| scholarly article | Q13442814 |
| P819 | ADS bibcode | 2014PNAS..11113355K |
| P356 | DOI | 10.1073/PNAS.1407086111 |
| P932 | PMC publication ID | 4169939 |
| P698 | PubMed publication ID | 25165400 |
| P50 | author | Benjamin Schuler | Q42316868 |
| Alessandro Barducci | Q45938114 | ||
| P2093 | author name string | Daniel Nettels | |
| Hagen Hofmann | |||
| Bengt Wunderlich | |||
| Ruth Kellner | |||
| P2860 | cites work | The C-terminal (331-376) sequence of Escherichia coli DnaJ is essential for dimerization and chaperone activity: a small angle X-ray scattering study in solution | Q81681117 |
| Hsp70 chaperones: cellular functions and molecular mechanism | Q24644472 | ||
| The Hsp90 chaperone machinery: conformational dynamics and regulation by co-chaperones | Q28249196 | ||
| Kinetics of molecular chaperone action | Q28259596 | ||
| Its substrate specificity characterizes the DnaJ co-chaperone as a scanning factor for the DnaK chaperone. | Q28354756 | ||
| Molecular chaperones in protein folding and proteostasis | Q29547715 | ||
| Molecular chaperones and protein quality control | Q29617795 | ||
| Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK | Q29618850 | ||
| Single-molecule spectroscopy of protein folding dynamics--expanding scope and timescales. | Q30425834 | ||
| FoldEco: a model for proteostasis in E. coli | Q30512981 | ||
| Two-focus fluorescence correlation spectroscopy: a new tool for accurate and absolute diffusion measurements | Q31097044 | ||
| Accurate prediction of DnaK-peptide binding via homology modelling and experimental data | Q33495541 | ||
| Hsp70 chaperones are non-equilibrium machines that achieve ultra-affinity by energy consumption | Q33648403 | ||
| Single-molecule spectroscopy of protein folding in a chaperonin cage. | Q33977568 | ||
| Gymnastics of molecular chaperones | Q34130957 | ||
| Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding | Q34242618 | ||
| Chaperonin-mediated protein folding: fate of substrate polypeptide | Q34285153 | ||
| FRET efficiency distributions of multistate single molecules | Q34336575 | ||
| Hsp70 chaperones accelerate protein translocation and the unfolding of stable protein aggregates by entropic pulling | Q34597309 | ||
| Single-molecule fluorescence reveals sequence-specific misfolding in multidomain proteins | Q35177787 | ||
| Compactness of the denatured state of a fast-folding protein measured by submillisecond small-angle x-ray scattering | Q35615881 | ||
| Ultrafast dynamics of protein collapse from single-molecule photon statistics. | Q35669661 | ||
| Single-molecule fluorescence spectroscopy of protein folding. | Q36180888 | ||
| Polymer scaling laws of unfolded and intrinsically disordered proteins quantified with single-molecule spectroscopy | Q36342960 | ||
| Mechanism of regulation of hsp70 chaperones by DnaJ cochaperones | Q36351463 | ||
| Molecular dimensions and their distributions in early folding intermediates | Q36379840 | ||
| Quantifying internal friction in unfolded and intrinsically disordered proteins with single-molecule spectroscopy. | Q36398007 | ||
| The mechanism of Hsp70 chaperones: (entropic) pulling the models together | Q36880635 | ||
| Random-coil behavior and the dimensions of chemically unfolded proteins | Q37493905 | ||
| How, when and why proteins collapse: the relation to folding | Q37959224 | ||
| Hsp70 chaperone dynamics and molecular mechanism | Q38135145 | ||
| The chaperone function of DnaK requires the coupling of ATPase activity with substrate binding through residue E171. | Q40791442 | ||
| DnaK, DnaJ and GrpE form a cellular chaperone machinery capable of repairing heat-induced protein damage. | Q40874220 | ||
| Unassisted refolding of urea unfolded rhodanese | Q41156149 | ||
| The E. coli dnaK gene product, the hsp70 homolog, can reactivate heat-inactivated RNA polymerase in an ATP hydrolysis-dependent manner | Q41205453 | ||
| Pulsed interleaved excitation | Q42251940 | ||
| The kinetic parameters and energy cost of the Hsp70 chaperone as a polypeptide unfoldase | Q42856450 | ||
| The conformational dynamics of the mitochondrial Hsp70 chaperone | Q43102725 | ||
| Thermosensor action of GrpE. The DnaK chaperone system at heat shock temperatures | Q44363996 | ||
| Microfluidic mixer designed for performing single-molecule kinetics with confocal detection on timescales from milliseconds to minutes | Q44589111 | ||
| A microfluidic mixing system for single-molecule measurements | Q45135920 | ||
| Role of backbone-solvent interactions in determining conformational equilibria of intrinsically disordered proteins | Q46594558 | ||
| Size-dependent disaggregation of stable protein aggregates by the DnaK chaperone machinery. | Q47239818 | ||
| Active solubilization and refolding of stable protein aggregates by cooperative unfolding action of individual hsp70 chaperones | Q47332944 | ||
| Temperature-controlled activity of DnaK-DnaJ-GrpE chaperones: protein-folding arrest and recovery during and after heat shock depends on the substrate protein and the GrpE concentration | Q47870320 | ||
| Investigation of the interaction between DnaK and DnaJ by surface plasmon resonance spectroscopy. | Q51604948 | ||
| CafeMol: A Coarse-Grained Biomolecular Simulator for Simulating Proteins at Work. | Q51607518 | ||
