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Journal Article
Annual Review of Biochemistry, ISSN 0066-4154, 6/2016, Volume 85, Issue 1, pp. 715 - 742
Molecular chaperones control the cellular folding, assembly, unfolding, disassembly, translocation, activation, inactivation, disaggregation, and degradation... 
Hsp70 | Hsp60 | unfoldases | Hsp104 | sHsps | protein homeostasis | heat-shock proteins | Hsp110 | small heat-shock proteins | Heat-shock proteins | Small heat-shock proteins | SHsps | Unfoldases | Protein homeostasis | BACTERIOPHAGE-LAMBDA | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | SUBUNIT BINDING-PROTEIN | ALPHA-B-CRYSTALLIN | QUALITY-CONTROL | RIBULOSEBISPHOSPHATE-CARBOXYLASE | HEAT-SHOCK-PROTEIN | ATP HYDROLYSIS | LAMBDA-DNA-REPLICATION | RIBULOSE-BISPHOSPHATE CARBOXYLASE | Protein Aggregates | Rhodospirillum rubrum - metabolism | Protein Unfolding | Humans | Mitochondrial Proteins - genetics | HSP110 Heat-Shock Proteins - chemistry | Mitochondrial Proteins - metabolism | Adenosine Triphosphate - metabolism | Escherichia coli - metabolism | Protein Structure, Quaternary | Chaperonin 60 - metabolism | HSP70 Heat-Shock Proteins - chemistry | Rhodospirillum rubrum - chemistry | Chaperonin 60 - chemistry | Chaperonin 60 - genetics | Gene Expression | Heat-Shock Proteins, Small - chemistry | Heat-Shock Proteins, Small - metabolism | Models, Molecular | HSP70 Heat-Shock Proteins - genetics | Escherichia coli - chemistry | Protein Folding | HSP70 Heat-Shock Proteins - metabolism | HSP110 Heat-Shock Proteins - genetics | Heat-Shock Proteins, Small - genetics | Mitochondrial Proteins - chemistry | Adenosine Triphosphate - chemistry | HSP110 Heat-Shock Proteins - metabolism | Molecular chaperones | Observations | Protein folding | Health aspects
Journal Article
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 04/2013, Volume 110, Issue 18, p. 7199
  Chaperonins are cage-like complexes in which nonnative polypeptides prone to aggregation are thought to reach their native state optimally. However, they... 
Proteins | Eukaryotes | Polypeptides | Adenosine triphosphatase
Journal Article
Journal Article
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 07/2013, Volume 288, Issue 29, pp. 21399 - 21411
Journal Article
Journal of Molecular Biology, ISSN 0022-2836, 04/2013, Volume 425, Issue 7, pp. 1158 - 1171
Journal Article
Annual Review of Biochemistry, ISSN 0066-4154, 01/2016, Volume 85, p. 715
  Molecular chaperones control the cellular folding, assembly, unfolding, disassembly, translocation, activation, inactivation, disaggregation, and degradation... 
Proteins | Enzymes | Molecules | Polypeptides | Experiments
Journal Article
Frontiers in Molecular Biosciences, ISSN 2296-889X, 07/2014, Volume 1, p. 7
The role of bacterial Hsp40, DnaJ, is to co-chaperone the binding of misfolded or alternatively folded proteins to bacterial Hsp70, DnaK, which is an... 
Aggregation | Protein disulfide isomerase | Cochaperones | Hsp70 | Unfolding | Chaperones | Misfolding | Thioredoxins | DNAJ Homologues | chaperones | protein disulfide isomerase
Journal Article