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The cytosolic DnaJ-like protein djp1p is involved specifically in peroxisomal protein import.
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Protein folding activity of Hsp70 is modified differentially by the hsp40 co-chaperones Sis1 and Ydj1.
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A role for the DnaJ homologue Scj1p in protein folding in the yeast endoplasmic reticulum.
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Protein translocation: is Hsp70 pulling my chain?
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Structural analysis of phylogenetically conserved J domain protein gene.
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Increased expression of Hsp40 chaperones, transcriptional factors, and ribosomal protein Rpp0 can cure yeast prions.
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Scanning mutagenesis identifies amino acid residues essential for the in vivo activity of the Escherichia coli DnaJ (Hsp40) J-domain.
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Nep98p is a component of the yeast spindle pole body and essential for nuclear division and fusion.
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Structure-function analysis of the auxilin J-domain reveals an extended Hsc70 interaction interface.
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Use of modular substrates demonstrates mechanistic diversity and reveals differences in chaperone requirement of ERAD.
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Global analysis of protein localization in budding yeast.
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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.
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Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain.
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The lumenal domain of Sec63p stimulates the ATPase activity of BiP and mediates BiP recruitment to the translocon in Saccharomyces cerevisiae.
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Role of the J-domain in the cooperation of Hsp40 with Hsp70.
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