Results 1 to 10 of about 5,899 (155)

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, Xiaogang Wu, Gaoqing Yuan   +2 more
exaly   +7 more sources

Cellular functions of the ClpP protease impacting bacterial virulence [PDF]

Frontiers in Molecular Biosciences, 2022
Proteostasis mechanisms significantly contribute to the sculpting of the proteomes of all living organisms. ClpXP is a central AAA+ chaperone-protease complex present in both prokaryotes and eukaryotes that facilitates the unfolding and subsequent ...
Walid Houry, Vaibhav Bhandari, Houry Walid A   +2 more
exaly   +6 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   +7 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   +6 more sources

Mechanism of allosteric activation in human mitochondrial ClpP protease [PDF]

Proceedings of the National Academy of Sciences of the United States of America
Abstract Human ClpP protease contributes to mitochondrial protein quality control by degrading misfolded proteins. ClpP is overexpressed in cancers such as acute myeloid leukemia (AML), where its inhibition leads to the accumulation of damaged respiratory chain subunits and cell death.
Siavash Vahidi, Matthew Kimber, Taylor Forrester   +2 more
exaly   +4 more sources

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

The ClpP protease is required for the stress tolerance and biofilm formation in Actinobacillus pleuropneumoniae. [PDF]

PLoS ONE, 2013
In the respiratory tract and lung tissue, a balanced physiological response is essential for Actinobacillus pleuropneumoniae to survive various types of challenges.
Fang Xie, Yanhe Zhang, Gang Li, Long Zhou, Siguo Liu, Chunlai Wang   +5 more
doaj   +5 more sources

Development of Antibiotics That Dysregulate the Neisserial ClpP Protease. [PDF]

ACS Infect Dis, 2020
Evolving antimicrobial resistance has motivated the search for novel targets and alternative therapies. Caseinolytic protease (ClpP) has emerged as an enticing new target since its function is conserved and essential for bacterial fitness, and because its inhibition or dysregulation leads to bacterial cell death.
Binepal G, Mabanglo MF, Goodreid JD, Leung E, Barghash MM, Wong KS, Lin F, Cossette M, Bansagi J, Song B, Balasco Serrão VH, Pai EF, Batey RA, Gray-Owen SD, Houry WA.   +14 more
europepmc   +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.
Walid Houry, Vaibhav Bhandari, Mark F Mabanglo   +2 more
exaly   +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