Results 11 to 20 of about 5,725 (156)

Reversible inhibition of the ClpP protease via an N-terminal conformational switch. [PDF]

Proc Natl Acad Sci U S A, 2018
Significance ClpP is a protease that degrades damaged or misfolded proteins. Consistent with its critical role in maintaining cellular homeostasis, inhibiting and dysregulating ClpP function has shown promise in fighting antibiotic resistance and in targeting cancer cells in acute myeloid leukemia.
Vahidi S, Ripstein ZA, Bonomi M, Yuwen T, Mabanglo MF, Juravsky JB, Rizzolo K, Velyvis A, Houry WA, Vendruscolo M, Rubinstein JL, Kay LE.   +11 more
europepmc   +6 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.
Geiger, S., Böttcher, T., Sieber, S., Cramer, P.   +3 more
openaire   +6 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
openaire   +4 more sources

Self-resistance mechanism to acyldepsipeptide antibiotics in the Streptomyces producer [PDF]

mBio
Clp proteases are ubiquitous in bacteria and play an important role in regulatory proteolysis and in maintaining protein homeostasis within the bacterial cell. They consist of a tetradecameric, proteolytic ClpP core and associated AAA+ Clp-ATPases.
Dhana Thomy, Laura Reinhardt, Elisa Liebhart, Mirita Franz-Wachtel, Boris Maček, Peter Sass, Heike Brötz-Oesterhelt   +6 more
doaj   +2 more sources

AAA+ chaperones and acyldepsipeptides activate the ClpP protease via conformational control [PDF]

Nature Communications, 2015
The Clp protease complex degrades a multitude of substrates, which are engaged by a AAA+ chaperone such as ClpX and subsequently digested by the dynamic, barrel-shaped ClpP protease. Acyldepsipeptides (ADEPs) are natural product-derived antibiotics that activate ClpP for chaperone-independent protein digestion.
Malte Gersch, Kirsten Famulla, Maria Dahmen, Christoph Göbl, Imran Malik, Klaus Richter, Vadim S. Korotkov, Peter Sass, Helga Rübsamen-Schaeff, Tobias Madl, Heike Brötz-Oesterhelt, Stephan A. Sieber   +11 more
openaire   +6 more sources

Discovery of coniferaldehyde as an inhibitor of caseinolytic protease to combat Staphylococcus aureus infections [PDF]

Molecular Medicine
The rising incidence of methicillin-resistant Staphylococcus aureus (MRSA) poses a significant threat to global public health, highlighting the urgent need for novel therapies and treatments in clinical settings.
Shufang Li, Yan Zhang, Jianfeng Wang, Hongfa Lv, Hongxia Ma, Lingcong Kong, Yonglin Zhou, Jingmin Gu, Wei Li, Qiaoling Zhang   +9 more
doaj   +2 more sources

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

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   +2 more sources

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

Commun Biol
Abstract 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. ClpC requires cooperation with adaptor proteins such as MecA for activation and complex formation with ClpP.
Azinas S, Wallden K, Katikaridis P, Jenne T, Schahl A, Mogk A, Carroni M.   +6 more
europepmc   +3 more sources

Antibiotic Acyldepsipeptides Stimulate the Streptomyces Clp-ATPase/ClpP Complex for Accelerated Proteolysis

mBio, 2022
Clp proteases consist of a proteolytic, tetradecameric ClpP core and AAA+ Clp-ATPases. Streptomycetes, producers of a plethora of secondary metabolites, encode up to five different ClpP homologs, and the composition of their unusually complex Clp ...
Laura Reinhardt, Dhana Thomy, Markus Lakemeyer, Linda Maria Westermann, Joaquin Ortega, Stephan A. Sieber, Peter Sass, Heike Brötz-Oesterhelt   +7 more
doaj   +1 more source

Technical data on the inhibition properties of some medicinal plant extracts towards caseinolytic protease proteolytic subunit of Plasmodium knowlesi

Data in Brief, 2021
Proteolytic subunit of the caseinolytic protease system of Plasmodium knowlesi (Pk-ClpP; EC 3.4.21.92) is considered a viable target for antimalarial drug development to eradicate P.
Raimalynah Abd Razak, Meiny Suzery, Rafida Razali, Zarina Amin, Ruzaidi Azli Mohd Mokhtar, Ping Chin Lee, Cahyo Budiman   +6 more
doaj   +1 more source