Results 11 to 20 of about 9,876 (190)

ClpP Protease, a Promising Antimicrobial Target. [PDF]

Int J Mol Sci, 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.
Moreno-Cinos C, Goossens K, Salado IG, Van Der Veken P, De Winter H, Augustyns K.   +5 more
europepmc   +7 more sources

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

Proc Natl Acad Sci U S A
AbstractHuman 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.
Goncalves MM, Uday AB, Forrester TJB, Currie SQW, Kim AS, Feng Y, Jitkova Y, Velyvis A, Harkness RW, Kimber MS, Schimmer AD, Zeytuni N, Vahidi S.   +12 more
europepmc   +5 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

Mycobacterium tuberculosis ClpP Proteases Are Co-transcribed but Exhibit Different Substrate Specificities [PDF]

PLoS ONE, 2013
PMCID: PMC3613350This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are ...
A Bellier, A Milano, A Singh, A Wawrzynow, AM Sherrid, AM Socha, Amanda C. Brown, Anil Kumar Tyagi, CA Pashley, D Weichart, DG Muttucumaru, DL Schuessler, Dorothée L. Schuessler, E Kruger, GR Stewart, H Brotz-Oesterhelt, H Ingvarsson, HI Boshoff, I Levchenko, J Braman, J Kirstein, J Ollinger, J Porankiewicz, JB Andersen, JH Kim, JM Flynn, LE Thomsen, LG Wayne, M Estorninho, M Gomez, MC Blokpoel, ND Rawlings, O Dussurget, P Carroll, P Carroll, P Gueneau de Novoa, R Manganelli, RM Raju, S Ahlawat, S Barik, S Engels, S Engels, S Mehra, S Russo, ST Cole, T Akopian, T Msadek, T Parish, Tanya Parish, Yoann Personne   +49 more
core   +22 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

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

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

The depletion of serine beta-lactamase-like protein (LACTB) ameliorates metabolic dysfunction-associated steatotic liver disease by reducing ubiquitin-mediated degradation of carnitine palmitoyltransferase 2. [PDF]

Diabetes Obes Metab
Abstract Aims Metabolic dysfunction–associated steatotic liver disease (MASLD) represents one of the most common chronic liver disorders worldwide, and its incidence continues to rise each year. Serine β‐lactamase‐like protein (LACTB) is a serine protease that plays a crucial role in lipid metabolism and hepatocellular carcinoma, but its function in ...
Shi W, Liu X, Wang N, Zhang Q, Gao J, Guan C, Li Y, Yang C, Bi S, Zou X, Zhong X.   +10 more
europepmc   +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

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