Mechanistic insights into bacterial AAA+ proteases and protein-remodelling machines

Mechanistic insights into bacterial AAA+ proteases and protein-remodelling machines

To maintain protein homeostasis, AAA+ proteolytic machines degrade damaged and unneeded proteins in bacteria, archaea and eukaryotes. This process involves the ATP-dependent unfolding of a target protein and its subsequent translocation into a self-compartmentalized proteolytic chamber. Related AAA+...

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Bibliografische gegevens
Hoofdauteurs:	Olivares, Adrian O., Baker, Tania, Sauer, Robert T.
Andere auteurs:	Massachusetts Institute of Technology. Department of Biology
Formaat:	Artikel
Taal:	en_US
Gepubliceerd in:	Nature Publishing Group 2017
Online toegang:	http://hdl.handle.net/1721.1/107469 https://orcid.org/0000-0002-1719-5399

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Division of labor between the pore-1 loops of the D1 and D2 AAA+ rings coordinates substrate selectivity of the ClpAP protease
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N domain of the Lon AAA+ protease controls assembly and substrate choice
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Functional and structural studies of AAA+ proteases
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Structure and function of ClpXP, a AAA+ proteolytic machine powered by probabilistic ATP hydrolysis
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The ClpS Adaptor Mediates Staged Delivery of N-End Rule Substrates to the AAA+ ClpAP Protease
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Interactions between a subset of substrate side chains and AAA+ motor pore loops determine grip during protein unfolding
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Single-Molecule Protein Unfolding and Translocation by an ATP-Fueled Proteolytic Machine
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Identification of the Cdc48•20S Proteasome as an Ancient AAA+ Proteolytic Machine
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Subunit asymmetry and roles of conformational switching in the hexameric AAA+ ring of ClpX
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door: Sundar, Shankar
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Mechanisms of CipS reprogramming of the AAA+ protease CipAP
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Mechanistic studies of the AAA+ molecular motor ClpXP
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