scholarly article | Q13442814 |
P50 | author | Petr Man | Q39186041 |
Julien Marcoux | Q42290757 | ||
Josef Chmelík | Q44019233 | ||
Petr Müller | Q57211611 | ||
Filip Trcka | Q83398820 | ||
Bořivoj Vojtěšek | Q91106258 | ||
P2093 | author name string | Michal Durech | |
Tomas Klumpler | |||
Pavla Vankova | |||
Alan Kadek | |||
Jiri Hausner | |||
Veronika Martinkova | |||
P2860 | cites work | Crystal structure of the stress-inducible human heat shock protein 70 substrate-binding domain in complex with peptide substrate | Q21090602 |
Chaperoned ubiquitylation--crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex | Q24296990 | ||
BAG-1 modulates the chaperone activity of Hsp70/Hsc70. | Q24313113 | ||
Regulated release of ERdj3 from unfolded proteins by BiP | Q24323860 | ||
Regulated association of misfolded endoplasmic reticulum lumenal proteins with P58/DNAJc3 | Q24324029 | ||
Determination of amide hydrogen exchange by mass spectrometry: a new tool for protein structure elucidation | Q24675910 | ||
The nucleotide exchange factors of Hsp70 molecular chaperones | Q26766367 | ||
Protein homeostasis as a therapeutic target for diseases of protein conformation | Q27003283 | ||
Structural insights into substrate binding by the molecular chaperone DnaK | Q27621983 | ||
Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine | Q27622332 | ||
Structure of a Bag/Hsc70 complex: convergent functional evolution of Hsp70 nucleotide exchange factors | Q27630011 | ||
Insights into Hsp70 Chaperone Activity from a Crystal Structure of the Yeast Hsp110 Sse1 | Q27648730 | ||
Structure of the Hsp110:Hsc70 nucleotide exchange machine | Q27650814 | ||
Novel adenosine-derived inhibitors of 70 kDa heat shock protein, discovered through structure-based design | Q27654001 | ||
The C-terminal BAG domain of BAG5 induces conformational changes of the Hsp70 nucleotide-binding domain for ADP-ATP exchange | Q27660188 | ||
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 | ||
Structure and function of Hip, an attenuator of the Hsp70 chaperone cycle | Q27685147 | ||
NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction | Q27758070 | ||
UCSF Chimera--a visualization system for exploratory research and analysis | Q27860666 | ||
Comparative protein modelling by satisfaction of spatial restraints | Q27860866 | ||
Molecular evolution of the HSP70 multigene family | Q27940113 | ||
The human HSP70 family of chaperones: where do we stand? | Q28071416 | ||
Substrate-binding domain conformational dynamics mediate Hsp70 allostery | Q28262765 | ||
Close and Allosteric Opening of the Polypeptide-Binding Site in a Human Hsp70 Chaperone BiP | Q28270851 | ||
Effect of constitutive 70-kDa heat shock protein polymerization on its interaction with protein substrate | Q28282091 | ||
Large-Scale Conformational Transitions and Dimerization Are Encoded in the Amino-Acid Sequences of Hsp70 Chaperones | Q28547971 | ||
Pathways of chaperone-mediated protein folding in the cytosol | Q29618887 | ||
Are molecular weights of proteins determined by superose 12 column chromatography correct? | Q33205462 | ||
Ionic contacts at DnaK substrate binding domain involved in the allosteric regulation of lid dynamics | Q33231727 | ||
High-throughput screen for small molecules that modulate the ATPase activity of the molecular chaperone DnaK. | Q33300867 | ||
Hsp70 chaperones are non-equilibrium machines that achieve ultra-affinity by energy consumption | Q33648403 | ||
The Hsp70/Hsp90 Chaperone Machinery in Neurodegenerative Diseases | Q33692255 | ||
Quaternary dynamics and plasticity underlie small heat shock protein chaperone function | Q33719580 | ||
The lid domain of Caenorhabditis elegans Hsc70 influences ATP turnover, cofactor binding and protein folding activity. | Q34221854 | ||
Hsp70 oligomerization is mediated by an interaction between the interdomain linker and the substrate-binding domain | Q34808252 | ||
Investigating the interaction between the neonatal Fc receptor and monoclonal antibody variants by hydrogen/deuterium exchange mass spectrometry | Q34884133 | ||
Versatile TPR domains accommodate different modes of target protein recognition and function | Q35056237 | ||
Balance between folding and degradation for Hsp90-dependent client proteins: a key role for CHIP. | Q35121021 | ||
A bipartite interaction between Hsp70 and CHIP regulates ubiquitination of chaperoned client proteins | Q35152082 | ||
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 | ||
Hsp70 forms antiparallel dimers stabilized by post-translational modifications to position clients for transfer to Hsp90. | Q35606383 | ||
Hsp70 chaperone ligands control domain association via an allosteric mechanism mediated by the interdomain linker | Q35847276 | ||
Functionality of Class A and Class B J-protein co-chaperones with Hsp70. | Q36062416 | ||
Physiological modulation of BiP activity by trans-protomer engagement of the interdomain linker | Q36169640 | ||
