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Clp chaperone–proteases: structure and function (CROSBI ID 244984)

Prilog u časopisu | pregledni rad (znanstveni) | međunarodna recenzija

Kress, Wolfgang ; Maglica, Željka ; Weber-Ban, Eilika Clp chaperone–proteases: structure and function // Research in microbiology, 160 (2009), 9; 618-628. doi: 10.1016/j.resmic.2009.08.006

Podaci o odgovornosti

Kress, Wolfgang ; Maglica, Željka ; Weber-Ban, Eilika

engleski

Clp chaperone–proteases: structure and function

Clp proteases are the most widespread energy-dependent proteases in bacteria. Their two-component architecture of protease core and ATPase rings results in an inventory of several Clp protease complexes that often coexist. Here, we present insights into Clp protease function, from their assembly to substrate recruitment and processing, and how this is coupled to the expense of energy.

ATP-dependent protease ; Endopeptidase ClpP ; ClpAP ; ClpXP ; ClpCP ; AAA ATPase ; Degradation

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Podaci o izdanju

160 (9)

2009.

618-628

objavljeno

0923-2508

10.1016/j.resmic.2009.08.006

Povezanost rada

Interdisciplinarne prirodne znanosti, Kemija

Poveznice
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