Results 81 to 90 of about 3,616 (191)
Redox BiologyVascular smooth muscle cells (VSMCs), known for their remarkable lifelong phenotypic plasticity, play a pivotal role in vascular pathologies through their ability to transition between different phenotypes. Our group discovered that the deficiency of the
Felipe Paredes +11 more
doaj +1 more source
Regulatory interplay of RpoS and RssB controls motility and colonization in Vibrio cholerae
International Journal of Medical Microbiology, 2022 Cholera is a life-threatening diarrheal disease caused by the human pathogenic bacterium Vibrio cholerae. Regulatory elements are essential for bacterial transition between the natural aquatic environment and the human host.
Martina Wölflingseder +4 more
doaj +1 more source
mLife, Volume 5, Issue 5, Page 651-664, October 2026.Abstract Persistent bacteria subpopulations showing multidrug tolerance pose significant challenges to antibiotic therapy. While the HipBA toxin–antitoxin (TA) system is known to play a role in persister formation, existing studies predominantly focus on its kinase activity and intracellular regulatory pathways, with limited attention to the ...
Jing Zhao +4 more
wiley +1 more source
Clpxp Degradation of Proteins Probed By Single-Molecule Fluorescence [PDF]
Biophysical Journal, 2010 ClpXP is an AAA+ protease that unfolds and degrades target proteins. ClpX, a hexameric ring-shaped ATPase, recognizes specific proteins and then powers their mechanical denaturation and translocation into the degradation chamber of ClpP where polypeptide bond cleavage occurs.
Shin, Yongdae +6 more
openaire +1 more source
Biological roles of the Podospora anserina mitochondrial Lon protease and the importance of its N-domain. [PDF]
PLoS ONE, 2012 Mitochondria have their own ATP-dependent proteases that maintain the functional state of the organelle. All multicellular eukaryotes, including filamentous fungi, possess the same set of mitochondrial proteases, unlike in unicellular yeasts, where ClpXP,
Céline Adam +5 more
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Single molecule fluorescence spectroscopy of ClpXP-mediated substrate degradation [PDF]
, 2009 Thesis (S.M.)--Massachusetts Institute of Technology, Dept. of Mechanical Engineering, 2009.Includes bibliographical references (leaves 67-71).Energy-dependent proteases, such as ClpXP, are responsible for the regulated destruction of proteins in ...
Shin, Yongdae
core
NOA1 is a substrate of the mitochondrial matrix protease complex ClpXP.
, 2014 (A) The C-terminus of NOA1 contains three motifs resembling known ClpX recognition motifs found in proteins of E.coli. (B) Exemplary Western blot analysis revealing increased concentrations of NOA1 in C2C12 cells after mutation of lysin690 and lysin691 ...
Marcus Krüger (277353) +5 more
core +1 more source
Substrate-translocating loops regulate mechanochemical coupling and power production in AAA+ protease ClpXP [PDF]
, 2016 ATP-dependent proteases of the AAA+ family, including Escherichia coli ClpXP and the eukaryotic proteasome, contribute to maintenance of cellular proteostasis.
Frank Kim +9 more
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Structure and function of ClpXP, a AAA+ proteolytic machine powered by probabilistic ATP hydrolysis
, 2021 ClpXP is an archetypical AAA+ protease, consisting of ClpX and ClpP. ClpX is an ATP-dependent protein unfoldase and polypeptide translocase, whereas ClpP is a self-compartmentalized peptidase.
Sauer, Robert T +7 more
core +1 more source
ClpAP proteolysis does not require rotation of the ClpA unfoldase relative to ClpP
eLife, 2020 AAA+ proteases perform regulated protein degradation in all kingdoms of life and consist of a hexameric AAA+ unfoldase/translocase in complex with a self-compartmentalized peptidase.
Sora Kim +4 more
doaj +1 more source