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 …
Thinking outside the box—novel antibacterials to tackle the resistance crisis
M Lakemeyer, W Zhao, FA Mandl… - Angewandte Chemie …, 2018 - Wiley Online Library
The public view on antibiotics as reliable medicines changed when reports about “resistant
superbugs” appeared in the news. While reasons for this resistance development are easily …
superbugs” appeared in the news. While reasons for this resistance development are easily …
Systematic analysis of drug combinations against Gram-positive bacteria
Drug combinations can expand options for antibacterial therapies but have not been
systematically tested in Gram-positive species. We profiled~ 8,000 combinations of 65 …
systematically tested in Gram-positive species. We profiled~ 8,000 combinations of 65 …
Evolution of resistance to a last-resort antibiotic in Staphylococcus aureus via bacterial competition
G Koch, A Yepes, KU Förstner, C Wermser, ST Stengel… - Cell, 2014 - cell.com
Antibiotic resistance is a key medical concern, with antibiotic use likely being an important
cause. However, here we describe an alternative route to clinically relevant antibiotic …
cause. However, here we describe an alternative route to clinically relevant antibiotic …
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 …
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 …
[HTML][HTML] Contribution of the Clp protease to bacterial survival and mitochondrial homoeostasis
A Illigmann, Y Thoma, S Pan, L Reinhardt… - Microbial …, 2021 - karger.com
Fast adaptation to environmental changes ensures bacterial survival, and proteolysis
represents a key cellular process in adaptation. The Clp protease system is a multi …
represents a key cellular process in adaptation. The Clp protease system is a multi …
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 …
Recent advances in Clp protease modulation to address virulence, resistance and persistence of MRSA infection
Y Ju, Q An, Y Zhang, K Sun, L Bai, Y Luo - Drug Discovery Today, 2021 - Elsevier
The Clp protease is an AAA+ protease that executes abnormally folded or malfunctioning
proteins, and has an important role in producing virulence factors, forming biofilms or …
proteins, and has an important role in producing virulence factors, forming biofilms or …
The development of small-molecule modulators for ClpP protease activity
The global spread of antibiotic resistance among important human pathogens emphasizes
the need to find new antibacterial drugs with a novel mode of action. The ClpP protease has …
the need to find new antibacterial drugs with a novel mode of action. The ClpP protease has …