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Journal Article
Current Opinion in Chemical Biology, ISSN 1367-5931, 06/2019, Volume 50, pp. 55 - 65
Journal Article
Journal of Medicinal Chemistry, ISSN 0022-2623, 07/2018, Volume 61, Issue 14, pp. 6163 - 6177
Cancer cells rely on the chaperone heat shock protein 70 (Hsp70) for survival and proliferation. Recently, benzothiazole rhodacyanines have been shown to bind... 
INTERDOMAIN LINKER | CHEMISTRY, MEDICINAL | TARGETING HSP70 | SMALL-MOLECULE | GENETIC SCREENS | ADENOSINE-DERIVED INHIBITORS | CHAPERONE | MAMMALIAN-CELLS | DRUG TARGETS | CANCER-THERAPY | HEAT-SHOCK-PROTEIN | breast cancer | non-oncogene addiction | chaperone | structure-activity relationships | proteostasis | allostery
Journal Article
Trends in Biochemical Sciences, ISSN 0968-0004, 02/2015, Volume 40, Issue 2, pp. 117 - 125
The conserved Hsp90 chaperone is an ATP-controlled machine that assists the folding and controls the stability of select proteins. Emerging data explain how... 
protein–protein interactions | protein folding | molecular chaperones | Alzheimer disease | heat shock proteins | intrinsically disordered proteins | HSP72 Heat-Shock Proteins | Molecular Chaperones | HSP90 Heat-Shock Proteins | Humans | Intrinsically Disordered Proteins | Protein Binding | Substrate Specificity | Ligands | Alzheimer Disease | Protein Folding | Protein Interaction Maps | Heat shock proteins | Molecular chaperones | Intrinsically disordered proteins | Protein folding | Protein-protein interactions | X-RAY SOLUTION | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | STRUCTURAL-ANALYSIS | ESCHERICHIA-COLI HSP90 | POSTTRANSLATIONAL MODIFICATIONS | protein-protein interactions | HEAT-SHOCK-PROTEIN | GLUCOCORTICOID-RECEPTOR | SUBSTRATE-BINDING | N-TERMINAL DOMAIN | MOLECULAR CHAPERONE | Protein Binding - genetics | Molecular Chaperones - metabolism | Molecular Chaperones - genetics | HSP72 Heat-Shock Proteins - metabolism | Molecular Chaperones - chemistry | HSP72 Heat-Shock Proteins - chemistry | Alzheimer Disease - pathology | HSP72 Heat-Shock Proteins - genetics | Protein Interaction Maps - genetics | Intrinsically Disordered Proteins - chemistry | Alzheimer Disease - metabolism | HSP90 Heat-Shock Proteins - chemistry | HSP90 Heat-Shock Proteins - metabolism | HSP90 Heat-Shock Proteins - genetics | Alzheimer Disease - genetics | Intrinsically Disordered Proteins - metabolism | Proteins | Protein binding
Journal Article
PLoS ONE, ISSN 1932-6203, 2011, Volume 6, Issue 10, p. 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 | Baking yeast | Machinery and equipment
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
Journal Article
Nature Cell Biology, ISSN 1465-7392, 03/2010, Volume 12, Issue 3, pp. 213 - 223
Impaired selective turnover of p62 by autophagy causes severe liver injury accompanied by the formation of p62-positive inclusions and upregulation of... 
OXIDATIVE STRESS | PROTEIN | MECHANISM | CUL3-BASED E3 LIGASE | STRUCTURAL BASIS | DLG MOTIFS | DEGRADATION | MICE | BETA-CELL MASS | INDUCTION | CELL BIOLOGY | Adaptor Proteins, Signal Transducing - chemistry | Liver - pathology | Microtubule-Associated Proteins - genetics | Cytoskeletal Proteins - genetics | Gene Expression - genetics | Protein Interaction Domains and Motifs - physiology | Sequestosome-1 Protein | Humans | Oxidative Stress - physiology | Crystallography, X-Ray | Hepatocytes - pathology | Autophagy - physiology | Intracellular Signaling Peptides and Proteins - metabolism | Hepatocytes - metabolism | Liver - physiopathology | Heat-Shock Proteins - genetics | Mutation - physiology | Transfection | Organ Size - genetics | Cytoskeletal Proteins - metabolism | NF-E2-Related Factor 2 - genetics | Inclusion Bodies - metabolism | Kelch-Like ECH-Associated Protein 1 | Cell Line | Binding, Competitive - physiology | Heat-Shock Proteins - metabolism | Liver - metabolism | Models, Molecular | Mice, Transgenic | Cytoskeletal Proteins - chemistry | Mice, Knockout | Protein Interaction Mapping | Autophagy-Related Protein 7 | Animals | Models, Biological | NF-E2-Related Factor 2 - metabolism | Adaptor Proteins, Signal Transducing - genetics | Calorimetry | Signal Transduction - physiology | Mice | Adaptor Proteins, Signal Transducing - metabolism | Heat-Shock Proteins - chemistry | Protein Binding - physiology | Autophagy (Cytology) | Care and treatment | Transcription factors | Liver diseases | Physiological aspects | Genetic aspects | Research
Journal Article