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Trends in Biochemical Sciences, ISSN 0968-0004, 02/2015, Volume 40, Issue 2, pp. 117 - 125
Journal Article
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 | Index Medicus | protein–protein interactions | Biological Sciences
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
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
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 | Protein Synthesis and Degradation
Journal Article
Genes and Development, ISSN 0890-9369, 09/2007, Volume 21, Issue 17, pp. 2172 - 2181
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 2017, Volume 292, Issue 31, pp. 12744 - 12753
Fe-S cofactors are composed of iron and inorganic sulfur in various stoichiometries. A complex assembly pathway conducts their initial synthesis and subsequent... 
HSPA9 | iron-response element (IRE) | mitochondrial respiratory chain complex | RESPIRATORY-CHAIN | ELEMENT-BINDING-PROTEIN | BIOCHEMISTRY & MOLECULAR BIOLOGY | FE-S CLUSTERS | ESCHERICHIA-COLI | HSC20 | metalloenzyme | HEAVY-SUBUNIT | RESPONSIVE ELEMENT | CYSTEINE DESULFURASE | MESSENGER-RNA | iron-sulfur protein | iron-sulfur cluster biogenesis | SCAFFOLD PROTEIN | TARGETED DELETION | energy metabolism | ISCU | Iron Regulatory Protein 1 - physiology | Electron Transport | Humans | Protein Multimerization | Homeostasis | Succinate Dehydrogenase - biosynthesis | Iron-Binding Proteins - chemistry | Iron-Regulatory Proteins - biosynthesis | Succinate Dehydrogenase - chemistry | Iron-Sulfur Proteins - chemistry | Molecular Chaperones - chemistry | Apoenzymes - metabolism | Iron-Regulatory Proteins - physiology | Iron-Regulatory Proteins - chemistry | Iron-Sulfur Proteins - biosynthesis | Carbon-Sulfur Lyases - physiology | HSP70 Heat-Shock Proteins - chemistry | Protein Interaction Domains and Motifs | HSP70 Heat-Shock Proteins - biosynthesis | Molecular Chaperones - biosynthesis | Iron-Binding Proteins - physiology | Response Elements | Iron Regulatory Protein 1 - chemistry | Carbon-Sulfur Lyases - biosynthesis | Mitochondrial Proteins - physiology | Models, Molecular | Mitochondrial Proteins - biosynthesis | Molecular Chaperones - physiology | Iron-Binding Proteins - biosynthesis | Protein Folding | Iron-Sulfur Proteins - physiology | Gene Expression Regulation, Enzymologic | Animals | Iron - physiology | Mitochondrial Proteins - chemistry | Apoenzymes - chemistry | HSP70 Heat-Shock Proteins - physiology | Succinate Dehydrogenase - physiology | Carbon-Sulfur Lyases - chemistry | Iron Regulatory Protein 1 - biosynthesis | Minireviews
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
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
Journal Article
Current Opinion in Chemical Biology, ISSN 1367-5931, 06/2019, Volume 50, pp. 55 - 65
Protein–protein interactions (PPIs) occur in complex networks. These networks are highly dependent on cellular context and can be extensively altered in... 
HEAT-SHOCK PROTEINS | USP7 | BIOPHYSICS | ACTIVE-SITE | SMALL-MOLECULE INHIBITORS | BIOCHEMISTRY & MOLECULAR BIOLOGY | SELECTIVE INHIBITORS | AAA-ATPASE | MUTATIONS | UBIQUITIN LIGASES | CANCER | ATPASE P97 | Virus diseases | Proteins | Homeostasis | Heat shock proteins | Biomedical engineering
Journal Article