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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 | Protein Synthesis and Degradation
Journal Article
Molecular Cell, ISSN 1097-2765, 09/2016, Volume 63, Issue 5, pp. 739 - 752
Journal Article
Cell Reports, ISSN 2211-1247, 05/2015, Volume 11, Issue 5, pp. 759 - 769
Journal Article
PLoS ONE, ISSN 1932-6203, 02/2016, Volume 11, Issue 2, p. 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
Journal Article
PLoS ONE, ISSN 1932-6203, 2011, Volume 6, Issue 10, p. 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 | Baking yeast | Parkinson's disease | Cell-free system | Homology | Activation | Biochemistry | Kinases | Synuclein | Cytosol | Machinery | Machinery and equipment | 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
Journal Article
The EMBO Journal, ISSN 0261-4189, 01/2018, Volume 37, Issue 2, pp. 282 - 299
Huntington's disease (HD) is a neurodegenerative disorder caused by an expanded CAG trinucleotide repeat in the huntingtin gene (HTT). Molecular chaperones... 
suppression | disaggregation | molecular chaperones | HttpolyQ | NPCs | EXPANDED HUNTINGTIN | HSP70 | PROTEIN AGGREGATION | BIOCHEMISTRY & MOLECULAR BIOLOGY | DRUG DISCOVERY | TOXICITY | CELLULAR-MODEL | CELL BIOLOGY | DISEASE | POLYGLUTAMINE AGGREGATION | STRESS | ATP | Neurons - pathology | HSC70 Heat-Shock Proteins - metabolism | Humans | Huntington Disease - pathology | Multiprotein Complexes - genetics | HSP110 Heat-Shock Proteins - chemistry | Multiprotein Complexes - metabolism | Protein Aggregation, Pathological - pathology | HEK293 Cells | Neurons - metabolism | HSP40 Heat-Shock Proteins - chemistry | Protein Aggregation, Pathological - genetics | HSC70 Heat-Shock Proteins - genetics | HSP40 Heat-Shock Proteins - metabolism | HSP40 Heat-Shock Proteins - genetics | Huntingtin Protein - metabolism | Huntington Disease - metabolism | Huntingtin Protein - chemistry | Caenorhabditis elegans | HSP110 Heat-Shock Proteins - genetics | Multiprotein Complexes - chemistry | Animals | HSC70 Heat-Shock Proteins - chemistry | Huntington Disease - genetics | Huntingtin Protein - genetics | HSP110 Heat-Shock Proteins - metabolism | Protein Aggregation, Pathological - metabolism | Huntingtons disease | Polyglutamine | Huntingtin | Neurodegenerative diseases | Fibrils | Trinucleotide repeats | Disaggregation | Agglomeration | Chaperones | Huntington's disease | Mammalian cells | Proteins | Fibrillogenesis | Hsc70 protein | Neuroscience | Protein Biosynthesis & Quality Control | Molecular Biology of Disease
Journal Article
Molecular Cell, ISSN 1097-2765, 10/2009, Volume 36, Issue 1, pp. 15 - 27
The multifunctional, stress-inducible molecular chaperone HSP70 has important roles in aiding protein folding and maintaining protein homeostasis. HSP70... 
PROTEINS | CHEMBIO | CELLCYCLE | CANCER-CELLS | HSP70 | CHAPERONE-MEDIATED AUTOPHAGY | NEGATIVE REGULATION | LYSOSOMAL MEMBRANE | BIOCHEMISTRY & MOLECULAR BIOLOGY | HEAT-SHOCK RESPONSE | APAF-1 APOPTOSOME | P53 PROTEINS | P62 | CELL-DEATH | CELL BIOLOGY | HSP70 Heat-Shock Proteins - antagonists & inhibitors | Microtubule-Associated Proteins - metabolism | Sequestosome-1 Protein | Humans | NF-kappa B - metabolism | Cathepsin L - metabolism | Autophagy - drug effects | DNA-Binding Proteins - metabolism | Caspases - metabolism | Lysosomes - metabolism | Protein Binding - drug effects | Lymphoma - pathology | Protein Interaction Domains and Motifs | Cell Death - drug effects | Lysosomes - drug effects | Cell Survival - drug effects | HSP40 Heat-Shock Proteins - metabolism | Tumor Suppressor Protein p53 - metabolism | Ubiquitin-Protein Ligases - metabolism | HSP70 Heat-Shock Proteins - genetics | Mice, Transgenic | Mice, Inbred Strains | Sulfonamides - pharmacology | Apoptotic Protease-Activating Factor 1 - metabolism | HSP70 Heat-Shock Proteins - metabolism | Transcription Factors - metabolism | Animals | Sulfonamides - therapeutic use | Lymphoma - prevention & control | Sulfonamides - metabolism | Cell Line, Tumor | Mice | Adaptor Proteins, Signal Transducing - metabolism | Protein Multimerization - drug effects | Protein Binding - physiology | Proteins | Heat shock proteins | Analysis | Tumors
Journal Article
Cell Stress & Chaperones, ISSN 1355-8145, 3/2017, Volume 22, Issue 2, pp. 191 - 200
Heat shock proteins (Hsps) are a set of highly conserved proteins involved in cellular repair and protective mechanisms. They counter protein misfolding and... 
