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Journal of Medicinal Chemistry, ISSN 0022-2623, 07/2018, Volume 61, Issue 14, pp. 6163 - 6177
Cancer cells rely on the chaperone heat shock protein 70 (Hsp70) for survival and proliferation. Recently, benzothiazole rhodacyanines have been shown to bind... 
INTERDOMAIN LINKER | CHEMISTRY, MEDICINAL | TARGETING HSP70 | SMALL-MOLECULE | GENETIC SCREENS | ADENOSINE-DERIVED INHIBITORS | CHAPERONE | MAMMALIAN-CELLS | DRUG TARGETS | CANCER-THERAPY | HEAT-SHOCK-PROTEIN | Index Medicus | breast cancer | non-oncogene addiction | chaperone | structure-activity relationships | proteostasis | allostery
Journal Article
Science, ISSN 0036-8075, 11/2015, Volume 350, Issue 6261, pp. 678 - 680
Journal Article
PLoS ONE, ISSN 1932-6203, 2011, Volume 6, Issue 10, pp. e26319 - e26319
Bacteria, fungi, protozoa, chromista and plants all harbor homologues of Hsp104, a AAA+ ATPase that collaborates with Hsp70 and Hsp40 to promote protein... 
YEAST | IN-VITRO | CAENORHABDITIS-ELEGANS | MOLECULAR CHAPERONES | MULTIDISCIPLINARY SCIENCES | AGGREGATED PROTEINS | ALPHA-SYNUCLEIN | SACCHAROMYCES-CEREVISIAE | HUNTINGTONS-DISEASE | HEAT-SHOCK-PROTEIN | NUCLEOTIDE EXCHANGE FACTORS | Mammals - metabolism | HSP40 Heat-Shock Proteins - metabolism | Biocatalysis | Humans | Adenosine Triphosphatases - metabolism | Rats | Substrate Specificity | HSP70 Heat-Shock Proteins - metabolism | HSP110 Heat-Shock Proteins - chemistry | Hydrolysis | Saccharomyces cerevisiae - metabolism | Cytosol - enzymology | Animals | Amyloid - metabolism | Cell-Free System | Adenosine Triphosphate - metabolism | Protein Structure, Quaternary | Saccharomyces cerevisiae Proteins - metabolism | Conserved Sequence | Protein Binding | HSP70 Heat-Shock Proteins - chemistry | HeLa Cells | HSP110 Heat-Shock Proteins - metabolism | HSP40 Heat-Shock Proteins - chemistry | Heat shock proteins | Prions | Cells | Adenosine triphosphatase | Yeast | Parkinson's disease | Cell-free system | Homology | Activation | Biochemistry | Kinases | Synuclein | Cytosol | Machinery | Fungi | Protein folding | Bacteria | Amyloid | Trends | Prion protein | Movement disorders | Adenosine triphosphate | Protozoa | Neurodegenerative diseases | Disaggregation | Hsp70 protein | Hsp40 protein | Mammals | Substrates | Aggregates | Hsc70 protein | Mutation | Alzheimers disease | Endoplasmic reticulum | ATP | Index Medicus
Journal Article
Science, ISSN 0036-8075, 9/2011, Volume 333, Issue 6048, pp. 1445 - 1449
Bacterial chromosomes are confined in submicrometer-sized nucleoids. Chromosome organization is facilitated by nucleoid-associated proteins (NAPs), but the... 
