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PLoS Biology, ISSN 1544-9173, 2015, Volume 13, Issue 2, pp. e1002049 - e1002049
Journal Article
PLoS ONE, ISSN 1932-6203, 2011, Volume 6, Issue 10, pp. e26319 - e26319
Bacteria, fungi, protozoa, chromista and plants all harbor homologues of Hsp104, a AAA+ ATPase that collaborates with Hsp70 and Hsp40 to promote protein... 
YEAST | IN-VITRO | CAENORHABDITIS-ELEGANS | MOLECULAR CHAPERONES | MULTIDISCIPLINARY SCIENCES | AGGREGATED PROTEINS | ALPHA-SYNUCLEIN | SACCHAROMYCES-CEREVISIAE | HUNTINGTONS-DISEASE | HEAT-SHOCK-PROTEIN | NUCLEOTIDE EXCHANGE FACTORS | Mammals - metabolism | HSP40 Heat-Shock Proteins - metabolism | Biocatalysis | Humans | Adenosine Triphosphatases - metabolism | Rats | Substrate Specificity | HSP70 Heat-Shock Proteins - metabolism | HSP110 Heat-Shock Proteins - chemistry | Hydrolysis | Saccharomyces cerevisiae - metabolism | Cytosol - enzymology | Animals | Amyloid - metabolism | Cell-Free System | Adenosine Triphosphate - metabolism | Protein Structure, Quaternary | Saccharomyces cerevisiae Proteins - metabolism | Conserved Sequence | Protein Binding | HSP70 Heat-Shock Proteins - chemistry | HeLa Cells | HSP110 Heat-Shock Proteins - metabolism | HSP40 Heat-Shock Proteins - chemistry | Heat shock proteins | Prions | Cells | Adenosine triphosphatase | Yeast | Parkinson's disease | Cell-free system | Homology | Activation | Biochemistry | Kinases | Synuclein | Cytosol | Machinery | Fungi | Protein folding | Bacteria | Amyloid | Trends | Prion protein | Movement disorders | Adenosine triphosphate | Protozoa | Neurodegenerative diseases | Disaggregation | Hsp70 protein | Hsp40 protein | Mammals | Substrates | Aggregates | Hsc70 protein | Mutation | Alzheimers disease | Endoplasmic reticulum | ATP | Index Medicus
Journal Article
Journal Article
Molecular Cell, ISSN 1097-2765, 2011, Volume 41, Issue 6, pp. 672 - 681
Heat shock protein 90 (Hsp90) is an essential molecular chaperone whose activity is regulated not only by cochaperones but also by distinct posttranslational... 
YEAST | CLIENT PROTEINS | ATP HYDROLYSIS | MOLECULAR CHAPERONES | BIOCHEMISTRY & MOLECULAR BIOLOGY | IN-VIVO | CASEIN KINASE-II | STEROID-RECEPTOR | CONFORMATIONAL STATES | HEAT-SHOCK-PROTEIN | CYCLE | CELL BIOLOGY | Fungal Proteins - chemistry | Phosphorylation | Molecular Chaperones - metabolism | Saccharomyces cerevisiae - genetics | Humans | Casein Kinase II - genetics | Molecular Chaperones - chemistry | Threonine - metabolism | Recombinant Fusion Proteins - metabolism | Cell Cycle Proteins - chemistry | Saccharomyces cerevisiae - metabolism | Cell Cycle Proteins - genetics | HSP90 Heat-Shock Proteins - chemistry | HSP90 Heat-Shock Proteins - genetics | Protein Structure, Tertiary | Protein Structure, Secondary | Cell Cycle Proteins - metabolism | Molecular Chaperones - genetics | Chaperonins - chemistry | Fungal Proteins - genetics | Recombinant Fusion Proteins - chemistry | Saccharomyces cerevisiae Proteins - genetics | Chaperonins - metabolism | Saccharomyces cerevisiae Proteins - metabolism | HSP90 Heat-Shock Proteins - metabolism | Recombinant Fusion Proteins - genetics | Chaperonins - genetics | Casein Kinase II - metabolism | Fungal Proteins - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Casein | Oncology, Experimental | Heat shock proteins | Amino acids | Research | Adenosine triphosphatase | Cancer | Index Medicus
Journal Article
Science, ISSN 0036-8075, 9/2011, Volume 333, Issue 6051, pp. 1891 - 1894
The unfolded protein response (UPR) detects the accumulation of unfolded proteins in the endoplasmic reticulum (ER) and adjusts the protein-folding capacity to... 
