (569) 569
crystal-structure (564) 564
biophysics (560) 560
genetics & heredity (545) 545
iron (540) 540
oncology (539) 539
phylogeny (539) 539
gene-expression (532) 532
mice, inbred c57bl (527) 527
tryptophan - metabolism (527) 527
dioxygenases - chemistry (515) 515
cloning (513) 513
protein (502) 502
purification (500) 500
activation (499) 499
signal transduction (489) 489
procollagen-proline dioxygenase - genetics (483) 483
binding sites (481) 481
medicine (479) 479
obesity - genetics (471) 471
oxygen - metabolism (467) 467
mechanism (465) 465
inflammation (462) 462
health aspects (447) 447
genetic research (444) 444
chemical properties (442) 442
interferon-gamma (442) 442
polymorphism, single nucleotide (438) 438
mixed function oxygenases - metabolism (434) 434
cell line, tumor (433) 433
more...
Library Location Library Location
Language Language
Language Language
X
Sort by Item Count (A-Z)
Filter by Count
English (14119) 14119
Chinese (126) 126
Japanese (104) 104
Russian (59) 59
German (42) 42
French (38) 38
Polish (15) 15
Korean (13) 13
Spanish (12) 12
Czech (11) 11
Portuguese (6) 6
Italian (2) 2
Swedish (2) 2
Ukrainian (2) 2
Arabic (1) 1
Dutch (1) 1
Finnish (1) 1
Indonesian (1) 1
Lithuanian (1) 1
Slovak (1) 1
Turkish (1) 1
more...
Publication Date Publication Date
Click on a bar to filter by decade
Slide to change publication date range


1. Full Text Functional analysis of active amino acid residues of the mercaptosuccinate dioxygenase of Variovorax paradoxus B4
by Brandt, Ulrike and Galant, Gulsina and Meinert-Berning, Christina and Steinbüchel, Alexander
Enzyme and Microbial Technology, ISSN 0141-0229, 01/2019, Volume 120, pp. 61 - 68
Thiol dioxygenases are non-heme mononuclear-iron proteins and belong to the cupin superfamily. In 2014, mercaptosuccinate dioxygenase (Msdo) of B4 was... 
Thiol dioxygenase | Active site structure | Site-directed mutagenesis | Mercaptosuccinate dioxygenase | EVOLUTION | CYSTEINE DIOXYGENASE | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | POLYTHIOESTERS | HOMOLOG | STRAIN | Amino Acid Sequence | Catalytic Domain | Dioxygenases - metabolism | Comamonadaceae - enzymology | Dioxygenases - chemistry | Mutagenesis, Site-Directed | Amino Acids - chemistry | Substrate Specificity | Cysteine Dioxygenase - chemistry | Cysteine Dioxygenase - metabolism | Amino Acids - genetics | Sequence Homology | Dioxygenases - genetics | Thiomalates - metabolism | Catalysis | Mutation | Cysteine Dioxygenase - genetics | Enzymes | Sulfites | Cysteine | Thiols | Analysis | Heme | Iron proteins | Cystine | Index Medicus
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
2. Full Text 4-Hydroxyphenylpyruvate dioxygenase and hydroxymandelate synthase: Exemplars of the α-keto acid dependent oxygenases
by Moran, Graham R
Archives of Biochemistry and Biophysics, ISSN 0003-9861, 02/2014, Volume 544, pp. 58 - 68
4-Hydroxyphenylpyruvate dioxygenase (HPPD) and hydroxymandelate synthase (HMS) are outliers within the α-keto acid dependent oxygenase (αKAO) family. HPPD and... 
