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Structural Basis of J Cochaperone Binding and Regulation of Hsp70

https://doi.org/10.1016/j.molcel.2007.08.022

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What this work says

Outgoing claims: the papers this work cites, builds on, or argues with.

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The 70‐kd mammalian heat shock proteins are structurally and functionally related to the uncoating protein that releases clathrin triskelia from coated vesicles.

inferredcites →https://doi.org/10.1002/j.1460-2075.1994.tb06433.xopenalex-snapshot

The chaperone function of DnaK requires the coupling of ATPase activity with substrate binding through residue E171.

inferredcites →https://doi.org/10.1006/jmre.1998.1626openalex-snapshot

Sensitivity Improvement of Transverse Relaxation-Optimized Spectroscopy

inferredcites →https://doi.org/10.1016/0092-8674(86)90532-5openalex-snapshot

Uncoating ATPase is a member of the 70 kilodalton family of stress proteins

inferredcites →https://doi.org/10.1016/j.jmb.2005.03.033openalex-snapshot

NMR Investigations of Allosteric Processes in a Two-domain Thermus thermophilus Hsp70 Molecular Chaperone

inferredcites →https://doi.org/10.1016/j.molcel.2005.09.028openalex-snapshot

Structural Basis of Interdomain Communication in the Hsc70 Chaperone

inferredcites →https://doi.org/10.1016/j.molcel.2007.02.020openalex-snapshot

Hsp70 Chaperone Ligands Control Domain Association via an Allosteric Mechanism Mediated by the Interdomain Linker

inferredcites →https://doi.org/10.1016/s0021-9258(18)99961-8openalex-snapshot

Structural basis of the 70-kilodalton heat shock cognate protein ATP hydrolytic activity. II. Structure of the active site with ADP or ATP bound to wild type and mutant ATPase fragment.

inferredcites →https://doi.org/10.1016/s0065-3233(01)59001-4openalex-snapshot

Hsp70 chaperone machines

inferredcites →https://doi.org/10.1016/s0076-6879(03)74014-2openalex-snapshot

Macromolecular TLS Refinement in REFMAC at Moderate Resolutions

inferredcites →https://doi.org/10.1016/s0092-8674(00)80928-9openalex-snapshot

The Hsp70 and Hsp60 Chaperone Machines

inferredcites →https://doi.org/10.1016/s0896-6273(01)00467-6openalex-snapshot

Uncoating of Clathrin-Coated Vesicles in Presynaptic Terminals

inferredcites →https://doi.org/10.1016/s1097-2765(00)80158-6openalex-snapshot

J Proteins Catalytically Activate Hsp70 Molecules to Trap a Wide Range of Peptide Sequences

inferredcites →https://doi.org/10.1021/bi034270gopenalex-snapshot

Structure−Function Analysis of the Auxilin J-Domain Reveals an Extended Hsc70 Interaction Interface,

inferredcites →https://doi.org/10.1021/bi0354740openalex-snapshot

Structure of the Functional Fragment of Auxilin Required for Catalytic Uncoating of Clathrin-Coated Vesicles

inferredcites →https://doi.org/10.1021/bi060411dopenalex-snapshot

Hsc70 Contacts Helix III of the J Domain from Polyomavirus T Antigens: Addressing a Dilemma in the Chaperone Hypothesis of How They Release E2F from pRb

inferredcites →https://doi.org/10.1021/bi973046mopenalex-snapshot

Structural Replacement of Active Site Monovalent Cations by the ε-Amino Group of Lysine in the ATPase Fragment of Bovine Hsc70,

inferredcites →https://doi.org/10.1021/bi990816gopenalex-snapshot

Mapping the Role of Active Site Residues for Transducing an ATP-Induced Conformational Change in the Bovine 70-kDa Heat Shock Cognate Protein,

inferredcites →https://doi.org/10.1038/378632a0openalex-snapshot

Role of auxilin in uncoating clathrin-coated vesicles

inferredcites →https://doi.org/10.1038/sj.embor.7400172openalex-snapshot

The J‐protein family: modulating protein assembly, disassembly and translocation

inferredcites →https://doi.org/10.1073/pnas.0306708101openalex-snapshot

Crystal structure and characterization of a cytochrome c peroxidase–cytochrome c site-specific cross-link

