Results 11 to 20 of about 13,032 (201)

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   +4 more sources

Human CLPP reverts the longevity phenotype of a fungal ClpP deletion strain [PDF]

Nature Communications, 2013
Mitochondrial maintenance crucially depends on the quality control of proteins by various chaperones, proteases and repair enzymes. While most of the involved components have been studied in some detail, little is known on the biological role of the ...
Fischer, Fabian, Hamann, Andrea, Weil, Andrea, Osiewacz, Heinz D.   +3 more
core   +5 more sources

Generation of Lasso Peptide-Based ClpP Binders [PDF]

International Journal of Molecular Sciences, 2021
The Clp protease system fulfills a plethora of important functions in bacteria. It consists of a tetradecameric ClpP barrel holding the proteolytic centers and two hexameric Clp-ATPase rings, which recognize, unfold, and then feed substrate proteins into
Heike Brötz-Oesterhelt, Malik, Imran T., Imran T. Malik, Hegemann, Julian D., Brötz-Oesterhelt, Heike, Julian D. Hegemann, Malik, Imran Tarik   +6 more
core   +4 more sources

Ureadepsipeptides as ClpP Activators

ACS Infectious Diseases, 2019
Acyldepsipeptides are a unique class of antibiotics that act via allosterically dysregulated activation of the bacterial caseinolytic protease (ClpP). The ability of ClpP activators to kill nongrowing bacteria represents a new opportunity to combat deep ...
John M. Elmore (4867525), Darcie J. Miller (233978), Ying Zhao (16546), Zhong Zheng (128181), Kim Lewis (20864), Miranda J. Wallace (4867528), Brian P. Conlon (3607313), Yong Li (15029), Richard E. Lee (284694), Robin B. Lee (520206), Elizabeth C. Griffith (1562614), Lei Yang (102719), Aman P. Singh (7541417), Martin N. Cheramie (7541423), Rajendra Tangallapally (2044195), William R. Shadrick (7541420), Jiuyu Liu (2428513), Michael D. LaFleur (7541426)   +17 more
core   +4 more sources

Elucidating the Molecular Impact of DA29‐Induced ClpP Chemoactivation on Mitochondrial Function [PDF]

The FASEB Journal, Volume 40, Issue 20, 31 October 2026.
A promising approach to tackling DIPG, a lethal pediatric brain tumor, relies on small molecules capable of activating the human mitochondrial protease hClpP. The novel piperazine‐based compound DA29 specifically activates endogenous hClpP, thereby compromising mtDNA levels, mitoribosomes, and OXPHOS complex subunits.
Francesca Rizzo, Morena Miciaccia, Maria Grazia Perrone, Antonio Scilimati, Paola Loguercio Polosa, Francesco Bruni   +5 more
wiley   +2 more sources

Pharmacological inhibition of CLPP stabilizes LETMD1 to boost thermogenesis and alleviate obesity [PDF]

Adipocyte
Obesity poses a severe global health burden, and activating adipose thermogenesis offers a promising therapeutic avenue. However, the contribution of mitochondrial proteostasis to thermogenic regulation remains elusive.
Huiwen Yuan, Yuqing Deng, Jingang Wang, Bing Luan, Zhen-Ning Zhang   +4 more
doaj   +2 more sources

Design, Synthesis, and Structure-Activity Relationships of Novel Piperidine-Fused Imidazolone ClpP Activators as Potential Anti-Cancer Agents [PDF]

Molecules
Caseinolytic protease P (ClpP) is essential for maintaining mitochondrial protein homeostasis, and its activation has emerged as an attractive cancer therapeutic strategy. However, ONC201 is currently the only approved ClpP activator, and its low potency
Shanshan Chen, Xinyi Lin, Min Guo, Ruqi Lei, Beijing Chen, Yubo Zhou, Aijun Qiao, Qi Huang, Mingliang Wang   +8 more
doaj   +2 more sources

Selective activator of human ClpP triggers cell cycle arrest to inhibit lung squamous cell carcinoma

Nature Communications, 2023
Chemo-activation of mitochondrial ClpP exhibits promising anticancer properties. However, we are currently unaware of any studies using selective and potent ClpP activators in lung squamous cell carcinoma.
Lin-Lin Zhou, Tao Zhang, Yun Xue, Chuan Yue, Yihui Pan, Pengyu Wang, Teng Yang, Meixia Li, Hu Zhou, Kan Ding, Jianhua Gan, Hongbin Ji, Cai-Guang Yang   +12 more
doaj   +2 more sources

Phylogenomics Clarifies Plastome Reduction and Phylogenetic Relationships in Monotropoideae [PDF]

Ecology and Evolution, Volume 16, Issue 10, October 2026.
Phylogenetic Relationships of the Ericaceae Family. ML bootstrap/MP jackknife supported tree from Freudenstein et al. based on (A) nuclear loci, (B) plastid loci, (C) mitochondrial loci, and (D) nuclear+plastid datasets (E). Our combined nuclear + plastid parsimony tree for main groups.
Guocui Deng, Kaili Duan, Niyan Xiang, Feng Gao, Peng Zhan, Rui Shu, Qingsong Lin, Qing Zuo, Tao Yuan   +8 more
wiley   +2 more sources

Small molecule activators of the mitochondrial protease ClpP induce senescence in triple-negative breast cancer cells and sensitize cells to the Bcl-2 inhibitor venetoclax [PDF]

Cell Death and Disease
ONC201 is a first-in-class, FDA-approved small molecule activator of the mitochondrial ATP-dependent caseinolytic peptidase P (ClpP). This and other related small molecules referred to as ClpP agonists, exert antiproliferative effects in several cancer ...
Sabrina C. D. Daglish, Owen G. Canterbury, Paul R. Graves, Sarah A. Carter, Sydney M. Beese, Brandon L. Mouery, Maggie A. Hynek, Elizabeth C. Moorman, Andrei J. Mistreanu, Aadra P. Bhatt, Nestor Tellez, Mitchell T. Butler, Lucas J. Aponte-Collazo, Emily M. J. Fennell, Laura E. Herring, Scott Lyons, C. Allie Mills, Hani Ashamalla, Edwin J. Iwanowicz, John P. Morris IV, James E. Bear, Yoshimi Endo Greer, Stanley Lipkowitz, Lee M. Graves   +23 more
doaj   +2 more sources