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Molecular Cell, ISSN 1097-2765, 2009, Volume 35, Issue 5, pp. 563 - 573
The target of rapamycin complex 1 (TORC1) is a central regulator of eukaryotic cell growth that is activated by a variety of hormones (e.g., insulin) and... 
CELLBIO | PROTEINS | SIGNALING | YEAST SACCHAROMYCES-CEREVISIAE | CELL-GROWTH CONTROL | SIGNALING PATHWAYS | FUNCTIONAL HOMOLOG | RAG GTPASES | VACUOLE FUSION | BIOCHEMISTRY & MOLECULAR BIOLOGY | AMINO-ACID PERMEASE | COMPONENT | GTP-BINDING PROTEINS | GAP1 PERMEASE | CELL BIOLOGY | Vacuoles - enzymology | Intracellular Membranes - enzymology | Saccharomyces cerevisiae - genetics | Multiprotein Complexes | Adaptor Proteins, Vesicular Transport - genetics | Saccharomyces cerevisiae - drug effects | Guanosine Triphosphate - metabolism | Adaptor Proteins, Vesicular Transport - metabolism | Vacuoles - drug effects | DNA-Binding Proteins - metabolism | Amino Acids - metabolism | Time Factors | Guanine Nucleotide Exchange Factors - metabolism | Protein-Serine-Threonine Kinases - antagonists & inhibitors | Guanosine Diphosphate - metabolism | Protein Synthesis Inhibitors - pharmacology | Protein-Serine-Threonine Kinases - metabolism | Guanine Nucleotide Exchange Factors - genetics | Signal Transduction | Saccharomyces cerevisiae Proteins - antagonists & inhibitors | Monomeric GTP-Binding Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | Amino Acid Transport Systems - metabolism | Sirolimus - pharmacology | Cycloheximide - pharmacology | Protein Transport | Transcription Factors - metabolism | Monomeric GTP-Binding Proteins - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Protein Binding | Saccharomyces cerevisiae - enzymology | Endosomes - enzymology | Intracellular Membranes - drug effects | Mutation | Saccharomyces cerevisiae - growth & development | Proteins | Purines | Amino acids | Gross domestic product | Guanosine | Index Medicus
Journal Article
Science, ISSN 0036-8075, 8/2010, Volume 329, Issue 5995, pp. 1085 - 1088
Recognition of lipids by proteins is important for their targeting and activation in many signaling pathways, but the mechanisms that regulate such... 
Inositols | Yeasts | Medical research | Starvation | Cell growth | Cell nucleus | REPORTS | pH | Lipids | Phospholipids | Lipid metabolism | YEAST | LOCALIZATION | HOMEOSTASIS | PROTEIN | MULTIDISCIPLINARY SCIENCES | H+-ATPASE | VACUOLAR | SACCHAROMYCES-CEREVISIAE | TRANSCRIPTION FACTOR | Vacuolar Proton-Translocating ATPases - genetics | Inositol - metabolism | Saccharomyces cerevisiae - genetics | Endoplasmic Reticulum - metabolism | Recombinant Fusion Proteins - metabolism | Vacuolar Proton-Translocating ATPases - metabolism | Proton-Translocating ATPases - metabolism | Saccharomyces cerevisiae - metabolism | Cell Nucleus - metabolism | Proton-Translocating ATPases - genetics | Cation Transport Proteins - metabolism | Protein Phosphatase 1 - genetics | Cation Transport Proteins - genetics | Genes, Fungal | Transcription, Genetic | Cell Membrane - metabolism | Active Transport, Cell Nucleus | Repressor Proteins - metabolism | Gene Expression Regulation, Fungal | Signal Transduction | Repressor Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | Protein Phosphatase 1 - metabolism | Inositol - genetics | Saccharomyces cerevisiae Proteins - metabolism | Glucose - metabolism | Protein Binding | Liposomes - metabolism | Phosphatidic Acids - metabolism | Mutation | Saccharomyces cerevisiae - growth & development | Hydrogen-Ion Concentration | Proteins | Biosynthesis | Research | Metabolism | Signal transduction | Membranes | Biochemistry | Cellular biology | Index Medicus
Journal Article
Journal of Biotechnology, ISSN 0168-1656, 04/2012, Volume 158, Issue 4, pp. 203 - 210
The cost of the lignocellulose-hydrolyzing enzymes used in the saccharification process of ethanol production from biomass accounts for a relatively high... 
