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 …
unneeded proteins in bacteria, archaea and eukaryotes. This process involves the ATP …
Bacterial proteases, untapped antimicrobial drug targets
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 …
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 …
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 …
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 …
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 …
important role in proteostasis of eukaryotic organelles and prokaryotic cells. Alteration of …
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 …
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 …
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
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 …
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 …
ATPases associated with diverse activities (AAA+) partners to execute ATP-dependent …