Results 11 to 20 of about 564,515 (340)

Penicillin-binding proteins exhibit functional redundancy during asymmetric cell division in Clostridioides difficile [PDF]

open access: yesJournal of Bacteriology
Peptidoglycan synthesis is an essential driver of bacterial growth and division. The final steps of this crucial process involve the polymerization of glycan strands by shape, elongation, division, and sporulation (SEDS) family glycosyltransferases and ...
Shailab Shrestha   +4 more
doaj   +2 more sources

Morphogenetic penicillin-binding proteins control virulence-associated type III secretion systems in Salmonella [PDF]

open access: yesInfection and Immunity
Type III protein secretion systems (T3SSs) function as multiprotein devices that span the envelope of Gram-negative bacteria using the peptidoglycan (PG) layer as scaffold.
Sónia Castanheira   +3 more
doaj   +2 more sources

Dynamical Behavior of β-Lactamases and Penicillin- Binding Proteins in Different Functional States and Its Potential Role in Evolution [PDF]

open access: yesEntropy, 2019
β-Lactamases are enzymes produced by bacteria to hydrolyze β-lactam-based antibiotics, and pose serious threat to public health through related antibiotic resistance.
Feng Wang   +3 more
doaj   +2 more sources

Penicillin-binding proteins and β-lactam resistance [PDF]

open access: bronzeFEMS Microbiology Reviews, 2008
A number of ways and means have evolved to provide resistance to eubacteria challenged by beta-lactams. This review is focused on pathogens that resist by expressing low-affinity targets for these antibiotics, the penicillin-binding proteins (PBPs). Even within this narrow focus, a great variety of strategies have been uncovered such as the acquisition
André Zapun   +2 more
openalex   +4 more sources

Predicting β-lactam susceptibility from the genome of Streptococcus pneumoniae and other mitis group streptococci

open access: yesFrontiers in Microbiology, 2023
IntroductionFor Streptococcus pneumoniae, β-lactam susceptibility can be predicted from the amino acid sequence of the penicillin-binding proteins PBP1a, PBP2b, and PBP2x.
Helle Brander Eriksen   +13 more
doaj   +1 more source

New noncovalent inhibitors of penicillin-binding proteins from penicillin-resistant bacteria. [PDF]

open access: yesPLoS ONE, 2011
BACKGROUND: Penicillin-binding proteins (PBPs) are well known and validated targets for antibacterial therapy. The most important clinically used inhibitors of PBPs β-lactams inhibit transpeptidase activity of PBPs by forming a covalent penicilloyl ...
Samo Turk   +10 more
doaj   +1 more source

Genetic characterization of penicillin-binding proteins of nonencapsulated Streptococcus pneumoniae in the postpneumococcal conjugate vaccine era in Japan

open access: yesInternational Journal of Infectious Diseases, 2022
Objectives: Nonencapsulated Streptococcus pneumoniae (NESp) is emerging after the introduction of pneumococcal conjugate vaccines (PCVs). This study aimed to elucidate the genetic characteristics of penicillin-binding proteins (PBPs; PBP1a, 2b, and 2x ...
Mitsuyo Kawaguchiya   +6 more
doaj   +1 more source

Kinetics of penicillin binding to penicillin-binding proteins of Staphylococcus aureus [PDF]

open access: yesBiochemical Journal, 1994
Reduced affinity of penicillin-binding proteins (PBPs) for binding penicillin has been proposed as a mechanism of beta-lactam antibiotic resistance in staphylococci. Penicillin binding by PBPs of three penicillin-susceptible and two penicillin-resistant strains of Staphylococcus aureus was studied in kinetic assays to determine rate constants, drug ...
H F, Chambers   +2 more
openaire   +2 more sources

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