| review article | Q7318358 |
| scholarly article | Q13442814 |
| P356 | DOI | 10.3390/IJMS20174122 |
| P953 | full work available at URL | https://www.mdpi.com/1422-0067/20/17/4122 |
| P932 | PMC publication ID | 6747476 |
| P698 | PubMed publication ID | 31450862 |
| P2093 | author name string | Arturo Muga | |
| Fernando Moro | |||
| Leire Dublang | |||
| Lorea Velasco | |||
| P2860 | cites work | Redox dynamics of manganese as a mitochondrial life-death switch. | Q37739913 |
| Assembly and function of the proteasome | Q37986626 | ||
| Deciphering the retinoblastoma protein phosphorylation code | Q38065487 | ||
| Regulation of molecular chaperones through post-translational modifications: decrypting the chaperone code | Q38086397 | ||
| Tau phosphorylation, molecular chaperones, and ubiquitin E3 ligase: clinical relevance in Alzheimer's disease | Q38237301 | ||
| A conserved HPD sequence of the J-domain is necessary for YDJ1 stimulation of Hsp70 ATPase activity at a site distinct from substrate binding | Q38358898 | ||
| Neuronal aggregates: formation, clearance, and spreading | Q38364757 | ||
| Cysteine string protein (CSP) and its role in preventing neurodegeneration | Q38388009 | ||
| Formation of a pathogen vacuole according to Legionella pneumophila: how to kill one bird with many stones. | Q38436575 | ||
| Chaperone-assisted protein aggregate reactivation: Different solutions for the same problem. | Q38544585 | ||
| Effects of macromolecular crowding agents on protein folding in vitro and in silico | Q38783045 | ||
| Heat shock proteins as potential targets for protective strategies in neurodegeneration | Q38815318 | ||
| In vivo aspects of protein folding and quality control | Q38882864 | ||
| Unraveling the CHIP:Hsp70 complex as an information processor for protein quality control | Q39013271 | ||
| Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade | Q39302623 | ||
| Characterization of stress sensitivity and chaperone activity of Hsp105 in mammalian cells | Q39545229 | ||
| Phosphorylation of Cysteine String Protein Triggers a Major Conformational Switch | Q39565659 | ||
| Systems-wide analysis of a phosphatase knock-down by quantitative proteomics and phosphoproteomics | Q39853507 | ||
| Real-time observation of the conformational dynamics of mitochondrial Hsp70 by spFRET. | Q41460745 | ||
| Unique peptide substrate binding properties of 110-kDa heat-shock protein (Hsp110) determine its distinct chaperone activity | Q41480929 | ||
| Evidence of multimeric forms of HSP70 with phosphorylation on serine and tyrosine residues--implications for roles of HSP70 in detection of GI cancers | Q41872840 | ||
| Specific Binding of Tetratricopeptide Repeat Proteins to Heat Shock Protein 70 (Hsp70) and Heat Shock Protein 90 (Hsp90) Is Regulated by Affinity and Phosphorylation | Q41884789 | ||
| Inducible HSP70 regulates superoxide dismutase-2 and mitochondrial oxidative stress in the endothelial cells from developing lungs. | Q41943801 | ||
| An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones | Q41959252 | ||
| Phosphorylation-dependent interaction of the synaptic vesicle proteins cysteine string protein and synaptotagmin I. | Q42123208 | ||
| Role of DnaJ G/F-rich domain in conformational recognition and binding of protein substrates | Q42400784 | ||
| Allosteric fine-tuning of the conformational equilibrium poises the chaperone BiP for post-translational regulation | Q42637818 | ||
| The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase | Q42856450 | ||
| Structural characterization of the substrate transfer mechanism in Hsp70/Hsp90 folding machinery mediated by Hop. | Q43984053 | ||
| Reduced folate carrier mutations are not the mechanism underlying methotrexate resistance in childhood acute lymphoblastic leukemia | Q44760816 | ||
