Enzyme inhibitor discovery by activity-based protein profiling
MJ Niphakis, BF Cravatt - Annual review of biochemistry, 2014 - annualreviews.org
Eukaryotic and prokaryotic organisms possess huge numbers of uncharacterized enzymes.
Selective inhibitors offer powerful probes for assigning functions to enzymes in native …
Selective inhibitors offer powerful probes for assigning functions to enzymes in native …
[HTML][HTML] ClpP protease, a promising antimicrobial target
C Moreno-Cinos, K Goossens, IG Salado… - International journal of …, 2019 - mdpi.com
The caseinolytic protease proteolytic subunit (ClpP) is a serine protease playing an
important role in proteostasis of eukaryotic organelles and prokaryotic cells. Alteration of …
important role in proteostasis of eukaryotic organelles and prokaryotic cells. Alteration of …
Activity-based proteome profiling of potential cellular targets of orlistat− an FDA-approved drug with anti-tumor activities
Orlistat, or tetrahydrolipstatin (THL), is an FDA-approved antiobesity drug with potential
antitumor activities. Cellular off-targets and potential side effects of Orlistat in cancer …
antitumor activities. Cellular off-targets and potential side effects of Orlistat in cancer …
The natural product cyclomarin kills Mycobacterium tuberculosis by targeting the ClpC1 subunit of the caseinolytic protease
EK Schmitt, M Riwanto, V Sambandamurthy… - Angewandte Chemie …, 2011 - infona.pl
Target practice: The target of the antibiotic cyclomarin A was identified in Mycobacterium.
Cyclomarin A (see structure) binds the regulatory subunit of the Clp protease complex with …
Cyclomarin A (see structure) binds the regulatory subunit of the Clp protease complex with …
Clp chaperones and proteases are central in stress survival, virulence and antibiotic resistance of Staphylococcus aureus
Intracellular proteolysis carried out by energy-dependent proteases is one of the most
conserved biological processes. In all cells proteolysis maintains and shapes the cellular …
conserved biological processes. In all cells proteolysis maintains and shapes the cellular …
Natural products and their biological targets: proteomic and metabolomic labeling strategies
T Böttcher, M Pitscheider… - Angewandte Chemie …, 2010 - Wiley Online Library
Activity‐based protein profiling (ABPP) has matured into a standard method for the fast,
sensitive, and selective identification of enzyme activity and inhibitors in proteomes. By …
sensitive, and selective identification of enzyme activity and inhibitors in proteomes. By …
ClpP inhibitors are produced by a widespread family of bacterial gene clusters
The caseinolytic protease (ClpP) is part of a highly conserved proteolytic complex whose
disruption can lead to antibacterial activity but for which few specific inhibitors have been …
disruption can lead to antibacterial activity but for which few specific inhibitors have been …
[HTML][HTML] AAA+ chaperones and acyldepsipeptides activate the ClpP protease via conformational control
The Clp protease complex degrades a multitude of substrates, which are engaged by a
AAA+ chaperone such as ClpX and subsequently digested by the dynamic, barrel-shaped …
AAA+ chaperone such as ClpX and subsequently digested by the dynamic, barrel-shaped …
Progress and prospects for small-molecule probes of bacterial imaging
O Kocaoglu, EE Carlson - Nature chemical biology, 2016 - nature.com
Fluorescence microscopy is an essential tool for the exploration of cell growth, division,
transcription and translation in eukaryotes and prokaryotes alike. Despite the rapid …
transcription and translation in eukaryotes and prokaryotes alike. Despite the rapid …
[HTML][HTML] Conformational control of the bacterial Clp protease by natural product antibiotics
IT Malik, H Brötz-Oesterhelt - Natural product reports, 2017 - pubs.rsc.org
Covering: up to 2017 The bacterial Clp protease is a highly conserved and structurally
versatile machine. It has gained a lot of recognition during the last decade as a novel …
versatile machine. It has gained a lot of recognition during the last decade as a novel …