Results 141 to 150 of about 5,899 (155)

The mitochondrial protease ClpP is a promising target for multiple myeloma treatment

Biochemical Pharmacology
Drug resistance and relapse are the major obstacles in multiple myeloma (MM) treatment, driving the search for novel therapeutics. The chemoactivation of mitochondrial caseinolytic protease P (ClpP) has shown to have anticancer effects on many tumors, but has seldom been elucidated in MM.
Xiang, Liu, Jinlong, Gu, Song, Liu, Jingcao, Huang, Linfeng, Li, Fangfang, Wang, Siyao, He, Ziyue, Mi, Yue, Zhang, Jingjing, Wen, Qianwen, Gao, Haonan, Yang, Yu, Feng, Hongmei, Luo, Xinyu, Zhai, Li, Zhang, Yuhuan, Zheng, Youfu, Luo, Ting, Niu   +18 more
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Lon and ClpP proteases participate in the physiological disintegration of bacterial inclusion bodies

Journal of Biotechnology, 2005
Aggregated protein is solubilized by the combined activity of chaperones ClpB, DnaK and small heat-shock proteins, and this could account, at least partially, for the physiological disintegration of bacterial inclusion bodies. In vivo, the involvement of proteases in this process had been suspected but not investigated.
Andrea, Vera, Anna, Arís, Mar, Carrió, Nuria, González-Montalbán, Antonio, Villaverde   +4 more
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Proteolytic Regulation in the Biosynthesis of Natural Product Via a ClpP Protease System

ACS Chemical Biology
Protein degradation is a tightly regulated biological process that maintains bacterial proteostasis. ClpPs are a highly conserved family of serine proteases that associate with the AAA + ATPase (an ATPase associated with diverse cellular activities) to degrade protein substrates. Identification and biochemical characterization of protein substrates for
Fumihiro Ishikawa, Chiharu Uchida, Genzoh Tanabe   +2 more
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Der Inhibitionsmechanismus der caseinolytischen Protease (ClpP)

Angewandte Chemie, 2013
Gersch, M., Gut, F., Korotkov, V., Lehmann, J., Böttcher, T., Rusch, M., Hedberg, C., Waldmann, H., Klebe, G., Sieber, S.   +9 more
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UNDERSTANDING THE ACTIVATION OF BACTERIAL PROTEASE CLPP BY ACYLDEPSIPEPTIDE ANTIBIOTIC

2014
Acyldepsipeptide (ADEP1) is an antibiotic that binds to Escherichia coli ClpP, mimicking the interaction that the protease typically establishes with ClpA/ClpX ATPases in bacterial cells. Binding of ADEP1 causes the N-terminal end of the ClpP to adopt a structured β-hairpin and triggers opening of the axial gate in the tetradecameric ClpP.
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Acyldepsipeptide Analogs Dysregulate Human Mitochondrial ClpP Protease Activity and Cause Apoptotic Cell Death

Cell Chemical Biology, 2018
Barbosa L R S, Sadhna Phanse, Robert Batey   +2 more
exaly  

Trapping and Proteomic Identification of Cellular Substrates of the ClpP Protease in Staphylococcus aureus

Journal of Proteome Research, 2013
Stephan Michalik, Lotte Jelsbak, Hanne Ingmer   +2 more
exaly  

Development of Antibiotics That Dysregulate the Neisserial ClpP Protease

ACS Infectious Diseases, 2020
Robert Batey, Keith S Wong, Emil F Pai
exaly  

Inhibition of the Mitochondrial Protease ClpP as a Therapeutic Strategy for Human Acute Myeloid Leukemia

Cancer Cell, 2015
Brian Raught, Jean Wang
exaly  

Regulation of adipose tissue biology by mitochondrial protease CLPP

Mitochondrien sind für die Aufrechterhaltung der zellulären Homöostase und die Orchestrierung von Signal-, Stoffwechsel- und Energieströmen von wesentlicher Bedeutung. Insbesondere im Zusammenhang mit Fettgewebe führt eine Fehlfunktion der Mitochondrien zu einer veränderten Differenzierung der Fettzellen, einem veränderten Fettstoffwechsel, einer ...
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