Results 181 to 190 of about 5,327 (202)
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Mechanically Watching the ClpXP Proteolytic Machinery
2016Energy-dependent protein degradation is studied through the dual bead ClpXP motility assay. Processing of folded proteins involves recognition, unfolding, translocation, and degradation stages. A dual optical trap, in a passive force-clamp geometry, exhibits bead-to-bead displacements that directly follow subprocesses underlying protein degradation ...
Juan Carlos, Cordova +2 more
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Abstract 4834: Mitochondrial ClpXP degrades serine phosphorylated protein aggregates
Cancer Research, 2023Abstract ClpXP is a serine protease localized to the mitochondrial matrix and maintains mitochondrial proteostasis by degrading damaged/aggregated respiratory chain complex proteins. Both inhibition and hyperactivation of ClpP lead to impaired OXPHOS function and kill leukemic cells in vitro and in vivo.
Yue Feng +7 more
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N-Terminal peptidic boronic acids selectively inhibit human ClpXP
Organic & Biomolecular Chemistry, 2010The synthesis and development of N-terminal peptidic boronic acids as protease inhibitors is reported. N-Terminal peptidic boronic acids interrogate the S' sites of the target protein for selectivity and provide a new strategy that complements the currently known peptidic alpha-amino boronic acids (C-terminal boronic acids). After screening a series of
Kenneth, Knott +4 more
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Determining ClpXP Substrates Under Different Nutrient Conditions in Escherichia coli
The FASEB Journal, 2017Cellular protein concentrations reflect a balance between synthesis, degradation, and dilution by cell growth. Synthesis is routinely analyzed in high‐throughput experiments, but fewer studies consider degradation, particularly under non‐optimal growth conditions such as starvation.
Celeste Peterson +5 more
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Unfolding and Translocation of Proteins Through an Alpha-Hemolysin Nanopore by ClpXP
2020Proteins present a significant challenge for nanopore-based sequence analysis. This is partly due to their stable tertiary structures that must be unfolded for linear translocation, and the absence of regular charge density. To address these challenges, here we describe how ClpXP, an ATP-dependent protein unfoldase, can be harnessed to unfold and ...
Jeff, Nivala +4 more
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Novel Adaptor-Dependent Domains Promote Processive Degradation by ClpXP
2011Protein degradation by ATP dependent proteases is a universally conserved process. Recognition of substrates by such proteases commonly occurs via direct interaction or with the aid of a regulatory adaptor protein. An example of this regulation is found in Caulobacter crescentus, where key regulatory proteins are proteolysed in a cell-cycle dependent ...
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Abstract 5425: Human mitochondrial ClpXP protease degrades serine phosphorylated substrates
Cancer ResearchAbstract ClpXP is an AAA+ protease located in mitochondria matrix. In human, ClpXP degrades damaged respiratory chain proteins and is essential for acute myeloid leukemia (AML) cell survival. This complex consists of the tetradecameric ClpP protease and regulatory particles ClpX.
Yue Feng +27 more
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ATP-dependent protein degradation and unfolding by ClpXP
GBM Annual Fall meeting Halle 2002, 2002R.T. Sauer +9 more
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