Results 41 to 50 of about 558,213 (199)

Staphylococcus aureus DivIB is a peptidoglycan-binding protein that is required for a morphological checkpoint in cell division [PDF]

, 2014
Bacterial cell division is a fundamental process that requires the coordinated actions of a number of proteins which form a complex macromolecular machine known as the divisome.
Bottomley, Amy L., Foster, Simon J., Garcia-Lara, Jorge, Hurd, Alexander F., Kabli, Azhar F., Turner, Robert D.   +5 more
core   +1 more source

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 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

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

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

X-ray studies of enzymes that interact with penicillins. [PDF]

, 1998
The technique of X-ray diffraction has been successfully applied to enzymes associated with peptidoglycan biosynthesis. The technique has taught us a great deal about the structures and catalytic mechanisms of penicillin-binding proteins and beta ...
Charlier, Paulette, Fonze, E., Kelly, J. A., Kuzin, A. P.   +3 more
core   +1 more source

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, Golemi-Kotra, Dasantila, Kim, Choonkeun, Meroueh, Samy O., Mobashery, Shahriar, Stemmler, Ann J., Stemmler, Timothy L., Vakulenko, Sergei B.   +7 more
core   +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

Penicillin-binding proteins in Actinobacteria [PDF]

The Journal of Antibiotics, 2014
Because some Actinobacteria, especially Streptomyces species, are β-lactam-producing bacteria, they have to have some self-resistant mechanism. The β-lactam biosynthetic gene clusters include genes for β-lactamases and penicillin-binding proteins (PBPs), suggesting that these are involved in self-resistance. However, direct evidence for the involvement
openaire   +2 more sources