scholarly article | Q13442814 |
P2093 | author name string | H Zhou | |
F W Dahlquist | |||
D F Lowry | |||
G C Flynn | |||
E B Bertelsen | |||
P2860 | cites work | Eukaryotic homologues of Escherichia coli dnaJ: a diverse protein family that functions with hsp70 stress proteins | Q24622449 |
Three-dimensional structure of the ATPase fragment of a 70K heat-shock cognate protein | Q27667092 | ||
Structural analysis of substrate binding by the molecular chaperone DnaK | Q27732810 | ||
NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone | Q27733313 | ||
Interplay of structure and disorder in cochaperonin mobile loops | Q27733719 | ||
Crystal structure of the nucleotide exchange factor GrpE bound to the ATPase domain of the molecular chaperone DnaK | Q27735852 | ||
Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy | Q27739077 | ||
NMR solution structure of the 21 kDa chaperone protein DnaK substrate binding domain: a preview of chaperone-protein interaction | Q27758070 | ||
Backbone dynamics of a free and phosphopeptide-complexed Src homology 2 domain studied by 15N NMR relaxation | Q27860508 | ||
Molecular evolution of the HSP70 multigene family | Q27940113 | ||
A mitochondrial homolog of bacterial GrpE interacts with mitochondrial hsp70 and is essential for viability | Q27972960 | ||
Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium | Q28253146 | ||
Heteronuclear three-dimensional NMR spectroscopy of the inflammatory protein C5a | Q28276423 | ||
Hip, a novel cochaperone involved in the eukaryotic hsc70/hsp40 reaction cycle | Q28569622 | ||
Backbone dynamics of proteins as studied by 15N inverse detected heteronuclear NMR spectroscopy: application to staphylococcal nuclease | Q29547582 | ||
Protein folding in the cell | Q29547792 | ||
Primary structure effects on peptide group hydrogen exchange | Q29614750 | ||
Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK | Q29618850 | ||
Characterization of the backbone dynamics of folded and denatured states of an SH3 domain | Q30176612 | ||
Comparison of the backbone dynamics of a folded and an unfolded SH3 domain existing in equilibrium in aqueous buffer. | Q30193714 | ||
The peptide-binding domain of the chaperone protein Hsc70 has an unusual secondary structure topology | Q30418425 | ||
Mutations altering heat shock specific subunit of RNA polymerase suppress major cellular defects of E. coli mutants lacking the DnaK chaperone | Q33923343 | ||
Analysis of the backbone dynamics of interleukin-1 beta using two-dimensional inverse detected heteronuclear 15N-1H NMR spectroscopy | Q34246390 | ||
The role of molecular chaperones in protein folding | Q34368042 | ||
New methods of structure refinement for macromolecular structure determination by NMR. | Q34469265 | ||
NMR structure determination of the Escherichia coli DnaJ molecular chaperone: secondary structure and backbone fold of the N-terminal region (residues 2-108) containing the highly conserved J domain. | Q35909875 | ||
Cooperation of GroEL/GroES and DnaK/DnaJ heat shock proteins in preventing protein misfolding in Escherichia coli | Q37276384 | ||
The conserved G/F motif of the DnaJ chaperone is necessary for the activation of the substrate binding properties of the DnaK chaperone | Q38298937 | ||
Identification of the peptide binding domain of hsc70. 18-Kilodalton fragment located immediately after ATPase domain is sufficient for high affinity binding | Q38313453 | ||
A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein | Q38357902 | ||
Chemical shifts as a tool for structure determination | Q40576242 | ||
Mitochondrial molecular chaperones: their role in protein translocation | Q40741572 | ||
Identification of a regulatory motif in Hsp70 that affects ATPase activity, substrate binding and interaction with HDJ-1. | Q40806764 | ||
Interaction of heavy chain binding protein (BiP/GRP78) with adenine nucleotides | Q40817891 | ||
Close encounters: why unstructured, polymeric domains can increase rates of specific macromolecular association | Q40823855 | ||
Eukaryotic DnaJ homologs and the specificity of Hsp70 activity | Q40826960 | ||
Interaction of Hsp70 chaperones with substrates | Q41465900 | ||
