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2006, Topics in current genetics, ISBN 3540325808, Volume 16., xvii, 299
Molecular chaperones interact with virtually every newly synthesized protein. Their role is not limited to this, as an increasing number of protein-protein... 
Molecular chaperones | Biochemistry
Book
2006, Handbook of experimental pharmacology, ISBN 9783540258759, Volume 172, viii, 442
Molecular chaperones are involved in a wide variety of essential cellular processes in living cells. A subset of molecular chaperones have been initially... 
Molecular chaperones | Physiological effect | Proteins | Medical Biochemistry | Biomedicine | Pharmacology/Toxicology | Cell Biology
Book
2000, Methods in molecular biology, ISBN 9780896037397, Volume 140., x, 212
In Chaperonin Protocols, Christine Schneider has assembled a unique collection of readily reproducible protocols for the study of chaperonins, intracellular... 
Molecular chaperones | Purification | Laboratory manuals | Molecular biology | Biochemistry, general | Biochemistry | Life Sciences
Book
1997, Guidebook series, ISBN 019859948X, xxvi, 554
Book
2014, Interactomics and Systems Biology, ISBN 1493911295
Web Resource
Journal of Biological Chemistry, ISSN 0021-9258, 01/2014, Volume 289, Issue 3, pp. 1402 - 1414
Background: There has been an expansion of the number of Hsp70 cochaperones in mammals, providing the opportunity for combinatorial assembly of permutations... 
Protein Complexes | Protein Misfolding | Cochaperones | HIGH-THROUGHPUT SCREEN | MOLECULAR CHAPERONES | BIOCHEMISTRY & MOLECULAR BIOLOGY | QUALITY-CONTROL | Hsp40 | Protein Folding | HSP110 CHAPERONES | HEAT-SHOCK-PROTEIN | NEGATIVE REGULATOR | Isothermal Titration Calorimetry | J-DOMAIN | ATP HYDROLYSIS | STRUCTURAL BASIS | Molecular Chaperone | HSC70 CHAPERONE | ATPases | Protein-Protein Interactions | Adaptor Proteins, Signal Transducing - chemistry | Molecular Chaperones - metabolism | Transcription Factors - chemistry | Humans | Multiprotein Complexes - genetics | Molecular Chaperones - chemistry | DNA-Binding Proteins - metabolism | HSP110 Heat-Shock Proteins - chemistry | Multiprotein Complexes - metabolism | HSP70 Heat-Shock Proteins - chemistry | HSP40 Heat-Shock Proteins - chemistry | Recombinant Proteins - metabolism | HSP40 Heat-Shock Proteins - metabolism | HSP40 Heat-Shock Proteins - genetics | Molecular Chaperones - genetics | Recombinant Proteins - chemistry | HSP70 Heat-Shock Proteins - genetics | Recombinant Proteins - genetics | Transcription Factors - genetics | DNA-Binding Proteins - genetics | DNA-Binding Proteins - chemistry | HSP70 Heat-Shock Proteins - metabolism | Transcription Factors - metabolism | HSP110 Heat-Shock Proteins - genetics | Multiprotein Complexes - chemistry | Apoptosis Regulatory Proteins | Adaptor Proteins, Signal Transducing - genetics | Adaptor Proteins, Signal Transducing - metabolism | HSP110 Heat-Shock Proteins - metabolism | Protein Binding - physiology | Index Medicus | Protein Synthesis and Degradation
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 | Bacteria | Adenosine triphosphatase | Substrates | Index Medicus | Biological Sciences
Journal Article
Biomolecular NMR Assignments, ISSN 1874-2718, 10/2013, Volume 7, Issue 2, pp. 289 - 292
Human lysyl aminoacyl tRNA synthetase (hLysRS) is integral to a variety of different functions ranging from protein biosynthesis, initiation of a... 
Chaperones
Journal Article
Journal Article
PLoS ONE, ISSN 1932-6203, 02/2016, Volume 11, Issue 2, pp. e0148517 - e0148517
Plasmodium falciparum, the human pathogen responsible for the most dangerous malaria infection, survives and develops in mature erythrocytes through the export... 
HSP70 CHAPERONES | J PROTEINS | DNAJ | YEAST HSP40 | PLASMODIUM-FALCIPARUM | CRYSTAL-STRUCTURE | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | MOLECULAR CHAPERONE | DIMERIZATION | PARASITE | Protein Aggregates | Molecular Chaperones - metabolism | Humans | Molecular Chaperones - chemistry | Recombinant Proteins | Protozoan Proteins - genetics | Thiosulfate Sulfurtransferase - metabolism | Protozoan Proteins - metabolism | Plasmodium falciparum - genetics | Plasmodium falciparum - metabolism | Protozoan Proteins - chemistry | HSP70 Heat-Shock Proteins - chemistry | HSP40 Heat-Shock Proteins - chemistry | HSP40 Heat-Shock Proteins - metabolism | HSP40 Heat-Shock Proteins - genetics | HSP40 Heat-Shock Proteins - isolation & purification | Molecular Chaperones - genetics | Adenosine Triphosphatases - metabolism | HSP70 Heat-Shock Proteins - genetics | HSP70 Heat-Shock Proteins - metabolism | Malaria, Falciparum - parasitology | Protozoan Proteins - isolation & purification | Protein Binding | HSP70 Heat-Shock Proteins - isolation & purification | Kinetics | Molecular Chaperones - isolation & purification | Plasmodium falciparum | Malaria | Heat shock proteins | Physiological aspects | Causes of | Genetic aspects | Research | Biotechnology | Yeast | Trafficking | Erythrocytes | Biochemistry | Chaperones | Parasites | Drug resistance | Cytosol | Proteins | Red blood cells | E coli | Protein folding | Protein transport | Recombinant | Vector-borne diseases | Hsp70 protein | Hsp40 protein | Exports | Rhodanese | Human behavior | Adenosine triphosphatase | Heat shock | Index Medicus
Journal Article
Proceedings of the National Academy of Sciences, ISSN 0027-8424, 08/2015, Volume 112, Issue 32, pp. 9908 - 9913
Journal Article
PLoS ONE, 09/2013, Volume 8, Issue 9
During the plant immune response, large-scale transcriptional reprogramming is modulated by numerous transcription (co) factors. The Arabidopsis basic leucine... 
Chaperones
Journal Article
PLoS ONE, 08/2013, Volume 8, Issue 8
Gaucher disease (GD) is the most common of the lysosomal storage disorders and is caused by defects in the GBA gene encoding glucocerebrosidase (GlcCerase).... 
Chaperones
Journal Article
PLoS ONE, 07/2013, Volume 8, Issue 7
Hsp90 is one of the most conserved and abundant molecular chaperones and is an essential component of the protective stress response; however, its roles in... 
Chaperones
Journal Article
PLoS ONE, 07/2013, Volume 8, Issue 7
Background Zymomonas mobilis ZM4 is a capable ethanologenic bacterium with high ethanol productivity and ethanol tolerance. Previous studies indicated that... 
Chaperones
Journal Article
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