Results 21 to 30 of about 635,610 (300)

Molecular Characterization of Penicillin-Binding Protein2x, 2b and 1a of Streptococcus pneumoniae Causing Invasive Pneumococcal Diseases in China: A Multicenter Study

open access: yesFrontiers in Microbiology, 2022
Streptococcus pneumoniae is a common human pathogen that can cause severe invasive pneumococcal diseases (IPDs). Penicillin-binding proteins (PBPs) are the targets for β-lactam antibiotics (BLAs), which are the common empirical drugs for treatment of ...
Menglan Zhou   +11 more
doaj   +1 more source

Penicillin-binding proteins in Clostridium perfringens [PDF]

open access: yesAntimicrobial Agents and Chemotherapy, 1981
The penicillin-binding proteins (PBPs) of Clostridium perfringens were studied. Six PBPs ranging in molecular weight from approximately 42,000 to 100,000 were detected in the cytoplasmic membrane. The relative affinities of the PBPs for 16 beta-lactam antibiotics were determined.
T F, Murphy, M, Barza, J T, Park
openaire   +2 more sources

Identification and Crystallization of Penicillin-Binding Protein/β-Lactamase Homolog (Rp46) from Ruegeria Pomeroyi

open access: yesCrystals, 2016
In spite of the enormous biological and clinical significance of penicillin-binding protein (PBP)/β-lactamase (βL), few of their many homologs (PBP)/βLs homologs) have been studied crystallographically, and have known functions.
Bum Han Ryu   +4 more
doaj   +1 more source

On Column Binding a Real-Time Biosensor for β-lactam Antibiotics Quantification

open access: yesMolecules, 2020
This work aimed to develop accurate, quick, and practical tools for the detection of residues of penicillin G antibiotic in biological and non-biological samples.
Shahla M. Abdullah, Shwan Rachid
doaj   +1 more source

Facilitation of penicillin haptenation to serum proteins. [PDF]

open access: yes, 1993
Traditionally, penicillin binding to serum proteins was believed to be a passive chemical process; however, it appears to be facilitated by serum factors.
Adkinson, N. Franklin, Jr.   +2 more
core   +3 more sources

The penicillin binding proteins of the genus Haemophilus [PDF]

open access: yesJournal of Medical Microbiology, 1988
We questioned whether the penicillin binding protein (PBP) profiles of representative strains from the 19 species varied within the genus Haemophilus and whether these profiles would be of taxonomic value. Seventeen of the 19 representative strains studied had distinct PBP profiles; only those of H. avium and H. paragallinarum were identical.
P M, Mendelman, D A, Serfass
openaire   +2 more sources

The penicillin binding protein 1A of Helicobacter pylori, its amoxicillin binding site and access routes

open access: yesGut Pathogens, 2021
Background Amoxicillin-resistant H. pylori strains are increasing worldwide. To explore the potential resistance mechanisms involved, the 3D structure modeling and access tunnel prediction for penicillin-binding proteins (PBP1A) was performed, based on ...
Bahareh Attaran   +7 more
doaj   +1 more source

Penicillin binding proteins as danger signals: meningococcal penicillin binding protein 2 activates dendritic cells through Toll-like receptor 4.

open access: yesPLoS ONE, 2011
Neisseria meningitidis is a human pathogen responsible for life-threatening inflammatory diseases. Meningococcal penicillin-binding proteins (PBPs) and particularly PBP2 are involved in bacterial resistance to β-lactams. Here we describe a novel function
Marcelo Hill   +15 more
doaj   +1 more source

Penicillin-binding proteins in Haemophilus influenzae [PDF]

open access: yesAntimicrobial Agents and Chemotherapy, 1981
The penicillin-binding proteins (PBPs) of Haemophilus influenzae were studied by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and fluorography. Eight major PBPs, ranging in molecular weights from 90,000 to 27,000, were detected. The pattern of molecular weights was different from that determined fro Escherichia coli or Pseudomonas ...
S D, Makover, R, Wright, E, Telep
openaire   +2 more sources

Penicillin-binding Proteins (PBP) and Lmo0441 (a PBP-like protein) play a role in Beta-lactam sensitivity of Listeria monocytogenes

open access: yesGut Pathogens, 2009
While seven penicillin-binding proteins (PBPs) or PBP-like proteins have been identified either by radiolabelled penicillin binding studies or genomic analysis, only PBP3 has been considered of interest for Beta-lactams activity against Listeria ...
Van de Velde Sébastien   +5 more
doaj   +1 more source

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