Results 41 to 50 of about 561,009 (296)

Penicillin-binding proteins in Clostridium perfringens [PDF]

Antimicrobial 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

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

PLoS 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, Ala-Eddine Deghmane, Mercedes Segovia, Maria Leticia Zarantonelli, Gaëlle Tilly, Philippe Blancou, Gaëlle Bériou, Régis Josien, Ignacio Anegon, Eva Hong, Corinne Ruckly, Aude Antignac, Meriem El Ghachi, Ivo Gomperts Boneca, Muhamed-Kheir Taha, Maria Cristina Cuturi   +15 more
doaj   +1 more source

In Silico Design and Molecular Docking Studies of Carbapenem Analogues Targeting Acinetobacter baumannii PBP1A Receptor

Al-Mustansiriyah Journal of Pharmaceutical Sciences, 2020
Carbapenems are considered as the most effective antibiotic against Acinetobacter baumannii infections, as the pathogen has a resistance to the most of the other beta-lactam antibiotics; however, recent studies proved that this pathogen has developed
Twana Salih, Hawzhin A. Salih
doaj   +1 more source

Surfactant-free purification of membrane protein complexes from bacteria: application to the staphylococcal penicillin-binding protein complex PBP2/PBP2a [PDF]

, 2014
Surfactant-mediated removal of proteins from biomembranes invariably results in partial or complete loss of function and disassembly of multi-protein complexes. We determined the capacity of styrene-co-maleic acid (SMA) co-polymer to remove components of
Dafforn, Timothy R, Foster, Simon J, Galley, Nicola F, Garcia-Lara, Jorge, Jamshad, Mohammed, Paulin, Sarah, Roper, David I, Rosado, Helena, Taylor, Peter W   +8 more
core   +3 more sources

Hfq mutation confers increased cephalosporin resistance in Klebsiella pneumoniae [PDF]

Archives of Biological Sciences, 2017
Klebsiella pneumoniae (K. pneumoniae), is an opportunistic pathogen raising significant public health concerns owing to its multi-drug resistance. Hfq, one of the main RNA-binding proteins, is a key post-transcriptional regulator.
Li Xinran, Yang Mingjuan, Ke Yuehua, Liu Mingyuan, Wang Yufei, Liu Shiwei, Bo Liu, Chen Zeliang   +7 more
doaj   +1 more source

Escherichia coli EHEC Germany outbreak preliminary functional annotation using BG7 system [PDF]

, 2011
We have annotated the European outbreak E. coli EHEC genome sequenced by BGI (6-2-2011) and assembled with MIRA by Nick Loman (6-2-2011 ). Our system BG7, Bacterial Genome annotation of Era7 Bioinformatics, predicts ORFs and annotates them based on ...
Eduardo Pareja, Eduardo Pareja-Tobes, Marina Manrique, Pablo Pareja-Tobes, Raquel Tobes   +4 more
core   +2 more sources

Penicillin-binding proteins in Proteus species [PDF]

Journal of Bacteriology, 1979
Penicillin-binding proteins in three species of Proteus, Proteus mirabilis, P. morganii, and P. rettgeri, were investigated by sodium dodecyl sulfate-polyacrylamide slab gel electrophoresis. Penicillin-binding proteins in these Proteus species were compared with those in Escherichia coli K-12.
S, Ohya, M, Yamazaki, S, Sugawara, M, Matsuhashi   +3 more
openaire   +2 more sources

Penicillin-binding proteins of Haemophilus ducreyi [PDF]

Antimicrobial Agents and Chemotherapy, 1989
The penicillin-binding protein (PBP) profile of Haemophilus ducreyi was determined by a whole-cell-labeling assay. Only two major PBPs, of molecular weights 90,000 (PBP 1) and 38,500 (PBP 2), were detected in six of eight strains studied. Competition binding experiments and the attendant morphological effects suggested that PBP 1 was either a ...
B C, Lee, L E, Bryan
openaire   +2 more sources

Identification of Mutations in the mrdA Gene Encoding PBP2 That Reduce Carbapenem and Diazabicyclooctane Susceptibility of Escherichia coli Clinical Isolates with Mutations in ftsI (PBP3) and Which Carry bla_NDM-1

mSphere, 2019
Penicillin-binding proteins (PBPs) are essential for bacterial cell wall biosynthesis, and several are clinically validated antibacterial targets of β-lactam antibiotics.
Srijan Ranjitkar, Folkert Reck, Xiaobo Ke, Qingming Zhu, Glenn McEnroe, Sara L. Lopez, Charles R. Dean   +6 more
doaj   +1 more source

Specificity determinants for lysine incorporation in staphylococcus aureus peptidoglycan as revealed by the structure of a MurE enzyme ternary complex [PDF]

, 2013
Background: MurE controls stereo chemical incorporation of Lysine or diaminopimelate into peptidoglycan stem peptides Results: The structure of S.aureus MurE reveals an unexpected lack of specificity for Lysine within the active site.
Barreteau, Basavannacharya, Basavannacharya, Battye, Bertrand, Bertrand, Boniface, Boniface, Bouhss, Brünger, Bugg, Bugg, Chen, Clancy, Clarke, Clarke, Collaborative Computational Project, Number 4, Cox, Cressina, Crouvoisier, Cruickshank, De Lencastre, DeLano, Emsley, Ernst, Ernst, Favini-Stabile, Figueiredo, Gardete, Girardin, Gordon, Gorrec, Huber, Hutton, Jones, Kabsch, Lee, Liebeke, Lloyd, Lloyd, Lundqvist, Lysenko, Matteï, McCoy, Mei, Mengin-Lecreulx, Mengin-Lecreulx, Mohammadi, Murshudov, Münch, Ornelas-Soares, Painter, Paradis-Bleau, Paradis-Bleau, Patin, Perdih, Ray, Read, Royet, Sauvage, Scheffers, Schneider, Schouten, Smith, Sosič, Sova, Thedieck, Vagin, Vollmer, Vollmer, Walker, Young, Zawadzke   +72 more
core   +2 more sources