Chaperones get Hip. Protein folding.
The discovery of a new co-chaperone, Hip, that interacts with Hsp70 underscores the complexity of the Hsp70 'chaperone machine' that mediates early steps of protein folding in cells.
Ziegelhoffer
T
T
Department of Biomolecular Chemistry, University of Wisconsin-Madison, Madison, Wisconsin 53706, USA.
Johnson
J L
JL
Craig
E A
EA
D000209:Acute-Phase Proteins / Q000378:metabolism*; D000951:Antigens, Neoplasm; D001426:Bacterial Proteins / Q000378:metabolism; D014408:Biomarkers, Tumor; D003600:Cytosol; D029968:Escherichia coli Proteins; D050956:HSP40 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins / Q000378:metabolism*; D006360:Heat-Shock Proteins / Q000378:metabolism; D006801:Humans; D037181:Lectins, C-Type; D008958:Models, Molecular; D018832:Molecular Chaperones / Q000378:metabolism*; D000073718:Pancreatitis-Associated Proteins; D017510:Protein Folding; D011956:Receptors, Cell Surface / Q000378:metabolism
D000209:Acute-Phase Proteins; D000951:Antigens, Neoplasm; D001426:Bacterial Proteins; D014408:Biomarkers, Tumor; D029968:Escherichia coli Proteins; C068113:GrpE protein, Bacteria; D050956:HSP40 Heat-Shock Proteins; D018840:HSP70 Heat-Shock Proteins; D006360:Heat-Shock Proteins; D037181:Lectins, C-Type; D018832:Molecular Chaperones; D000073718:Pancreatitis-Associated Proteins; C000612141:REG3A protein, human; D011956:Receptors, Cell Surface; C063842:dnaK protein, E coli