Yeasts | Messenger RNA | Ungulates | REPORTS | Amino acids | Ligands | Dimers | Coefficients | Goods and services tax | Monomers | Unfolded protein response | IRE1P | MESSENGER-RNA | SPECIFICITY | MECHANISM | PATHWAY | MULTIDISCIPLINARY SCIENCES | BIP | ENDOPLASMIC-RETICULUM | TRANSCRIPTION FACTOR | BINDING | REVEALS | Fungal Proteins - chemistry | Membrane Glycoproteins - metabolism | Membrane Glycoproteins - chemistry | Protein Multimerization | Stress, Physiological | Endoplasmic Reticulum - metabolism | Cathepsin A - chemistry | Cathepsin A - metabolism | HSP70 Heat-Shock Proteins - chemistry | Protein Interaction Domains and Motifs | Binding Sites | Protein-Serine-Threonine Kinases - metabolism | Glutathione Transferase - metabolism | Mutant Proteins - metabolism | Saccharomyces cerevisiae Proteins - genetics | Unfolded Protein Response | Protein Folding | HSP70 Heat-Shock Proteins - metabolism | Mutant Proteins - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Hydrophobic and Hydrophilic Interactions | Protein Binding | Protein Conformation | Protein-Serine-Threonine Kinases - chemistry | Fluorescence Polarization | Fungal Proteins - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Research | Properties | Endoplasmic reticulum | Ligands (Biochemistry) | Protein binding | Signal transduction | Membranes | Cellular biology | Kinases | Protein folding | Index Medicus
Journal Article
Nature Communications, ISSN 2041-1723, 12/2017, Volume 8, Issue 1, pp. 1287 - 15
Iron-sulfur (Fe/S) clusters are essential protein cofactors crucial for many cellular functions including DNA maintenance, protein translation, and energy... 
IRON-SULFUR CLUSTER | ACYL CARRIER PROTEIN | CYSTEINE DESULFURASE | FRATAXIN | ARABIDOPSIS-THALIANA | BIOGENESIS | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | X-RAY | SCAFFOLD PROTEIN | Fungal Proteins - chemistry | Humans | Protein Multimerization | Iron-Sulfur Proteins - genetics | Crystallography, X-Ray | Iron-Binding Proteins - chemistry | Mitochondrial Proteins - genetics | Iron-Sulfur Proteins - chemistry | Iron-Binding Proteins - metabolism | Multiprotein Complexes - metabolism | Carbon-Sulfur Lyases - genetics | Mitochondrial Proteins - metabolism | X-Ray Diffraction | Iron-Regulatory Proteins - chemistry | Protein Stability | Amino Acid Sequence | Chaetomium - chemistry | Mutagenesis, Site-Directed | Acyl Carrier Protein - metabolism | Models, Molecular | Scattering, Small Angle | Iron-Regulatory Proteins - metabolism | Mitochondria - metabolism | Fungal Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | Static Electricity | Carbon-Sulfur Lyases - metabolism | Chaetomium - genetics | Iron-Regulatory Proteins - genetics | Molecular Dynamics Simulation | Sequence Homology, Amino Acid | Acyl Carrier Protein - chemistry | Multiprotein Complexes - chemistry | Acyl Carrier Protein - genetics | Mitochondrial Proteins - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Iron-Binding Proteins - genetics | Protein Conformation | Iron-Sulfur Proteins - metabolism | Carbon-Sulfur Lyases - chemistry | Amino Acid Substitution | Fungal Proteins - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Iron | Small angle X ray scattering | Crystallography | Cofactors | Proteins | Energy balance | Mitochondria | X-ray scattering | Frataxin | Energy conversion | Acyl carrier protein | Clusters | X ray scattering | Catalysis | Ferredoxin | Sulfur | Chemical synthesis | Deoxyribonucleic acid--DNA | Crystal structure | Lipids | Index Medicus
Journal Article
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 | Index Medicus | 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
Nature, ISSN 0028-0836, 05/2016, Volume 534, Issue 7605, pp. 133 - 137
Ribosome biogenesis is a highly complex process in eukaryotes, involving temporally and spatially regulated ribosomal protein (r-protein) binding and ribosomal... 
