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 …

[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 …

Activity-based proteome profiling of potential cellular targets of orlistat− an FDA-approved drug with anti-tumor activities

PY Yang, K Liu, MH Ngai, MJ Lear… - Journal of the …, 2010 - ACS Publications
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 …

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 …

Clp chaperones and proteases are central in stress survival, virulence and antibiotic resistance of Staphylococcus aureus

D Frees, U Gerth, H Ingmer - International Journal of Medical Microbiology, 2014 - Elsevier
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 …

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 …

ClpP inhibitors are produced by a widespread family of bacterial gene clusters

EJ Culp, D Sychantha, C Hobson, AC Pawlowski… - Nature …, 2022 - nature.com
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 …

[HTML][HTML] AAA+ chaperones and acyldepsipeptides activate the ClpP protease via conformational control

M Gersch, K Famulla, M Dahmen, C Göbl… - Nature …, 2015 - nature.com
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 …

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 …

[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 …