inferredcites →https://doi.org/10.1073/pnas.0401313101openalex-snapshot

The 70-kDa heat shock protein chaperone nucleotide-binding domain in solution unveiled as a molecular machine that can reorient its functional subdomains

inferredcites →https://doi.org/10.1073/pnas.042670999openalex-snapshot

Mutagenesis of a functional chimeric gene in yeast identifies mutations in the simian virus 40 large T antigen J domain

inferredcites →https://doi.org/10.1073/pnas.91.22.10345openalex-snapshot

The ATP hydrolysis-dependent reaction cycle of the Escherichia coli Hsp70 system DnaK, DnaJ, and GrpE.

inferredcites →https://doi.org/10.1073/pnas.94.23.12366openalex-snapshot

Attenuated T 2 relaxation by mutual cancellation of dipole–dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

inferredcites →https://doi.org/10.1073/pnas.95.26.15223openalex-snapshot

Interaction of the Hsp70 molecular chaperone, DnaK, with its cochaperone DnaJ

inferredcites →https://doi.org/10.1073/pnas.95.26.15229openalex-snapshot

Mutations in the DnaK chaperone affecting interaction with the DnaJ cochaperone

inferredcites →https://doi.org/10.1073/pnas.96.10.5452openalex-snapshot

Mechanism of regulation of Hsp70 chaperones by DnaJ cochaperones

inferredcites →https://doi.org/10.1074/jbc.272.31.19594openalex-snapshot

Functional Interaction of the Auxilin J Domain with the Nucleotide- and Substrate-binding Modules of Hsc70

inferredcites →https://doi.org/10.1074/jbc.274.29.20110openalex-snapshot

Interaction of BiP with the J-domain of the Sec63p Component of the Endoplasmic Reticulum Protein Translocation Complex

inferredcites →https://doi.org/10.1074/jbc.m313967200openalex-snapshot

NMR Study of Nucleotide-induced Changes in the Nucleotide Binding Domain of Thermus thermophilus Hsp70 Chaperone DnaK

inferredcites →https://doi.org/10.1074/jbc.m600847200openalex-snapshot

Amide Hydrogen Exchange Reveals Conformational Changes in Hsp70 Chaperones Important for Allosteric Regulation

inferredcites →https://doi.org/10.1074/jbc.m609020200openalex-snapshot

Allosteric Regulation of Hsp70 Chaperones Involves a Conserved Interdomain Linker

inferredcites →https://doi.org/10.1083/jcb.135.4.925openalex-snapshot

Mechanism of clathrin basket dissociation: separate functions of protein domains of the DnaJ homologue auxilin.

inferredcites →https://doi.org/10.1093/emboj/16.7.1501openalex-snapshot

Substrate specificity of the DnaK chaperone determined by screening cellulose‐bound peptide libraries

inferredcites →https://doi.org/10.1107/s0108767303005488openalex-snapshot

Multiparametric scaling of diffraction intensities

inferredcites →https://doi.org/10.1107/s0108767390002355openalex-snapshot

Slow-cooling protocols for crystallographic refinement by simulated annealing

inferredcites →https://doi.org/10.1107/s0108767390010224openalex-snapshot

Improved methods for building protein models in electron density maps and the location of errors in these models

inferredcites →https://doi.org/10.1107/s0907444900013780openalex-snapshot

An approach to multi-copy search in molecular replacement

inferredcites →https://doi.org/10.1107/s0907444903028956openalex-snapshot

Likelihood-enhanced fast rotation functions

inferredcites →https://doi.org/10.1107/s1744309105040303openalex-snapshot

Crystallization of a functionally intact Hsc70 chaperone

inferredcites →https://doi.org/10.1110/ps.051406805openalex-snapshot

Not all J domains are created equal: Implications for the specificity of Hsp40–Hsp70 interactions