60S MATURATION | RNA | BIOGENESIS | PARTICLE | NASCENT RIBOSOMES | MULTIDISCIPLINARY SCIENCES | CRYO-EM | ELECTRON-MICROSCOPY | SACCHAROMYCES-CEREVISIAE | ASSOCIATION | SUBUNIT | RNA, Fungal - ultrastructure | GTP Phosphohydrolases - ultrastructure | Saccharomyces cerevisiae - ultrastructure | DNA, Ribosomal Spacer - metabolism | RNA, Ribosomal - genetics | GTP Phosphohydrolases - chemistry | Saccharomyces cerevisiae - metabolism | Cell Nucleus - metabolism | Ribosome Subunits, Large, Eukaryotic - metabolism | DNA, Ribosomal Spacer - genetics | Base Sequence | DNA, Ribosomal Spacer - ultrastructure | Ribosome Subunits, Large, Eukaryotic - chemistry | Models, Molecular | Ribonucleoproteins - metabolism | Nuclear Proteins - chemistry | Saccharomyces cerevisiae - chemistry | RNA, Ribosomal - ultrastructure | Saccharomyces cerevisiae - cytology | Ribosomal Proteins - isolation & purification | GTP Phosphohydrolases - metabolism | Saccharomyces cerevisiae Proteins - metabolism | GTP-Binding Proteins - metabolism | Saccharomyces cerevisiae Proteins - chemistry | Ribosomal Proteins - chemistry | Ribosome Subunits, Large, Eukaryotic - ultrastructure | Nuclear Proteins - ultrastructure | Molecular Sequence Data | Cytoplasm - metabolism | Ribosomal Proteins - metabolism | Ribosomal Proteins - ultrastructure | Saccharomyces cerevisiae Proteins - isolation & purification | RNA, Fungal - genetics | Active Transport, Cell Nucleus | Ribonucleoproteins - chemistry | Saccharomyces cerevisiae Proteins - ultrastructure | Catalytic Domain | GTP-Binding Proteins - chemistry | RNA, Ribosomal - metabolism | Nuclear Proteins - metabolism | GTP-Binding Proteins - ultrastructure | DNA, Ribosomal Spacer - chemistry | Cell Nucleus - ultrastructure | Rotation | RNA, Fungal - metabolism | Cryoelectron Microscopy | Protein Binding | Cell Nucleus - chemistry | Ribonucleoproteins - ultrastructure | Nucleolus organizer region | Protein research | Research | Ribosomes | Protein binding | Genetic research | Proteins | Polypeptides | Molecular structure | Ribonucleic acid--RNA | Index Medicus
Journal Article
The Journal of Cell Biology, ISSN 0021-9525, 5/2008, Volume 181, Issue 3, pp. 497 - 510
Autophagy is a membrane-mediated intracellular degradation system. The serine/threonine kinase Atg1 plays an essential role in autophagosome formation.... 
Yeasts | Starvation | NIH 3T3 cells | Microscopy | Neurons | Cell lines | Antibodies | Cultured cells | Focal adhesions | Gene expression regulation | COMPLEX | MOLECULAR MACHINERY | FOCAL ADHESION | GENE | C-ELEGANS | AXONAL ELONGATION | HUMAN BREAST-CANCER | SACCHAROMYCES-CEREVISIAE | SERINE/THREONINE KINASE | SELF-DIGESTION | CELL BIOLOGY | Protein Kinases - metabolism | Protein Kinases - genetics | Microtubule-Associated Proteins - genetics | Fibroblasts - physiology | Microtubule-Associated Proteins - metabolism | Protein-Tyrosine Kinases - metabolism | Humans | Autophagy - physiology | Recombinant Fusion Proteins - metabolism | Autophagy-Related Protein-1 Homolog | Intracellular Membranes - ultrastructure | Protein-Tyrosine Kinases - genetics | Protein-Serine-Threonine Kinases - metabolism | Focal Adhesion Protein-Tyrosine Kinases - metabolism | Phagosomes - metabolism | Protein-Serine-Threonine Kinases - genetics | Fungal Proteins - genetics | Mice, Knockout | Focal Adhesion Protein-Tyrosine Kinases - genetics | Animals | Autophagy-Related Protein 5 | Recombinant Fusion Proteins - genetics | Fibroblasts - cytology | Mice | TOR Serine-Threonine Kinases | Intracellular Membranes - metabolism | Fungal Proteins - metabolism | Allelomorphism | Muridae | Physiological aspects | Cell physiology | Research | Properties | Binding proteins | Identification and classification | Phosphotransferases | Proteins | Biochemistry | Mammals | Kinases | Rodents | Cells | Index Medicus
Journal Article