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|a Baker, Tania
|e author
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|a Massachusetts Institute of Technology. Department of Biology
|e contributor
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|a Baker, Tania
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|a Sauer, Robert T.
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|a Sauer, Robert T
|e author
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|a ClpXP, an ATP-powered unfolding and protein-degradation machine
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|b Elsevier,
|c 2014-01-27T16:28:47Z.
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|z Get fulltext
|u http://hdl.handle.net/1721.1/84570
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|a ClpXP is a AAA+ protease that uses the energy of ATP binding and hydrolysis to perform mechanical work during targeted protein degradation within cells. ClpXP consists of hexamers of a AAA+ ATPase (ClpX) and a tetradecameric peptidase (ClpP). Asymmetric ClpX hexamers bind unstructured peptide tags in protein substrates, unfold stable tertiary structure in the substrate, and then translocate the unfolded polypeptide chain into an internal proteolytic compartment in ClpP. Here, we review our present understanding of ClpXP structure and function, as revealed by two decades of biochemical and biophysical studies. This article is part of a Special Issue entitled: AAA ATPases: Structure and function.
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|a National Institutes of Health (U.S.) (Grant AI-15706)
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|a National Institutes of Health (U.S.) (Grant AI-16892)
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|a National Institutes of Health (U.S.) (Grant 499224)
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|a Howard Hughes Medical Institute
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|a en_US
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|a Article
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|t Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
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