Proteasomes and their kin: proteases in the machine age
CM Pickart, RE Cohen - Nature reviews Molecular cell biology, 2004 - nature.com
CM Pickart, RE Cohen
Nature reviews Molecular cell biology, 2004•nature.comAbstract'Chambered proteases', including the eukaryotic 26S proteasome, use the energy of
ATP to drive the unfolding and translocation of a polypeptide substrate into a chamber of
sequestered proteolytic active sites. These proteases have diverse functions and are found
in all three kingdoms of life. Understanding chambered proteases requires answers to two
questions—how do these remarkable machines select the correct target proteins and how
do they bring about the processive degradation of these molecules?
ATP to drive the unfolding and translocation of a polypeptide substrate into a chamber of
sequestered proteolytic active sites. These proteases have diverse functions and are found
in all three kingdoms of life. Understanding chambered proteases requires answers to two
questions—how do these remarkable machines select the correct target proteins and how
do they bring about the processive degradation of these molecules?
Abstract
'Chambered proteases', including the eukaryotic 26S proteasome, use the energy of ATP to drive the unfolding and translocation of a polypeptide substrate into a chamber of sequestered proteolytic active sites. These proteases have diverse functions and are found in all three kingdoms of life. Understanding chambered proteases requires answers to two questions — how do these remarkable machines select the correct target proteins and how do they bring about the processive degradation of these molecules?
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