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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 | Index Medicus
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 9/2009, Volume 106, Issue 37, pp. 15604 - 15609
Small heat shock proteins (sHSPs) serve as a first line of defense against stress-induced cell damage by binding and maintaining denaturing proteins in a... 
Proteins | Oligomers | Aggregation | Molecular chaperones | Substrate specificity | Teeth | Dimers | Biochemistry | Small heat shock proteins | Binding sites | Intrinsic disorder | Alpha-crystallin | Cross-linking | P-benzoylphenylalanine | Protein-protein interactions | DOMAIN | HUMAN-DISEASE | MECHANISM | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | ALPHA-B-CRYSTALLIN | MODEL | T4 LYSOZYME | MASS-SPECTROMETRY | protein-protein interactions | cross-linking | 1,1'-BI(4-ANILINO)NAPHTHALENE-5,5'-DISULFONIC ACID | alpha-crystallin | MISSENSE MUTATION | intrinsic disorder | Molecular Chaperones - metabolism | Phenylalanine - analogs & derivatives | Humans | Molecular Sequence Data | Molecular Chaperones - chemistry | Genetic Variation | Heat-Shock Proteins - genetics | Plant Proteins - chemistry | Plant Proteins - metabolism | Protein Interaction Domains and Motifs | Binding Sites | Peas - metabolism | Recombinant Proteins - metabolism | Amino Acid Sequence | Cross-Linking Reagents | Mutagenesis, Site-Directed | Heat-Shock Proteins, Small - chemistry | Heat-Shock Proteins - metabolism | Heat-Shock Proteins, Small - metabolism | Molecular Chaperones - genetics | Models, Molecular | Recombinant Proteins - chemistry | Recombinant Proteins - genetics | Heat-Shock Proteins, Small - genetics | Plant Proteins - genetics | Animals | Benzophenones | Protein Binding | Peas - genetics | Heat-Shock Proteins - chemistry | Heat shock proteins | Observations | Protein binding | Molecules | Substrates | Adenosine triphosphatase | Index Medicus | protein–protein interactions | Biological Sciences
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
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
Molecular Cell, ISSN 1097-2765, 09/2016, Volume 63, Issue 6, pp. 951 - 964
Huntington’s disease is one of several neurodegenerative disorders characterized by the aggregation of polyglutamine (polyQ)-expanded mutant protein. How polyQ... 
POLYGLUTAMINE | PROTEIN | FUS | BIOCHEMISTRY & MOLECULAR BIOLOGY | MUTANT HUNTINGTIN | PHASE-TRANSITION | DISEASE | MUTATIONS | INCLUSION-BODY FORMATION | AGGREGATION | PROTEOSTASIS | CELL BIOLOGY | Protein Aggregates | Neurons - pathology | Humans | Protein Multimerization | Peptides - genetics | Green Fluorescent Proteins - genetics | Recombinant Fusion Proteins - metabolism | Ribosomal Proteins - metabolism | Peptides - metabolism | Neurons - metabolism | Gene Ontology | Green Fluorescent Proteins - metabolism | Gene Expression | HSP40 Heat-Shock Proteins - metabolism | HSP40 Heat-Shock Proteins - genetics | Peptides - chemistry | Ribosomal Proteins - genetics | Huntingtin Protein - metabolism | Molecular Sequence Annotation | Bacterial Proteins - genetics | Solubility | Spectrometry, Fluorescence | Single Molecule Imaging - methods | Protein Interaction Mapping | Animals | Cell Line, Tumor | Recombinant Fusion Proteins - genetics | Bacterial Proteins - metabolism | Luminescent Proteins - genetics | Mice | HeLa Cells | Huntingtin Protein - genetics | Mutation | Luminescent Proteins - metabolism | Ubiquitin | Fluorescence spectroscopy | Nervous system diseases | RNA | Heat shock proteins | Fluorescence | Biosynthesis | Genetic transcription | Oligomers | Analysis | Cellular signal transduction | Research institutes | Binding proteins | Protein binding | Index Medicus
Journal Article
Clinical Cancer Research, ISSN 1078-0432, 05/2012, Volume 18, Issue 9, pp. 2502 - 2514
Purpose: The clinical use of BRAF inhibitors is being hampered by the acquisition of drug resistance. This study shows the potential therapeutic use of the... 