4-Hydroxyphenylpyruvate dioxygenase | Oxygenase | Dioxygenase | Molecular oxygen | Hydroxymandelate synthase | Ferrous | α-Keto acid | FERROUS ACTIVE-SITE | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | alpha-Keto acid | P-HYDROXYPHENYLPYRUVATE DIOXYGENASE | TAURINE/ALPHA-KETOGLUTARATE DIOXYGENASE | SPIN FE(IV) COMPLEX | (4-HYDROXYPHENYL)PYRUVATE DIOXYGENASE | NIH-SHIFT | BIOPHYSICS | 2-HIS-1-CARBOXYLATE FACIAL TRIAD | CATALYTIC MECHANISM | NONHEME IRON ENZYME | 4-Hydroxyphenylpyruvate Dioxygenase - antagonists & inhibitors | Dioxygenases - metabolism | Bacteria - chemistry | Dioxygenases - chemistry | 4-Hydroxyphenylpyruvate Dioxygenase - metabolism | Humans | Mandelic Acids - metabolism | Models, Molecular | Substrate Specificity | Mandelic Acids - chemistry | Animals | Bacteria - enzymology | Protein Conformation | 4-Hydroxyphenylpyruvate Dioxygenase - chemistry
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
3. QM/MM-Simulationen ergeben synergetische Substrat- und Sauerstoffaktivierung in Salicylat-Dioxygenase
by Subhendu Roy and Johannes Kastner
Angewandte Chemie, ISSN 0044-8249, 01/2016, Volume 128, Issue 3, p. 1182
  Salicylat-1,2-Dioxygenase (SDO) ist das erste bekannte Enzym, das die oxidative Spaltung eines einfach hydroxylierten Aromaten, Salicylat, statt der... 
Dioxygenase
Journal Article
Details down arrow
4. Full Text Structure and function of atypically coordinated enzymatic mononuclear non-heme-Fe(II) centers
by Buongiorno, Daniela and Straganz, Grit D
Coordination Chemistry Reviews, ISSN 0010-8545, 01/2013, Volume 257, Issue 2, pp. 541 - 563
► The Cupin fold provides metal binding motif plasticity. ► The 2-His binding motif offers a platform for halogenations. ► The 3-His binding motif affects the... 
Metal binding motif | Dioxygenase | Structure–function relationships | Facial triad | Enzyme catalysis | Dioxygen activation | Structure-function relationships | RING-CLEAVING DIOXYGENASES | MOUSE CYSTEINE DIOXYGENASE | TAURINE/ALPHA-KETOGLUTARATE DIOXYGENASE | METHIONINE SALVAGE PATHWAY | CHEMISTRY, INORGANIC & NUCLEAR | PSEUDOMONAS-PAUCIMOBILIS TMY1009 | NONHEME IRON ENZYMES | 2-HIS-1-CARBOXYLATE FACIAL TRIAD | ELECTRON-PARAMAGNETIC-RESONANCE | CYANOBACTERIUM LYNGBYA-MAJUSCULA | CONTAINING QUERCETIN 2,3-DIOXYGENASE | Enzymes | Taurine | Flavonoids | Cysteine | Peptides | Flavones | Bioflavonoids | Collateralized debt obligations | TauD, taurine hydroxylase | acac, acetylacetone (2,4-pentanedione) | BsQDO, quercetin 2,3-dioxygenase from Bacillus subtilis | 2OH-1,3-Ph2PD, 2-hydroxy-1,3-diphenylpropanedione | CS2, clavaminate synthase | 6-Ph2TPA, N,N-bis[(6-phenyl-2-pyridyl)methyl]-N-[(2-pyridyl)-methyl]amine | QDO, quercetin 2,3-dioxygenase | MNHEs, mononuclear non-heme-Fe(II) dependent enzymes | EPR, electron paramagnetic resonance | XAS, X-ray absorption spectroscopy | Review | Dke1, diketone dioxygenase | ADO, cysteamine dioxygenase | GDO, gentisate 1,2-dioxygenase | fla, flavonolate | SDO, salicylate 1,2-dioxygenase | HNDO, hydroxy-2-naphthoate dioxygenase | CDO, cysteine dioxygenase | HADO, 3-hydroxyanthranilate 3,4-dioxygenase | HGDO, homogentisate 1,2-dioxygenase | NRP, nonribosomal peptide | EXAFS, extended X-ray absorption fine structure spectroscopy | α-KG, α-ketoglutarate | DFT, density functional theory | CarOs, carotenoid oxygenases | MCD, magnetic circular dichroism | AO, apocarotenoid 15,15′-oxygenase | ARD, aci-reductone dioxygenase | PDB, protein data bank | CGDO, 5-chloro-gentisate 1,2-dioxygenase | OTf-, trifluormethanesulfonate | 1,3-bis(2-pyridylimino)isoindoline, ind | CD, circular dichroism
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
5. Full Text Oncometabolite 2-Hydroxyglutarate Is a Competitive Inhibitor of α-Ketoglutarate-Dependent Dioxygenases
by Xu, Yan-hui and Xu, Wei and Yang, Chen and Yang, Ying and Yang, Hui and Liu, Li-xia and Liu, Ying and Liu, Jing and Wang, Bin and Wang, Ping and Wang, Pu and Kim, Se-Hee and Ito, Shinsuke and Xiao, Meng-Tao and Jiang, Wen-qing and Zhang, Yi and Zhang, Jin-ye and Frye, Stephen and Lei, Qun-ying and Guan, Kun-Liang and Zhao, Shi-min and Xiong, Yue
Cancer Cell, ISSN 1535-6108, 2011, Volume 19, Issue 1, pp. 17 - 30
and mutations occur frequently in gliomas and acute myeloid leukemia, leading to simultaneous loss and gain of activities in the production of α-ketoglutarate... 
