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Pseudo-structures for the 20 common amino acids for use in studies of protein conformations by measurements of intramolecular proton-proton distance constraints with nuclear magnetic resonance.
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Nucleotide sequence of the Escherichia coli dnaJ gene and purification of the gene product.
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The nucleotide sequence of the Escherichia coli K12 dnaJ+ gene. A gene that encodes a heat shock protein.
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Identification of structural motifs from protein coordinate data: secondary structure and first-level supersecondary structure.
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Escherichia coli heat shock gene mutants are defective in proteolysis.
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DnaK, DnaJ, and GrpE heat shock proteins negatively regulate heat shock gene expression by controlling the synthesis and stability of sigma 32.
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Escherichia coli DnaJ and GrpE heat shock proteins jointly stimulate ATPase activity of DnaK.
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Monomerization of RepA dimers by heat shock proteins activates binding to DNA replication origin.
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The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy.
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Successive action of DnaK, DnaJ and GroEL along the pathway of chaperone-mediated protein folding.
Nature. 1992 Apr 23;356(6371):683-9
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A module of the DnaJ heat shock proteins found in malaria parasites.
Trends Biochem Sci. 1992 Apr;17(4):129
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Stereospecific assignment of beta-methylene protons in larger proteins using 3D 15N-separated Hartmann-Hahn and 13C-separated rotating frame Overhauser spectroscopy.
J Biomol NMR. 1991 May;1(1):13-22
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Gradient-tailored excitation for single-quantum NMR spectroscopy of aqueous solutions.
J Biomol NMR. 1992 Nov;2(6):661-5
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A simple and sensitive experiment for measurement of JCC couplings between backbone carbonyl and methyl carbons in isotopically enriched proteins.
J Biomol NMR. 1993 Jul;3(4):487-93
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Primary structure effects on peptide group hydrogen exchange.
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The conserved G/F motif of the DnaJ chaperone is necessary for the activation of the substrate binding properties of the DnaK chaperone.
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1H and 15N magnetic resonance assignments, secondary structure, and tertiary fold of Escherichia coli DnaJ(1-78).
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1H, 13C and 15N chemical shift referencing in biomolecular NMR.
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A zinc finger-like domain of the molecular chaperone DnaJ is involved in binding to denatured protein substrates.
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Real time kinetics of the DnaK/DnaJ/GrpE molecular chaperone machine action.
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A conserved HPD sequence of the J-domain is necessary for YDJ1 stimulation of Hsp70 ATPase activity at a site distinct from substrate binding.
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A bipartite signaling mechanism involved in DnaJ-mediated activation of the Escherichia coli DnaK protein.
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Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain.
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NMR structure of the J-domain and the Gly/Phe-rich region of the Escherichia coli DnaJ chaperone.
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Binding of an N-terminal rhodanese peptide to DnaJ and to ribosomes.
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AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR.
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A function for the QKRAA amino acid motif: mediating binding of DnaJ to DnaK. Implications for the association of rheumatoid arthritis with HLA-DR4.
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Torsion-angle molecular dynamics as a new efficient tool for NMR structure calculation.
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Role of the J-domain in the cooperation of Hsp40 with Hsp70.
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Isotope effects in peptide group hydrogen exchange.
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Control of folding and membrane translocation by binding of the chaperone DnaJ to nascent polypeptides.
Proc Natl Acad Sci U S A. 1993 Nov 1;90(21):10216-20
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The NH2-terminal 108 amino acids of the Escherichia coli DnaJ protein stimulate the ATPase activity of DnaK and are sufficient for lambda replication.
J Biol Chem. 1994 Feb 18;269(7):5446-51
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The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data.
J Biomol NMR. 1994 Mar;4(2):171-80
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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.
Proc Natl Acad Sci U S A. 1994 Nov 22;91(24):11343-7
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Initiation of the DNA replication of bacteriophage lambda in Escherichia coli K12.
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