Results 161 to 170 of about 13,032 (201)

Structural and mechanistic insights into caseinolytic protease inhibition for antimicrobial development against Pseudomonas plecoglossicida. [PDF]

PLoS Pathog
Chen J, Zhang P, Guan H, Gong B, Li X, Li Z, Li F, Zhou B, Chen X, Chen X, Ouyang S, Zhang YA.   +11 more
europepmc   +1 more source

Mitochondrial Dysfunction in Ulcerative Colitis: Pathogenic Mechanisms and Novel Therapeutics. [PDF]

J Biochem Mol Toxicol
Ran H, Zhou S, Zou H, Deng J, Yin F.
europepmc   +1 more source

Transcriptome Analysis Identifies Proteostasis and Cell Survival Pathway Disruption in Peripartum Cardiomyopathy, Leading to Heart Failure. [PDF]

Cells
Choubey P, Montoya-Uribe V, Matter ML.
europepmc   +1 more source

ClpP Protease, a Promising Antimicrobial Target [PDF]

International Journal of Molecular Sciences, 2019
: The caseinolytic protease proteolytic subunit (ClpP) is a serine protease playing an important role in proteostasis of eukaryotic organelles and prokaryotic cells.
Hans De Winter, Koen Augustyns, Irene Garcia   +2 more
exaly   +6 more sources

A Conformational Switch Underlies ClpP Protease Function [PDF]

Angewandte Chemie - International Edition, 2011
A “breathing” protein: The first structure of the virulence regulator and heat shock protein ClpP from Staphylococcus aureus reveals a previously unobserved compressed state of the ClpP barrel. A conformational switch in the active center “handle region”
Patrick Cramer, Stephan A. Sieber, Thomas Böttcher   +2 more
exaly   +7 more sources

Substrates and Interactors of the ClpP Protease in the Mitochondria

Current Opinion in Chemical Biology, 2022
The ClpP protease is found across eukaryotic and prokaryotic organisms. It is well-characterized in bacteria where its function is important in maintaining protein homeostasis. Along with its ATPase partners, it has been shown to play critical roles in the regulation of enzymes involved in important cellular pathways.
Walid A Houry, Vaibhav Bhandari, Mark F Mabanglo   +2 more
exaly   +3 more sources

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The Mechanism of Caseinolytic Protease (ClpP) Inhibition

Angewandte Chemie - International Edition, 2013
Christian Hedberg, Gerhard Klebe, Stephan A. Sieber   +2 more
exaly   +6 more sources

Selective Activation of Human Caseinolytic Protease P (ClpP)

Angewandte Chemie - International Edition, 2018
AbstractCaseinolytic protease P (ClpP) is the proteolytic component of the ClpXP protein degradation complex. Eukaryotic ClpP was recently found to act within the mitochondria‐specific unfolded protein response (UPRmt). However, its detailed function and dedicated regulation remain largely unexplored.
Leonhard M Kick, Matthias Stahl, Klaus Richter   +2 more
exaly   +4 more sources

Structural insights into the evolutionary simplification of human ClpP activators

Structure, 2023
In this issue of Structure, Mabanglo et al. characterize five ClpP agonists termed TRs. The co-crystal structures reveal more robust shape and charge complementarities than the anti-cancer agent ONC201. These novel compounds are of potential therapeutic interest because they enhance ClpP proteolytic activity and have an inhibitory effect on tumor cell ...
Lin-Lin, Zhou, Cai-Guang, Yang
openaire   +2 more sources

The regulation of Porphyromonas gingivalis biofilm formation by ClpP

Biochemical and Biophysical Research Communications, 2019
Porphyromonas gingivalis is one of the most commonly detected pathogens in periodontal disease and root canal infections. Its viability and pathogenicity are greatly increased in plaque biofilms. Some caseinolytic proteases (Clp) reportedly regulate biofilm formation by various pathogenic bacteria, including P. gingivalis.
Lu, He, Hongyuan, Wang, Ru, Zhang, Hong, Li   +3 more
openaire   +2 more sources