Results 61 to 70 of about 10,075 (175)
Purification of the Caseinolytic protease ClpP.
, 2022 The caseinolytic protease P (ClpP) is an essential protein for bacteria and bacterial derived organelles. It belongs to the AAA+ family of proteases and has proteolytic activity, thereby, it plays an important role in protein digestion. This protease is involved in essential processes such as, cellular regulatory mechanisms, protein homeostasis ...
Pedrós Manzanares, Laura +1 more
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Acta Biochimica et Biophysica SinicaCurrently, platinum agents remain the mainstay of chemotherapy for ovarian cancer (OC). However, cisplatin (DDP) resistance is a major reason for chemotherapy failure.
Kou Xinxin +3 more
doaj +1 more source
Cell Division Protein FtsZ Is Unfolded for N-Terminal Degradation by Antibiotic-Activated ClpP
mBio, 2020 Antibiotic acyldepsipeptides (ADEPs) deregulate ClpP, the proteolytic core of the bacterial Clp protease, thereby inhibiting its native functions and concomitantly activating it for uncontrolled proteolysis of nonnative substrates.
Nadine Silber +5 more
doaj +1 more source
The Journal of Pathology, Volume 269, Issue 2, Page 149-163, June 2026.Abstract The conceptualization of mitochondria, previously restricted to their function as cellular ‘powerhouses’, has evolved to recognize their function as central coordinating hubs for the orchestration of cancer cell metabolism, signaling, and fate determination.
Woo Hyun Park
wiley +1 more source
Scientific ReportsChronic lumbopelvic pain (CLPP) and its associated disabilities significantly affect women's social, professional, and personal lives. However, the specific factors contributing to CLPP in women remain unclear. To address this gap, this prospective cross-
Jasmine Kaur Chawla +4 more
doaj +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
Aging Cell, Volume 25, Issue 6, June 2026.Aged mouse skeletal muscle exhibits greater mtUPR transcriptional initiation following repeated physical stress than young mice, coinciding with reduced mitochondrial proteostatic reserve and heightened oxidative burden. We implicate a mtROS‐JNK‐CHOP axis as a contributor to the enhanced response.
Grant R. Laskin +2 more
wiley +1 more source
Protein degradation in bacteria: focus on the ClpP protease
Nippon Saikingaku ZasshiProteins in the cells are born (synthesized), work, and die (decomposed). In the life of a protein, its birth is obviously important, but how it dies is equally important in living organisms. Proteases secreted into the outside of cells are used to decompose the external proteins and the degradation products are taken as the nutrients.
Fumihiro, Ishikawa +3 more
openaire +2 more sources
AAA+ protein unfoldases—the Moirai of the proteome
FEBS Letters, Volume 600, Issue 10, Page 1444-1474, May 2026.AAA+ unfoldases are essential molecular motors that power protein degradation and disaggregation. This review integrates recent cryo‐electron microscopy (cryo‐EM) structures and single‐molecule biophysical data to reconcile competing models of substrate translocation.
Stavros Azinas, Marta Carroni
wiley +1 more source
Animal Research and One Health, Volume 4, Issue 2, Page 167-184, May 2026.Unregulated inflammation increases non‐esterified fatty acids (NEFAs), and triggers multi‐pathway hepatocyte damage including oxidative stress, mitochondrial dysfunction, and metabolic disorders in dairy cows. ABSTRACT Circulating concentrations of nonesterified fatty acids (NEFAs) are elevated due to lipid mobilization from adipose tissue in ...
Siqing Mao +12 more
wiley +1 more source