Results 61 to 70 of about 564,515 (340)

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

The porin and the permeating antibiotic: A selective diffusion barrier in gram-negative bacteria [PDF]

open access: yes, 2008
Gram-negative bacteria are responsible for a large proportion of antibiotic resistant bacterial diseases. These bacteria have a complex cell envelope that comprises an outer membrane and an inner membrane that delimit the periplasm.
A Baslé   +95 more
core   +1 more source

Rampant exchange of the structure and function of extramembrane domains between membrane and water soluble proteins. [PDF]

open access: yes, 2013
Of the membrane proteins of known structure, we found that a remarkable 67% of the water soluble domains are structurally similar to water soluble proteins of known structure. Moreover, 41% of known water soluble protein structures share a domain with an
Bowie, James U   +3 more
core   +3 more sources

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

Hanks-Type Serine/Threonine Protein Kinases and Phosphatases in Bacteria: Roles in Signaling and Adaptation to Various Environments [PDF]

open access: yes, 2018
Reversible phosphorylation is a key mechanism that regulates many cellular processes in prokaryotes and eukaryotes. In prokaryotes, signal transduction includes two-component signaling systems, which involve a membrane sensor histidine kinase and a ...
Janczarek, Monika   +3 more
core   +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

Increased bile resistance in Salmonella enterica mutants lacking Prc periplasmic protease [PDF]

open access: yes, 2013
Prc is a periplasmic protease involved in processing of penicillin-binding protein 3 (PBP3). Lack of Prc suppressesbile sensitivity in Dam-, Wec-, PhoP-, DamX-, and SeqA- mutants of Salmonella enterica, and increases bile resistance in thewild type ...
Francisco García-del Portillo   +4 more
core   +1 more source

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