Results 181 to 190 of about 4,851 (193)
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Regulation of ClpP : role of substrate gating and activation by ClpX
2010AAA+ self-compartmentalized proteases are an important class of proteome regulators that operate to selectively degrade protein substrates. All of these enzymes share the architectural theme of a hexameric ring unfoldase stacked axially onto a barrel-like peptidase, with six- or seven-fold symmetry and sequestered active sites.
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Large nucleotide‐dependent movement of the N‐terminal domain of the ClpX chaperone
EMBO Journal, 2006Walid A Houry, Guillaume Thibault
exaly
Mechanism and consequences of Mu transpososome remodeling by the ClpX chaperone
2003E. coli ClpX is a member of the Clp/Hsp100 family of ATPases that remodel multi-component complexes and facilitate ATP-dependent protein degradation. Protein remodelers alter the biological activity of their substrates, typically by changing the quaternary structure of their target proteins.
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Role of ClpX and ClpP in serotype 2 stress tolerance and virulence
Microbiological Research, 2019Yue Zhang, Huochun Yao, Zihao Pan
exaly
ClpX(P) Generates Mechanical Force to Unfold and Translocate Its Protein Substrates
Cell, 2011Rodrigo A Maillard +2 more
exaly