Results 31 to 40 of about 399,815 (205)

Resistance to β-lactam antibiotics conferred by point mutations in penicillin-binding proteins PBP3, PBP4 and PBP6 in Salmonella enterica. [PDF]

open access: yesPLoS ONE, 2014
Penicillin-binding proteins (PBPs) are enzymes responsible for the polymerization of the glycan strand and the cross-linking between glycan chains as well as the target proteins for β-lactam antibiotics.
Song Sun, Maria Selmer, Dan I Andersson
doaj   +1 more source

PBP4 Is Likely Involved in Cell Division of the Longitudinally Dividing Bacterium Candidatus Thiosymbion Oneisti

open access: yesAntibiotics, 2021
Peptidoglycan (PG) is essential for bacterial survival and maintaining cell shape. The rod-shaped model bacterium Escherichia coli has a set of seven endopeptidases that remodel the PG during cell growth.
Jinglan Wang   +4 more
doaj   +1 more source

The effect of MurM and a branched cell wall structure on penicillin resistance in Streptococcus pneumoniae

open access: yesJournal of Bacteriology
The aminoacyltransferase MurM is an important penicillin resistance determinant in Streptococcus pneumoniae. This enzyme attaches a serine or alanine to the side chain of lysine, the third residue of the pentapeptide of lipid II, resulting in branched ...
Ragnhild Sødal Gjennestad   +7 more
doaj   +1 more source

Novel Penicillin Analogues as Potential Antimicrobial Agents; Design, Synthesis and Docking Studies. [PDF]

open access: yesPLoS ONE, 2015
A number of penicillin derivatives (4a-h) were synthesized by the condensation of 6-amino penicillinic acid (6-APA) with non-steroidal anti-inflammatory drugs as antimicrobial agents.
Zaman Ashraf   +3 more
doaj   +1 more source

Subfamily-specific adaptations in the structures of two penicillin-binding proteins from Mycobacterium tuberculosis. [PDF]

open access: yesPLoS ONE, 2014
Beta-lactam antibiotics target penicillin-binding proteins including several enzyme classes essential for bacterial cell-wall homeostasis. To better understand the functional and inhibitor-binding specificities of penicillin-binding proteins from the ...
Daniil M Prigozhin   +8 more
doaj   +1 more source

Non-Beta-Lactamase-Producing Penicillin-Resistant Enterococcus faecium in a Clinical Setting

open access: yesCanadian Journal of Infectious Diseases, 1990
Six clinical isolates of Enterococcus faecium highly resistant to penicillin are reported. These strains did not produce beta-lactamase and no plasmid DNA could be detected.
Daniel Eymard   +6 more
doaj   +1 more source

Hyperosmotic stress induces PARP1‐mediated HPF1‐dependent mono(ADP‐ribosyl)ation

open access: yesFEBS Letters, EarlyView.
Sorbitol‐induced hyperosmotic stress rapidly induces reversible mono(ADP‐ribosyl)ation (MARylation) on PARP1 without the signs of genotoxic signaling. We show that PARP1 autoMARylation is HPF1 dependent and forms hydroxylamine‐resistant O‐glycosidic linkages.
Anna Georgina Kopasz   +11 more
wiley   +1 more source

Single nucleotide polymorphisms in genes encoding penicillin-binding proteins in β-lactamase-negative ampicillin-resistant Haemophilus influenzae in Japan

open access: yesBMC Research Notes, 2018
Objective β-Lactamase-negative ampicillin-resistant Haemophilus influenzae is a common opportunistic pathogen of hospital- and community-acquired infections, harboring multiple single nucleotide polymorphisms in the ftsI gene, which codes for penicillin ...
Kazuhisa Misawa   +14 more
doaj   +1 more source

An isoform of 14‐3‐3 protein regulates transbilayer lipid movement at the plasma membrane

open access: yesFEBS Letters, EarlyView.
Loss of 14‐3‐3ζ in CHO cells confers resistance to exogenous phosphatidylserine (PS) and impairs endocytosis‐independent inward flip‐flop of fluorescent PS at the plasma membrane. RNAi‐mediated knockdown reproduces this defect, while no additive effect is seen in ATP11C‐deficient cells.
Akiko Yamaji‐Hasegawa   +3 more
wiley   +1 more source

Septin 9 PB domains coordinate centrosome positioning and microtubule acetylation to control epithelial polarity

open access: yesFEBS Letters, EarlyView.
Septin 9 polybasic domains couple phosphoinositide‐rich membrane binding to centrosome positioning, Golgi organization, and microtubule acetylation to control epithelial polarity. Their loss disrupts this axis, causing centrosome mispositioning, Golgi fragmentation, reduced microtubule acetylation, and polarity inversion via upregulation of the ...
Ting ting Cai   +4 more
wiley   +1 more source

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