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ribonucleoside-triphosphate reductase (89) 89
ribonucleoside triphosphate reductase (44) 44
index medicus (40) 40
biochemistry & molecular biology (33) 33
enzymes (32) 32
dna biosynthesis (28) 28
replication (28) 28
humans (24) 24
ribonucleotide reductases - metabolism (21) 21
research (20) 20
ribonucleotide reductase (20) 20
dna repair (19) 19
article (18) 18
cancer (18) 18
nucleotides (18) 18
analysis (17) 17
hydroxyurea (16) 16
deoxyribonucleotides (15) 15
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ethanolamine ammonia-lyase (14) 14
methylmalonyl-coa mutase (14) 14
mutation (14) 14
chemistry, inorganic & nuclear (13) 13
chemistry, multidisciplinary (13) 13
coenzyme b-12 (13) 13
dna (12) 12
kinetics (12) 12
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ribonucleotides (12) 12
data processing (11) 11
hydrogen-atom abstraction (11) 11
catalysis (10) 10
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gemcitabine (10) 10
iron (10) 10
ribonucleotide reductases - genetics (10) 10
amino acids (9) 9
cell cycle (9) 9
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lactobacillus-leichmannii (9) 9
metabolism (9) 9
models, molecular (9) 9
proteins (9) 9
survival (9) 9
amino acid sequence (8) 8
carbon bond homolysis (8) 8
cell biology (8) 8
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chemical properties (8) 8
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escherichia-coli (8) 8
genomes (8) 8
phosphorylation (8) 8
physiological aspects (8) 8
tumors (8) 8
x-ray-structure (8) 8
adenosylcobalamin (7) 7
coenzyme b 12 (7) 7
dissociation energy (7) 7
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glutamate mutase (7) 7
mitochondria (7) 7
mitochondrial dna (7) 7
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cell cycle proteins - metabolism (6) 6
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coenzyme b (6) 6
dependent glutamate mutase (6) 6
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Journal Article
Leukemia Research, ISSN 0145-2126, 2007, Volume 32, Issue 1, pp. 71 - 77
Abstract Triapine® is a potent ribonucleotide reductase (RR) inhibitor that depletes intracellular deoxyribonculeotide pools, especially dATP. We designed a... 
Hematology, Oncology and Palliative Medicine | Rbonucleotide reductase | Fludarabine | Myeloproliferative disorders | Triapine | Refractory acute leukemia | CHRONIC MYELOGENOUS LEUKEMIA | CELLS | RESPONSE CRITERIA | NERVOUS-SYSTEM TOXICITY | HYDROXYUREA | myeloproliferative disorders | rbonucleotide reductase | INTERNATIONAL WORKING GROUP | INDUCTION THERAPY | METABOLISM | ONCOLOGY | refractory acute leukemia | fludarabine | ARA-C | HEMATOLOGY | MYELODYSPLASTIC SYNDROMES | Recurrence | Pyridines - administration & dosage | Humans | Middle Aged | Antineoplastic Combined Chemotherapy Protocols - adverse effects | Male | Treatment Outcome | Myeloproliferative Disorders - drug therapy | Vidarabine - analogs & derivatives | Thiosemicarbazones - administration & dosage | Antineoplastic Combined Chemotherapy Protocols - therapeutic use | Precursor Cell Lymphoblastic Leukemia-Lymphoma - diet therapy | Leukemia, Myeloid, Acute - drug therapy | Adult | Female | Aged | Vidarabine - administration & dosage | Myelodysplastic Syndromes - drug therapy | Antimitotic agents | Care and treatment | Oncology, Experimental | Bone marrow | Nucleosides | Clinical trials | Transplantation | Research | Antineoplastic agents | Cancer | Adenosine | nucleoside analogs | Ribonucleoside-triphosphate reductase | Toxicity | Leukemia | Malignancy | Fever | Metabolic acidosis | Myeloproliferative diseases | triapine | ribonucleotide reductase
Journal Article
Free Radical Biology and Medicine, ISSN 0891-5849, 02/2012, Volume 52, Issue 4, pp. 803 - 810
Ribonucleotide reductase (RNR) activity requires an electron donor, which in bacteria, yeast, and plants is usually either reduced thioredoxin (Trx) or reduced... 
