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Nature, ISSN 0028-0836, 06/2009, Volume 459, Issue 7248, pp. 852 - 856
Cells normally grow to a certain size before they enter mitosis and divide. Entry into mitosis depends on the activity of Cdk1, which is inhibited by the Wee1... 
FISSION YEAST | WEE1 | PHOSPHORYLATION | NIM1/CDR1 MITOTIC INDUCER | PROTEIN-KINASE | NEGATIVE REGULATION | MULTIDISCIPLINARY SCIENCES | GROWTH | DIVISION PLANE | DUAL-SPECIFICITY KINASE | SCHIZOSACCHAROMYCES-POMBE | Protein Kinases - metabolism | Cell Polarity | Phosphorylation | Mitosis | Protein-Tyrosine Kinases - metabolism | Cell Cycle Proteins - metabolism | Nuclear Proteins - metabolism | Protein Transport | Cell Cycle Proteins - antagonists & inhibitors | Schizosaccharomyces - metabolism | Nuclear Proteins - antagonists & inhibitors | ras-GRF1 - metabolism | Protein-Serine-Threonine Kinases - antagonists & inhibitors | Schizosaccharomyces pombe Proteins - metabolism | Cell Cycle - physiology | G2 Phase | Protein-Serine-Threonine Kinases - metabolism | Schizosaccharomyces - cytology | Fungal Proteins - metabolism | Protein-Tyrosine Kinases - antagonists & inhibitors | Schizosaccharomyces pombe Proteins - antagonists & inhibitors | Arctic research | Cell cycle | Physiological aspects | Cell physiology | Genetic aspects | Research | Protein kinases | Proteins | Cell growth | Kinases | Molecular biology | Monitoring systems | ras-GRF1 | Protein-Serine-Threonine Kinases | Schizosaccharomyces pombe Proteins | Fungal Proteins | Cellular Biology | Nuclear Proteins | Life Sciences | Cell Cycle | Protein Kinases | Protein-Tyrosine Kinases | Cell Cycle Proteins | Schizosaccharomyces
Journal Article
Cell, ISSN 0092-8674, 2004, Volume 119, Issue 7, pp. 969 - 979
The regulation of ribosome biogenesis in response to environmental conditions is a key aspect of cell growth control. Ribosomal protein (RP) genes are... 
HEAD PROTEIN | YEAST | RAPAMYCIN | RECRUITMENT | RNA-POLYMERASE-I | SIGNALING PATHWAY | BIOCHEMISTRY & MOLECULAR BIOLOGY | CELL-GROWTH | FHA DOMAIN | SACCHAROMYCES-CEREVISIAE | MASS-SPECTROMETRY | CELL BIOLOGY | Consensus Sequence | Transcription Factors - chemistry | Saccharomyces cerevisiae - genetics | Phosphatidylinositol 3-Kinases - metabolism | Phosphatidylinositol 3-Kinases - antagonists & inhibitors | Repressor Proteins - antagonists & inhibitors | Ribosomal Proteins - metabolism | Saccharomyces cerevisiae - metabolism | Cell Nucleus - metabolism | Protein Binding - drug effects | Trans-Activators - genetics | Active Transport, Cell Nucleus | Phosphorylation - drug effects | Genes, Fungal - genetics | Protein-Serine-Threonine Kinases - metabolism | Repressor Proteins - metabolism | Proto-Oncogene Proteins p21(ras) - metabolism | Cyclic AMP-Dependent Protein Kinases - metabolism | Gene Expression Regulation, Fungal | Promoter Regions, Genetic | Ribosomal Proteins - genetics | Saccharomyces cerevisiae Proteins - antagonists & inhibitors | Intracellular Signaling Peptides and Proteins | Repressor Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | Transcription Factors - genetics | Sirolimus - pharmacology | Amino Acid Motifs | Phosphotransferases (Alcohol Group Acceptor) - metabolism | Transcription Factors - metabolism | Phosphotransferases (Alcohol Group Acceptor) - antagonists & inhibitors | Two-Hybrid System Techniques | Saccharomyces cerevisiae Proteins - metabolism | Trans-Activators - metabolism | Trans-Activators - antagonists & inhibitors | Forkhead Transcription Factors | Saccharomyces cerevisiae Proteins - chemistry | Rapamycin | Chemical properties | Research | Ribosomal proteins | Genetic regulation | Protein kinases | Life Sciences
Journal Article
Journal of Enzyme Inhibition and Medicinal Chemistry, ISSN 1475-6366, 12/2012, Volume 27, Issue 6, pp. 759 - 772
Inhibition of the metalloenzyme carbonic anhydrase (CA; EC 4.2.1.1) has pharmacologic applications in the field of anti-glaucoma, anti-convulsant and... 
