Results 41 to 50 of about 152,432 (174)
a-Amino Diphenyl Phosphonates as Novel Inhibitors of Escherichia coli ClpP Protease
, 2022 S.774-797Increased Gram-negative bacteria resistance to antibiotics is becoming a global problem, and new classes of antibiotics with novel mechanisms of action are required. The caseinolytic protease subunit P (ClpP) is a serine protease conserved among
Salado, I.G. +14 more
core +2 more sources
Reversible inhibition of the ClpP protease via an N-terminal conformational switch. [PDF]
Proc Natl Acad Sci U S A, 2018 Significance ClpP is a protease that degrades damaged or misfolded proteins. Consistent with its critical role in maintaining cellular homeostasis, inhibiting and dysregulating ClpP function has shown promise in fighting antibiotic resistance and in targeting cancer cells in acute myeloid leukemia.
Vahidi S +11 more
europepmc +4 more sources
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
ClpA mediates directional translocation of substrate proteins into the ClpP protease [PDF]
Proceedings of the National Academy of Sciences, 2001 The intracellular degradation of many proteins is mediated in an ATP-dependent manner by large assemblies comprising a chaperone ring complex associated coaxially with a proteolytic cylinder, e.g., ClpAP, ClpXP, and HslUV in prokaryotes, and the 26S proteasome in eukaryotes. Recent studies of the chaperone ClpA indicate that it
B G, Reid +3 more
openaire +2 more sources
Metabolic Perturbations in a Bacillus subtilis clpP Mutant during Glucose Starvation
Metabolites, 2017 Proteolysis is essential for all living organisms to maintain the protein homeostasis and to adapt to changing environmental conditions. ClpP is the main protease in Bacillus subtilis, and forms complexes with different Clp ATPases.
Daniel Schultz +3 more
doaj +1 more source
Frontiers in Microbiology, 2021 The ClpX ATPase is critical for resistance to cell envelope targeting antibiotics in Bacillus anthracis, however, it is unclear whether this is due to its function as an independent chaperone or as part of the ClpXP protease.
Lang Zou +5 more
doaj +1 more source
Identification of an Unusual Intein in Chloroplast ClpP Protease of Chlamydomonas eugametos [PDF]
Journal of Biological Chemistry, 1997 The proteasome-like ClpP protease is widely distributed and structurally conserved among bacteria and eukaryotic cell organelles. In Chlamydomonas eugametos, however, the chloroplast clpP gene predicted a much larger ClpP protein containing large insertion sequences (ISs).
S, Wang, X Q, Liu
openaire +2 more sources
Alpha-synuclein suppresses mitochondrial protease ClpP to trigger mitochondrial oxidative damage and neurotoxicity [PDF]
, 2019 Both α-Synuclein (αSyn) accumulation and mitochondrial dysfunction have been implicated in the pathology of Parkinson's disease (PD). Although studies suggest that αSyn and its missense mutant, A53T, preferentially accumulate in the mitochondria, the ...
Zarabi, S +9 more
core +1 more source
eLife, 2020 The ClpXP degradation machine consists of a hexameric AAA+ unfoldase (ClpX) and a pair of heptameric serine protease rings (ClpP) that unfold, translocate, and subsequently degrade client proteins.
Zev A Ripstein +4 more
doaj +1 more source
Mitofusin-2 Down-Regulation Predicts Progression of Non-Muscle Invasive Bladder Cancer
Diagnostics, 2021 Identification of markers predicting disease outcome is a major clinical issue for non-muscle invasive bladder cancer (NMIBC). The present study aimed to determine the role of the mitochondrial proteins Mitofusin-2 (Mfn2) and caseinolytic protease P ...
Antonella Cormio +9 more
doaj +1 more source