inferredcites →https://doi.org/10.1111/j.1600-0854.2006.00497.xopenalex-snapshot

Keep the Traffic Moving: Mechanism of the Hsp70 Motor

inferredcites →https://doi.org/10.1126/science.272.5268.1606openalex-snapshot

Structural Analysis of Substrate Binding by the Molecular Chaperone DnaK

inferredcites →https://doi.org/10.1126/science.275.5298.387openalex-snapshot

Functional Specificity Among Hsp70 Molecular Chaperones

inferredcites →https://doi.org/10.1126/science.282.5394.1669openalex-snapshot

Structure of a Covalently Trapped Catalytic Complex of HIV-1 Reverse Transcriptase: Implications for Drug Resistance

inferredcites →https://doi.org/10.1126/science.8469987openalex-snapshot

Structure of DNA Polymerase I Klenow Fragment Bound to Duplex DNA

inferredcites →https://doi.org/10.1128/jvi.79.15.9982-9990.2005openalex-snapshot

Genetic Analysis of the Polyomavirus DnaJ Domain

inferredcites →https://doi.org/10.1142/9789811235795_0006openalex-snapshot

Attenuated T2 relaxation by mutual cancellation of dipole–dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution

inferredcites →https://doi.org/10.1379/1466-1268(2003)008<0309:mfrohf>2.0.co;2openalex-snapshot

Mechanisms for regulation of Hsp70 function by Hsp40

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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Hsp70 – a master regulator in protein degradation

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Mixed‐class J‐domain protein scaffolds promote expanded aggregate handling and multivalent Hsp70 engagement during functional disaggregase assembly

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Hsp70 Chaperones

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HSP40 / DNAJ Chaperones

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D NAJC 6 M utations A ssociated W ith E arly‐ O nset P arkinson's D isease

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Biochemical and structural studies on the high affinity of Hsp70 for ADP

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General Structural and Functional Features of Molecular Chaperones

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Molecular chaperones are nanomachines that catalytically unfold misfolded and alternatively folded proteins

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Homology model and potential virus-capsid binding site of a putative HEV receptor Grp78

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Steered molecular dynamics simulation of the binding of the bovine auxilin J domain to the Hsc70 nucleotide-binding domain

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Targeting of Heat Shock Protein HSPA6 (HSP70B′) to the Periphery of Nuclear Speckles is Disrupted by a Transcription Inhibitor Following Thermal Stress in Human Neuronal Cells

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A disulfide-bonded DnaK dimer is maintained in an ATP-bound state

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The remarkable multivalency of the Hsp70 chaperones

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Role of molecular chaperons governing heat stress response in goats

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GDP-bound Rab27a regulates clathrin disassembly through HSPA8 after insulin secretion

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Post-transcriptional Inhibition of Hsc70-4/HSPA8 Expression Leads to Synaptic Vesicle Cycling Defects in Multiple Models of ALS

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ATP-Induced Conformational Changes in Hsp70: Molecular Dynamics and Experimental Validation of an in Silico Predicted Conformation

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Binding of a Small Molecule at a Protein–Protein Interface Regulates the Chaperone Activity of Hsp70–Hsp40

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Fine-Tuning Multiprotein Complexes Using Small Molecules

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Nucleotide-Dependent Interactions within a Specialized Hsp70/Hsp40 Complex Involved in Fe–S Cluster Biogenesis

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Heat Shock Protein 70 (Hsp70) as an Emerging Drug Target

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Regulated association of misfolded endoplasmic reticulum lumenal proteins with P58/DNAJc3

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Structure of clathrin coat with bound Hsc70 and auxilin: mechanism of Hsc70‐facilitated disassembly

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An interdomain sector mediating allostery in Hsp70 molecular chaperones

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Structural characterization of the substrate transfer mechanism in Hsp70/Hsp90 folding machinery mediated by Hop

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The HSP70 chaperone machinery: J proteins as drivers of functional specificity

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Chaperone machines for protein folding, unfolding and disaggregation

