Proteomic data from human cell cultures refine mechanisms of chaperone-mediated protein homeostasis

Keyphrases

• Polypeptide 100%
• Chaperone 100%
• Protein Homeostasis 100%
• Proteomics Data 100%
• Human Cell Culture 100%
• Human Cells 66%
• Crowded Environment 66%
• Co-chaperone 66%
• Folding Enzymes 66%
• Meta-analysis 33%
• Small Heat Shock Protein (sHSP) 33%
• Protein Folding 33%
• Native Protein 33%
• Total Protein 33%
• Aging 33%
• Cell Death 33%
• Adenosine Triphosphate 33%
• Misfolding 33%
• Misfolded Proteins 33%
• Tissue Loss 33%
• Protein Use 33%
• Multifunctional Protein 33%
• Molecular Chaperone 33%
• Nascent Polypeptide 33%
• Human Cell Lines 33%
• Heat Shock Protein 70 (HSP70) 33%
• Error-prone 33%
• Protein Mass 33%
• Heat Shock Protein 60 (HSP60) 33%
• Unfolded Proteins 33%
• Stable Components 33%
• Cell Concentration 33%
• Heat Shock Protein 90 (Hsp90) 33%
• High-throughput Proteomics 33%
• Molecular Folding 33%
• HSP70 Heat-shock Proteins 33%
• Conformational Diseases 33%
• Toxic Aggregates 33%
• Protein Conformers 33%
• Cellular Proteostasis 33%
• Toxic Conformer 33%

Biochemistry, Genetics and Molecular Biology

• Protein Homeostasis 100%
• Human Cell Culture 100%
• Proteomics 100%
• Enzyme 66%
• Hsp70 66%
• Heat Shock Protein 33%
• Protein Folding 33%
• Cell Death 33%
• Adenosine Triphosphate 33%
• Hsp90 33%
• Chaperone Protein 33%