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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
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
Plant Physiology, ISSN 0032-0889, 10/2016, Volume 172, Issue 2, pp. 1221 - 1236
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 12/2012, Volume 109, Issue 50, pp. 20407 - 20412
Small heat shock proteins (sHsps) are molecular chaperones that prevent the aggregation of nonnative proteins. The sHsps investigated to date mostly form... 
Proteins | Aggregation | Oligomers | Molecular chaperones | Protein refolding | Escherichia coli | Deinococcus | Dimers | Small heat shock proteins | Crystal structure | Protein aggregation | Heat stress | Chaperone evolution | Chaperone function | Stress response | SEDIMENTATION-VELOCITY EXPERIMENTS | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | chaperone evolution | ALPHA-B-CRYSTALLIN | IBPB | CITRATE SYNTHASE | DISAGGREGATION | CHAPERONE ACTIVITY | heat stress | stress response | HSP26 | protein aggregation | UNFOLDING PROTEINS | DEINOCOCCUS-RADIODURANS | chaperone function | Molecular Chaperones - metabolism | Protein Multimerization | Bacterial Proteins - chemistry | Stress, Physiological | Molecular Sequence Data | Crystallography, X-Ray | Molecular Chaperones - chemistry | Deinococcus - metabolism | Deinococcus - genetics | Protein Structure, Quaternary | Recombinant Proteins - metabolism | Amino Acid Sequence | Microscopy, Electron, Transmission | Recombinant Proteins - ultrastructure | Heat-Shock Proteins, Small - chemistry | Heat-Shock Proteins, Small - metabolism | Bacterial Proteins - genetics | Molecular Chaperones - genetics | Models, Molecular | Recombinant Proteins - chemistry | Escherichia coli Proteins - metabolism | Recombinant Proteins - genetics | Heat-Shock Proteins, Small - ultrastructure | Protein Folding | Sequence Homology, Amino Acid | Heat-Shock Proteins, Small - genetics | Escherichia coli Proteins - genetics | Bacterial Proteins - metabolism | Bacterial Proteins - ultrastructure | Escherichia coli Proteins - chemistry | Heat shock proteins | Physiological aspects | Health aspects | Biological Sciences
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 2/2010, Volume 107, Issue 5, pp. 2007 - 2012
Journal Article