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Allosteric opening of the polypeptide-binding site when an Hsp70 binds ATP

inferred← citeshttps://doi.org/10.1038/nsmb.2608openalex-snapshot

Structure and function of Hip, an attenuator of the Hsp70 chaperone cycle

inferred← citeshttps://doi.org/10.1038/nsmb.3272openalex-snapshot

Clathrin-coat disassembly illuminates the mechanisms of Hsp70 force generation

inferred← citeshttps://doi.org/10.1038/nsmb.3349openalex-snapshot

Structural insights into a unique Hsp70-Hsp40 interaction in the eukaryotic ribosome-associated complex

inferred← citeshttps://doi.org/10.1038/s41422-021-00526-5openalex-snapshot

Hsp70 chaperones TDP-43 in dynamic, liquid-like phase and prevents it from amyloid aggregation

inferred← citeshttps://doi.org/10.1038/s41467-021-26189-9openalex-snapshot

Structural and functional consequences of NEDD8 phosphorylation

inferred← citeshttps://doi.org/10.1038/s41467-023-41150-8openalex-snapshot

The self-association equilibrium of DNAJA2 regulates its interaction with unfolded substrate proteins and with Hsc70

inferred← citeshttps://doi.org/10.1038/s41467-024-44933-9openalex-snapshot

Structure of the M. tuberculosis DnaK−GrpE complex reveals how key DnaK roles are controlled

inferred← citeshttps://doi.org/10.1038/s41467-026-77686-8openalex-snapshot

Quantitative proteomics reveals coordinated changes in the proteome during replicative senescence

inferred← citeshttps://doi.org/10.1038/s41593-019-0530-0openalex-snapshot

Exome sequencing in amyotrophic lateral sclerosis implicates a novel gene, DNAJC7, encoding a heat-shock protein

inferred← citeshttps://doi.org/10.1038/s41594-023-00973-1openalex-snapshot

Structural inventory of cotranslational protein folding by the eukaryotic RAC complex

inferred← citeshttps://doi.org/10.1038/s44319-025-00376-xopenalex-snapshot

HSC70 coordinates COP9 signalosome and SCF ubiquitin ligase activity to enable a prompt stress response

inferred← citeshttps://doi.org/10.1039/9781849731201-00216openalex-snapshot

Non-Canonical Ligand-Binding Events as Detected by NMR

inferred← citeshttps://doi.org/10.1039/9781849739689-00065openalex-snapshot

Structure and Function of Hsp70 Molecular Chaperones

inferred← citeshttps://doi.org/10.1039/c2mb25145kopenalex-snapshot

Molecular chaperones DnaK and DnaJ share predicted binding sites on most proteins in the E. coli proteome

inferred← citeshttps://doi.org/10.1042/bcj20200434openalex-snapshot

Structural–functional diversity of malaria parasite's PfHSP70-1 and PfHSP40 chaperone pair gives an edge over human orthologs in chaperone-assisted protein folding

inferred← citeshttps://doi.org/10.1042/bj20110500openalex-snapshot

Structural analysis of the Sil1–Bip complex reveals the mechanism for Sil1 to function as a nucleotide-exchange factor

inferred← citeshttps://doi.org/10.1042/bst20200381openalex-snapshot

The HSP70 chaperone as sensor of the NEDD8 cycle upon DNA damage

inferred← citeshttps://doi.org/10.1073/pnas.0702132105openalex-snapshot

BiP mutants that are unable to interact with endoplasmic reticulum DnaJ proteins provide insights into interdomain interactions in BiP

inferred← citeshttps://doi.org/10.1073/pnas.0900746106openalex-snapshot

Identification of a consensus motif in substrates bound by a Type I Hsp40

inferred← citeshttps://doi.org/10.1073/pnas.1014448108openalex-snapshot

Allosteric signal transmission in the nucleotide-binding domain of 70-kDa heat shock protein (Hsp70) molecular chaperones

inferred← citeshttps://doi.org/10.1073/pnas.1111220108openalex-snapshot

Heat shock protein 70 kDa chaperone/DnaJ cochaperone complex employs an unusual dynamic interface

inferred← citeshttps://doi.org/10.1073/pnas.1120597109openalex-snapshot

Evaluation of competing J domain:Hsp70 complex models in light of existing mutational and NMR data

inferred← citeshttps://doi.org/10.1073/pnas.1121554109openalex-snapshot

Reply to Sousa et al.: Evaluation of competing J domain:Hsp70 complex models in light of methods used