BREAST-CANCER | TRANSCRIPTIONAL ACTIVITY | IDH2 MUTATIONS | ONCOLOGY | PROLYL HYDROXYLATION | INTEGRATED GENOMIC ANALYSIS | 2-OXOGLUTARATE OXYGENASES | ACUTE MYELOID-LEUKEMIA | HIF-ALPHA | HISTONE DEMETHYLATION | FAMILY | CELL BIOLOGY | Dioxygenases - metabolism | Histone Demethylases - antagonists & inhibitors | Gene Expression - genetics | Caenorhabditis elegans Proteins - chemistry | Humans | Ketoglutaric Acids - chemistry | Glioma - genetics | F-Box Proteins | Oxidoreductases, N-Demethylating - antagonists & inhibitors | Ketoglutaric Acids - pharmacology | Cytosine - metabolism | Hypoxia-Inducible Factor 1, alpha Subunit - metabolism | Glutarates - chemistry | Oxidoreductases, N-Demethylating - metabolism | DNA-Binding Proteins - antagonists & inhibitors | Glioma - enzymology | Endostatins - metabolism | Models, Molecular | Isocitrate Dehydrogenase - genetics | Histone Demethylases - metabolism | Dioxygenases - antagonists & inhibitors | Amino Acid Substitution - physiology | Procollagen-Proline Dioxygenase - genetics | Cell Line, Tumor | Isocitrate Dehydrogenase - metabolism | Glutarates - pharmacology | Histones - metabolism | Jumonji Domain-Containing Histone Demethylases - metabolism | Caenorhabditis elegans - enzymology | Cytosine - analogs & derivatives | Gene Expression - drug effects | Caenorhabditis elegans Proteins - metabolism | Isocitrate Dehydrogenase - antagonists & inhibitors | Glioma - metabolism | Procollagen-Proline Dioxygenase - metabolism | DNA-Binding Proteins - metabolism | Mixed Function Oxygenases | Biocatalysis - drug effects | Jumonji Domain-Containing Histone Demethylases - antagonists & inhibitors | Jumonji Domain-Containing Histone Demethylases - chemistry | Procollagen-Proline Dioxygenase - antagonists & inhibitors | Ketoglutaric Acids - metabolism | Oxalates - pharmacology | Binding, Competitive | Proto-Oncogene Proteins - metabolism | Proto-Oncogene Proteins - antagonists & inhibitors | Catalytic Domain | Proto-Oncogene Proteins - genetics | Hypoxia-Inducible Factor-Proline Dioxygenases | DNA-Binding Proteins - genetics | Homeodomain Proteins - genetics | Animals | 5-Methylcytosine - metabolism | Caenorhabditis elegans Proteins - antagonists & inhibitors | Glutarates - metabolism
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
6. Full Text JunD Reduces Tumor Angiogenesis by Protecting Cells from Oxidative Stress
by Gerald, Damien and Berra, Edurne and Frapart, Yves M and Chan, Denise A and Giaccia, Amato J and Mansuy, Daniel and Pouysségur, Jacques and Yaniv, Moshe and Mechta-Grigoriou, Fatima
Cell, ISSN 0092-8674, 2004, Volume 118, Issue 6, pp. 781 - 794
Reactive oxygen species (ROS) are implicated in the pathophysiology of various diseases, including cancer. In this study, we show that JunD, a member of the... 
