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ATP-dependent specificity component of the Clp protease.
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results illustrate that ClpX overexpression is a good and simple model to study the underlying mechanisms of the UPRmt in mammalian cells.
Loss of mitochondrial peptidase Clpp (zeige CLPP Proteine) leads to infertility, hearing loss plus growth retardation via accumulation of CLPX, mtDNA and inflammatory factors.
The mutation in CLPX inactivates its ATPase activity, resulting in coassembly of mutant and WT protomers to form an enzyme with reduced activity. The presence of low-activity CLPX increases the posttranslational stability of ALAS, causing increased ALAS protein and ALA levels, leading to abnormal accumulation of PPIX.
Walker B mutation in human CLPX exhibits improved interaction with the model unfolded substrate casein and several putative physiological substrates in vitro.
human ClpX, a novel mtDNA regulator, maintains mtDNA nucleoid distribution through TFAM (zeige TFAM Proteine) function as a chaperone rather than as a protease and its involvement in mtDNA segregation.
Results reveal that the ssrA tag interacts with different loops that form the top, middle, and lower portions of the central channel of the ClpX hexamer.
ATP-dependent specificity component of the Clp protease. It directs the protease to specific substrates. Can perform chaperone functions in the absence of clpP (By similarity).
ATP-dependent Clp protease ATP-binding subunit clpX-like, mitochondrial
, caseinolytic protease X
, ClpX caseinolytic protease X homolog
, energy-dependent regulator of proteolysis
, caseinolytic peptidase X