inferred← citeshttps://doi.org/10.1073/pnas.1811105115openalex-snapshot

Allosteric landscapes of eukaryotic cytoplasmic Hsp70s are shaped by evolutionary tuning of key interfaces

inferred← citeshttps://doi.org/10.1073/pnas.1914376117openalex-snapshot

Kinetics of the conformational cycle of Hsp70 reveals the importance of the dynamic and heterogeneous nature of Hsp70 for its function

inferred← citeshttps://doi.org/10.1073/pnas.2218217120openalex-snapshot

Data-driven large-scale genomic analysis reveals an intricate phylogenetic and functional landscape in J-domain proteins

inferred← citeshttps://doi.org/10.1073/pnas.2314781120openalex-snapshot

Human proteins curing yeast prions

inferred← citeshttps://doi.org/10.1074/jbc.m109.061697openalex-snapshot

ATPase Domain and Interdomain Linker Play a Key Role in Aggregation of Mitochondrial Hsp70 Chaperone Ssc1

inferred← citeshttps://doi.org/10.1074/jbc.m110.102186openalex-snapshot

J Domain Co-chaperone Specificity Defines the Role of BiP during Protein Translocation

inferred← citeshttps://doi.org/10.1074/jbc.m110.124149openalex-snapshot

Mutagenesis Reveals the Complex Relationships between ATPase Rate and the Chaperone Activities of Escherichia coli Heat Shock Protein 70 (Hsp70/DnaK)

inferred← citeshttps://doi.org/10.1074/jbc.m111.275057openalex-snapshot

Unique Peptide Substrate Binding Properties of 110-kDa Heat-shock Protein (Hsp110) Determine Its Distinct Chaperone Activity

inferred← citeshttps://doi.org/10.1074/jbc.m111.294728openalex-snapshot

The C-terminal Helices of Heat Shock Protein 70 Are Essential for J-domain Binding and ATPase Activation

inferred← citeshttps://doi.org/10.1074/jbc.m112.339655openalex-snapshot

Structure and Mechanistic Insights into Novel Iron-mediated Moonlighting Functions of Human J-protein Cochaperone, Dph4

inferred← citeshttps://doi.org/10.1074/jbc.m113.521997openalex-snapshot

Binding of Human Nucleotide Exchange Factors to Heat Shock Protein 70 (Hsp70) Generates Functionally Distinct Complexes in Vitro

inferred← citeshttps://doi.org/10.1074/jbc.m114.596288openalex-snapshot

A Functional DnaK Dimer Is Essential for the Efficient Interaction with Hsp40 Heat Shock Protein

inferred← citeshttps://doi.org/10.1074/jbc.m803557200openalex-snapshot

Impaired Interdomain Communication in Mitochondrial Hsp70 Results in the Loss of Inward-directed Translocation Force

inferred← citeshttps://doi.org/10.1074/jbc.m803923200openalex-snapshot

Functional Divergence between Co-chaperones of Hsc70

inferred← citeshttps://doi.org/10.1074/mcp.m116.058131openalex-snapshot

Novel Entropically Driven Conformation-specific Interactions with Tomm34 Protein Modulate Hsp70 Protein Folding and ATPase Activities

inferred← citeshttps://doi.org/10.1080/07391102.2013.834849openalex-snapshot

Plasmodium falciparumHsp70-x: a heat shock protein at the host–parasite interface

inferred← citeshttps://doi.org/10.1083/jcb.201205012openalex-snapshot

Biogenesis of the mitochondrial Hsp70 chaperone

inferred← citeshttps://doi.org/10.1093/jb/mvp194openalex-snapshot

Mechanism and components of endoplasmic reticulum-associated degradation

inferred← citeshttps://doi.org/10.1093/jmcb/mjac037openalex-snapshot

The complex of Fas-associated factor 1 with Hsp70 stabilizes the adherens junction integrity by suppressing RhoA activation

inferred← citeshttps://doi.org/10.1093/pcp/pcq089openalex-snapshot

Crystallographic and Functional Analyses of J-Domain of JAC1 Essential for Chloroplast Photorelocation Movement in Arabidopsis thaliana

