Results 181 to 190 of about 18,135 (204)
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ClpP: A structurally dynamic protease regulated by AAA+ proteins

Journal of Structural Biology, 2012
Proteolysis is an important process for many aspects of bacterial physiology. Clp proteases carry out a large proportion of protein degradation in bacteria. These enzymes assemble in complexes that combine the protease ClpP and the unfoldase, ClpA or ClpX.
John A, Alexopoulos   +2 more
openaire   +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   +13 more
openaire   +2 more sources

An amino acid domino effect orchestrates ClpP's conformational states

Current Opinion in Chemical Biology, 2017
Maintaining the cellular protein homeostasis means managing life on the brink of death. This balance is largely based on precise fine-tuning of enzyme activities. For instance, the ClpP protease possesses several conformational switches which are fundamental to regulating its activity.
Matthias, Stahl, Stephan A, Sieber
openaire   +2 more sources

The regulation of Porphyromonas gingivalis biofilm formation by ClpP

Biochemical and Biophysical Research Communications, 2019
Porphyromonas gingivalis is one of the most commonly detected pathogens in periodontal disease and root canal infections. Its viability and pathogenicity are greatly increased in plaque biofilms. Some caseinolytic proteases (Clp) reportedly regulate biofilm formation by various pathogenic bacteria, including P. gingivalis.
Lu, He   +3 more
openaire   +2 more sources

The development of small-molecule modulators for ClpP protease activity

Molecular BioSystems, 2017
Deregulating ClpP activity either through inhibition or overactivation could lead to antibacterial activity.
Fei, Ye, Jiahui, Li, Cai-Guang, Yang
openaire   +2 more sources

Patenting perspective of modulators of ClpP endopeptidase: 2019-present

Expert Opinion on Therapeutic Patents
ClpP is a highly conserved serine protease that plays a crucial role in maintaining protein homeostasis in both bacterial cells and human mitochondria. Several studies have demonstrated the potential of ClpP as a drug target, with ClpP modulators, including both inhibitors and activators, showing promise in treating a range of conditions such as drug ...
Zhenyu, Wang   +3 more
openaire   +2 more sources

The Role of ClpP in Protein Expression of Streptococcus pneumoniae

Current Microbiology, 2011
Previous reports suggest that ClpP proteolytic activity is important not only for cell physiology but also for regulation of virulence properties of Streptococcus pneumoniae (S. pneumoniae). In order to get a more comprehensive picture of the role of ClpP protease on protein expression in S. pneumoniae D39 and how it relates to physiology and virulence,
Qun, Zhang   +6 more
openaire   +2 more sources

Selektive Aktivierung der humanen caseinolytischen Protease P (ClpP)

Angewandte Chemie, 2018
AbstractDie caseinolytische Protease P (ClpP) ist die proteolytische Komponente des Protein‐Abbau‐Komplexes ClpXP. Ihre genaue Funktion und Regulation sind größtenteils unerforscht. Hier stellen wir eine niedermolekulare Verbindung (D9) vor, die durch Nachahmung des natürlichen Chaperons ClpX als potenter und Spezies‐selektiver Aktivator der humanen ...
Matthias Stahl   +9 more
openaire   +1 more source

Assessing CLPPs using MicroResp™

Journal of Soils and Sediments, 2007
Stephen J. Chapman   +2 more
openaire   +1 more source

Der Inhibitionsmechanismus der caseinolytischen Protease (ClpP)

Angewandte Chemie, 2013
Gersch, M.   +9 more
openaire   +2 more sources

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