BREAST-CANCER | MULTIPLE-MYELOMA | APOPTOSIS | PHASE-II TRIAL | TANESPIMYCIN 17-AAG | TRASTUZUMAB | ONCOLOGY | BIM | ACQUIRED-RESISTANCE | MELANOMA-CELLS | POTENTIAL MECHANISM | Prospective Studies | Apoptosis - drug effects | Humans | Extracellular Signal-Regulated MAP Kinases - antagonists & inhibitors | Phosphatidylinositol 3-Kinases - antagonists & inhibitors | Immunoenzyme Techniques | Forkhead Transcription Factors - metabolism | Colony-Forming Units Assay | Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization | Phthalic Acids - pharmacology | Proto-Oncogene Proteins c-akt - metabolism | Real-Time Polymerase Chain Reaction | Proto-Oncogene Proteins B-raf - metabolism | Membrane Proteins - genetics | Melanoma - pathology | Reverse Transcriptase Polymerase Chain Reaction | Blotting, Western | Apoptosis Regulatory Proteins - metabolism | Proto-Oncogene Proteins B-raf - antagonists & inhibitors | Indoles - adverse effects | Membrane Proteins - antagonists & inhibitors | Signal Transduction - drug effects | HSP90 Heat-Shock Proteins - antagonists & inhibitors | Cell Line, Tumor | HSP90 Heat-Shock Proteins - metabolism | Mice | Mice, Inbred BALB C | Forkhead Box Protein O3 | Azabicyclo Compounds - pharmacology | Phosphatidylinositol 3-Kinases - metabolism | Extracellular Signal-Regulated MAP Kinases - metabolism | Extracellular Signal-Regulated MAP Kinases - genetics | Proto-Oncogene Proteins c-akt - genetics | Proto-Oncogene Proteins c-bcl-2 - metabolism | Flow Cytometry | Bcl-2-Like Protein 11 | Apoptosis Regulatory Proteins - genetics | Membrane Proteins - metabolism | Forkhead Transcription Factors - antagonists & inhibitors | Melanoma - metabolism | Proto-Oncogene Proteins - metabolism | Proto-Oncogene Proteins - antagonists & inhibitors | RNA, Messenger - genetics | Proto-Oncogene Proteins - genetics | Forkhead Transcription Factors - genetics | Phosphatidylinositol 3-Kinases - genetics | Animals | Proto-Oncogene Proteins B-raf - genetics | Melanoma - drug therapy | Myeloid Cell Leukemia Sequence 1 Protein | Apoptosis Regulatory Proteins - antagonists & inhibitors | Fluorescent Antibody Technique | Sulfonamides - adverse effects | Proto-Oncogene Proteins c-bcl-2 - antagonists & inhibitors | Cell Proliferation - drug effects | Protein Kinase Inhibitors - pharmacology | Proto-Oncogene Proteins c-bcl-2 - genetics | Proto-Oncogene Proteins c-akt - antagonists & inhibitors | Drug Resistance, Neoplasm - drug effects | Index Medicus
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
Journal of Biological Chemistry, ISSN 0021-9258, 01/2014, Volume 289, Issue 3, pp. 1402 - 1414
Background: There has been an expansion of the number of Hsp70 cochaperones in mammals, providing the opportunity for combinatorial assembly of permutations... 
