Results 81 to 90 of about 7,556 (201)
Protein purification to analyze AAA+ proteolytic machine in vitro [PDF]
, 2011 The ATP-dependent ClpXP protease of Escherichia coli consists of two subunits, the ClpP subunit, which has the proteolytic activity and the AAA+ motor ClpX, which mechanically unfolds and translocates substrates for ClpP degradation.
Rojas, Diego F.
core +2 more sources
Solution Structure of the Dimeric Zinc Binding Domain of the Chaperone ClpX [PDF]
Journal of Biological Chemistry, 2003 ClpX (423 amino acids), a member of the Clp/Hsp100 family of molecular chaperones and the protease, ClpP, comprise a multimeric complex supporting targeted protein degradation in Escherichia coli. The ClpX sequence consists of an NH2-terminal zinc binding domain (ZBD) and a COOH-terminal ATPase domain.
Logan W, Donaldson +2 more
openaire +2 more sources
MicrobiologyOpen, Volume 15, Issue 2, April 2026.The genomes of coagulase‐negative staphylococci (CoNS) isolated during sequential ear and eye infections in a healthy adult are analyzed. We highlight the identification of a community‐acquired S. capitis subsp. urealyticus ST1 lineage carrying a mosaic SCCmec IV element, linking common skin commensals to multidrug‐resistant strains associated with ...
Soo Sum Lean +6 more
wiley +1 more source
ClpXP protease targets long-lived DNA translocation states of a helicase-like motor to cause restriction alleviation [PDF]
, 2014 We investigated how Escherichia coli ClpXP targets the helicase-nuclease (HsdR) subunit of the bacterial Type I restriction–modification enzyme EcoKI during restriction alleviation (RA).
Diffin, Fiona M +2 more
core +2 more sources
Interdisciplinary Medicine, Volume 4, Issue 2, March 2026.The sulfonated zwitterionic photosensitizer (PYSO3) is synthesized by reacting maleic anhydride derivatives with 4‐aminopyridine to form PY, followed by sulfonation with 1,4‐butane sultone. It exhibits both photothermal and photodynamic properties, enabling effective eradication of MRSA and biofilms, as well as promoting wound healing in mice ...
Changxu Zhu +10 more
wiley +1 more source
The Mycobacterium tuberculosis ClpP1P2 Protease Interacts Asymmetrically with Its ATPase Partners ClpX and ClpC1. [PDF]
PLoS ONE, 2015 Clp chaperone-proteases are cylindrical complexes built from ATP-dependent chaperonerings that stack onto a proteolytic ClpP double-ring core to carry out substrate protein degradation.Interaction of the ClpP particle with the chaperone is mediated by an
Julia Leodolter +2 more
doaj +1 more source
Heliyon, 2023 A rare case of bacteremia caused by Escherichia albertii, in a 50-year-old male with liver cirrhosis was reported. Clear, colorless, and circular colonies were recovered on blood agar after 24 h of aerobic incubation at 37 °C.
Qian Liu +13 more
doaj +1 more source
Segregation of molecules at cell division reveals native protein localization [PDF]
, 2014 We introduce a non-intrusive method exploiting post-division single-cell variability to validate protein localization. The results show that Clp proteases, widely reported to form biologically relevant foci, are in fact uniformly distributed inside ...
Baker, Tania A. +4 more
core +1 more source
Molecular Nutrition &Food Research, Volume 70, Issue 6, 29 March 2026.Probiogenomic and in vitro analyses revealed that Lacticaseibacillus paracasei UFTM 2.9 does not exhibit virulence determinants, produces inhibitory compounds against pathogenic bacteria, and possesses 170 genes associated with probiotics, which corroborates its metabolic versatility and potential for survival and functionality in the gastrointestinal ...
Bárbara R. Fonseca +11 more
wiley +1 more source
Crystal structure of Mycobacterium tuberculosis ClpP1P2 suggests a model for peptidase activation by AAA+ partner binding and substrate delivery [PDF]
, 2014 Caseinolytic peptidase P (ClpP), a double-ring peptidase with 14 subunits, collaborates with ATPases associated with diverse activities (AAA+) partners to execute ATP-dependent protein degradation.
Carney, Daniel W. +3 more
core +1 more source