Results 11 to 20 of about 400,542 (252)

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

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

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

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

Penicillin-binding proteins of bdellovibrios [PDF]

open access: yesJournal of Bacteriology, 1988
We examined the predacious gram-negative bacterium Bdellovibrio bacteriovorous 109J and free-living strains 109J-A1 and 109J-KA1 derived therefrom for penicillin-binding proteins (PBPs). We compared their PBPs with those of the host bacterium, Escherichia coli, and with those of a facultatively predacious bdellovibrio, B. stolpii UKi2, grown axenically.
J T, Park, S, Mahadevan
openaire   +2 more sources

Penicillin-binding proteins in bacteria [PDF]

open access: yesAntimicrobial Agents and Chemotherapy, 1980
The penicilllin-binding proteins (PBPs) of several gram-positive and gram-negative bacteria have been examined. The results indicate that: (i) PBPs are membrane proteins with molecular weights ranging from 40,000 to 120,000. When extracted with Triton X-100 from sonicated cells, they appear to fall into two patterns: one found in rods and the other in ...
N H, Georgopapadakou, F Y, Liu
openaire   +2 more sources

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