Results 61 to 70 of about 152,432 (174)

Protein degradation in bacteria: focus on the ClpP protease

Nippon Saikingaku Zasshi
Proteins in the cells are born (synthesized), work, and die (decomposed). In the life of a protein, its birth is obviously important, but how it dies is equally important in living organisms. Proteases secreted into the outside of cells are used to decompose the external proteins and the degradation products are taken as the nutrients.
Fumihiro, Ishikawa, Michio, Homma, Genzoh, Tanabe, Takayuki, Uchihashi   +3 more
openaire   +2 more sources

Synthesis and Characterization of Small Molecule Dysregulators of the Bacterial ClpP Protease [PDF]

, 2018
Caseinolytic protease P (ClpP) is a protease highly conserved in bacteria and eukaryotes. With an ATPase partner, it functions to maintain protein homeostasis and regulated elimination of folded proteins.
Zhou, Jin Lin
core   +1 more source

Chloroplast Genome Characterization and Phylogenetic Implications of Reyesia and Salpiglossis (Salpiglossideae, Solanaceae)

Ecology and Evolution, Volume 16, Issue 11, November 2026.
We generated and compared the complete chloroplast genomes of Reyesia chilensis and Salpiglossis sinuata, two representative species of the tribe Salpiglossideae (subfamily Cestroideae) within Solanaceae. Comparative plastome analyses revealed highly conserved genome organization, codon usage, and repeat composition, while phylogenetic analyses ...
Jie Huang, Suyun Nong, Yancheng Zhang, Weibin Xu   +3 more
wiley   +1 more source

Mitochondrial Protease ClpP is a Target for the Anticancer Compounds ONC201 and Related Analogues [PDF]

ACS Chemical Biology, 2019
Abstract ONC201 is a first-in-class imipridone molecule currently in clinical trials for the treatment of multiple cancers. Despite enormous clinical potential, the mechanism of action is controversial. To investigate the mechanism of ONC201 and identify compounds with improved potency, we tested a series of novel ONC201 analogues (TR
Paul R. Graves, Lucas J. Aponte-Collazo, Emily M. J. Fennell, Adam C. Graves, Andrew E. Hale, Nedyalka Dicheva, Laura E. Herring, Thomas S. K. Gilbert, Michael P. East, Ian M. McDonald, Matthew R. Lockett, Hani Ashamalla, Nathaniel J. Moorman, Donald S. Karanewsky, Edwin J. Iwanowicz, Ekhson Holmuhamedov, Lee M. Graves   +16 more
openaire   +2 more sources

Disrupting α-Synuclein–ClpP interaction restores mitochondrial function and attenuates neuropathology in Parkinson’s disease models

Molecular Neurodegeneration
Background Mitochondrial dysfunction and α-Synuclein (αSyn) aggregation are defining features of Parkinson’s disease (PD), yet the mechanistic link between them remains poorly understood.
Di Hu, Xiaoyan Sun, Xin Qi
doaj   +1 more source

The Complete Chloroplast Genome of Dioscorea hypoglauca: Comparative Genomics and Phylogenetic Insights

Ecology and Evolution, Volume 16, Issue 10, October 2026.
We assembled and characterized the complete chloroplast genome of Dioscorea hypoglauca, a medicinally important yam species from southern China. The 153,219 bp genome exhibits a typical quadripartite structure, containing 129 genes (84 protein‐coding, 37 tRNA, and 8 rRNA genes), and comparative analyses with 22 other Dioscorea species revealed dynamic ...
Gang Li, Daofeng Gong, Xiang Cheng, Meng Li, Na Chen, Lei Cheng   +5 more
wiley   +1 more source

Validation of the Essential ClpP Protease in Mycobacterium tuberculosis as a Novel Drug Target [PDF]

Journal of Bacteriology, 2012
ABSTRACT Mycobacterium tuberculosis is a pathogen of major global importance. Validated drug targets are required in order to develop novel therapeutics for drug-resistant strains and to shorten therapy. The Clp protease complexes provide a means for quality control of cellular proteins; the proteolytic activity of ...
Juliane, Ollinger, Theresa, O'Malley, Edward A, Kesicki, Joshua, Odingo, Tanya, Parish   +4 more
openaire   +2 more sources

Trapping and proteomic identification of cellular substrates of the ClpP protease in Staphylococcus aureus

, 2013
In the important human pathogen Staphylococcus aureus the cytoplasmic ClpP protease is essential for mounting cellular stress responses and for virulence.
Lotte Jelsbak, Stefanie Krieger, Julie H. Andersen, Dorte Frees, Anders N. Varming, Dirk Albrecht, Knut Ohlsen, Michael Hecker, Ohlsen, Knut, Hecker, Michael, Hanne Ingmer, Albrecht, Dirk, Jelsbak, Lotte, Ulf Gerth, Ingmer, Hanne, Jingyuan Feng, Krieger, Stefanie, Feng, Jingyuan, Frees, Dorte, Andersen, Julie H., Gerth, Ulf, Stephan Michalik, Michalik, Stephan, Varming, Anders Nissen   +23 more
core   +1 more source

Investigating the Interaction Mechanism of ClpP Protease with Small Molecule Antimicrobials Using H/D Exchange Mass Spectrometry [PDF]

, 2022
The caseinolytic protease P (ClpP) is a cylindrical serine protease that works together with energy-dependent unfoldases to degrade target proteins. In prokaryotes, the ClpP degradation machinery plays an essential role in maintaining proteostasis and is
Brozdnychenko, Dmytro
core   +1 more source

Structure-function analysis of the bacterial ClpE-ClpP AAA+ protease. [PDF]

J Biol Chem
General and regulatory proteolysis in bacteria is executed by a set of ATP-dependent proteases composed of hexameric ring-forming AAA+ proteins and associated peptidase barrels (e.g., ClpP). These AAA+ proteases play crucial roles in stress protection and bacterial virulence. Here, we provide the first biochemical characterization of the potential drug
De Rosa M, Maag L, Flemming D, Sinning I, Carroni M, Mogk A.   +5 more
europepmc   +4 more sources