inferred← citeshttps://doi.org/10.1101/2024.06.27.600868openalex-snapshot

Inclusion of Hsp70 co-chaperone and RNA binding activities facilitate optimal function of spliceosomal disassembly factor Cwf23 in intron-rich Schizosaccharomyces pombe

inferred← citeshttps://doi.org/10.1101/2025.11.14.688390openalex-snapshot

Dephosphorylation of YES kinase-mediated co-chaperone DNAJB6b phosphorylation attenuates tau protein aggregation

inferred← citeshttps://doi.org/10.1101/583864openalex-snapshot

The NEDD8 cycle controlled by NEDP1 upon DNA damage is a regulatory module of the HSP70 ATPase activity

inferred← citeshttps://doi.org/10.1101/830802openalex-snapshot

Mutations in Auxilin cause parkinsonism via impaired clathrin-mediated trafficking at the Golgi apparatus and synapse

inferred← citeshttps://doi.org/10.1101/cshperspect.a016725openalex-snapshot

Molecular Structure, Function, and Dynamics of Clathrin-Mediated Membrane Traffic

inferred← citeshttps://doi.org/10.1107/s0907444909053979openalex-snapshot

Direct inter-subdomain interactions switch between the closed and open forms of the Hsp70 nucleotide-binding domain in the nucleotide-free state

inferred← citeshttps://doi.org/10.1107/s0907444913010640openalex-snapshot

Combining crystallography and EPR: crystal and solution structures of the multidomain cochaperone DnaJ

inferred← citeshttps://doi.org/10.1111/febs.14936openalex-snapshot

DNAJC proteins and pathways to parkinsonism

inferred← citeshttps://doi.org/10.1111/febs.70535openalex-snapshot

Hsp70 diversification and repurposing across the tree of life: Lessons from the evolutionary and mechanistic trajectory of the Hsp70–Hsp110 chaperone system

inferred← citeshttps://doi.org/10.1111/tra.12085openalex-snapshot

Hsc70‐induced Changes in Clathrin‐Auxilin Cage Structure Suggest a Role for Clathrin Light Chains in Cage Disassembly

inferred← citeshttps://doi.org/10.1128/jvi.00807-22openalex-snapshot

Hsp70 Inhibits the Replication of Fowl Adenovirus Serotype 4 by Suppressing Viral Hexon with the Assistance of DnaJC7

inferred← citeshttps://doi.org/10.1128/mcb.00628-19openalex-snapshot

Growth-Regulated Hsp70 Phosphorylation Regulates Stress Responses and Prion Maintenance

inferred← citeshttps://doi.org/10.1128/mcb.00842-09openalex-snapshot

Cwc23, an Essential J Protein Critical for Pre-mRNA Splicing with a Dispensable J Domain

inferred← citeshttps://doi.org/10.1128/mmbr.05018-11openalex-snapshot

Biology of the Heat Shock Response and Protein Chaperones: Budding Yeast (Saccharomyces cerevisiae) as a Model System

inferred← citeshttps://doi.org/10.1134/s1021443721010167openalex-snapshot

Molecular Cloning and Expression Analysis of Auxilin-Like Gene StAL1 in Potato (Solanum tuberosum)

inferred← citeshttps://doi.org/10.1139/o09-175openalex-snapshot

Mechanisms of the Hsp70 chaperone systemThis paper is one of a selection of papers published in this special issue entitled “Canadian Society of Biochemistry, Molecular & Cellular Biology 52nd Annual Meeting — Protein Folding: Principles and Diseases” and has undergone the Journal's usual peer…

inferred← citeshttps://doi.org/10.1146/annurev-biochem-060208-092442openalex-snapshot

Molecular Chaperone Functions in Protein Folding and Proteostasis

inferred← citeshttps://doi.org/10.1146/annurev-biochem-060713-035829openalex-snapshot

Bringing Dynamic Molecular Machines into Focus by Methyl-TROSY NMR

inferred← citeshttps://doi.org/10.11606/d.41.2020.tde-27112019-154350openalex-snapshot

