Results 11 to 20 of about 5,166 (218)

P-1357. Comparative In Vitro Activity of Sulbactam-Durlobactam and Ampicillin-Sulbactam Against A. baumannii with and without PBP3 Mutation [PDF]

open access: goldOpen Forum Infectious Diseases
Abstract Background Treatment options for Acinetobacter baumannii are limited. The Infectious Diseases Society of America (IDSA) currently recommends the use of sulbactam-containing regimens whenever possible.
Thomas Lavoie   +2 more
europepmc   +4 more sources

PBP5 Complementation of a PBP3 Deficiency inEnterococcus hirae [PDF]

open access: greenJournal of Bacteriology, 2006
ABSTRACTThe low susceptibility of enterococci to β-lactams is due to the activity of the low-affinity penicillin-binding protein 5 (PBP5). One important feature of PBP5 is its ability to substitute for most, if not all, penicillin-binding proteins when they are inhibited.
Serge Leimanis   +6 more
openalex   +4 more sources

SAR and Structural Analysis of Siderophore-Conjugated Monocarbam Inhibitors of Pseudomonas aeruginosa PBP3 [PDF]

open access: greenACS Medicinal Chemistry Letters, 2015
A main challenge in the development of new agents for the treatment of Pseudomonas aeruginosa infections is the identification of chemotypes that efficiently penetrate the cell envelope and are not susceptible to established resistance mechanisms. Siderophore-conjugated monocarbams are attractive because of their ability to hijack the bacteria's iron ...
Kerry E. Murphy-Benenato   +15 more
openalex   +4 more sources

Molecular epidemiology of nontypeable haemophilus influenzae causing community-acquired pneumonia in adults [PDF]

open access: yesPLoS ONE, 2016
Nontypeable Haemophilus influenzae (NTHi) is an opportunistic pathogen which causes a variety of respiratory infections. The objectives of the study were to determine its antimicrobial susceptibility, to characterize the b-lactam resistance, and to ...
Ardanuy Tisaire, María Carmen   +7 more
core   +3 more sources

The integral membrane FtsW protein and peptidoglycan synthase PBP3 form a subcomplex in Escherichia coli [PDF]

open access: greenMicrobiology, 2010
During the cell cycle of rod-shaped bacteria, two morphogenetic processes can be discriminated: length growth of the cylindrical part of the cell and cell division by formation of two new cell poles. The morphogenetic protein complex responsible for the septation during cell division (the divisome) includes class A and class B penicillin-binding ...
Claudine Fraipont   +6 more
openalex   +6 more sources

Interaction of FtsA and PBP3 proteins in the Escherichia coli septum [PDF]

open access: greenJournal of Bacteriology, 1986
Mutations in the ftsA gene of Escherichia coli conferred a higher resistance to lysis induced by penicillin or by a combination of cefsulodin and furazlocillin. The ftsA2 allele codes for an FtsA protein which is inactive at 42 degrees C but is able to regain its activity once it is transferred back to 30 degrees C; ftsA2 filaments formed at 42 degrees
Antonio Tormo   +4 more
openalex   +4 more sources

Hybrid proteins of the transglycosylase and the transpeptidase domains of PBP1B and PBP3 of Escherichia coli [PDF]

open access: greenJournal of Bacteriology, 1995
The construction of hybrid proteins of PBP1B and PBP3 has been described. One hybrid protein (PBP1B/3) contained the transglycosylase domain of PBP1B and the transpeptidase domain of PBP3. In the other hybrid protein, the putative transglycosylase domain of PBP3 was coupled to the transpeptidase domain of PBP1B (PBP3/1B).
C A Zijderveld   +3 more
openalex   +6 more sources

Structural Characterization of Diazabicyclooctane β-Lactam “Enhancers” in Complex with Penicillin-Binding Proteins PBP2 and PBP3 of Pseudomonas aeruginosa

open access: goldmBio, 2021
Antibiotic resistance is a significant clinical problem. Developing novel antibiotics that overcome known resistance mechanisms is highly desired.
Malligarjunan Rajavel   +12 more
openalex   +4 more sources

Crystal Structure of a Peptidoglycan Synthesis Regulatory Factor (PBP3) from Streptococcus pneumoniae [PDF]

open access: yesJournal of Biological Chemistry, 2005
Penicillin-binding proteins (PBPs) are membrane-associated enzymes which perform critical functions in the bacterial cell division process. The single d-Ala,d-Ala (d,d)-carboxypeptidase in Streptococcus pneumoniae, PBP3, has been shown to play a key role in control of availability of the peptidoglycal substrate during cell growth.
Cecile Morlot   +2 more
exaly   +4 more sources

PBP3 inhibition elicits adaptive responses in Pseudomonas aeruginosa [PDF]

open access: bronzeMolecular Microbiology, 2006
SummaryAdaptive evolution depends on both the genetic variability in a population of organisms and the selection of the better adapted genotypes. However, for the fittest variants to be selected they must survive over a sufficient period under the new conditions.
Jesús Blázquez   +5 more
openalex   +3 more sources

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