Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Ahmed El Zoeiby"'
Autor:
Adil Adatia, Jean-Nicolas Boursiquot, Dawn Goodyear, Chrystyna Kalicinsky, Amin Kanani, Susan Waserman, Michelle M. L. Nguyen, Abhinav Wadhwa, Jessica Weiss, Ahmed El-Zoeiby, Stephen Betschel
Publikováno v:
Allergy, Asthma & Clinical Immunology, Vol 20, Iss 1, Pp 1-10 (2024)
Abstract Background Hereditary angioedema with normal C1-inhibitor function (HAE nC1-INH) and idiopathic angioedema of unknown etiology (AE-UNK) are rare conditions that cause recurrent subcutaneous and submucosal swelling. The characteristics and cl
Externí odkaz:
https://doaj.org/article/2fb08afda580450ba465e4bced14692b
Autor:
Tania N. Petruzziello, Seyedreza Seyedirashti, Bamini Jayabalasingham, Russell E. Bishop, Wenyi Jia, Ahmed El Zoeiby
Publikováno v:
Journal of Biological Chemistry. 279:44966-44975
The biogenesis of biological membranes hinges on the coordinated trafficking of membrane lipids between distinct cellular compartments. The bacterial outer membrane enzyme PagP confers resistance to host immune defenses by transferring a palmitate ch
Publikováno v:
Journal of Endotoxin Research. 10:107-112
The enzymology of palmitate addition to lipid A can be traced to the early discovery of monosaccharide lipid A precursors, but the functional importance of lipid A palmitoylation in bacterial resistance to the host immune response has emerged only re
Autor:
Mélanie Beaumont, Normand Voyer, Roger C. Levesque, Ahmed El Zoeiby, François Sanschagrin, Eric Dubuc
Publikováno v:
Bioorganic & Medicinal Chemistry. 11:1583-1592
We have developed a screening assay by thin-layer chromatography (TLC) to identify inhibitors for the bacterial essential enzymes MurA, -B, and -C. Libraries of compounds were synthesized using the mix-and-split combinatorial chemistry approach. Scre
Autor:
Roger C. Levesque, François Sanschagrin, Pierre Claver Havugimana, Alain Garnier, Ahmed El Zoeiby
Publikováno v:
FEMS Microbiology Letters. 201:229-235
Bacterial peptidoglycan is the cell wall component responsible for maintaining cell integrity against osmotic pressure. Biosynthesis of the cytoplasmic precursor UDP-N-acetylmuramyl pentapeptide is catalyzed by the Mur enzymes. Genomic analysis of th
Autor:
Christopher G. Dowson, Alexander Tomasz, Roger C. Levesque, Gianfranco De Pascale, David I. Roper, Anita C. Catherwood, Timothy D. H. Bugg, Ahmed El Zoeiby, Andrea M. Gilbey, Adrian J. Lloyd, Anne M. Blewett
Publikováno v:
The Journal of biological chemistry. 283(10)
MurM is an aminoacyl ligase that adds l-serine or l-alanine as the first amino acid of a dipeptide branch to the stem peptide lysine of the pneumococcal peptidoglycan. MurM activity is essential for clinical pneumococcal penicillin resistance. Analys
Publikováno v:
Journal of endotoxin research. 11(3)
The presence of palmitate in a minor fraction of lipid A has been known since the chemical structure of lipid A was first elucidated, but the functional importance in bacterial pathogenesis of regulated lipid A palmitoylation has become clear only re
Objectives The machinery of peptidoglycan biosynthesis is an ideal site at which to look for novel antimicrobial targets. Phage display was used to develop novel peptide inhibitors for MurC, an essential enzyme involved in the early steps of biosynth
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::219eb2c83a230e9feb57a496ea2410e8
https://nrc-publications.canada.ca/eng/view/object/?id=f49c999a-9989-4401-817c-4e8423ce9097
https://nrc-publications.canada.ca/eng/view/object/?id=f49c999a-9989-4401-817c-4e8423ce9097
Publikováno v:
Molecular microbiology. 47(1)
One of the biggest challenges for recent medical research is the continuous development of new antibiotics interacting with bacterial essential mechanisms. The machinery for peptidoglycan biosynthesis is a rich source of crucial targets for antibacte
Publikováno v:
FEMS microbiology letters. 183(2)
We cloned and sequenced the murC gene from Pseudomonas aeruginosa encoding a protein of 53 kDa. Multiple alignments with 20 MurC peptide sequences from different bacteria confirmed the presence of highly conserved regions having sequence identities r