Bioethanol | Biomass | Lignocellulose | Cell surface display | XYLANASE | ACID | FUEL ETHANOL | CELLULOSIC BIOMASS | COFERMENTATION | LIQUID HOT-WATER | PRETREATMENT | BIOTECHNOLOGY & APPLIED MICROBIOLOGY | LIGNOCELLULOSIC HYDROLYSATE | FERMENTATION | EXPRESSION | Aldehyde Reductase - genetics | Xylans - metabolism | D-Xylulose Reductase - genetics | Oryza - metabolism | Saccharomyces cerevisiae - genetics | Endo-1,4-beta Xylanases - genetics | Polysaccharides - genetics | Glucuronates - metabolism | D-Xylulose Reductase - metabolism | Pichia - enzymology | Xylose - genetics | Saccharomyces cerevisiae - metabolism | Pichia - metabolism | Lignin - metabolism | beta-Glucosidase - genetics | Glucuronates - genetics | Escherichia coli - metabolism | beta-Glucosidase - metabolism | Aldehyde Reductase - metabolism | Endo-1,4-beta Xylanases - metabolism | Metabolic Engineering - methods | Xylose - metabolism | Ethanol - metabolism | Phosphotransferases (Alcohol Group Acceptor) - genetics | Trichoderma - genetics | Oligosaccharides - metabolism | Saccharomyces cerevisiae Proteins - genetics | Fermentation | Phosphotransferases (Alcohol Group Acceptor) - metabolism | Polysaccharides - metabolism | Hydrolysis | Xylans - genetics | Aspergillus oryzae - genetics | Escherichia coli - genetics | Saccharomyces cerevisiae Proteins - metabolism | Saccharomyces cerevisiae - enzymology | Lignin - genetics | Aspergillus oryzae - metabolism | Oligosaccharides - genetics | Trichoderma - metabolism | Xylitol | Enzymes | Alcohol, Denatured | Alcohol | Production processes | Sugars | Production data | Rice | Alcohols | Monosaccharides | Index Medicus
Journal Article
Science, ISSN 0036-8075, 7/2012, Volume 337, Issue 6090, pp. 93 - 96
The transport of pyruvate, the end product of glycolysis, into mitochondria is an essential process that provides the organelle with a major oxidative fuel.... 
Essential amino acids | Yeasts | Lactates | Cell growth | Mitochondria | Dehydrogenases | REPORTS | Mitochondrial membranes | Amino acids | Keto acids | Implementation maturity model | CATABOLISM | TRANSPORT | SPECIFICITY | LIPOIC ACID | MEMBRANE | MULTIDISCIPLINARY SCIENCES | SACCHAROMYCES-CEREVISIAE | LACTOCOCCUS-LACTIS | DEHYDROGENASE | Proprotein Convertase 2 | Proprotein Convertase 1 - genetics | Saccharomyces cerevisiae - genetics | Thioctic Acid - biosynthesis | Molecular Sequence Data | Lactococcus lactis - metabolism | Anion Transport Proteins - chemistry | Mitochondrial Membrane Transport Proteins - genetics | Thioctic Acid - metabolism | Saccharomyces cerevisiae - metabolism | Biological Transport | Culture Media | Pyruvic Acid - metabolism | Proprotein Convertase 1 - chemistry | Lactococcus lactis - genetics | Recombinant Proteins - metabolism | Amino Acid Sequence | Leucine - metabolism | Mitochondrial Membrane Transport Proteins - chemistry | Mitochondrial Membrane Transport Proteins - metabolism | Proprotein Convertase 1 - metabolism | Biosynthetic Pathways | Mitochondria - metabolism | Saccharomyces cerevisiae Proteins - genetics | Anion Transport Proteins - metabolism | Mitochondrial Membranes - metabolism | Animals | Valine - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Mice | Anion Transport Proteins - genetics | Saccharomyces cerevisiae - growth & development | Saccharomyces cerevisiae Proteins - chemistry | Plant mitochondria | Genetic aspects | Research | Plant molecular biology | Proteins | Glycoproteins | Yeast | Mutagenesis | Index Medicus
Journal Article
Science, ISSN 0036-8075, 7/2012, Volume 337, Issue 6090, pp. 96 - 100
Pyruvate constitutes a critical branch point in cellular carbon metabolism. We have identified two proteins, Mpc1 and Mpc2, as essential for mitochondrial... 