Expression and nitrogen-15 labeling of proteins for proton and nitrogen-15 nuclear magnetic resonance | Q44456602 | ||
ATPase kinetics of recombinant bovine 70 kDa heat shock cognate protein and its amino-terminal ATPase domain | Q46067955 | ||
DnaK ATPase activity revisited | Q46718808 | ||
Long-range motional restrictions in a multidomain zinc-finger protein from anisotropic tumbling. | Q52341521 | ||
Precise vicinal coupling constants 3JHN alpha in proteins from nonlinear fits of J-modulated [15N,1H]-COSY experiments. | Q52422094 | ||
Backbone dynamics of calmodulin studied by 15N relaxation using inverse detected two-dimensional NMR spectroscopy: the central helix is flexible. | Q52443969 | ||
Divergent effects of ATP on the binding of the DnaK and DnaJ chaperones to each other, or to their various native and denatured protein substrates. | Q54606140 | ||
The DnaK chaperone system of Escherichia coli: quaternary structures and interactions of the DnaK and GrpE components. | Q54617449 | ||
Uncoupling of peptide-stimulated ATPase and clathrin-uncoating activity in deletion mutant of hsc70. | Q54639781 | ||
Characterization of a functionally important mobile domain of GroES. | Q54654548 | ||
Reconstitution of a nine-protein system that initiates bacteriophage lambda DNA replication. | Q54733874 | ||
Identification of 1H resonances from the bait region of human alpha 2-macroglobulin and effects of proteases and methylamine | Q68975988 | ||
The ATPase core of a clathrin uncoating protein | Q70161623 | ||
Nucleotide-induced conformational changes in the ATPase and substrate binding domains of the DnaK chaperone provide evidence for interdomain communication | Q71921283 | ||
Large modular proteins by NMR | Q71958801 | ||
The role of ATP in the functional cycle of the DnaK chaperone system | Q72300885 | ||
Kinetic characterization of the ATPase cycle of the DnaK molecular chaperone | Q74024061 | ||
P433 | issue | 2 | |
P407 | language of work or name | English | Q1860 |
P921 | main subject | molecular mass | Q182854 |
P304 | page(s) | 343-54 | |
P577 | publication date | 1999-02-01 | |
P1433 | published in | Protein Science | Q7251445 |
P1476 | title | Topology and dynamics of the 10 kDa C-terminal domain of DnaK in solution | |
P478 | volume | 8 |
Q35152082 | A bipartite interaction between Hsp70 and CHIP regulates ubiquitination of chaperoned client proteins |
Q52656766 | A cluster of diagnostic Hsp68 amino acid sites that are identified in Drosophila from the melanogaster species group are concentrated around beta-sheet residues involved with substrate binding. |
Q27653249 | Allosteric Coupling between the Lid and Interdomain Linker in DnaK Revealed by Inhibitor Binding Studies |
Q28266387 | Allostery in the Hsp70 chaperone proteins |
Q41959252 | An interdomain energetic tug-of-war creates the allosterically active state in Hsp70 molecular chaperones |
Q27936582 | Ecm10, a novel hsp70 homolog in the mitochondrial matrix of the yeast Saccharomyces cerevisiae |
Q47372406 | Fine tuning of a biological machine: DnaK gains improved chaperone activity by altered allosteric communication and substrate binding |
Q37810586 | Flexible Nets of Malleable Guardians: Intrinsically Disordered Chaperones in Neurodegenerative Diseases |
Q30354473 | HSPA8/HSC70 chaperone protein: structure, function, and chemical targeting. |
Q40392313 | Heat-shock cognate 70 is required for the activation of heat-shock factor 1 in mammalian cells |
Q34545594 | Hsp70 chaperone machines. |
Q24681842 | Interaction of murine BiP/GRP78 with the DnaJ homologue MTJ1 |
Q93222384 | Recent advances in the structural and mechanistic aspects of Hsp70 molecular chaperones |
Q27655465 | Solution conformation of wild-type E. coli Hsp70 (DnaK) chaperone complexed with ADP and substrate |
Q28118960 | The C-terminal helices of heat shock protein 70 are essential for J-domain binding and ATPase activation |
Q34386414 | The substrate binding domain of DnaK facilitates slow protein refolding |
Q41843035 | Tracking the interplay between bound peptide and the lid domain of DnaK, using molecular dynamics |
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