HYPOXIA-INDUCIBLE FACTOR | PARAMAGNETIC-RESONANCE | MITOCHONDRIAL RESPIRATORY-CHAIN | MESSENGER-RNA | PROLYL HYDROXYLATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | GENE-EXPRESSION | FACTOR-I | CYCLE PROGRESSION | ENDOTHELIAL GROWTH-FACTOR | TRANSCRIPTIONAL RESPONSE | CELL BIOLOGY | Neoplasms - metabolism | Proto-Oncogene Proteins c-jun - physiology | Reactive Oxygen Species - metabolism | Antioxidants - metabolism | Humans | ras Proteins - metabolism | Vascular Endothelial Growth Factor A - metabolism | Hypoxia-Inducible Factor 1, alpha Subunit | Procollagen-Proline Dioxygenase - metabolism | Neoplasms - genetics | Neovascularization, Pathologic - physiopathology | Gene Expression Regulation, Neoplastic - genetics | Proto-Oncogene Proteins c-jun - genetics | Oxidative Stress - genetics | Neoplasms - blood supply | Up-Regulation - genetics | Hypoxia-Inducible Factor-Proline Dioxygenases | Dioxygenases | Iron - metabolism | Hydrogen Peroxide - metabolism | Transcription Factors - metabolism | Reactive Oxygen Species - antagonists & inhibitors | Animals | Neovascularization, Pathologic - genetics | Neovascularization, Pathologic - metabolism | Oxidative stress | Genetic transcription | Research | Neovascularization | Up-Regulation | Vascular Endothelial Growth Factor A | Reactive Oxygen Species | ras Proteins | Oxidative Stress | Hydrogen Peroxide | Biochemistry, Molecular Biology | Gene Expression Regulation, Neoplastic | Neovascularization, Pathologic | Iron | Neoplasms | Antioxidants | Life Sciences | Transcription Factors | Procollagen-Proline Dioxygenase | Proto-Oncogene Proteins c-jun | Cancer
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
7. Full Text 4-Hydroxyphenylpyruvate dioxygenase catalysis: Identification of catalytic residues and production of a hydroxylated intermediate shared with a structurally unrelated enzyme
by Raspail, Corinne and Graindorge, Matthieu and Moreau, Yohann and Crouzy, Serge and Lefèbvre, Bertrand and Robin, Adeline Y and Dumas, Renaud and Matringe, Michel
Journal of Biological Chemistry, ISSN 0021-9258, 07/2011, Volume 286, Issue 29, pp. 26061 - 26070
4-Hydroxyphenylpyruvate dioxygenase (HPPD) catalyzes the conversion of 4-hydroxyphenylpyruvate (HPP) into homogentisate. HPPD is the molecular target of very... 
DENSITY | POTENT INHIBITOR | HYDROXYMANDELATE SYNTHASE | ACID | NONHEME IRON ENZYMES | STREPTOMYCES-AVERMITILIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | HEREDITARY TYROSINEMIA | CRYSTAL-STRUCTURES | P-HYDROXYPHENYLPYRUVATE DIOXYGENASE | (4-HYDROXYPHENYL)PYRUVATE DIOXYGENASE | Catalytic Domain | Biocatalysis | Mutagenesis, Site-Directed | 4-Hydroxyphenylpyruvate Dioxygenase - metabolism | Hydroxylation | Oxidation-Reduction | Models, Molecular | Homogentisic Acid - metabolism | Intramolecular Transferases - metabolism | 4-Hydroxyphenylpyruvate Dioxygenase - genetics | Conserved Sequence | Delftia acidovorans - enzymology | Kinetics | Mutation | 4-Hydroxyphenylpyruvate Dioxygenase - chemistry | Index Medicus | Life Sciences | Biochemistry, Molecular Biology | Enzyme Structure | Dioxygenase | Enzyme Catalysis | Enzyme Mutation | Enzymology | Metabolism | Metalloenzymes
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
8. Full Text We two alone will sing: the two-substrate α-keto acid-dependent oxygenases
by He, Panqing and Moran, Graham R
Current Opinion in Chemical Biology, ISSN 1367-5931, 2009, Volume 13, Issue 4, pp. 443 - 450
4-Hydroxyphenylpyruvate dioxygenase (HPPD) and hydroxymandelate synthase (HMS) are the only two known members of the α-keto acid-dependent oxygenases that... 
