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Journal Article
Annual Review of Biochemistry, ISSN 0066-4154, 6/2017, Volume 86, Issue 1, pp. 97 - 122
A healthy proteome is essential for cell survival. Protein misfolding is linked to a rapidly expanding list of human diseases, ranging from neurodegenerative... 
neurodegenerative diseases | aging | molecular chaperones | proteostasis | protein aggregation | misfolded protein clearance | Aging | Protein aggregation | Misfolded protein clearance | Proteostasis | Molecular chaperones | Neurodegenerative diseases | UBIQUITIN LIGASE | BIOCHEMISTRY & MOLECULAR BIOLOGY | AGGREGATED PROTEINS | ER-ASSOCIATED DEGRADATION | HEAT-SHOCK | ALPHA-SYNUCLEIN | DAMAGED PROTEINS | EUKARYOTIC STRESS GRANULES | ASYMMETRIC INHERITANCE | MISFOLDED PROTEINS | Proteostasis Deficiencies - metabolism | Protein Biosynthesis | Molecular Chaperones - metabolism | Humans | Amyloidogenic Proteins - chemistry | Prion Proteins - metabolism | Cell Compartmentation | Aging - genetics | Protein Aggregation, Pathological - pathology | Proteolysis | Prion Proteins - chemistry | Prion Proteins - genetics | Protein Aggregation, Pathological - genetics | Amyloidogenic Proteins - genetics | Neurodegenerative Diseases - pathology | Gene Expression Regulation | Molecular Chaperones - genetics | Protein Refolding | Proteostasis Deficiencies - pathology | Neurodegenerative Diseases - genetics | Neurodegenerative Diseases - metabolism | Protein Folding | Aging - pathology | Proteostasis Deficiencies - genetics | Amyloidogenic Proteins - metabolism | Protein Conformation | Protein Aggregation, Pathological - metabolism | Aging - metabolism | Physiological aspects | Research | Protein folding | Proteomics | Cell survival | Pathogenesis | Spatial discrimination | Homeostasis | Agglomeration | Chaperones | Disease control | Machinery | Diseases | Proteins | Neurological diseases | Compartments | Quality control | Amyloid | Aberration | Protein interaction | Neurological disorders | Plaques | Cancer | Fitness
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
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
Trends in Biochemical Sciences, ISSN 0968-0004, 02/2015, Volume 40, Issue 2, pp. 117 - 125
Journal Article