Mechanistic insights into bacterial AAA+ proteases and protein-remodelling machines

AO Olivares, TA Baker, RT Sauer - Nature Reviews Microbiology, 2016 - nature.com
To maintain protein homeostasis, AAA+ proteolytic machines degrade damaged and
unneeded proteins in bacteria, archaea and eukaryotes. This process involves the ATP …

Bacterial proteases, untapped antimicrobial drug targets

E Culp, GD Wright - The Journal of antibiotics, 2017 - nature.com
Bacterial proteases are an extensive collection of enzymes that have vital roles in cell
viability, stress response and pathogenicity. Although their perturbation clearly offers the …

Regulated proteolysis in bacteria

SA Mahmoud, P Chien - Annual review of biochemistry, 2018 - annualreviews.org
Regulated proteolysis is a vital process that affects all living things. Bacteria use energy-
dependent AAA+ proteases to power degradation of misfolded and native regulatory …

The role of ClpP protease in bacterial pathogenesis and human diseases

V Bhandari, KS Wong, JL Zhou… - ACS chemical …, 2018 - ACS Publications
In prokaryotic cells and eukaryotic organelles, the ClpP protease plays an important role in
proteostasis. The disruption of the ClpP function has been shown to influence the infectivity …

The tuberculosis drug discovery and development pipeline and emerging drug targets

K Mdluli, T Kaneko, A Upton - Cold Spring …, 2015 - perspectivesinmedicine.cshlp.org
The recent accelerated approval for use in extensively drug-resistant and multidrug-resistant-
tuberculosis (MDR-TB) of two first-in-class TB drugs, bedaquiline and delamanid, has …

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 …

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 …

Phenyl esters are potent inhibitors of caseinolytic protease P and reveal a stereogenic switch for deoligomerization

MW Hackl, M Lakemeyer, M Dahmen… - Journal of the …, 2015 - ACS Publications
Caseinolytic protease P (ClpP) represents a central bacterial degradation machinery that is
involved in cell homeostasis and pathogenicity. The functional role of ClpP has been studied …

Restriction of the conformational dynamics of the cyclic acyldepsipeptide antibiotics improves their antibacterial activity

DW Carney, KR Schmitz, JV Truong… - Journal of the …, 2014 - ACS Publications
The cyclic acyldepsipeptide (ADEP) antibiotics are a new class of antibacterial agents that
kill bacteria via a mechanism that is distinct from all clinically used drugs. These molecules …

Crystal structure of Mycobacterium tuberculosis ClpP1P2 suggests a model for peptidase activation by AAA+ partner binding and substrate delivery

KR Schmitz, DW Carney, JK Sello… - Proceedings of the …, 2014 - National Acad Sciences
Caseinolytic peptidase P (ClpP), a double-ring peptidase with 14 subunits, collaborates with
ATPases associated with diverse activities (AAA+) partners to execute ATP-dependent …