Results 51 to 60 of about 561,009 (296)
Emerging Infectious Diseases, 2003 Streptococcus pneumoniae and Neisseria meningitidis have very similar mechanisms of resistance to penicillin G. Although penicillin resistance is now common in S. pneumoniae, it is still rare in N. meningitidis.
L. Temime +3 more
doaj +1 more source
Resistance to β-lactam antibiotics conferred by point mutations in penicillin-binding proteins PBP3, PBP4 and PBP6 in Salmonella enterica. [PDF]
PLoS ONE, 2014 Penicillin-binding proteins (PBPs) are enzymes responsible for the polymerization of the glycan strand and the cross-linking between glycan chains as well as the target proteins for β-lactam antibiotics.
Song Sun, Maria Selmer, Dan I Andersson
doaj +1 more source
Rampant exchange of the structure and function of extramembrane domains between membrane and water soluble proteins. [PDF]
, 2013 Of the membrane proteins of known structure, we found that a remarkable 67% of the water soluble domains are structurally similar to water soluble proteins of known structure. Moreover, 41% of known water soluble protein structures share a domain with an
Bowie, James U +3 more
core +3 more sources
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
Thrombospondin-3 augments injury-induced cardiomyopathy by intracellular integrin inhibition and sarcolemmal instability. [PDF]
, 2019 Thrombospondins (Thbs) are a family of five secreted matricellular glycoproteins in vertebrates that broadly affect cell-matrix interaction. While Thbs4 is known to protect striated muscle from disease by enhancing sarcolemmal stability through increased
Brody, Matthew J +11 more
core +6 more sources
Hanks-Type Serine/Threonine Protein Kinases and Phosphatases in Bacteria: Roles in Signaling and Adaptation to Various Environments [PDF]
, 2018 Reversible phosphorylation is a key mechanism that regulates many cellular processes in prokaryotes and eukaryotes. In prokaryotes, signal transduction includes two-component signaling systems, which involve a membrane sensor histidine kinase and a ...
Janczarek, Monika +3 more
core +1 more source
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 +2 more
openaire +3 more sources
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 +4 more
doaj +1 more source
Journal of BacteriologyThe 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 +7 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 +3 more
doaj +1 more source