Results 131 to 140 of about 147,909 (161)

Exploring the Antibiotic Potential of a Serine Protease from <i>Solanum trilobatum</i> Against <i>Staphylococcus aureus</i> Biofilms. [PDF]

Infect Dis Rep
Radhakrishnan M, Balu KE, Karthik L, Nagampalli RSK, Nadendla EK, Krishnasamy G.   +5 more
europepmc   +1 more source

The gut-brain axis in Binge Eating Disorder: From microbial dysbiosis to vagal dysfunction and therapeutic intervention. [PDF]

Gut Microbes Rep
Rossetti C, Aeschlimann L, Praz L, Boutrel B.   +3 more
europepmc   +1 more source

Immune System Controls Gut Bacterial and Host Peptide Signals in Appetite Regulation: Towards Specific Immunotherapy of Eating Disorders.

Neuroimmunomodulation
Fetissov SO.
europepmc   +1 more source

A Photocrosslinking Probe to Capture the Substrates of Caseinolytic Protease P

Angewandte Chemie - International Edition
Protein homeostasis in bacteria is regulated by proteases such as the tetradecameric caseinolytic protease P (ClpP). Although substrates of ClpP have been successfully deciphered in genetically engineered cells, methods which directly trap processed ...
Christina Ludwig, Stephan A. Sieber, Thomas F Gronauer   +2 more
exaly   +5 more sources

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Targeting Caseinolytic Protease P and Its AAA1 Chaperone for Tuberculosis Treatment

Drug Discovery Today, 2023
Caseinolytic protease P with its AAA1 chaperone, known as Mycobacterium tuberculosis (Mtb)ClpP1P2 proteolytic machinery, maintains protein homeostasis in Mtb cells and is essential for bacterial survival. It is regarded as an important biological target with the potential to address the increasingly serious issue of multidrug-resistant (MDR) TB.
Lang Bai, Youfu Luo, Zhiqiang Qiu
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.
Matthias Stahl, Vadim S. Korotkov, Dóra Balogh, Leonhard M. Kick, Malte Gersch, Axel Pahl, Pavel Kielkowski, Klaus Richter, Sabine Schneider, Stephan A. Sieber   +9 more
openaire   +3 more sources

Identification, Structure, and Caseinolytic Properties of Milk-Clotting Proteases From Moringa oleifera Flowers

Food Research International, 2022
The protein extract of Moringa oleifera flowers is reported to have milk-clotting activity (MCA), but information regarding its protease is unclear. In this study, two milk-clotting proteases (MoFP 12 and MoFP 13) with molecular weights of 42.304 kDa and 31.741 kDa, respectively, were isolated and identified from M.
Qiong Zhao, Aixiang Huang
exaly   +3 more sources

Design and synthesis of tailored human caseinolytic protease P inhibitors

Chemical Communications, 2018
To expedite functional studies of human ClpP we introduce tailored small molecule inhibitors. These compounds are active against the proteolytic ClpXP complex. Target identification elucidates anti-proliferative effects against cancer cells.
Thomas F. Gronauer, Melanie M. Mandl, Markus Lakemeyer, Mathias W. Hackl, Martina Meßner, Vadim S. Korotkov, Johanna Pachmayr, Stephan A. Sieber   +7 more
openaire   +2 more sources

Antibodies Against Homologous Microbial Caseinolytic Proteases P Characterise Primary Biliary Cirrhosis

Journal of Hepatology, 2002
Antibodies to caseinolytic protease P(177-194) (ClpP(177-194)) of the proteolytic subunit of the Clp complex of Escherichia coli (E. coli) are uniquely present in primary biliary cirrhosis (PBC). Molecular mimicry between the regulatory subunit ClpX and the principal T-cell epitope of pyruvate dehydrogenase complex (PDC-E2) in PBC, has been proposed to
Andrew Kenneth Burroughs, Diego Vergani, Dimitrios P. Bogdanos   +2 more
exaly   +4 more sources