Results 41 to 50 of about 17,783 (200)

Matrix metalloproteinase 13 modulates intestinal epithelial barrier integrity in inflammatory diseases by activating TNF [PDF]

, 2013
Several pathological processes, such as sepsis and inflammatory bowel disease (IBD), are associated with impairment of intestinal epithelial barrier. Here, we investigated the role of matrix metalloproteinase MMP13 in these diseases.
Albanese CT, An Staes, Carlos López‐Otin, Claude Libert, Elien Van Wonterghem, Eline Dejonckheere, Filip Van Hauwermeiren, Kitagawa H, Kris Gevaert, Lesuffleur T, Nusrat A, Riet De Rycke, Roosmarijn E. Vandenbroucke, Schmitz H, Smirnova MG, Sofie Lodens   +15 more
core   +3 more sources

Cell Division Protein FtsZ Is Unfolded for N-Terminal Degradation by Antibiotic-Activated ClpP

mBio, 2020
Antibiotic acyldepsipeptides (ADEPs) deregulate ClpP, the proteolytic core of the bacterial Clp protease, thereby inhibiting its native functions and concomitantly activating it for uncontrolled proteolysis of nonnative substrates.
Nadine Silber, Stefan Pan, Sina Schäkermann, Christian Mayer, Heike Brötz-Oesterhelt, Peter Sass   +5 more
doaj   +1 more source

ClpP protease modulates bacterial growth, stress response, and bacterial virulence in Brucella abortus

Veterinary Research, 2023
The process of intracellular proteolysis through ATP-dependent proteases is a biologically conserved phenomenon. The stress responses and bacterial virulence of various pathogenic bacteria are associated with the ATP-dependent Clp protease. In this study,
Dongjie Sun, Yufu Liu, Xiaowei Peng, Hao Dong, Hui Jiang, Xuezheng Fan, Yu Feng, Jiali Sun, Kun Han, Qiang Gao, Jianrui Niu, Jiabo Ding   +11 more
doaj   +1 more source

Molecular Characterization of the ClpC AAA+ ATPase in the Biology of Chlamydia trachomatis

mBio, 2023
Bacterial AAA+ unfoldases are crucial for bacterial physiology by recognizing specific substrates and, typically, unfolding them for degradation by a proteolytic component. The caseinolytic protease (Clp) system is one example where a hexameric unfoldase
Stefan Pan, Aaron A. Jensen, Nicholas A. Wood, Beate Henrichfreise, Heike Brötz-Oesterhelt, Derek J. Fisher, Peter Sass, Scot P. Ouellette   +7 more
doaj   +1 more source

Inside the adaptation process of Lactobacillus delbrueckii subsp. lactis to bile [PDF]

, 2012
Progressive adaptation to bile might render some lactobacilli able to withstand physiological bile salt concentrations. In this work, the adaptation to bile was evaluated on previously isolated dairy strains of Lactobacillus delbrueckii subsp. lactis 200
Burns, Patricia, González de los Reyes-Gavilán, Clara, Margolles Barros, Abelardo, Reinheimer, Jorge A., Ruas-Madiedo, Patricia, Ruíz García, Lorena, Sánchez García, Borja, Vinderola, Gabriel   +7 more
core   +1 more source

Simultaneous Ablation of the Catalytic AMPK α-Subunit SNF1 and Mitochondrial Matrix Protease CLPP Results in Pronounced Lifespan Extension

Frontiers in Cell and Developmental Biology, 2021
Organismic aging is known to be controlled by genetic and environmental traits. Pathways involved in the control of cellular metabolism play a crucial role.
Daniela Heinz, Evgeniia Krotova, Andrea Hamann, Heinz D. Osiewacz   +3 more
doaj   +1 more source

Open and compressed conformations of Francisella tularensis ClpP [PDF]

, 2017
Caseinolytic proteases are large oligomeric assemblies responsible for maintaining protein homeostasis in bacteria and in so doing influence a wide range of biological processes.
Alexopoulos, Battye, Bond, Brötz-Oesterhelt, Böttcher, Böttcher, Chen, Cruickshank, Emsley, Evans, Frees, Gasteiger, Geiger, Gersch, Holm, Hunter, Ingvarsson, Kabsch, Krissinel, Lee, McCoy, Moynie, Murshudov, Sievers, Sowole, Touw, Winn, Yu, Zhang   +28 more
core   +2 more sources

Cross genome comparisons of serine proteases in Arabidopsis and rice

BMC Genomics, 2006
Background Serine proteases are one of the largest groups of proteolytic enzymes found across all kingdoms of life and are associated with several essential physiological pathways.
Sowdhamini R, Tripathi Lokesh P
doaj   +1 more source

Pyrazinamide triggers degradation of its target aspartate decarboxylase

Nature Communications, 2020
It has been shown that the bioactive component of pyrazinamide, pyrazinoic acid (POA), blocks coenzyme A biosynthesis in M. tuberculosis by binding to the aspartate decarboxylase PanD.
Pooja Gopal, Jickky Palmae Sarathy, Michelle Yee, Priya Ragunathan, Joon Shin, Shashi Bhushan, Junhao Zhu, Tatos Akopian, Olga Kandror, Teck Kwang Lim, Martin Gengenbacher, Qingsong Lin, Eric J. Rubin, Gerhard Grüber, Thomas Dick   +14 more
doaj   +1 more source

Factor XI Deficiency Alters the Cytokine Response and Activation of Contact Proteases during Polymicrobial Sepsis in Mice. [PDF]

PLoS ONE, 2016
Sepsis, a systemic inflammatory response to infection, is often accompanied by abnormalities of blood coagulation. Prior work with a mouse model of sepsis induced by cecal ligation and puncture (CLP) suggested that the protease factor XIa contributed to ...
Charles E Bane, Ivan Ivanov, Anton Matafonov, Kelli L Boyd, Qiufang Cheng, Edward R Sherwood, Erik I Tucker, Stephen T Smiley, Owen J T McCarty, Andras Gruber, David Gailani   +10 more
doaj   +1 more source