Thermal stress | Aggregation | Neurodegenerative diseases | Neurons | Protein refolding | Cell nucleus | Thermal shock | Heat shock proteins | Cellular differentiation | RNA splicing | Biomedicine, general | Biochemistry, general | Nuclear speckles | Neurosciences | HSPA1A (Hsp70–1) | DNAJA1 (Hsp40–4) | Human neuronal SH-SY5Y cells | HSPH1 (Hsp105α) | Cell Biology | DNAJB1 (Hsp40–1) | Biomedicine | Immunology | Cancer Research | HSPA8 (Hsc70) | HSPA6 HSP70B | CELASTROL | DNAJB1 (Hsp40-1) | MOLECULAR CHAPERONES | ALZHEIMERS-DISEASE | AMYOTROPHIC-LATERAL-SCLEROSIS | HSPH1 (Hsp105 alpha) | CELL BIOLOGY | DNAJA1 (Hsp40-4) | HEAT-SHOCK PROTEINS | ARIMOCLOMOL | HSPA1A (Hsp70-1) | TRANSGENIC MOUSE MODEL | AGGREGATION | PROGRESSION | HSP40 Heat-Shock Proteins - metabolism | Temperature | HSC70 Heat-Shock Proteins - metabolism | Heat-Shock Proteins - metabolism | Humans | Protein Refolding | Neurons - cytology | Heat-Shock Response - physiology | HSP70 Heat-Shock Proteins - metabolism | HSP110 Heat-Shock Proteins - chemistry | RNA Splicing | HSC70 Heat-Shock Proteins - chemistry | Cell Differentiation - drug effects | Cell Line, Tumor | HSP70 Heat-Shock Proteins - chemistry | Neurons - metabolism | HSP110 Heat-Shock Proteins - metabolism | HSP40 Heat-Shock Proteins - chemistry | Microscopy, Fluorescence | Heat-Shock Proteins - chemistry | Tretinoin - pharmacology | Proteins | Nervous system diseases | Magneto-electric machines | RNA | Machinery | Neurophysiology | Protein binding | Original Paper
Journal Article
Biomedical Journal, ISSN 2319-4170, 05/2013, Volume 36, Issue 3, pp. 106 - 117
Heat shock protein 90 (Hsp90) is an ATP-dependent molecular chaperone which is essential in eukaryotes. It is required for the activation and stabilization of... 
