Results 1 to 10 of about 10,075 (175)

Mitochondrial Protease ClpP: Cancer Marker and Drug Target [PDF]

Pharmaceuticals
Background: The human mitochondrial ClpP is a serine protease located in the mitochondrial matrix responsible for degrading short lived regulatory proteins as well as misfolded or damaged proteins, thereby maintaining cellular homeostasis.
Domenico Armenise, Olga Maria Baldelli, Anselma Liturri, Gianfranco Cavallaro, Cosimo Gianluca Fortuna, Savina Ferorelli, Morena Miciaccia, Maria Grazia Perrone, Antonio Scilimati   +8 more
doaj   +4 more sources

Effects of ClpP protease on biofilm formation of Enterococcus faecalis [PDF]

Journal of Applied Oral Science, 2021
Enterococcus faecalis (E. faecalis), one of the main pathogens responsible for refractory periapical periodontitis and nosocomial infections, exhibits markedly higher pathogenicity in biofilms. Objectives Studies have shown that caseinolytic protease P
Ying FENG, Hongyuan WANG, HE Lu, LIU Yi, LI Hong   +4 more
doaj   +6 more sources

Bacterial ClpP Protease Is a Potential Target for Methyl Gallate [PDF]

Frontiers in Microbiology, 2021
Methyl gallate (MG) is an effective microbicide with great potential application in the integrated management of plant diseases and an important potential drug for clinical application. However, its target remains unknown.
Dehong Zheng, Yanan Xu, Gaoqing Yuan, Xiaogang Wu, Qiqin Li   +4 more
doaj   +3 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.
Carlos Moreno-Cinos, Kenneth Goossens, Irène G Salado   +2 more
exaly   +4 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.
Mark F Mabanglo, Vaibhav Bhandari, Walid A Houry   +2 more
exaly   +3 more sources

Targeting mitochondrial ClpP: structural insights and therapeutic potential of ClpP agonists in cancer therapy

Oncology Reviews
Mitochondrial “powerhouses” play a central function in cellular metabolism and energy generation. Their dysregulation is directly correlated with a myriad of diseases, among them cancer. The serine protease ClpP, accompanied by its cochaperone ClpX, is a
Mowei Kong, Yang Yu, Shuai Shao, Chunxiang Zhang   +3 more
doaj   +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.
Thomas Böttcher, Stephan A Sieber
exaly   +5 more sources

Disrupting α-Synuclein–ClpP interaction restores mitochondrial function and attenuates neuropathology in Parkinson’s disease models [PDF]

Molecular Neurodegeneration
Background Mitochondrial dysfunction and α-Synuclein (αSyn) aggregation are defining features of Parkinson’s disease (PD), yet the mechanistic link between them remains poorly understood.
Di Hu, Xiaoyan Sun, Xin Qi
doaj   +2 more sources

Structure of the central Staphylococcus aureus AAA+ protease MecA/ClpC/ClpP [PDF]

Communications Biology
Bacterial AAA+ proteases are composed of a AAA+ partner (e.g., ClpC) and an associated peptidase (e.g., ClpP). They represent ATP-fuelled and self-compartmentalized proteolytic machines that are crucial for stress resistance and virulence.
Stavros Azinas, Karin Wallden, Panagiotis Katikaridis, Timo Jenne, Adrien Schahl, Axel Mogk, Marta Carroni   +6 more
doaj   +2 more sources

Targeting the Mitochondrial Protease ClpP for Anticancer Therapy [PDF]

Journal of Medicinal Chemistry
Cancer cells depend on mitochondrial reprogramming for growth, but this raises reactive oxygen species (ROS), increasing reliance on protein quality control (PQC) repair mechanisms. The mitochondrial proteome is maintained through a robust PQC composed of chaperones and proteases, including the mitochondrial matrix protease caseinolytic protease P ...
Zhongli Xu, Dmitry Pokushalov, Md Kabir, Youngeun Lee, Mrittika Chattopadhyay, Edmund C. Jenkins, Cessarina Choo, H. Ümit Kaniskan, Doris Germain, Jian Jin   +9 more
openaire   +3 more sources