Yeasts | Mitochondria | Diet | Plasmids | Drosophila | REPORTS | Amino acids | Oxidation | Respiration | Sugars | Medical schools | RAT-LIVER | TRANSPORT | COMPLEX | MECHANISM | IDENTIFICATION | MULTIDISCIPLINARY SCIENCES | Metabolomics | Humans | Molecular Sequence Data | Mitochondrial Proteins - genetics | Drosophila Proteins - metabolism | Drosophila melanogaster - genetics | Anion Transport Proteins - chemistry | Mitochondrial Membrane Transport Proteins - genetics | Drosophila melanogaster - metabolism | Saccharomyces cerevisiae - metabolism | Amino Acids - metabolism | Biological Transport | Mitochondrial Proteins - metabolism | Pyruvic Acid - metabolism | Amino Acid Sequence | Mitochondrial Membrane Transport Proteins - chemistry | Mitochondrial Membrane Transport Proteins - metabolism | Oxidation-Reduction | Carbohydrate Metabolism | Mitochondria - metabolism | Drosophila Proteins - chemistry | Saccharomyces cerevisiae Proteins - genetics | Anion Transport Proteins - metabolism | Citric Acid Cycle | Mitochondrial Membranes - metabolism | Point Mutation | Animals | Drosophila melanogaster - chemistry | Mitochondrial Proteins - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Drosophila Proteins - genetics | Anion Transport Proteins - genetics | Saccharomyces cerevisiae Proteins - chemistry | Cell metabolism | Pyruvates | Chemical properties | Research | Molecular biology | Proteins | Yeast | Metabolism | Index Medicus | Carriers | Human | Bacteria | Transport | Transporter
Journal Article
Science, ISSN 0036-8075, 5/2003, Volume 300, Issue 5620, pp. 805 - 808
Journal Article
Nature, ISSN 0028-0836, 2014, Volume 505, Issue 7484, pp. 564 - 568
Journal Article
Cell, ISSN 0092-8674, 04/2011, Volume 145, Issue 1, pp. 54 - 66
Journal Article
Nature, ISSN 0028-0836, 02/2017, Volume 542, Issue 7641, pp. 377 - 380
The spliceosome excises introns from pre-mRNAs in two sequential transesterifications-branching and exon ligation(1)-catalysed at a single catalytic metal site... 
2ND STEP | ANGSTROM RESOLUTION | ELECTRON CRYOMICROSCOPY | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | FUNCTIONAL INTERACTIONS | CATALYTIC CENTER | CRYO-EM STRUCTURE | SPLICING FACTOR | SITE CHOICE | PRE-MESSENGER-RNA | RNA Helicases - metabolism | Spliceosomes - chemistry | Saccharomyces cerevisiae - genetics | Cell Cycle Proteins - ultrastructure | Ribonucleoprotein, U5 Small Nuclear - metabolism | RNA Splicing Factors - chemistry | Saccharomyces cerevisiae - ultrastructure | Ribonucleoprotein, U4-U6 Small Nuclear - metabolism | Ribonucleoprotein, U4-U6 Small Nuclear - ultrastructure | RNA Helicases - ultrastructure | RNA Splicing Factors - metabolism | DNA-Binding Proteins - metabolism | Saccharomyces cerevisiae - metabolism | Spliceosomes - metabolism | RNA Splicing | Ribonucleoproteins, Small Nuclear - ultrastructure | RNA, Small Nuclear - genetics | Protein Domains | Ribonucleoprotein, U5 Small Nuclear - ultrastructure | Adenosine Triphosphatases - ultrastructure | DEAD-box RNA Helicases - metabolism | DEAD-box RNA Helicases - chemistry | Saccharomyces cerevisiae Proteins - ultrastructure | Catalytic Domain | Biocatalysis | RNA Splice Sites - genetics | Cell Cycle Proteins - metabolism | Adenosine Triphosphatases - metabolism | Exons - genetics | Spliceosomes - ultrastructure | Saccharomyces cerevisiae - chemistry | Cryoelectron Microscopy | DNA-Binding Proteins - ultrastructure | RNA-Binding Proteins - ultrastructure | RNA Splicing Factors - ultrastructure | Ribonuclease H - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Adenosine - metabolism | Protein Binding | DEAD-box RNA Helicases - ultrastructure | RNA-Binding Proteins - metabolism | Ribonucleoproteins, Small Nuclear - metabolism | Saccharomyces cerevisiae Proteins - chemistry | RNA sequencing | Methods | Mutation | Catalysis | Ribonucleic acid--RNA | Binding sites | Crystal structure | Index Medicus
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Journal Article