| Mammalian SOD2 is exclusively located in mitochondria and not present in peroxisomes. | Q44800193 | ||
| Plasma levels of heat shock protein 70 in patients with prostate cancer: a potential biomarker for prostate cancer | Q44997136 | ||
| Proteomic analysis of in vivo phosphorylated synaptic proteins. | Q45168689 | ||
| Solubilization of aggregated proteins by ClpB/DnaK relies on the continuous extraction of unfolded polypeptides | Q45181636 | ||
| Human and yeast Hsp110 chaperones exhibit functional differences | Q46858675 | ||
| DnaJ recruits DnaK to protein aggregates | Q46913678 | ||
| Molecular Mechanism of J-Domain-Triggered ATP Hydrolysis by Hsp70 Chaperones | Q47228277 | ||
| Complete suppression of Htt fibrilization and disaggregation of Htt fibrils by a trimeric chaperone complex | Q47322329 | ||
| Proteomics of phosphorylation and protein dynamics during fertilization and meiotic exit in the Xenopus egg. | Q47354937 | ||
| The Role of Cysteine String Protein α Phosphorylation at Serine 10 and 34 by Protein Kinase Cγ for Presynaptic Maintenance. | Q47372346 | ||
| Cracking the Chaperone Code: Cellular Roles for Hsp70 Phosphorylation | Q47442205 | ||
| Domain Mapping of Heat Shock Protein 70 Reveals That Glutamic Acid 446 and Arginine 447 Are Critical for Regulating Superoxide Dismutase 2 Function | Q49814595 | ||
| Cellular Handling of Protein Aggregates by Disaggregation Machines | Q49914168 | ||
| Phosphorylation of heat shock protein 40 (Hsp40/DnaJB1) by mitogen-activated protein kinase-activated protein kinase 5 (MK5/PRAK). | Q50337043 | ||
| Expression profiling in multistage hepatocarcinogenesis: identification of HSP70 as a molecular marker of early hepatocellular carcinoma. | Q52025753 | ||
| HSP70 colocalizes with PLK1 at the centrosome and disturbs spindle dynamics in cells arrested in mitosis by arsenic trioxide. | Q53062812 | ||
| Phosphorylation at tyrosine-524 influences nuclear accumulation of HSP72 with heat stress. | Q54048540 | ||
| Hsp110 protects heat-denatured proteins and confers cellular thermoresistance. | Q54147754 | ||
| Protein Folding: A Perspective from Theory and Experiment. | Q54308010 | ||
| Mechanics of Hsp70 chaperones enables differential interaction with client proteins. | Q54369498 | ||
| Molecular basis for regulation of the heat shock transcription factor sigma32 by the DnaK and DnaJ chaperones. | Q54414189 | ||
| The NH2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for lambda replication. | Q54639983 | ||
| Dissecting Structure-Encoded Determinants of Allosteric Cross-Talk between Post-Translational Modification Sites in the Hsp90 Chaperones. | Q55218904 | ||
| Probing aggrephagy using chemically-induced protein aggregates | Q57471972 | ||
| Hsp70 chaperone: a master player in protein homeostasis | Q58553656 | ||
| Allosteric landscapes of eukaryotic cytoplasmic Hsp70s are shaped by evolutionary tuning of key interfaces | Q58612179 | ||
| The Physics of Entropic Pulling: A Novel Model for the Hsp70 Motor Mechanism. | Q64987892 | ||
| Modulation of substrate specificity of the DnaK chaperone by alteration of a hydrophobic arch | Q73220607 | ||
| Multistep mechanism of substrate binding determines chaperone activity of Hsp70 | Q73943514 | ||
| The chaperoning activity of hsp110. Identification of functional domains by use of targeted deletions | Q77772392 | ||
| Allosteric regulation of Hsp70 chaperones involves a conserved interdomain linker | Q79278307 | ||
| Determining the stoichiometry and interactions of macromolecular assemblies from mass spectrometry | Q80093527 | ||
| DnaK-mediated association of ClpB to protein aggregates. A bichaperone network at the aggregate surface | Q84447521 | ||
| Protein-Protein Interactions in the Molecular Chaperone Network | Q88254002 | ||
| Regulation of Human Hsc70 ATPase and Chaperone Activities by Apg2: Role of the Acidic Subdomain | Q90308729 | ||
