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Nature Structural and Molecular Biology, ISSN 1545-9993, 07/2013, Volume 20, Issue 7, pp. 900 - 907
The 70-kilodalton (kDa) heat-shock proteins (Hsp70s) are ubiquitous molecular chaperones essential for cellular protein folding and proteostasis. Each Hsp70... 
INTERDOMAIN COMMUNICATION | WILD-TYPE | PEPTIDE-BINDING | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | CELL BIOLOGY | SHOCK COGNATE PROTEIN | MOLECULAR CHAPERONE DNAK | SUBSTRATE-BINDING | CONFORMATIONAL-CHANGES | BIOPHYSICS | STRUCTURE VALIDATION | STRUCTURAL BASIS | Allosteric Regulation | Molecular Sequence Data | Crystallography, X-Ray | Mutation, Missense | Recombinant Fusion Proteins - metabolism | Peptides - metabolism | Adenosine Triphosphate - metabolism | Escherichia coli - metabolism | Conserved Sequence | HSP70 Heat-Shock Proteins - chemistry | Binding Sites | Dimerization | Protein Structure, Tertiary | Amino Acid Sequence | Models, Molecular | Escherichia coli Proteins - metabolism | HSP70 Heat-Shock Proteins - genetics | Recombinant Fusion Proteins - chemistry | Saccharomyces cerevisiae Proteins - genetics | Protein Folding | HSP70 Heat-Shock Proteins - metabolism | Protein Interaction Mapping | Sequence Homology, Amino Acid | Sequence Alignment | Hydrogen Bonding | Escherichia coli - genetics | Escherichia coli Proteins - genetics | Protein Binding | Adenosine Triphosphatases - chemistry | Protein Conformation | Adenosine Triphosphatases - genetics | Escherichia coli Proteins - chemistry | Saccharomyces cerevisiae Proteins - chemistry | Heat shock proteins | Physiological aspects | Homeostasis | Research | Structure | ABC transporters | Biochemistry | Polypeptides | Molecular biology | Index Medicus
Journal Article
Journal Article
Molecular Systems Biology, ISSN 1744-4292, 2011, Volume 7, Issue 1, pp. 511 - n/a
Biological function and cellular responses to environmental perturbations are regulated by a complex interplay of DNA, RNA, proteins and metabolites inside... 
Mycoplasma pneumoniae | protein turnover | mRNA–protein | quantitative proteomics | protein homeostasis | mRNA-protein | CRYSTAL-STRUCTURE | BIOCHEMISTRY & MOLECULAR BIOLOGY | PATHOGEN LEPTOSPIRA-INTERROGANS | ESCHERICHIA-COLI PROTEOME | YEAST PROTEOME | MASS-SPECTROMETRY | MYCOPLASMA-PNEUMONIAE | STATISTICAL-MODEL | ABUNDANCE | GENOME-REDUCED BACTERIUM | GENE-EXPRESSION | Genome, Bacterial | Proteome - genetics | RNA Processing, Post-Transcriptional | Mycoplasma pneumoniae - metabolism | Electrophoresis, Polyacrylamide Gel | RNA, Messenger - genetics | Bacterial Proteins - genetics | Databases, Genetic | Mycoplasma pneumoniae - genetics | Gene Expression Profiling | RNA, Messenger - metabolism | Sequence Analysis, RNA | Culture Media | Mass Spectrometry | Bacterial Proteins - metabolism | Protein Processing, Post-Translational | Gene Expression Regulation, Bacterial | Proteome - metabolism | Cell culture | Regulations | Noise | Copy number | Chaperones | Protein turnover | Osmotic stress | Complexity | Proteins | Protein composition | Efficiency | Stable isotopes | DnaK protein | Biomolecules | Deoxyribonucleic acid--DNA | Quantitative analysis | Stresses | Noise propagation | Spectroscopy | Translation | Computer simulation | DNA topoisomerase | Elongation factor EF-Tu | Mass spectroscopy | RNA polymerase | Gene expression | Molecular chains | Correlation analysis | Ordinary differential equations | Scientific imaging | Mass spectrometry | Stoichiometry | Batch culture | Transcription | Noise reduction | DNA damage | Amino acids | Genomes | DNA-directed RNA polymerase | Biological effects | Metabolites | Mathematical models | Elongation | Biodegradation | Composition | Integration | mRNA turnover | Heat shock proteins | Abundance | Ribonucleic acid--RNA | Biological activity | Stress | Simulation | Differential equations | Stochasticity | Heat shock | Index Medicus
Journal Article
Protein Science, ISSN 0961-8368, 11/2017, Volume 26, Issue 11, pp. 2207 - 2220
The Hsp70 chaperone system plays a critical role in cellular homeostasis by binding to client protein molecules. We have recently shown by methyl‐TROSY NMR... 