Hsp90 | conformational cycle | clients | posttranslational modifications | ATPase | co-chaperones | Animals | HSP90 Heat-Shock Proteins - antagonists & inhibitors | HSP90 Heat-Shock Proteins - physiology | Humans | HSP90 Heat-Shock Proteins - chemistry | Protein Conformation | Protein Processing, Post-Translational | Molecular Chaperones - physiology | Signal transduction | Antibiotics | Protein folding | Breast cancer | Kinases | Machinery | Binding sites | Hsp90 can be secreted as well and it promotes tumor invasiveness. Blocking the secreted Hsp90 led to a significant inhibition of tumor metastasis. Structure of Hsp90 Top Structurally | nucleotide binding is not the only determinant for Hsp90 conformation. The interaction with co-chaperones and client protein also influences the conformational rearrangement of Hsp90. | p23/Sba1 | eNOS | in which the ATP lid is closed but the N-domains are still open. The N-terminal dimerization leads to the formation of the second intermediate state (I2) | while Hsp90β is constitutively expressed. Hsp90 analogues also exist in other cellular compartments such as Grp94 in the endoplasmic reticulum | the M-domain contributes to the interaction sites for client proteins and some co-chaperones. The C-domain is essential for the dimerization of Hsp90. Interestingly | Hsp90 works together with a large group of cofactors | the activation of its client protein | MutL (GHKL) domain ATPases | Therefore | Binding of Aha1 induces a partially closed Hsp90 conformation and accelerates the progression of the ATPase cycle dramatically. | Different from other well-known molecular chaperone like Hsp70 and GroEL/ES | Interestingly | 113 | which acts as a core modulator in plant immunity. During the recruitment and activation of NLRs | more than 200 Hsp90 client proteins have been identified (see http://www.picard.ch/downloads/Hsp90interactors.pdf ). Besides the well-studied clients such as protein kinases and SHRs | 115 | termed co-chaperones. Co-chaperones form defined binary or ternary complexes with Hsp90 | 116 | Our understanding of the Hsp90 machinery has been greatly advanced by research of the last decades. However | 118 | Function and Regulation of the Hsp90 Machinery. Biomed J 2013;36:106-17 How to cite this URL: Li J | leading to an asymmetric intermediate complex. Hsp90 adopts the ATPase-active (closed) conformation after binding of ATP. p23/Sba1 stabilizes the closed state of Hsp90 | and protein degradation. Interestingly | the lid segment is very flexible | and the NLR protein may dissociate from Hsp90. Hsp90 complexes in RNA processing Recent studies showed that Hsp90 is also involved in the assembly of small nucleolar ribonucleoproteins (snoRNPs) and RNA polymerase. | 15 | the lid segment promotes ATP hydrolysis. Once ATP is hydrolyzed | with 1 min–1 for yeast Hsp90 and 0.1 min–1 for human Hsp90. | hyperphosphorylation also leads to a decreased Hsp90 activity. In yeast | although a TPR domain is present in Sgt1 as well | California | Germany Date of Submission 05-Sep-2012 Date of Acceptance 02-Nov-2012 Date of Web Publication 10-Jun-2013 Correspondence Address: Johannes Buchner Center for Integrated Protein Science | the M-domain in blue | which weakens the binding of Hop/Sti1 and promotes its exit from the complex. Potentially another PPIase (dashed line) associates to form the "late complex" together with Hsp90 and p23/Sba1. After the hydrolysis of ATP | posttranslational modifications of Hsp90 | and protein degradation | 125 | 5 | the protein phosphatase PP5 (yeast homologue Ppt1) | 6 | in eukaryotic Hsp90 | such as mitochondrial/chloroplast protein import (Tom70/Toc64) | 9 | In Ppt1 knockout strains | posttranslational modifications How to cite this article: Li J | Hsp90 is a homodimer and each protomer contains three flexibly linked regions | p23 is a conformation-specific co-chaperone which binds exclusively to the closed conformation of Hsp90. | 24 | viral infection | 27 | Fkbp51 | They regulate the function of Hsp90 in different ways such as inhibition and activation of the ATPase of Hsp90 as well as recruitment of specific client proteins to the cycle. Interestingly | such as double-stranded DNA protein kinase | in which the ATP lid is closed but the N-domains are still open. Then | 132 | one of the most abundant and conserved molecular chaperones | and the C-domain in orange. Click here to view Conformational dynamics of Hsp90 Top Hsp90 is a weak ATPase and the turnover rates are very low | After fast ATP binding | Hsp90 adopts a "V"- shaped form | 35 | the maturation of protein kinases also requires the Hsp70 chaperone machinery [Figure 3]B. In the early stage | Research on the assembly of Hsp90 with SHRs had shown that several distinct complexes are formed during the maturation processes. | phosphorylation affects the conformational cycle of Hsp90 | Hsp90 stabilizes and promotes the correct folding of its client proteins | recent results imply that p53 may be destabilized by Hsp90 | and ch-Hsp90 in the chloroplast. | Chaperone cycle for protein kinases Similar to SHRs | 40 | 43 | the potentiation effects do not strictly depend on the PPIase activity of Fkbp52 as PPIase-deficient mutants are also able to potentiate GR transactivation | Technical University of Munich. Lichtenbergstrasse 4 |