Results 111 to 120 of about 152,432 (174)

Stress induction of the Bacillus subtilis clpP gene encoding a homologue of the proteolytic component of the Clp protease and the involvement of ClpP and ClpX in stress tolerance

, 1998
International audienceThe Bacillus subtilis clpP gene, encoding the proteolytic component of the Clp or Ti protease, was cloned and sequenced. The amount of clpP-specific mRNA increased after heat shock, salt and ethanol stress, as well as after ...
Elke Krüger, Ulf Gerth, Tarek Msadek, Michael Hecker, Gerth, Ulf, Krüger, Elke, Derré, Isabelle, Hecker, Michael, Msadek, Tarek, Isabelle Derré   +9 more
core   +1 more source

Dynamic Oligomerization Processes and Functional Characterization of Bacterial ClpP Protease

YAKUGAKU ZASSHI
ClpP protease is a highly conserved serine protease that plays a crucial role in bacterial protein quality control alongside its partner AAA+ ATPases. ClpP assembles into a barrel-shaped tetradecamer that degrades unfolded or misfolded proteins translocated by ATP-driven unfoldases, such as ClpC, ClpX, or ClpA.
openaire   +2 more sources

Harmaline to Human Mitochondrial Caseinolytic Serine Protease Activation for Pediatric Diffuse Intrinsic Pontine Glioma Treatment

Pharmaceuticals
Diffuse intrinsic pontine glioma (DIPG), affecting children aged 4–7 years, is a rare, aggressive tumor that originates in the pons and then spreads to nearby tissue.
Morena Miciaccia, Francesca Rizzo, Antonella Centonze, Gianfranco Cavallaro, Marialessandra Contino, Domenico Armenise, Olga Maria Baldelli, Roberta Solidoro, Savina Ferorelli, Pasquale Scarcia, Gennaro Agrimi, Veronica Zingales, Elisa Cimetta, Simone Ronsisvalle, Federica Maria Sipala, Paola Loguercio Polosa, Cosimo Gianluca Fortuna, Maria Grazia Perrone, Antonio Scilimati   +18 more
doaj   +1 more source

Ureadepsipeptides as ClpP Activators

, 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   +1 more source

Structure-guided development of selective caseinolytic protease P agonists as antistaphylococcal agents

Cell Reports Medicine
Summary: Methicillin-resistant Staphylococcus aureus is a ubiquitous pathogen, posing a serious threat to human health worldwide. Thus, there is a high demand for antibiotics with distinct targets. Caseinolytic protease P (ClpP) is a promising target for
Tao Zhang, Pengyu Wang, Hailing Zhou, Bingyan Wei, Yanling Zhao, Jiahui Li, Min Zhang, Wenjuan Wu, Lefu Lan, Jianhua Gan, Cai-Guang Yang   +10 more
doaj   +1 more source

Structure of the central Staphylococcus aureus AAA+ protease MecA/ClpC/ClpP

Communications Biology
Abstract Bacterial AAA+ proteases are composed of a AAA+ partner (e.g. ClpC) and an associated peptidase (e.g. ClpP). They represent ATP-fuelled and self-compartmentalized proteolytic machines that are crucial for stress resistance and virulence.
Stavros Azinas, Karin Wallden, Panagiotis Katikaridis, Timo Jenne, Adrien Schahl, Axel Mogk, Marta Carroni   +6 more
openaire   +3 more sources

Subunit Stoichiometry, Evolution, and Functional Implications of an Asymmetric Plant Plastid ClpP/R Protease Complex in Arabidopsis    

, 2011
The caseinolytic protease (Clp) protease system has been expanded in plant plastids compared with its prokaryotic progenitors. The plastid Clp core protease consists of five different proteolytic ClpP proteins and four different noncatalytic ClpR ...
Paul Dominic B. Olinares, Klaas J. van Wijk, Jitae Kim, Jerrold I. Davis   +3 more
core   +1 more source

Imipridone Anticancer Compounds Ectopically Activate the ClpP Protease and Represent a New Scaffold for Antibiotic Development. [PDF]

Genetics, 2020
Jacques S, van der Sloot AM, C Huard C, Coulombe-Huntington J, Tsao S, Tollis S, Bertomeu T, Culp EJ, Pallant D, Cook MA, Bonneil E, Thibault P, Wright GD, Tyers M.   +13 more
europepmc   +1 more source

Targeting ClpP Protease: Emerging Therapeutic Strategies and Small-Molecule Modulators in Drug Discovery. [PDF]

Med Res Rev
Liu L, Yu M, Li X, Xu J, Xie S, Xu S, Yao H.   +6 more
europepmc   +1 more source

Allosteric control of the bacterial ClpC/ClpP protease and its hijacking by antibacterial peptides. [PDF]

EMBO J
Jenne T, Engelhardt L, Baronaite I, Levy D, Riven I, Malolepszy M, Azinas S, Sych T, Sezgin E, Flemming D, Sinning I, Haran G, Carroni M, Mogk A.   +13 more
europepmc   +1 more source