| DnaK functions as a central hub in the E. coli chaperone network. | Q52627947 | ||
| Hsp70 proteins bind Hsp100 regulatory M domains to activate AAA+ disaggregase at aggregate surfaces. | Q54323301 | ||
| Mechanics of Hsp70 chaperones enables differential interaction with client proteins. | Q54369498 | ||
| The power stroke of the DnaK/DnaJ/GrpE molecular chaperone system. | Q54563745 | ||
| The second step of ATP binding to DnaK induces peptide release. | Q54577048 | ||
| ATP-induced protein-Hsp70 complex dissociation requires K+ but not ATP hydrolysis. | Q54649801 | ||
| Dual Function of Protein Confinement in Chaperonin-Assisted Protein Folding | Q58007379 | ||
| Biophysical Characterization of Two Different Stable Misfolded Monomeric Polypeptides That Are Chaperone-Amenable Substrates | Q58428190 | ||
| Intramolecular Distances and Dynamics from the Combined Photon Statistics of Single-Molecule FRET and Photoinduced Electron Transfer | Q59332454 | ||
| Probing Protein-Chaperone Interactions with Single-Molecule Fluorescence Spectroscopy | Q59332539 | ||
| Detection and Analysis of Protein Aggregation with Confocal Single Molecule Fluorescence Spectroscopy | Q59332567 | ||
| The grpE protein of Escherichia coli. Purification and properties | Q69814368 | ||
| Kinetic role of early intermediates in protein folding | Q73070815 | ||
| Control of the DnaK chaperone cycle by substoichiometric concentrations of the co-chaperones DnaJ and GrpE | Q74325958 | ||
| P433 | issue | 37 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | molecular chaperones | Q422496 |
| spectroscopy | Q483666 | ||
| P1104 | number of pages | 6 | |
| P304 | page(s) | 13355-13360 | |
| P577 | publication date | 2014-08-27 | |
| P1433 | published in | Proceedings of the National Academy of Sciences of the United States of America | Q1146531 |
| P1476 | title | Single-molecule spectroscopy reveals chaperone-mediated expansion of substrate protein | |
| P478 | volume | 111 |
| Q34543463 | Alternative modes of client binding enable functional plasticity of Hsp70. |
| Q92740144 | Bacterial Hsp70 resolves misfolded states and accelerates productive folding of a multi-domain protein |
| Q53839637 | Chaperones convert the energy from ATP into the nonequilibrium stabilization of native proteins. |
| Q47698068 | Conformational Heterogeneity and FRET Data Interpretation for Dimensions of Unfolded Proteins |
| Q38611961 | Conformational heterogeneity in the Hsp70 chaperone-substrate ensemble: identified from analysis of NMR-detected titration data |
| Q49819851 | Conserved conformational selection mechanism of Hsp70 chaperone-substrate interactions. |
| Q92039391 | Efficient conversion of chemical energy into mechanical work by Hsp70 chaperones |
| Q52375447 | Extreme disorder in an ultrahigh-affinity protein complex. |
| Q92987534 | Fine Tuning: Effects of Post-Translational Modification on Hsp70 Chaperones |
| Q40558741 | Fluorescence fluctuation of an antigen-antibody complex: circular dichroism, FCS and smFRET of enhanced GFP and its antibody |
| Q46296500 | Formal Models of Biological Systems |
| Q30009135 | Heterogeneous binding of the SH3 client protein to the DnaK molecular chaperone |
| Q38356312 | How hsp70 molecular machines interact with their substrates to mediate diverse physiological functions |
| Q36931060 | Hsp70 biases the folding pathways of client proteins |
| Q35989823 | Mapping the conformation of a client protein through the Hsp70 functional cycle |
| Q26779046 | Metazoan Hsp70-based protein disaggregases: emergence and mechanisms |
| Q33920604 | Modeling Hsp70/Hsp40 interaction by multi-scale molecular simulations and coevolutionary sequence analysis |
| Q101574557 | Molecular dissection of amyloid disaggregation by human HSP70 |
| Q37060996 | Pharmacological chaperone reshapes the energy landscape for folding and aggregation of the prion protein |
| Q47142856 | Probing Small Molecule Binding to Unfolded Polyprotein Based on its Elasticity and Refolding |
| Q41018550 | Promiscuous binding by Hsp70 results in conformational heterogeneity and fuzzy chaperone-substrate ensembles |
| Q59332330 | Rapid Microfluidic Dilution for Single-Molecule Spectroscopy of Low-Affinity Biomolecular Complexes |
| Q48061494 | Rapid Microfluidic Dilution for Single-Molecule Spectroscopy of Low-Affinity Biomolecular Complexes. |
| Q93222384 | Recent advances in the structural and mechanistic aspects of Hsp70 molecular chaperones |
| Q90118044 | Selective Binding of HSC70 and its Co-Chaperones to Structural Hotspots on CFTR |
| Q50577647 | Slow Interconversion in a Heterogeneous Unfolded-State Ensemble of Outer-Membrane Phospholipase A. |
| Q93117098 | The Hsp70 chaperone network |
| Q86176623 | The Hsp90 ensemble: coordinated Hsp90-cochaperone complexes regulate diverse cellular processes |
| Q39200186 | The chaperone toolbox at the single-molecule level: From clamping to confining |
| Q39144895 | The remarkable multivalency of the Hsp70 chaperones |
| Q48024832 | Thermodynamic Bounds on the Ultra- and Infra-affinity of Hsp70 for Its Substrates |
| Q47279123 | X-Linked Inhibitor of Apoptosis Protein (XIAP) is a Client of Heat Shock Protein 70 (Hsp70) and a Biomarker of its Inhibition |
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