Results 51 to 60 of about 635,610 (300)

Designing a novel multi-epitope vaccine to evoke a robust immune response against pathogenic multidrug-resistant Enterococcus faecium bacterium

open access: yesGut Pathogens, 2022
Enterococcus faecium is an emerging ESKAPE bacterium that is capable of causing severe public health complications in humans. There are currently no licensed treatments or vaccinations to combat the deadly pathogen.
Jyotirmayee Dey   +8 more
doaj   +1 more source

Penicillin-binding proteins in Proteus species [PDF]

open access: yesJournal 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   +3 more
openaire   +2 more sources

Clinical characteristics, specific resistance patterns, and molecular mechanisms of carbapenem-resistant Morganella morganii isolates

open access: yesFrontiers in Cellular and Infection Microbiology
ObjectivesThe emergence and spread of carbapenem-resistant Morganella morganii (M. morganii) pose a serious global challenge. This study aimed to investigate the clinical characteristics, resistance patterns, and molecular mechanisms of carbapenem ...
Xiangkuo Zheng   +8 more
doaj   +1 more source

Studies on Resistance to Vegetative (Vip3A) and Crystal (Cry1A) Insecticidal Toxins of Bacillus thuringiensis in Heliothis virescens (Fabricius) [PDF]

open access: yes, 2009
Bacillus thuringiensis (Bt) toxins expressed in commercial transgenic crop varieties are all δ-endotoxins (Cry toxins) but the identification of novel vegetative insecticidal proteins (Vip toxins) has extended the range of insecticidal proteins derived
Pickett, Brian R, Pickett, Brian R
core   +1 more source

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

open access: yesFEMS 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   +2 more
openaire   +3 more sources

Integrative structural biology of the penicillin-binding protein-1 from Staphylococcus aureus, an essential component of the divisome machinery

open access: yesComputational and Structural Biotechnology Journal, 2021
The penicillin-binding proteins are the enzyme catalysts of the critical transpeptidation crosslinking polymerization reaction of bacterial peptidoglycan synthesis and the molecular targets of the penicillin antibiotics.
Siseth Martínez-Caballero   +12 more
doaj   +1 more source

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

open access: yes, 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   +4 more
core   +2 more sources

Modulation of MRSA virulence gene expression by the wall teichoic acid enzyme TarO

open access: yesNature Communications, 2023
The two-component regulatory system VraRS regulates transcription of penicillin-binding protein 2 in response to cell wall antimicrobials. Here, Lu et al.
Yunfu Lu   +13 more
doaj   +1 more source

Perturbed cholesterol and vesicular trafficking associated with dengue blocking in Wolbachia-infected Aedes aegypti cells [PDF]

open access: yes, 2017
Wolbachia are intracellular maternally inherited bacteria that can spread through insect populations and block virus transmission by mosquitoes, providing an important approach to dengue control.
Ant, Thomas H.   +9 more
core   +7 more sources

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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