Efeito das chaperonas BAG2 e DNAJB6 na degradação proteica em modelos celulares de doenças neurodegenerativas

inferred← citeshttps://doi.org/10.1177/1087057110380571openalex-snapshot

High-Throughput Screen for Escherichia coli Heat Shock Protein 70 (Hsp70/DnaK): ATPase Assay in Low Volume by Exploiting Energy Transfer

inferred← citeshttps://doi.org/10.1186/1743-422x-8-471openalex-snapshot

DnaJ homolog Hdj2 Facilitates Japanese Encephalitis Virus Replication

inferred← citeshttps://doi.org/10.1247/csf.12017openalex-snapshot

A Novel Mammalian ER-located J-protein, DNAJB14, Can Accelerate ERAD of Misfolded Membrane Proteins

inferred← citeshttps://doi.org/10.1371/journal.pbio.3000606openalex-snapshot

Proteome-wide identification of HSP70/HSC70 chaperone clients in human cells

inferred← citeshttps://doi.org/10.1371/journal.pcbi.1000931openalex-snapshot

Role of Hsp70 ATPase Domain Intrinsic Dynamics and Sequence Evolution in Enabling its Functional Interactions with NEFs

inferred← citeshttps://doi.org/10.1371/journal.pcbi.1003624openalex-snapshot

ATPase Subdomain IA Is a Mediator of Interdomain Allostery in Hsp70 Molecular Chaperones

inferred← citeshttps://doi.org/10.1371/journal.pcbi.1007913openalex-snapshot

Two-step mechanism of J-domain action in driving Hsp70 function

inferred← citeshttps://doi.org/10.1371/journal.pone.0022337openalex-snapshot

The Crystal Structure of the Human Co-Chaperone P58IPK

inferred← citeshttps://doi.org/10.1371/journal.pone.0033980openalex-snapshot

The Lid Domain of Caenorhabditis elegans Hsc70 Influences ATP Turnover, Cofactor Binding and Protein Folding Activity

inferred← citeshttps://doi.org/10.1371/journal.pone.0047521openalex-snapshot

Transcription Elongation Factor GreA Has Functional Chaperone Activity

inferred← citeshttps://doi.org/10.1371/journal.pone.0103518openalex-snapshot

Crystal Structure of the Stress-Inducible Human Heat Shock Protein 70 Substrate-Binding Domain in Complex with Peptide Substrate

inferred← citeshttps://doi.org/10.1371/journal.pone.0110443openalex-snapshot

Rapid Isolation of Extracellular Vesicles from Cell Culture and Biological Fluids Using a Synthetic Peptide with Specific Affinity for Heat Shock Proteins

inferred← citeshttps://doi.org/10.1523/jneurosci.4505-12.2013openalex-snapshot

A Role for an Hsp70 Nucleotide Exchange Factor in the Regulation of Synaptic Vesicle Endocytosis

inferred← citeshttps://doi.org/10.1534/genetics.120.303190openalex-snapshot

The Yeast Hsp70 Cochaperone Ydj1 Regulates Functional Distinction of Ssa Hsp70s in the Hsp90 Chaperoning Pathway

inferred← citeshttps://doi.org/10.1677/jme-08-0116openalex-snapshot

From hatching to dispatching: the multiple cellular roles of the Hsp70 molecular chaperone machinery

inferred← citeshttps://doi.org/10.17957/ijab/14.0024openalex-snapshot

Relationships between DNAJA1 Expression and Beef Tenderness: Effects of Electrical Stimulation and Post-mortem Aging in two Muscles

inferred← citeshttps://doi.org/10.18632/oncotarget.4954openalex-snapshot

The joining of the Hsp90 and Hsp70 chaperone cycles yields transient interactions and stable intermediates: insights from mass spectrometry

inferred← citeshttps://doi.org/10.21007/etd.cghs.2008.0155openalex-snapshot

Studies to Characterize the Requirements for the Binding and Release of ERdj3, a Mammalian ER DnaJ Homolog, from Substrates

inferred← citeshttps://doi.org/10.2141/jpsa.2023012openalex-snapshot

RNA-sequencing Reveals Differentially Expressed Genes of Laying Hens Fed Baihu Decoction Under Heat Shock