FERROUS ACTIVE-SITE | HYDROXYMANDELATE SYNTHASE | BIOPHYSICS | STREPTOMYCES-AVERMITILIS | STRUCTURAL BASIS | BIOCHEMISTRY & MOLECULAR BIOLOGY | HYDROXYPHENYLPYRUVATE DIOXYGENASE | CRYSTAL-STRUCTURES | 4-HYDROXYPHENYLPYRUVATE DIOXYGENASE | KETOGLUTARATE DIOXYGENASE | (4-HYDROXYPHENYL)PYRUVATE DIOXYGENASE | ELECTRONIC-STRUCTURE | 4-Hydroxyphenylpyruvate Dioxygenase - antagonists & inhibitors | Dioxygenases - antagonists & inhibitors | Dioxygenases - metabolism | Animals | 4-Hydroxyphenylpyruvate Dioxygenase - metabolism | Humans | 4-Hydroxyphenylpyruvate Dioxygenase - analysis | Dioxygenases - analysis | Models, Molecular | Substrate Specificity | Crystallography, X-Ray
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
9. Full Text The different catalytic roles of the metal-binding ligands in human 4-hydroxyphenylpyruvate dioxygenase
by Huang, Chih-Wei and Liu, Hsiu-Chen and Shen, Chia-Pei and Chen, Yi-Tong and Lee, Sung-Jai and Lloyd, Matthew D and Lee, Hwei-Jen
Biochemical Journal, ISSN 0264-6021, 05/2016, Volume 473, Issue 9, pp. 1179 - 1189
4-Hydroxyphenylpyruvate dioxygenase (HPPD) is a non-haem iron(II)-dependent oxygenase that catalyses the conversion of 4-hydroxyphenylpyruvate (HPP) to... 
4-hydroxyphenylpyruvate dioxygenase | Metal-binding motif | Non-haem fe(II)-dependent oxygenase | 2-His-1-carboxylate facial triad | Iron-binding ligands | CLEAVING CATECHOLIC DIOXYGENASE | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | P-HYDROXYPHENYLPYRUVATE DIOXYGENASE | TAURINE/ALPHA-KETOGLUTARATE DIOXYGENASE | DEACETOXYCEPHALOSPORIN C SYNTHASE | metal-binding motif | (4-HYDROXYPHENYL)PYRUVATE DIOXYGENASE | TYROSINEMIA TYPE-I | CLAVAMINIC ACID SYNTHASE | NONHEME IRON(II) ENZYMES | iron-binding ligands | non-haem Fe(II)-dependent oxygenase | 4-Hydroxyphenylpyruvate Dioxygenase - genetics | Humans | Iron - chemistry | Models, Molecular | Ligands | Mutation, Missense | 4-Hydroxyphenylpyruvate Dioxygenase - chemistry | Iron - metabolism | Amino Acid Substitution | Index Medicus
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
10. Full Text 4‑Hydroxyphenylpyruvate Dioxygenase Inhibitors: From Chemical Biology to Agrochemicals
by Ndikuryayo, Ferdinand and Moosavi, Behrooz and Yang, Wen-Chao and Yang, Guang-Fu
Journal of Agricultural and Food Chemistry, ISSN 0021-8561, 10/2017, Volume 65, Issue 39, pp. 8523 - 8537
The development of new herbicides is receiving considerable attention to control weed biotypes resistant to current herbicides. Consequently, new enzymes are... 
