Results 151 to 160 of about 152,432 (174)

The Mechanism of Caseinolytic Protease (ClpP) Inhibition

Angewandte Chemie - International Edition, 2013
Christian Hedberg, Gerhard Klebe, Stephan A. Sieber   +2 more
exaly   +6 more sources

Dynamics of the ClpP Serine Protease: A Model for Self-Compartmentalized Proteases

Critical Reviews in Biochemistry and Molecular Biology, 2014
ClpP is a highly conserved serine protease present in most bacterial species and in the mitochondria of mammalian cells. It forms a cylindrical tetradecameric complex arranged into two stacked heptamers. The two heptameric rings of ClpP enclose a roughly spherical proteolytic chamber of about 51 Å in diameter with 14 Ser-His-Asp proteolytic active ...
Walid A Houry, Adedeji Ologbenla, Kaiyin Liu   +2 more
exaly   +3 more sources

Selective Activation of Human Caseinolytic Protease P (ClpP)

Angewandte Chemie - International Edition, 2018
AbstractCaseinolytic protease P (ClpP) is the proteolytic component of the ClpXP protein degradation complex. Eukaryotic ClpP was recently found to act within the mitochondria‐specific unfolded protein response (UPRmt). However, its detailed function and dedicated regulation remain largely unexplored.
Leonhard M Kick, Matthias Stahl, Klaus Richter   +2 more
exaly   +4 more sources

ClpP: A Distinctive Family of Cylindrical Energy-Dependent Serine Proteases

FEBS Letters, 2007
Processes maintaining protein homeostasis in the cell are governed by the activities of molecular chaperones that mainly assist in the folding of polypeptide chains and by a large class of proteases that regulate protein levels through degradation. ClpP proteases define a distinctive family of cylindrical, energy‐dependent serine proteases that are ...
Walid A Houry
exaly   +3 more sources

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.
Joaquin Ortega, Alba Guarné
exaly   +3 more sources

Acyldepsipeptide Analogs Dysregulate Human Mitochondrial ClpP Protease Activity and Cause Apoptotic Cell Death

Cell Chemical Biology, 2018
Acyldepsipeptides (ADEPs) are potential antibiotics that dysregulate the activity of the highly conserved tetradecameric bacterial ClpP protease, leading to bacterial cell death. Here, we identified ADEP analogs that are potent dysregulators of the human
Leandro Barbosa, Sadhna Phanse, Robert A. Batey   +2 more
exaly   +2 more sources

Characterization of mouse Clpp protease cDNA, gene, and protein

Mammalian Genome, 2000
Mutations that cause accumulation or rapid degradation owing to protein misfolding are a frequent cause of inherited disease in humans. In Escherichia coli, Clpp protease is one of the components of the protein quality control system that handles misfolded proteins.
Andresen, B S, Corydon, T J; id_orcid 0000-0003-3588-6350, Wilsbech, M, Bross, P; id_orcid 0000-0001-9526-8525, Hindkjaer, T F, Bolund, L, Gregersen, N, Schroeder, L D   +7 more
openaire   +3 more sources

The Role of ClpP Protease in Bacterial Pathogenesis and Human Diseases

ACS Chemical Biology, 2018
In prokaryotic cells and eukaryotic organelles, the ClpP protease plays an important role in proteostasis. The disruption of the ClpP function has been shown to influence the infectivity and virulence of a number of bacterial pathogens. More recently, ClpP has been found to be involved in various forms of carcinomas and in Perrault syndrome, which is ...
Vaibhav Bhandari, Keith S. Wong, Jin Lin Zhou, Mark F. Mabanglo, Robert A. Batey, Walid A. Houry   +5 more
openaire   +2 more sources

The Antibiotic ADEP Reprogrammes ClpP, Switching It From a Regulated to an Uncontrolled Protease

EMBO Molecular Medicine, 2009
A novel class of antibiotic acyldepsipeptides (designated ADEPs) exerts its unique antibacterial activity by targeting the peptidase caseinolytic protease P (ClpP). ClpP forms proteolytic complexes with heat shock proteins (Hsp100) that select and process substrate proteins for ClpP-mediated degradation. Here, we analyse the molecular mechanism of ADEP
Heike Brötz-Oesterhelt, Kürşad Turgay, Axel Mogk   +2 more
exaly   +3 more sources

The development of small-molecule modulators for ClpP protease activity

Molecular BioSystems, 2016
Abstract The global spread of antibiotic resistance among important human pathogens emphasizes the need to find new antibacterial drugs with a novel mode of action. The ClpP protease has been shown to demonstrate its pivotal importance to both the survival and the virulence of pathogenic bacteria during host infection.
Fei, Ye, Jiahui, Li, Cai-Guang, Yang
openaire   +2 more sources