sulphonamide | x-ray crystallography | imaging of hypoxic tumours | Carbonic anhydrase | glaucoma | anti-cancer agent | dithiocarbamate | Glaucoma | X-ray crystallography | Anti-cancer agent | Dithiocarbamate | Sulphonamide | Imaging of hypoxic tumours | MYCOBACTERIUM-TUBERCULOSIS | INCORPORATING 1,3,5-TRIAZINE MOIETIES | CHEMISTRY, MEDICINAL | ACTIVE-SITE | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | THERAPEUTIC APPLICATIONS | CRYSTALLOGRAPHIC ANALYSIS | PH-DEPENDENT ACTIVITY | X-RAY | ISOZYME-II | CRYPTOCOCCUS-NEOFORMANS | Fungal Proteins - chemistry | Anti-Infective Agents - pharmacology | Humans | Bacteria - drug effects | Bacterial Proteins - chemistry | Crystallography, X-Ray | Fungal Proteins - antagonists & inhibitors | Isoenzymes - chemistry | Structure-Activity Relationship | Carbonic Anhydrases - chemistry | Carbonic Anhydrases - metabolism | Bacteria - growth & development | Thiocarbamates - pharmacology | Isoenzymes - metabolism | Fungi - growth & development | Bacterial Proteins - antagonists & inhibitors | Catalytic Domain | Fungi - drug effects | Carbonic Anhydrase Inhibitors - chemical synthesis | Carbonic Anhydrase Inhibitors - pharmacology | Sulfonamides - pharmacology | Drug Discovery | Anti-Infective Agents - chemical synthesis | Sulfonamides - chemical synthesis | Thiocarbamates - chemical synthesis | Bacterial Proteins - metabolism | Molecular Docking Simulation | Isoenzymes - antagonists & inhibitors | Fungal Proteins - metabolism
Journal Article
Journal Article
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 1/2013, Volume 110, Issue 4, pp. 1315 - 1320
The influenza A virus M2 proton channel (A/M2) is the target of the antiviral drugs amantadine and rimantadine, whose use has been discontinued due to... 
Protons | Molecules | Quaternary ammonium compounds | Amines | Influenza A virus | Molecular structure | Drug interactions | Antivirals | Viruses | Ion channels | MOLECULAR-DYNAMICS | PROTEIN | MECHANISM | MULTIDISCIPLINARY SCIENCES | ADAMANTANE RESISTANCE | M2-S31N inhibitor | membrane protein structure | PROTON CHANNEL | NMR | TRANSPORT | A(H3N2) | M2-S31N mutant structure | MUTATIONS | AMANTADINE RESISTANCE | Influenza A virus - chemistry | Viral Matrix Proteins - genetics | Humans | Influenza A virus - genetics | Structure-Activity Relationship | Amantadine - chemistry | Antiviral Agents - chemistry | Drug Design | Nuclear Magnetic Resonance, Biomolecular | Genes, Fungal | Binding Sites | Antiviral Agents - pharmacology | Recombinant Proteins - antagonists & inhibitors | Amantadine - chemical synthesis | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Amantadine - analogs & derivatives | Drug Resistance, Viral - genetics | Viral Matrix Proteins - chemistry | Viral Matrix Proteins - antagonists & inhibitors | Antiviral Agents - chemical synthesis | Mutation | Influenza A virus - drug effects | Amantadine - pharmacology | Influenza viruses | Drug resistance in microorganisms | Physiological aspects | Microbiological chemistry | Research | Health aspects | Biological Sciences | Physical Sciences
Journal Article
Journal of cell science, ISSN 0021-9533, 08/2015, Volume 128, Issue 15, pp. 2842 - 2853
Journal Article
EMBO Molecular Medicine, ISSN 1757-4676, 03/2013, Volume 5, Issue 3, pp. 332 - 343
Aminoacyl‐tRNA synthetases (ARSs) are essential and ubiquitous ‘house‐keeping’ enzymes responsible for charging amino acids to their cognate tRNAs and... 
therapeutics | tRNA | human disease | aminoacyl‐tRNA synthetases (ARSs) | Aminoacyl-tRNA synthetases (ARSs) | Human disease | TRNA | Therapeutics | ANTIFUNGAL AGENT | MEDICINE, RESEARCH & EXPERIMENTAL | aminoacyl-tRNA synthetases (ARSs) | BRAIN-STEM | NONCANONICAL FUNCTION | PROTEIN-SYNTHESIS | LEUKOENCEPHALOPATHY | GENE | CAUSES MYOPATHY | LACTIC-ACIDOSIS | MUTATIONS | SPINAL-CORD INVOLVEMENT | Aminoacylation | Charcot-Marie-Tooth Disease - enzymology | Humans | Fungal Proteins - antagonists & inhibitors | Antifungal Agents - therapeutic use | Charcot-Marie-Tooth Disease - genetics | Anti-Bacterial Agents - therapeutic use | Amino Acyl-tRNA Synthetases - metabolism | Amino Acyl-tRNA Synthetases - genetics | Mitochondrial Diseases - genetics | Bacterial Proteins - antagonists & inhibitors | Enzyme Replacement Therapy | Mitochondrial Diseases - drug therapy | Genetic Predisposition to Disease | Gene Expression Regulation | Charcot-Marie-Tooth Disease - drug therapy | Mitochondrial Diseases - enzymology | Amino Acyl-tRNA Synthetases - therapeutic use | Phenotype | Animals | Bacterial Proteins - metabolism | Protein Biosynthesis - drug effects | Mutation | Amino Acyl-tRNA Synthetases - antagonists & inhibitors | Fungal Proteins - metabolism | Aminoacyl-tRNA synthetases | Protein biosynthesis | Transfer RNA | Heart | Enzymes | Editing | Exploration | Cardiovascular disease | Amino acids | Mammals | Hearing impairment | Peripheral neuropathy | Cell adhesion & migration | Proteins | Signal transduction | Angiogenesis | Genotype & phenotype | Antibiotics | Protein synthesis | Etiology | Ataxia | Autoimmune diseases | Reviews
Journal Article