Chemical biology | 4-hydroxyphenylpyruvate dioxygenase | Inhibitor | Agrochemical | Herbicide | HYDROXYMANDELATE SYNTHASE | HOMOGENTISATE PHYTYLTRANSFERASE | FOOD SCIENCE & TECHNOLOGY | HERBICIDAL ACTIVITY | P-HYDROXYPHENYLPYRUVATE DIOXYGENASE | AMYCOLATOPSIS-ORIENTALIS | SYNECHOCYSTIS SP PCC-6803 | agrochemical | (4-HYDROXYPHENYL)PYRUVATE DIOXYGENASE | chemical biology | inhibitor | MOLECULAR-FIELD ANALYSIS | STREPTOMYCES-AVERMITILIS | AGRICULTURE, MULTIDISCIPLINARY | herbicide | FUNCTIONAL ASSIGNMENT | CHEMISTRY, APPLIED | 4-Hydroxyphenylpyruvate Dioxygenase - antagonists & inhibitors | Arabidopsis - enzymology | 4-Hydroxyphenylpyruvate Dioxygenase - metabolism | Plants, Genetically Modified - drug effects | Herbicides - chemistry | Enzyme Inhibitors - pharmacology | Herbicides - pharmacology | Structure-Activity Relationship | Recombinant Proteins | Weed Control | Agrochemicals - pharmacology | Homogentisic Acid - metabolism | Molecular Structure | Phenylpyruvic Acids - metabolism | Catalysis | 4-Hydroxyphenylpyruvate Dioxygenase - chemistry | Agrochemicals - chemistry | Drug Resistance
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
11. Full Text Transformation by the (R)-enantiomer of 2-hydroxyglutarate linked to EGLN activation
by Koivunen, Peppi and Lee, Sungwoo and Duncan, Christopher G and Lopez, Giselle and Lu, Gang and Ramkissoon, Shakti and Losman, Julie A and Joensuu, Päivi and Bergmann, Ulrich and Gross, Stefan and Travins, Jeremy and Weiss, Samuel and Looper, Ryan and Ligon, Keith L and Verhaak, Roel G. W and Yan, Hai and Kaelin Jr, William G
Nature, ISSN 0028-0836, 03/2012, Volume 483, Issue 7390, pp. 484 - 488
The identification of succinate dehydrogenase (SDH), fumarate hydratase (FH) and isocitrate dehydrogenase (IDH) mutations in human cancers has rekindled the... 
HYPOXIA-INDUCIBLE FACTOR | CELLS | ACTIVE-SITE | OXYGEN SENSING PATHWAY | MULTIDISCIPLINARY SCIENCES | L-2-HYDROXYGLUTARIC ACIDURIA | PROLYL 4-HYDROXYLASES | MUTATIONS | ONCOMETABOLITE 2-HYDROXYGLUTARATE | TUMORS | HYDROXYLASES | Dioxygenases - metabolism | Humans | Hypoxia-Inducible Factor 1 - metabolism | Glioma - metabolism | Procollagen-Proline Dioxygenase - metabolism | Glioma - genetics | Cell Transformation, Neoplastic - genetics | Glioma - pathology | Glutarates - chemistry | Nuclear Proteins - genetics | Oncogenes | Astrocytes - cytology | Astrocytes - drug effects | Cell Line | Glioma - enzymology | Isocitrate Dehydrogenase - genetics | Nuclear Proteins - metabolism | Hypoxia-Inducible Factor-Proline Dioxygenases | Enzyme Activation - drug effects | Cell Transformation, Neoplastic - metabolism | Dioxygenases - genetics | Procollagen-Proline Dioxygenase - genetics | Cell Line, Tumor | Isocitrate Dehydrogenase - metabolism | Cell Proliferation - drug effects | Glutarates - metabolism | Cell Transformation, Neoplastic - drug effects | Glutarates - pharmacology | Astrocytes - metabolism | Genetic aspects | Gene mutations | Enantiomers | Properties | Identification and classification | Cancer cells | Hypoxia | Polypeptides | Mutation | Microbiology | Gene expression | Brain cancer
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
12. Full Text Oncometabolites d- and l‑2-Hydroxyglutarate Inhibit the AlkB Family DNA Repair Enzymes under Physiological Conditions
by Chen, Fangyi and Bian, Ke and Tang, Qi and Fedeles, Bogdan I and Singh, Vipender and Humulock, Zachary T and Essigmann, John M and Li, Deyu
Chemical Research in Toxicology, ISSN 0893-228X, 04/2017, Volume 30, Issue 4, pp. 1102 - 1110
Cancer-associated mutations often lead to perturbed cellular energy metabolism and accumulation of potentially harmful oncometabolites. One example is the... 