DNA replication | Hepatocyte | Mouse | Thioredoxin reductase | Glutathione | EARLY EMBRYONIC LETHALITY | THIOREDOXIN REDUCTASE 1 | MAMMALIAN THIOREDOXIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | RIBONUCLEOSIDE-DIPHOSPHATE REDUCTASE | RESPONSE ELEMENT | REDOX SYSTEMS | GENE | ENDOCRINOLOGY & METABOLISM | S-PHASE | HYDROGEN DONOR SYSTEM | Cell Proliferation | Liver - enzymology | Exons | Glutathione - metabolism | Molecular Sequence Data | Thioredoxin Reductase 1 - deficiency | Glutathione Disulfide - metabolism | Hepatocytes - metabolism | Liver - growth & development | Isoenzymes - metabolism | Base Sequence | Thioredoxins - metabolism | Transcription, Genetic | Hepatocytes - physiology | Isoenzymes - genetics | Liver - metabolism | Mice, Inbred C57BL | DNA Replication | Thioredoxin Reductase 2 - genetics | Glutathione - physiology | Thioredoxin Reductase 2 - metabolism | Animals | Heterozygote | Liver - cytology | Mice | Thioredoxin Reductase 1 - genetics | Histones - metabolism | Proliferating Cell Nuclear Antigen - metabolism | Hepatocytes - enzymology | Thioredoxin Reductase 1 - metabolism | Antigen-antibody reactions | Messenger RNA | Growth | Liver | DNA | Genes | Albumin | Genetic research | Thioredoxin | Cells | RNA | DNA polymerases | DNA biosynthesis | Enzymes | Thioredoxin-disulfide reductase | Buthionine sulfoximine | Hepatocytes | Ribonucleoside-triphosphate reductase | Glutaredoxin | Replication | mRNA | glutathione reductase | mouse | hepatocyte | glutathione | thioredoxin reductase
Journal Article
Journal Article
Apoptosis, ISSN 1360-8185, 3/2011, Volume 16, Issue 3, pp. 256 - 271
We previously reported that HSV-2 R1, the R1 subunit (ICP10; UL39) of herpes simplex virus type-2 ribonucleotide reductase, protects cells against apoptosis... 
Biochemistry, general | Caspase-8 | ICP10 | ICP6 | Biomedicine | FasL | Viral inhibitor of apoptosis | Cancer Research | Oncology | Virology | Cell Biology | DEATH DOMAIN | ACTIVATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | NECROSIS-FACTOR-ALPHA | TRIGGERED APOPTOSIS | MEDIATED APOPTOSIS | FLICE-INHIBITORY PROTEIN | SIGNALING COMPLEX | CELL BIOLOGY | IN-VITRO | BLOCKS APOPTOSIS | UP-REGULATION | Protein Structure, Tertiary | Cell Survival - drug effects | Apoptosis - drug effects | Humans | Caspase 8 - metabolism | Fas-Associated Death Domain Protein - metabolism | Caspase 8 - chemistry | JNK Mitogen-Activated Protein Kinases - metabolism | NF-kappa B - metabolism | Extracellular Signal-Regulated MAP Kinases - metabolism | Protein Subunits - metabolism | Herpes Simplex - metabolism | Tumor Necrosis Factor-alpha - pharmacology | Herpes Simplex - virology | Fas Ligand Protein - pharmacology | Herpesvirus 1, Human - enzymology | Signal Transduction - drug effects | Gene Deletion | Protein Binding - drug effects | Cytoprotection - drug effects | Ribonucleotide Reductases - metabolism | Cell Line, Tumor | Herpesvirus 2, Human - enzymology | Proto-Oncogene Proteins c-akt - metabolism | Fas antigen | CD95 antigen | Extracellular signal-regulated kinase | ICP10 protein | AKT protein | Survival | 1-Phosphatidylinositol 3-kinase | Deletion mutant | death receptors | FADD protein | Infection | Signal transduction | NF- Kappa B protein | FasL protein | Molecular modelling | Overexpression | Ribonucleoside-triphosphate reductase | c-Jun amino-terminal kinase | Tumor necrosis factor- alpha | Apoptosis
Journal Article
Journal of Chemical Theory and Computation, ISSN 1549-9618, 09/2010, Volume 6, Issue 9, pp. 2770 - 2781
Ribonucleotide reductase (RNR) is the key enzyme in the biosynthesis of deoxyribonucleotides. The enzyme has thus an attractive target for chemotherapies that... 
H BOND ACTIVATION | DENSITY | ANAEROBIC ESCHERICHIA-COLI | ENZYME | 5'-DIPHOSPHATE | PHYSICS, ATOMIC, MOLECULAR & CHEMICAL | ATOMIC CHARGES | CHEMISTRY, PHYSICAL | MODEL | INHIBITORS | 2'-DEOXY-2'-METHYLIDENECYTIDINE | GEMCITABINE | Enzymes | Chemotherapy | Hybrids | scaffolds | Ribonucleoside-triphosphate reductase | Models | Monomers | deoxyribonucleotides
Journal Article
Annual Review of Biochemistry, ISSN 0066-4154, 7/2011, Volume 80, Issue 1, pp. 733 - 767
Journal Article