Results 41 to 50 of about 384,367 (304)

Penicillin-Binding Proteins and β-Lactam Resistance [PDF]

FEMS Microbiology Reviews, 2008
A number of ways and means have evolved to provide resistance to eubacteria challenged by beta-lactams. This review is focused on pathogens that resist by expressing low-affinity targets for these antibiotics, the penicillin-binding proteins (PBPs). Even within this narrow focus, a great variety of strategies have been uncovered such as the acquisition
Zapun, André, Macheboeuf, Pauline, Vernet, Thierry   +2 more
openaire   +3 more sources

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

Journal 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, Maria Victoria Heggenhougen, Anja Ruud Winther, Johanne Moldstad, Vegard Eldholm, Morten Kjos, Leiv Sigve Håvarstein, Daniel Straume   +7 more
doaj   +1 more source

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, Inna V Krieger, John P Huizar, Daniela Mavrici, Geoffrey S Waldo, Li-Wei Hung, James C Sacchettini, Thomas C Terwilliger, Tom Alber   +8 more
doaj   +1 more source

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
openaire   +2 more sources

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, Andre Dascal, John Hiscott, Sonia Gioseffini, Janet Stevenson, Joseph Portnoy, Jack Mendelson   +6 more
doaj   +1 more source

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

PLoS 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, Abdul Bais, Md Maniruzzaman Manir, Umar Niazi   +3 more
doaj   +1 more source

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

Antibiotics, 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, Laura Alvarez, Silvia Bulgheresi, Felipe Cava, Tanneke den Blaauwen   +4 more
doaj   +1 more source

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, T, Grebe, D, Zähner, J B, Stock   +3 more
openaire   +2 more sources

Multiple ETS family transcription factors bind mutant p53 via distinct interaction regions

FEBS Letters, EarlyView.
Mutant p53 gain‐of‐function is thought to be mediated by interaction with other transcription factors. We identify multiple ETS transcription factors that can bind mutant p53 and found that this interaction can be promoted by a PXXPP motif. ETS proteins that strongly bound mutant p53 were upregulated in ovarian cancer compared to ETS proteins that ...
Stephanie A. Metcalf, Nicholas F. Downing, Kaitlyn M. Mills, Samuel C. Metcalfe, Alexander E. Kritzer, Lindsey D. Mayo, Peter C. Hollenhorst   +6 more
wiley   +1 more source

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

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, Norihito Tarumoto, Shinsuke Tamura, Morichika Osa, Takaaki Hamamoto, Atsushi Yuki, Yuji Kouzaki, Kazuo Imai, Runtuwene Lucky Ronald, Toshiyuki Yamaguchi, Takashi Murakami, Shigefumi Maesaki, Yutaka Suzuki, Akihiko Kawana, Takuya Maeda   +14 more
doaj   +1 more source