Hsp70 | conformational heterogeneity | molecular chaperones | methyl‐TROSY NMR | NMR titrations | methyl-TROSY NMR | SYSTEM | GRPE | BIOCHEMISTRY & MOLECULAR BIOLOGY | ESCHERICHIA-COLI | METHYL-GROUPS | MOLECULAR-WEIGHT PROTEINS | HEAT-SHOCK PROTEINS | DNAK CHAPERONE | SPECTROSCOPY | CLIENT PROTEIN | BINDING | Molecular Chaperones - metabolism | Humans | Substrate Specificity | Telomeric Repeat Binding Protein 1 - genetics | Telomeric Repeat Binding Protein 1 - metabolism | Molecular Chaperones - chemistry | Telomeric Repeat Binding Protein 1 - chemistry | Cloning, Molecular | Escherichia coli - metabolism | HSP70 Heat-Shock Proteins - chemistry | Protein Interaction Domains and Motifs | Binding Sites | Recombinant Proteins - metabolism | Amino Acid Sequence | Protein Conformation, alpha-Helical | Gene Expression | Magnetic Resonance Spectroscopy | Molecular Chaperones - genetics | Models, Molecular | Recombinant Proteins - chemistry | Escherichia coli Proteins - metabolism | HSP70 Heat-Shock Proteins - genetics | Recombinant Proteins - genetics | Protein Folding | HSP70 Heat-Shock Proteins - metabolism | Sequence Homology, Amino Acid | Sequence Alignment | Protein Conformation, beta-Strand | Escherichia coli - genetics | Escherichia coli Proteins - genetics | Protein Binding | Kinetics | Escherichia coli Proteins - chemistry | Proteins | Heat shock proteins | Nuclear magnetic resonance spectroscopy | Analysis | Escherichia coli | Protein binding | Binding | Magnetic resonance spectroscopy | Nuclear magnetic resonance--NMR | DnaK protein | Homeostasis | Titration | Hsp70 protein | Chaperones | NMR spectroscopy | Heat shock | Index Medicus
Journal Article
Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, 4/2011, Volume 108, Issue 17, pp. 6915 - 6920
Yeast Hsp104 and its bacterial homolog, ClpB, are Clp/Hsp100 molecular chaperones and AAA+ ATPases. Hsp104 and ClpB collaborate with the Hsp70 and DnaK... 
Proteins | Yeasts | Protein refolding | Plasmids | Prions | Escherichia coli | Adenosine triphosphatases | Cell aggregates | Heat tolerance | Chimeras | GrpE | M-domain | DnaJ | Nucleotide exchange factor | Hsp40 | CLPB | MECHANISM | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | MACHINERY | AGGREGATED PROTEINS | SACCHAROMYCES-CEREVISIAE | nucleotide exchange factor | DNAK | PRION PROPAGATION | N-TERMINAL DOMAIN | CHAPERONE SYSTEM | Protein Structure, Secondary | Endopeptidase Clp | Heat-Shock Proteins - metabolism | Escherichia coli Proteins - metabolism | HSP70 Heat-Shock Proteins - genetics | Saccharomyces cerevisiae Proteins - genetics | Escherichia coli - chemistry | Recombinant Fusion Proteins | Saccharomyces cerevisiae - chemistry | HSP70 Heat-Shock Proteins - metabolism | Saccharomyces cerevisiae - metabolism | Heat-Shock Proteins - genetics | Escherichia coli - genetics | Escherichia coli - metabolism | Saccharomyces cerevisiae Proteins - metabolism | Escherichia coli Proteins - genetics | HSP70 Heat-Shock Proteins - chemistry | Escherichia coli Proteins - chemistry | Heat-Shock Proteins - chemistry | Saccharomyces cerevisiae Proteins - chemistry | Heat shock proteins | Physiological aspects | Genetic aspects | Yeast fungi | Adenosine triphosphatase | Temperature | Yeast | Collaboration | Amino acids | Mutation | Cells | Index Medicus | Biological Sciences
Journal Article
PLoS ONE, ISSN 1932-6203, 06/2015, Volume 10, Issue 6, pp. e0129445 - e0129445
Journal Article
Journal of Biological Chemistry, ISSN 0021-9258, 01/2014, Volume 289, Issue 2, pp. 848 - 867
Journal Article
PLoS ONE, ISSN 1932-6203, 12/2012, Volume 7, Issue 12, pp. e50927 - e50927
Journal Article