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245	1	0	_aMolecular Chaperones and Protein Quality Control
490	0		_vCell, 125(3), p.443-451, 2006
520	3		_aIn living cells, both newly made and preexisting polypeptide chains are at constant risk for misfolding and aggregation. In accordance with the wide diversity of misfolded forms, elaborate quality-control strategies have evolved to counter these inevitable mishaps. Recent reports describe the removal of aggregates from the cytosol; reveal mechanisms for protein quality control in the endoplasmic reticulum; and provide new insight into two classes of molecular chaperones, the Hsp70 system and the AAA+ (Hsp100)unfoldases.
700	1	2	_aBukau,B.
700	1	2	_aWeissman, J.
700	1	2	_aHorwich, A.
856	4	0	_uhttps://drive.google.com/file/d/1an-MbuuMagSl5EEJawl6nqc5n8C4p3-x/view?usp=drivesdk _zPara ver el documento ingresa a Google con tu cuenta: @cicy.edu.mx
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