Protein Complexes | Protein Misfolding | Cochaperones | HIGH-THROUGHPUT SCREEN | MOLECULAR CHAPERONES | BIOCHEMISTRY & MOLECULAR BIOLOGY | QUALITY-CONTROL | Hsp40 | Protein Folding | HSP110 CHAPERONES | HEAT-SHOCK-PROTEIN | NEGATIVE REGULATOR | Isothermal Titration Calorimetry | J-DOMAIN | ATP HYDROLYSIS | STRUCTURAL BASIS | Molecular Chaperone | HSC70 CHAPERONE | ATPases | Protein-Protein Interactions | Adaptor Proteins, Signal Transducing - chemistry | Molecular Chaperones - metabolism | Transcription Factors - chemistry | Humans | Multiprotein Complexes - genetics | Molecular Chaperones - chemistry | DNA-Binding Proteins - metabolism | HSP110 Heat-Shock Proteins - chemistry | Multiprotein Complexes - metabolism | HSP70 Heat-Shock Proteins - chemistry | HSP40 Heat-Shock Proteins - chemistry | Recombinant Proteins - metabolism | HSP40 Heat-Shock Proteins - metabolism | HSP40 Heat-Shock Proteins - genetics | Molecular Chaperones - genetics | Recombinant Proteins - chemistry | HSP70 Heat-Shock Proteins - genetics | Recombinant Proteins - genetics | Transcription Factors - genetics | DNA-Binding Proteins - genetics | DNA-Binding Proteins - chemistry | HSP70 Heat-Shock Proteins - metabolism | Transcription Factors - metabolism | HSP110 Heat-Shock Proteins - genetics | Multiprotein Complexes - chemistry | Apoptosis Regulatory Proteins | Adaptor Proteins, Signal Transducing - genetics | Adaptor Proteins, Signal Transducing - metabolism | HSP110 Heat-Shock Proteins - metabolism | Protein Binding - physiology | Index Medicus | Protein Synthesis and Degradation
Journal Article
Molecular Cell, ISSN 1097-2765, 04/2010, Volume 38, Issue 1, pp. 89 - 100
Heat shock proteins 70 (Hsp70) represent a ubiquitous and conserved family of molecular chaperones involved in a plethora of cellular processes. The dynamics... 
PROTEINS | ALLOSTERIC REGULATION | INTERDOMAIN COMMUNICATION | PRECURSOR PROTEINS | SUBSTRATE-BINDING | STRUCTURAL BASIS | MOLECULAR CHAPERONES | BIOCHEMISTRY & MOLECULAR BIOLOGY | PROBABILITY-DISTRIBUTION ANALYSIS | RESONANCE ENERGY-TRANSFER | PROTEIN IMPORT MOTOR | SACCHAROMYCES-CEREVISIAE | CELL BIOLOGY | Calcium-Transporting ATPases - chemistry | Molecular Chaperones - metabolism | Humans | Bacterial Proteins - chemistry | Adenosine Diphosphate - chemistry | Molecular Chaperones - chemistry | Adenosine Triphosphate - metabolism | Fluorescence Resonance Energy Transfer | Calcium-Transporting ATPases - metabolism | HSP70 Heat-Shock Proteins - chemistry | Membrane Proteins - metabolism | HSP40 Heat-Shock Proteins - chemistry | HSP40 Heat-Shock Proteins - metabolism | Bacterial Proteins - genetics | Models, Molecular | Escherichia coli Proteins - metabolism | HSP70 Heat-Shock Proteins - genetics | Mitochondria - metabolism | Protein Folding | HSP70 Heat-Shock Proteins - metabolism | Membrane Proteins - chemistry | Saccharomyces cerevisiae Proteins - metabolism | Escherichia coli Proteins - genetics | Bacterial Proteins - metabolism | Protein Conformation | Adenosine Diphosphate - metabolism | Adenosine Triphosphate - chemistry | Escherichia coli Proteins - chemistry | Saccharomyces cerevisiae Proteins - chemistry | Proteins | Hydrolysis | Analysis | Physiological aspects | Fluorescence | Heat shock proteins | Nucleotides | Index Medicus
Journal Article