Results 161 to 170 of about 13,300 (205)

Targeting mitochondrial proteases CLPP and LONP1 via disruption of mitochondrial redox homeostasis induces proteotoxic stress and suppresses tumor progression. [PDF]

Cell Commun Signal
Nandha SR, Patwardhan RS, Sharma D, Sandur SK, Checker R.   +4 more
europepmc   +1 more source

Recent Advances in the Structural Studies of the Proteolytic ClpP/ClpX Molecular Machine. [PDF]

Biomolecules
Audibert A, Boisbouvier J, Vermot A.
europepmc   +1 more source

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Assessment of the structure-activity relationship and antileukemic activity of diacylpyramide compounds as human ClpP agonists

European Journal of Medicinal Chemistry, 2023
Human caseinolytic protease P (ClpP) is required for the regulatory hydrolysis of mitochondrial proteins. Allosteric ClpP agonists dysfunctionally activate mitochondrial ClpP in antileukemic therapies. We previously developed ZG111, a potent ClpP agonist
Cai-Guang Yang, Jianhua Gan, Yihui Pan   +2 more
exaly   +2 more sources

Substrates and interactors of the ClpP protease in the mitochondria.

Current Opinion in Chemical Biology, 2021
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.
M. Mabanglo, Vaibhav Bhandari, W. Houry
semanticscholar   +3 more sources

Discovery of CLPP-1071 as an Exceptionally Potent and Orally Efficacious Human ClpP Activator with Strong In Vivo Antitumor Activity

Journal of Medicinal Chemistry
Human sapiens caseinolytic protease P (ClpP) is essential for maintaining mitochondrial proteome homeostasis, and its activation is increasingly recognized as a promising cancer therapy strategy.
Beijing Chen, Mingyang Sun, Chun Zhang, Qi Huang, Dan Teng, Linghao Hu, Huicong Ma, Xinyi Lin, Zan Huang, Renzhao Gui, Xiaobei Hu, Lei Xu, Mingyue Zheng, Yubo Zhou, Jia Li, Mingliang Wang   +15 more
semanticscholar   +3 more sources

ClpP Peptidase as a Plausible Target for the Discovery of Novel Antibiotics.

Current Drug Targets, 2023
Antimicrobial resistance (AMR) to currently available antibiotics/drugs is a global threat. It is desirable to develop new drugs that work through a novel target(s) to avoid drug resistance.
Smriti Bhardwaj, K. Roy
semanticscholar   +3 more sources

Patenting perspective of modulators of ClpP endopeptidase: 2019-present

Expert Opinion on Therapeutic Patents
Introduction ClpP is a highly conserved serine protease that plays a crucial role in maintaining protein homeostasis in both bacterial cells and human mitochondria.
Zhenyu Wang, Liqin He, Zi-qi Fan, Youfu Luo   +3 more
semanticscholar   +3 more sources

A Conformational Switch Underlies ClpP Protease Function

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” results in closure of the active sites and opening of equatorial pores.
Stephan Sieber, Thomas Böttcher
exaly   +5 more sources

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. Alteration of ClpP function has been proved to affect the virulence and infectivity of a number of pathogens.
Hans De Winter, Koen Augustyns, Irène Garcia   +2 more
exaly   +4 more sources

The Mechanism of Caseinolytic Protease (ClpP) Inhibition

Angewandte Chemie - International Edition, 2013
Christian Hedberg, Stephan Sieber, Herbert Waldmann   +2 more
exaly   +4 more sources