inferred← citeshttps://doi.org/10.21708/avb.2013.7.4.3273openalex-snapshot

Heat shock protein Hsp70: structure and action in response to cellular stress

inferred← citeshttps://doi.org/10.2174/092986609788490230openalex-snapshot

Hsp70 Structure, Function, Regulation and Influence on Yeast Prions

inferred← citeshttps://doi.org/10.2174/092986611794475057openalex-snapshot

The Molecular Chaperone Hsp70 Family Members Function by a Bidirectional Heterotrophic Allosteric Mechanism

inferred← citeshttps://doi.org/10.32607/20758251-2010-2-4-66-71openalex-snapshot

Modeling of the Full-Size 3D Structure of Human Chaperone Hsp70 and Study of Its Interdomain Interactions

inferred← citeshttps://doi.org/10.33612/diss.220760500openalex-snapshot

Molecular and clinical determinants of pathogenic protein aggregation

inferred← citeshttps://doi.org/10.3389/fcell.2022.906453openalex-snapshot

Safeguarding Lysosomal Homeostasis by DNAJC5/CSPα-Mediated Unconventional Protein Secretion and Endosomal Microautophagy

inferred← citeshttps://doi.org/10.3389/fgene.2018.00445openalex-snapshot

Environmental Stress Responses of DnaJA1, DnaJB12 and DnaJC8 in Apis cerana cerana

inferred← citeshttps://doi.org/10.3389/fgene.2020.00821openalex-snapshot

A Novel Potentially Pathogenic Rare Variant in the DNAJC7 Gene Identified in Amyotrophic Lateral Sclerosis Patients From Mainland China

inferred← citeshttps://doi.org/10.3389/fgene.2021.689922openalex-snapshot

Deciphering Network Crosstalk: The Current Status and Potential of miRNA Regulatory Networks on the HSP40 Molecular Chaperone Network

inferred← citeshttps://doi.org/10.3389/fmolb.2014.00012openalex-snapshot

Structural mechanisms of chaperone mediated protein disaggregation

inferred← citeshttps://doi.org/10.3389/fmolb.2015.00035openalex-snapshot

DNAJs: more than substrate delivery to HSPA

inferred← citeshttps://doi.org/10.3389/fmolb.2022.1045616openalex-snapshot

The role of heat shock proteins in preventing amyloid toxicity

inferred← citeshttps://doi.org/10.3389/fmolb.2023.1216192openalex-snapshot

The Plasmodium falciparum exported J domain proteins fine-tune human and malarial Hsp70s: pathological exploitation of proteostasis machinery

inferred← citeshttps://doi.org/10.3389/fncel.2018.00027openalex-snapshot

Revisiting the Role of Clathrin-Mediated Endoytosis in Synaptic Vesicle Recycling

inferred← citeshttps://doi.org/10.3389/fnins.2017.00248openalex-snapshot

The Role of Co-chaperones in Synaptic Proteostasis and Neurodegenerative Disease

inferred← citeshttps://doi.org/10.3389/fphys.2022.1068873openalex-snapshot

Characterisation of the heat shock protein Tid and its involvement in stress response regulation in Apis cerana

inferred← citeshttps://doi.org/10.3389/fpls.2023.1279540openalex-snapshot

Exploration of the truncated cytosolic Hsp70 in plants - unveiling the diverse T1 lineage and the conserved T2 lineage

inferred← citeshttps://doi.org/10.3390/biom12101391openalex-snapshot

Leveraging the Structure of DNAJA1 to Discover Novel Potential Pancreatic Cancer Therapies

inferred← citeshttps://doi.org/10.3390/biom9100543openalex-snapshot

The Link That Binds: The Linker of Hsp70 as a Helm of the Protein’s Function

inferred← citeshttps://doi.org/10.3390/cancers3043921openalex-snapshot

Inducible Hsp70 in the Regulation of Cancer Cell Survival: Analysis of Chaperone Induction, Expression and Activity

inferred← citeshttps://doi.org/10.3390/cells14030204openalex-snapshot

More than Just Protein Folding: The Epichaperome, Mastermind of the Cancer Cell

inferred← citeshttps://doi.org/10.3390/ijms25084209openalex-snapshot

Heat Shock Response and Heat Shock Proteins: Current Understanding and Future Opportunities in Human Diseases

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