Penicillin‐degrading activities of peptides from pneumococcal penicillin‐binding proteins [PDF]
European Journal of Biochemistry, 1988 Trypsin treatment of native penicillin‐binding proteins (PBPs) 1a, 2 b and 3 from Streptococcus pneumoniae resulted in the formation of stable peptides containing the β‐lactam‐binding site with molecular masses ranging from 26 kDa to 36 kDa.Whereas the PBP 1a peptide (Ia) was enzymatically rather unstable, the PBP 2b peptide (IIb) and the PBP 3 peptide
H, Ellerbrok, R, Hakenbeck
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Subfamily-specific adaptations in the structures of two penicillin-binding proteins from Mycobacterium tuberculosis. [PDF]
PLoS 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
Mechanisms of action of hESC-secreted proteins that enhance human and mouse myogenesis. [PDF]
, 2014 Adult stem cells grow poorly in vitro compared to embryonic stem cells, and in vivo stem cell maintenance and proliferation by tissue niches progressively deteriorates with age.
CONBOY, Irina M +6 more
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β‐Lactam resistance in Streptococcus pneumoniae: penicillin‐binding proteins and non‐penicillin‐binding proteins [PDF]
Molecular Microbiology, 1999 The β‐lactams are by far the most widely used and efficacious of all antibiotics. Over the past few decades, however, widespread resistance has evolved among most common pathogens. Streptococcus pneumoniae has become a paradigm for understanding the evolution of resistance mechanisms, the simplest of which, by far, is the production of β‐lactamases. As
R, Hakenbeck +3 more
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The Importance of a Critical Protonation State and the Fate of the Catalytic Steps in Class A β-Lactamases and Penicillin-binding Proteins [PDF]
, 2004 b-Lactamases and penicillin-binding proteins are bacterial enzymes involved in antibiotic resistance to b-lactam antibiotics and biosynthetic assembly of cell wall, respectively.
Bulychev, Alexey +7 more
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Non-Beta-Lactamase-Producing Penicillin-Resistant Enterococcus faecium in a Clinical Setting
Canadian 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
CD4+ Th immunogenicity of the Ascaris spp. secreted products [PDF]
, 2020 Ascaris spp. is a major health problem of humans and animals alike, and understanding the immunogenicity of its antigens is required for developing urgently needed vaccines.
Bertazzon, Miriam +6 more
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Hyperosmotic stress induces PARP1‐mediated HPF1‐dependent mono(ADP‐ribosyl)ation
FEBS 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
BMC 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]
, 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
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