Proteins | Molecules | DNA | Genes | Imaging | REPORTS | Cell lines | Genetic loci | Gene expression regulation | Genomes | Chromosomes | CELLS | STRUCTURING PROTEIN | CAULOBACTER-CRESCENTUS | MULTIDISCIPLINARY SCIENCES | ESCHERICHIA-COLI | GENE-EXPRESSION | OPTICAL RECONSTRUCTION MICROSCOPY | H-NS PROTEIN | BINDING | GENOME | Molecular Chaperones - metabolism | DNA, Bacterial - metabolism | Factor For Inversion Stimulation Protein - metabolism | Fimbriae Proteins - metabolism | Protein Multimerization | DNA, Bacterial - chemistry | Genetic Loci | Recombinant Fusion Proteins - metabolism | Escherichia coli K12 - ultrastructure | DNA-Binding Proteins - metabolism | Integration Host Factors - metabolism | Chromosomes, Bacterial - metabolism | Escherichia coli K12 - metabolism | Cell Division | Nucleic Acid Conformation | Binding Sites | Repressor Proteins - metabolism | Protein Structure, Tertiary | Genome, Bacterial | Repressor Proteins - chemistry | Operon | Repressor Proteins - genetics | Escherichia coli Proteins - metabolism | Chromosomes, Bacterial - ultrastructure | Fimbriae Proteins - genetics | Escherichia coli Proteins - genetics | Fimbriae Proteins - chemistry | Escherichia coli K12 - genetics | Escherichia coli Proteins - chemistry | Gene Expression Regulation, Bacterial | Cellular proteins | Research | Properties | Bacterial genetics | E coli | Microbiology | Bacterial proteins | Index Medicus
Journal Article
Journal Article
Journal of Cell Biology, ISSN 0021-9525, 2017, Volume 216, Issue 8, pp. 2295 - 2304
Disturbances in endoplasmic reticulum (ER) homeostasis create a condition termed ER stress. This activates the unfolded protein response (UPR), which alters... 
YEAST | OXIDATIVE STRESS | MOLECULAR CHAPERONES | GUANIDINE-HYDROCHLORIDE | MISFOLDED PROTEIN | MEMBRANE-PROTEIN | ENDOPLASMIC-RETICULUM | QUALITY-CONTROL | SACCHAROMYCES-CEREVISIAE | TRANSMEMBRANE PROTEIN | CELL BIOLOGY | Protein Aggregates | Basic-Leucine Zipper Transcription Factors - metabolism | Molecular Chaperones - metabolism | Membrane Glycoproteins - metabolism | Saccharomyces cerevisiae - genetics | Endoplasmic Reticulum - metabolism | Prion Proteins - metabolism | Saccharomyces cerevisiae - metabolism | Endoplasmic Reticulum - pathology | Time Factors | Proteomics - methods | Protein-Serine-Threonine Kinases - metabolism | Repressor Proteins - metabolism | Molecular Chaperones - genetics | Protein-Serine-Threonine Kinases - genetics | Ubiquitin-Protein Ligases - metabolism | Repressor Proteins - genetics | Genotype | Basic-Leucine Zipper Transcription Factors - genetics | Saccharomyces cerevisiae Proteins - genetics | Unfolded Protein Response | Protein Aggregation, Pathological | Membrane Glycoproteins - genetics | Phenotype | Endoplasmic Reticulum Stress | Saccharomyces cerevisiae Proteins - metabolism | Mutation | Ubiquitin-Protein Ligases - genetics | Cellular proteins | Stress (Physiology) | Analysis | Prions | Stresses | Homeostasis | Agglomeration | Chaperones | Gene expression | Stress | Proteins | Degradation | Correlation analysis | Protein folding | Quality control | Amyloid | Prion protein | Protein interaction | Endoplasmic reticulum | Index Medicus
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 | Molecules | Substrates | Adenosine triphosphatase | Index Medicus | protein–protein interactions | Biological Sciences
Journal Article
2007, Advances in Experimental Medicine and Biology, ISBN 0387399747, Volume 594., xviii, 201
This book is authored by an exciting mixture of top experts and young rising stars from the fields of molecular chaperones and stress adaptation. In addition... 
Heat shock proteins | Stress (Physiology) | Molecular chaperones | Protein folding | Life Sciences | Biochemistry, general | Biophysics/Biomedical Physics | Immunology | Cell Biology
Book
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
Cellular and Molecular Life Sciences, ISSN 1420-682X, 4/2014, Volume 71, Issue 8, pp. 1477 - 1504
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