| Modulation of Amyloid States by Molecular Chaperones | Q91518635 | ||
| A Legionella pneumophila Kinase Phosphorylates the Hsp70 Chaperone Family to Inhibit Eukaryotic Protein Synthesis | Q92084893 | ||
| The Hsp70 chaperone network | Q93117098 | ||
| Dynamic Phosphorylation of the C Terminus of Hsp70 Regulates the Mitochondrial Import of SOD2 and Redox Balance | Q93372373 | ||
| Function, evolution, and structure of J-domain proteins | Q93383323 | ||
| The co-chaperone CHIP regulates protein triage decisions mediated by heat-shock proteins | Q24290709 | ||
| Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis | Q24294864 | ||
| Protein kinase CK2 phosphorylates Hsp105 alpha at Ser509 and modulates its function | Q24529920 | ||
| Molecular chaperones as HSF1-specific transcriptional repressors | Q24606489 | ||
| Phospho3D 2.0: an enhanced database of three-dimensional structures of phosphorylation sites | Q24608245 | ||
| Not all J domains are created equal: implications for the specificity of Hsp40-Hsp70 interactions | Q24644464 | ||
| Misfolded proteins partition between two distinct quality control compartments | Q24651093 | ||
| Cooperative regulation of p53 by modulation of ternary complex formation with CBP/p300 and HDM2 | Q24655602 | ||
| The nucleotide exchange factors of Hsp70 molecular chaperones | Q26766367 | ||
| The influence of C-terminal extension on the structure of the “J-domain” in E. coli DnaJ | Q27617982 | ||
| Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine | Q27622332 | ||
| The crystal structure of the yeast Hsp40 Ydj1 complexed with its peptide substrate | Q27642692 | ||
| Insights into Hsp70 Chaperone Activity from a Crystal Structure of the Yeast Hsp110 Sse1 | Q27648730 | ||
| Structure of the Hsp110:Hsc70 nucleotide exchange machine | Q27650814 | ||
| Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding | Q27650844 | ||
| Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP | Q27678317 | ||
| Structure and dynamics of the ATP-bound open conformation of Hsp70 chaperones | Q27683212 | ||
| Lysine 71 of the chaperone protein Hsc70 Is essential for ATP hydrolysis | Q27732843 | ||
| Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain | Q27733312 | ||
| UCSF Chimera--a visualization system for exploratory research and analysis | Q27860666 | ||
| Molecular chaperones of the Hsp110 family act as nucleotide exchange factors of Hsp70s | Q27931808 | ||
| Protein folding activity of Hsp70 is modified differentially by the hsp40 co-chaperones Sis1 and Ydj1. | Q27932695 | ||
| The yeast Hsp110, Sse1p, exhibits high-affinity peptide binding | Q27932962 | ||
| Mixed Hsp90-cochaperone complexes are important for the progression of the reaction cycle | Q27935652 | ||
| Systematic functional prioritization of protein posttranslational modifications | Q27936051 | ||
| CDK-dependent Hsp70 Phosphorylation controls G1 cyclin abundance and cell-cycle progression | Q27938574 | ||
| Chaperone network in the yeast cytosol: Hsp110 is revealed as an Hsp70 nucleotide exchange factor | Q27940000 | ||
| The C-terminal helices of heat shock protein 70 are essential for J-domain binding and ATPase activation | Q28118960 | ||
| Principles that govern the folding of protein chains | Q28236872 | ||
| A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles | Q28247080 | ||
| The regulation of protein phosphorylation | Q28252420 | ||
| PhosphoSitePlus, 2014: mutations, PTMs and recalibrations | Q28254001 | ||
| Substrate-binding domain conformational dynamics mediate Hsp70 allostery | Q28262765 | ||
| C-terminal phosphorylation of Hsp70 and Hsp90 regulates alternate binding to co-chaperones CHIP and HOP to determine cellular protein folding/degradation balances | Q28271643 | ||