In Vivo Conformational Dynamics of Hsp90 and Its Interactors | Q37233917 | ||
Mechanisms of the Hsp70 chaperone system | Q37746993 | ||
Hsp70 in cancer: back to the future | Q38263003 | ||
Characterization of a lidless form of the molecular chaperone DnaK: deletion of the lid increases peptide on- and off-rate constants | Q38300849 | ||
The assembly and intermolecular properties of the Hsp70-Tomm34-Hsp90 molecular chaperone complex | Q38609122 | ||
ATSAS 2.8: a comprehensive data analysis suite for small-angle scattering from macromolecular solutions | Q38624857 | ||
The E3 ubiquitin ligase CHIP mediates ubiquitination and proteasomal degradation of PRMT5. | Q38812367 | ||
Bag1 functions in vivo as a negative regulator of Hsp70 chaperone activity | Q39450832 | ||
Blue light-induced LOV domain dimerization enhances the affinity of Aureochrome 1a for its target DNA sequence | Q40120168 | ||
Hsp70 Reduces alpha-Synuclein Aggregation and Toxicity | Q40573441 | ||
Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1. | Q40806764 | ||
Novel Entropically Driven Conformation-specific Interactions with Tomm34 Protein Modulate Hsp70 Protein Folding and ATPase Activities | Q41098204 | ||
A disulfide-bonded DnaK dimer is maintained in an ATP-bound state | Q41834098 | ||
Allosteric fine-tuning of the conformational equilibrium poises the chaperone BiP for post-translational regulation | Q42637818 | ||
Binding of ATP and ATP analogues to the uncoating ATPase Hsc70 (70 kDa heat-shock cognate protein). | Q42983805 | ||
Tuning of chaperone activity of Hsp70 proteins by modulation of nucleotide exchange. | Q43589335 | ||
Tom34: a cytosolic cochaperone of the Hsp90/Hsp70 protein complex involved in mitochondrial protein import | Q43805347 | ||
Destabilization of peptide binding and interdomain communication by an E543K mutation in the bovine 70-kDa heat shock cognate protein, a molecular chaperone. | Q43997162 | ||
Solution small-angle X-ray scattering study of the molecular chaperone Hsc70 and its subfragments | Q44420567 | ||
Conformation transitions of the polypeptide-binding pocket support an active substrate release from Hsp70s | Q44710284 | ||
The combination of hydrogen/deuterium exchange or chemical cross-linking techniques with mass spectrometry: mapping of human 14-3-3ζ homodimer interface | Q45226549 | ||
Hsp110 cooperates with different cytosolic HSP70 systems in a pathway for de novo folding | Q46203005 | ||
Direct comparison of a stable isolated Hsp70 substrate-binding domain in the empty and substrate-bound states | Q46794845 | ||
Dimerization of the human E3 ligase CHIP via a coiled-coil domain is essential for its activity. | Q47070627 | ||
Molecular Mechanism of J-Domain-Triggered ATP Hydrolysis by Hsp70 Chaperones | Q47228277 | ||
Role of salt bridges in the dimer interface of 14-3-3ζ in dimer dynamics, N-terminal α-helical order, and molecular chaperone activity | Q47434201 | ||
Enhanced tau pathology via RanBP9 and Hsp90/Hsc70 chaperone complexes. | Q47670971 | ||
Characterization of homodimer interfaces with cross-linking mass spectrometry and isotopically labeled proteins. | Q48125124 | ||
Cancer cell responses to Hsp70 inhibitor JG-98: Comparison with Hsp90 inhibitors and finding synergistic drug combinations. | Q50354200 | ||
Investigation of the interaction between DnaK and DnaJ by surface plasmon resonance spectroscopy. | Q51604948 | ||
Substrate Binding Switches the Conformation at the Lynchpin Site in the Substrate-Binding Domain of Human Hsp70 to Enable Allosteric Interdomain Communication. | Q52689024 | ||
Mechanics of Hsp70 chaperones enables differential interaction with client proteins. | Q54369498 | ||
Effect of nucleotides, peptides, and unfolded proteins on the self-association of the molecular chaperone HSC70 | Q71245482 | ||
Polymerization of 70-kDa Heat Shock Protein by Yeast DnaJ in ATP | Q72055097 | ||
Multistep mechanism of substrate binding determines chaperone activity of Hsp70 | Q73943514 | ||
Proteasome inhibition leads to the activation of all members of the heat-shock-factor family | Q77144797 | ||
Structural insight into the calcium ion modulated interdomain electron transfer in cellobiose dehydrogenase | Q87094361 | ||
P433 | issue | 2 | |
P304 | page(s) | 320-337 | |
P577 | publication date | 2018-11-20 | |
P1433 | published in | Molecular & Cellular Proteomics | Q6895932 |
P1476 | title | Human Stress-inducible Hsp70 Has a High Propensity to Form ATP-dependent Antiparallel Dimers That Are Differentially Regulated by Cochaperone Binding | |
P478 | volume | 18 |
Q90293433 | Oligomerization of Hsp70: Current Perspectives on Regulation and Function |
Q89599057 | Structural Dynamics of Lytic Polysaccharide Monooxygenase during Catalysis |
Q90384798 | The Link That Binds: The Linker of Hsp70 as a Helm of the Protein's Function |
Q64113400 | Tomm34 is commonly expressed in epithelial ovarian cancer and associates with tumour type and high FIGO stage |
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