Ketoglutaric Acids - analysis | AlkB Homolog 2, Alpha-Ketoglutarate-Dependent Dioxygenase - antagonists & inhibitors | Glutarates - analysis | Stereoisomerism | Humans | Recombinant Proteins - chemistry | Enzyme Assays | Chromatography, High Pressure Liquid | Recombinant Proteins - biosynthesis | AlkB Homolog 3, Alpha-Ketoglutarate-Dependent Dioxygenase - genetics | Ketoglutaric Acids - chemistry | Recombinant Proteins - isolation & purification | AlkB Homolog 2, Alpha-Ketoglutarate-Dependent Dioxygenase - genetics | AlkB Homolog 3, Alpha-Ketoglutarate-Dependent Dioxygenase - antagonists & inhibitors | Base Sequence | DNA Repair | AlkB Homolog 3, Alpha-Ketoglutarate-Dependent Dioxygenase - metabolism | Inhibitory Concentration 50 | Protein Binding | AlkB Homolog 2, Alpha-Ketoglutarate-Dependent Dioxygenase - metabolism | Glutarates - chemistry | Glutarates - metabolism | Kinetics | Ketoglutaric Acids - metabolism | Index Medicus | ALKBH3 | ALKBH2 | 2-hydroxyglutarate | DNA repair inhibition | tumorigenesis | oncometabolite | AlkB
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights
13. Full Text Real-Time PCR quantification of PAH-ring hydroxylating dioxygenase (PAH-RHD α) genes from Gram positive and Gram negative bacteria in soil and sediment samples
by Cébron, Aurélie and Norini, Marie-Paule and Beguiristain, Thierry and Leyval, Corinne
Journal of Microbiological Methods, ISSN 0167-7012, 2008, Volume 73, Issue 2, pp. 148 - 159
Real-Time PCR based assays were developed to quantify Gram positive (GP) and Gram negative (GN) bacterial populations that are capable of degrading the... 
Soil | PAH-ring hydroxylating dioxygenase alpha subunit (PAH-RHD α) | Real-Time PCR | Sediment | PAH-bacterial degraders | PAH-ring hydroxylating dioxygenase alpha subunit (PAH-RHD | PHENANTHRENE DEGRADATION | POLYCYCLIC AROMATIC-HYDROCARBONS | BIOCHEMICAL RESEARCH METHODS | MICROBIOLOGY | soil | sediment | NEW-ZEALAND SOILS | POLYMERASE-CHAIN-REACTION | CATABOLIC GENE | NAPHTHALENE DIOXYGENASE | REVERSE TRANSCRIPTION-PCR | PAH-ring hydroxylating dioxygenase alpha subunit (PAH-RHD alpha) | MOLECULAR-CLONING | NAHAC GENE | NUCLEOTIDE-SEQUENCE | Dioxygenases - metabolism | Soil Microbiology | Bacterial Proteins - genetics | Gram-Positive Bacteria - enzymology | DNA Primers - genetics | Gene Dosage | Phylogeny | Polymerase Chain Reaction - methods | Gram-Negative Bacteria - enzymology | Gram-Positive Bacteria - genetics | Sequence Homology, Amino Acid | Geologic Sediments - microbiology | Colony Count, Microbial - methods | DNA, Bacterial - genetics | Dioxygenases - genetics | Polycyclic Aromatic Hydrocarbons - metabolism | Sensitivity and Specificity | RNA, Ribosomal, 16S - genetics | Bacterial Proteins - metabolism | Gram-Negative Bacteria - genetics | Biodegradation | Polycyclic aromatic hydrocarbons | RNA | Genes | Physiological aspects | Genetic research | Bacteria | Physicians (General practice) | Bacterial genetics | Soil microbiology | Sediments (Geology) | Environmental Sciences
Journal Article
Details down arrow
Digital rights down arrow
loading Loading Rights