| The variable C-terminus of cysteine string proteins modulates exocytosis and protein-protein interactions | Q28299147 | ||
| Nuclear localization mechanism of Hsp105beta and its possible function in mammalian cells | Q28588659 | ||
| Different localization of Hsp105 family proteins in mammalian cells | Q28594969 | ||
| Molecular chaperones in protein folding and proteostasis | Q29547715 | ||
| The HSP70 chaperone machinery: J proteins as drivers of functional specificity | Q29616140 | ||
| The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation | Q29616141 | ||
| A tissue-specific atlas of mouse protein phosphorylation and expression | Q29616549 | ||
| Molecular chaperones and protein quality control | Q29617795 | ||
| Evolution, energy landscapes and the paradoxes of protein folding. | Q30370011 | ||
| Structural insights into the chaperone activity of the 40-kDa heat shock protein DnaJ: binding and remodeling of a native substrate | Q30429318 | ||
| Asymmetric segregation of protein aggregates is associated with cellular aging and rejuvenation. | Q30481495 | ||
| Multisite phosphorylation disrupts arginine-glutamate salt bridge networks required for binding of cytoplasmic linker-associated protein 2 (CLASP2) to end-binding protein 1 (EB1). | Q30514537 | ||
| Pathways of allosteric regulation in Hsp70 chaperones. | Q30667048 | ||
| In vivo bipartite interaction between the Hsp40 Sis1 and Hsp70 in Saccharomyces cerevisiae | Q31145668 | ||
| Cooperativity within proximal phosphorylation sites is revealed from large-scale proteomics data | Q33526509 | ||
| Interaction of the Hsp70 molecular chaperone, DnaK, with its cochaperone DnaJ. | Q33574540 | ||
| Key features of an Hsp70 chaperone allosteric landscape revealed by ion-mobility native mass spectrometry and double electron-electron resonance | Q33737717 | ||
| Phosphomimetic mutation of cysteine string protein-α increases the rate of regulated exocytosis by modulating fusion pore dynamics in PC12 cells | Q33793296 | ||
| Phosphorylation-induced conformational changes in the retinoblastoma protein inhibit E2F transactivation domain binding | Q33855297 | ||
| The mammalian disaggregase machinery: Hsp110 synergizes with Hsp70 and Hsp40 to catalyze protein disaggregation and reactivation in a cell-free system | Q34056277 | ||
| Phosphorylation in protein-protein binding: effect on stability and function. | Q34095295 | ||
| Phosphorylation of cysteine string protein by protein kinase A. Implications for the modulation of exocytosis | Q34095436 | ||
| The origins of protein phosphorylation | Q34126615 | ||
| Metazoan Hsp70 machines use Hsp110 to power protein disaggregation | Q34300523 | ||
| Small heat shock proteins potentiate amyloid dissolution by protein disaggregases from yeast and humans | Q34313725 | ||
| Extensive lipidation of a Torpedo cysteine string protein. | Q34330430 | ||
| Molecular chaperone functions in protein folding and proteostasis | Q34349321 | ||
| Phosphorylation-regulated degradation of the tumor-suppressor form of PED by chaperone-mediated autophagy in lung cancer cells. | Q34400928 | ||
| Protein posttranslational modifications: the chemistry of proteome diversifications | Q34465021 | ||
| Crucial HSP70 co-chaperone complex unlocks metazoan protein disaggregation | Q34488383 | ||
| Protein aggregation in crowded environments. | Q34532811 | ||
| Hsp70 chaperones accelerate protein translocation and the unfolding of stable protein aggregates by entropic pulling | Q34597309 | ||
| Estimation of macromolecule concentrations and excluded volume effects for the cytoplasm of Escherichia coli | Q34626779 | ||
| Membrane transporters and folate homeostasis: intestinal absorption and transport into systemic compartments and tissues | Q34658009 | ||
| Balance between folding and degradation for Hsp90-dependent client proteins: a key role for CHIP. | Q35121021 | ||
