Results 11 to 20 of about 152,432 (174)

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, Irene Garcia   +2 more
exaly   +8 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

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 J B Forrester   +2 more
exaly   +4 more sources

Regulation of Cyclic Lipopeptide Biosynthesis inPseudomonas fluorescensby the ClpP Protease [PDF]

Journal of Bacteriology, 2009
ABSTRACTCyclic lipopeptides produced byPseudomonasspecies exhibit potent surfactant and broad-spectrum antibiotic properties. Their biosynthesis is governed by large multimodular nonribosomal peptide synthetases, but little is known about the genetic regulatory network.
de Bruijn, I., Raaijmakers, J.M.
openaire   +4 more sources

Molybdopterin biosynthesis pathway contributes to the regulation of SaeRS two-component system by ClpP in Staphylococcus aureus [PDF]

Virulence, 2022
In Staphylococcus aureus, the SaeRS two-component system is essential for the bacterium’s hemolytic activity and virulence. The Newman strain of S. aureus contains a variant of SaeS sensor kinase, SaeS L18P.
Na Zhao, Yanan Wang, Junlan Liu, Ziyu Yang, Ying Jian, Hua Wang, Mahmoud Ahmed, Min Li, Taeok Bae, Qian Liu   +9 more
doaj   +2 more sources

Mitochondrial protease ClpP supplementation ameliorates diet-induced NASH in mice

Journal of Hepatology, 2022
Mitochondrial dysfunction is considered a pathogenic linker in the development of non-alcoholic steatohepatitis (NASH). Inappropriate mitochondrial protein-quality control, possibly induced by insufficiency of the mitochondrial matrix caseinolytic protease P (ClpP), can potentially cause mitochondrial dysfunction.
Sung-E Choi, Yoonjung Hwang, Soo-Jin Lee, Hyunkyung Jung, Tae Hwan Shin, Youngho Son, Seokho Park, Seung Jin Han, Hae Jin Kim, Kwan Woo Lee, Gwang Lee, Jongsook Kim Kemper, Hyun Kyu Song, Yup Kang   +13 more
openaire   +3 more sources

The ATP-Dependent Protease ClpP Inhibits Biofilm Formation by Regulating Agr and Cell Wall Hydrolase Sle1 in Staphylococcus aureus [PDF]

Frontiers in Cellular and Infection Microbiology, 2017
Biofilm causes hospital-associated infections on indwelling medical devices. In Staphylococcus aureus, Biofilm formation is controlled by intricately coordinated network of regulating systems, of which the ATP-dependent protease ClpP shows an inhibitory ...
Qian Liu, Xing Wang, Juanxiu Qin, Sen Cheng, Won-Sik Yeo, Lei He, Xiaowei Ma, Xiaoyun Liu, Min Li, Taeok Bae   +9 more
doaj   +2 more sources

Targeting eIF5A combats breast cancer progression by ClpP‐dependent mitochondrial oxidative stress

Interdisciplinary Medicine
Breast cancer (BC) poses a persistent global health challenge, necessitating new therapeutic targets. The oncogenic translation factor Eukaryotic translation initiation factor 5A (eIF5A), while implicated in other cancers, lacks a mechanistic definition ...
Jinmei Zhu, Baoyuan Tang, Bei Xie, Haohua Deng, Haitang Yang, Lei Ma, Ziqing Zhang, Yicheng Ma, Xingyuan Ma, Shuaiyang Wang, Jing Li, Lei Zhao, Wengui Shi, Linjing Li   +13 more
doaj   +2 more sources

Purification of the Caseinolytic protease ClpP.

, 2022
The caseinolytic protease P (ClpP) is an essential protein for bacteria and bacterial derived organelles. It belongs to the AAA+ family of proteases and has proteolytic activity, thereby, it plays an important role in protein digestion. This protease is involved in essential processes such as, cellular regulatory mechanisms, protein homeostasis ...
Pedrós Manzanares, Laura, Brötz-Oesterhelt, Heike   +1 more
openaire   +2 more sources

UNDERSTANDING THE ACTIVATION OF BACTERIAL PROTEASE CLPP BY ACYLDEPSIPEPTIDE ANTIBIOTIC [PDF]

, 2014
Acyldepsipeptide (ADEP1) is an antibiotic that binds to Escherichia coli ClpP, mimicking the interaction that the protease typically establishes with ClpA/ClpX ATPases in bacterial cells. Binding of ADEP1 causes the N-terminal end of the ClpP to adopt a structured β-hairpin and triggers opening of the axial gate in the tetradecameric ClpP.
Ahsan, Bilal
openaire   +3 more sources