Results 41 to 50 of about 3,616 (191)
Strain-Dependent Recognition of a Unique Degradation Motif by ClpXP in
mSphere, 2016 Streptococcus mutans, a dental pathogen, has a remarkable ability to cope with environmental stresses. Under stress conditions, cytoplasmic proteases play a major role in controlling the stability of regulatory proteins and preventing accumulation of ...
Biswanath Jana +2 more
doaj +1 more source
Cryo-EM structure of the ClpXP protein degradation machinery [PDF]
Nature Structural & Molecular Biology, 2019 Abstract The ClpXP machinery is a two component protease complex performing targeted protein degradation in bacteria and eukaryotes. The complex consists of the AAA+ chaperone ClpX and the peptidase ClpP. The hexameric ClpX utilizes the energy of ATP binding and hydrolysis to engage, unfold and translocate substrates ...
Christos Gatsogiannis +4 more
openaire +5 more sources
Dynamics of Substrate Denaturation and Translocation by the ClpXP Degradation Machine [PDF]
Molecular Cell, 2000 ClpXP is a protein machine composed of the ClpX ATPase, a member of the Clp/Hsp100 family of remodeling enzymes, and the ClpP peptidase. Here, ClpX and ClpXP are shown to catalyze denaturation of GFP modified with an ssrA degradation tag. ClpX translocates this denatured protein into the proteolytic chamber of ClpP and, when proteolysis is blocked ...
Kim, Yong-In +4 more
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Engineering Synthetic Adaptors and Substrates for Controlled ClpXP Degradation [PDF]
Journal of Biological Chemistry, 2009 Facile control of targeted intracellular protein degradation has many potential uses in basic science and biotechnology. One promising approach to this goal is to redesign adaptor proteins, which can regulate proteolytic specificity by tethering substrates to energy-dependent AAA+ proteases.
Joseph H, Davis +2 more
openaire +2 more sources
eLife, 2020 The ClpXP degradation machine consists of a hexameric AAA+ unfoldase (ClpX) and a pair of heptameric serine protease rings (ClpP) that unfold, translocate, and subsequently degrade client proteins.
Zev A Ripstein +4 more
doaj +1 more source
Frontiers in Microbiology, 2021 The ClpX ATPase is critical for resistance to cell envelope targeting antibiotics in Bacillus anthracis, however, it is unclear whether this is due to its function as an independent chaperone or as part of the ClpXP protease.
Lang Zou +5 more
doaj +1 more source
Subunit-specific isotope labelling of heteromeric complexes using cell-free protein expression: application to the 760 kDa ClpXP molecular machine. [PDF]
RSC Chem BiolInternational audienceAn optimised, economical cell-free protocol for producing perdeuterated, methyl-labelled samples of the ClpXP machine, with separate labelling of the ClpX and ClpP components, enables the acquisition of high-resolution 2D methyl ...
Audibert A +11 more
europepmc +2 more sources
Scientific Reports, 2018 Protein degradation is a fundamental process in all living cells and is essential to remove both damaged proteins and intact proteins that are no longer needed by the cell.
Xinying Shi +4 more
doaj +1 more source
Molecular Glue Degraders of TEM β‐Lactamases by Periplasmic Protease DegP
Angewandte Chemie, EarlyView.Molecular glues are developed that target TEM‐family β‐lactamases to the bacterial protease DegP for degradation. β‐Lactamase inhibitor tazobactam is identified as accelerating TEM β‐lactamase degradation by DegP, which is further enhanced by linkerless incorporation of dipeptides enriched among DegP substrates.
Emilia K. Taylor +8 more
wiley +2 more sources
Characterization of Phd degradation by ClpXP [PDF]
, 2013 Proteolysis of Phd is required for the addictive response. ClpXP recognizes and degrades the Phd protein of the P1 plasmid addiction operon, however its mechanism of degradation is currently unknown.
Mertz, Nikki
core +1 more source