| Client-loading conformation of the Hsp90 molecular chaperone revealed in the cryo-EM structure of the human Hsp90:Hop complex | Q35129923 | ||
| Sequestration of toxic oligomers by HspB1 as a cytoprotective mechanism | Q35139418 | ||
| Compartment-specific aggregases direct distinct nuclear and cytoplasmic aggregate deposition | Q35205006 | ||
| Heterogeneity and dynamics in the assembly of the heat shock protein 90 chaperone complexes | Q35517904 | ||
| A functional DnaK dimer is essential for the efficient interaction with Hsp40 heat shock protein | Q35580778 | ||
| Hsp72 is targeted to the mitotic spindle by Nek6 to promote K-fiber assembly and mitotic progression | Q35594561 | ||
| Hsp70 forms antiparallel dimers stabilized by post-translational modifications to position clients for transfer to Hsp90. | Q35606383 | ||
| Ultrasensitivity part II: multisite phosphorylation, stoichiometric inhibitors, and positive feedback | Q35619490 | ||
| Computational prediction of protein-protein interactions | Q35619593 | ||
| Dependence of endoplasmic reticulum-associated degradation on the peptide binding domain and concentration of BiP. | Q35670486 | ||
| Human Hsp70 Disaggregase Reverses Parkinson's-Linked α-Synuclein Amyloid Fibrils | Q35753373 | ||
| A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates. | Q35843729 | ||
| Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker | Q35847276 | ||
| Anchoring of both PKA-RIIα and 14-3-3θ regulates retinoic acid induced 16 mediated phosphorylation of heat shock protein 70. | Q36021070 | ||
| Functionality of Class A and Class B J-protein co-chaperones with Hsp70. | Q36062416 | ||
| The structure of Legionella pneumophila LegK4 type four secretion system (T4SS) effector reveals a novel dimeric eukaryotic-like kinase | Q36106568 | ||
| Molecular mechanisms used by chaperones to reduce the toxicity of aberrant protein oligomers. | Q36140162 | ||
| Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones | Q36351463 | ||
| Activation of superoxide dismutases: putting the metal to the pedal | Q36530953 | ||
| Identification and characterization of a 66-68-kDa protein as a methotrexate-binding protein in murine leukemia L1210 cells | Q36636433 | ||
| Insights into the structural dynamics of the Hsp110-Hsp70 interaction reveal the mechanism for nucleotide exchange activity | Q36954881 | ||
| Structural and functional diversities between members of the human HSPB, HSPH, HSPA, and DNAJ chaperone families. | Q37192484 | ||
| Cell-to-cell transmission of non-prion protein aggregates. | Q37200740 | ||
| Global analysis of phosphorylation and ubiquitylation cross-talk in protein degradation | Q37404493 | ||
| Multisite protein phosphorylation--from molecular mechanisms to kinetic models | Q37479970 | ||
| An expanding arsenal of experimental methods yields an explosion of insights into protein folding mechanisms | Q37506106 | ||
| Functional divergence and evolutionary turnover in mammalian phosphoproteomes | Q37509572 | ||
| P275 | copyright license | Creative Commons Attribution 4.0 International | Q20007257 |
| P6216 | copyright status | copyrighted | Q50423863 |
| P433 | issue | 17 | |
| P407 | language of work or name | English | Q1860 |
| P304 | page(s) | 4122 | |
| P577 | publication date | 2019-01-01 | |
| 2019-08-23 | |||
| P1433 | published in | International Journal of Molecular Sciences | Q3153277 |
| P1476 | title | The Complex Phosphorylation Patterns that Regulate the Activity of Hsp70 and Its Cochaperones | |
| The Complex Phosphorylation Patterns That Regulate the Activity of Hsp70 and Its Cochaperones | |||
| P478 | volume | 20 |
| Q90154496 | Phosphorylation switches protein disulfide isomerase activity to maintain proteostasis and attenuate ER stress | cites work | P2860 |
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