Zobrazeno 1 - 10
of 47
pro vyhledávání: '"Adriana I. Vasil"'
Publikováno v:
Pharmaceuticals, Vol 7, Iss 4, Pp 366-391 (2014)
A new class of antimicrobial agents with lower rates of resistance and different targets is urgently needed because of the rapidly increasing resistance to classical antibiotics. Amphipathic cationic α-helical antimicrobial peptides (AMPs) represent
Externí odkaz:
https://doaj.org/article/0ff4551a9d1f4fe09e04380e83a8004f
Autor:
Maitane Ibarguren, David J. López, L.-Ruth Montes, Jesús Sot, Adriana I. Vasil, Michael L. Vasil, Félix M. Goñi, Alicia Alonso
Publikováno v:
Journal of Lipid Research, Vol 52, Iss 4, Pp 635-645 (2011)
The binding and early stages of activity of a phospholipase C/sphingomyelinase from Pseudomonas aeruginosa on giant unilamellar vesicles (GUV) have been monitored using fluorescence confocal microscopy. Both the lipids and the enzyme were labeled wit
Externí odkaz:
https://doaj.org/article/b3b35bdeb32e46f59e1d85086373c6ed
Publikováno v:
mBio, Vol 5, Iss 1 (2014)
ABSTRACT Pseudomonas aeruginosa strains of non-cystic fibrosis (non-CF) origin do not produce significant amounts of extracellular alginate and are nonmucoid. In CF, such isolates can become mucoid through mutation of one of the genes (mucA, mucB, mu
Externí odkaz:
https://doaj.org/article/a72b6c2cdbef42c894cd0e44bc67f8a2
Autor:
Michael L. Vasil, Daphné Truan, Morten K. Grøftehauge, Adriana I. Vasil, Paul W. Denny, Ehmke Pohl
Publikováno v:
International Journal of Molecular Sciences
International journal of molecular sciences, 2015, Vol.16(7), pp.15971-15984 [Peer Reviewed Journal]
International Journal of Molecular Sciences, Vol 16, Iss 7, Pp 15971-15984 (2015)
Volume 16
Issue 7
Pages 15971-15984
International journal of molecular sciences, 2015, Vol.16(7), pp.15971-15984 [Peer Reviewed Journal]
International Journal of Molecular Sciences, Vol 16, Iss 7, Pp 15971-15984 (2015)
Volume 16
Issue 7
Pages 15971-15984
As part of the ongoing effort to functionally and structurally characterize virulence factors in the opportunistic pathogen Pseudomonas aeruginosa, we determined the crystal structure of YcaC co-purified with the target protein at resolutions of 2.34
Publikováno v:
Pharmaceuticals, Vol 7, Iss 4, Pp 366-391 (2014)
Pharmaceuticals; Volume 7; Issue 4; Pages: 366-391
Pharmaceuticals
Pharmaceuticals; Volume 7; Issue 4; Pages: 366-391
Pharmaceuticals
A new class of antimicrobial agents with lower rates of resistance and different targets is urgently needed because of the rapidly increasing resistance to classical antibiotics. Amphipathic cationic α-helical antimicrobial peptides (AMPs) represent
Autor:
Adriana I. Vasil, Jesús Sot, Maitane Ibarguren, L.-Ruth Montes, Michael L. Vasil, Alicia Alonso, Félix M. Goñi
Publikováno v:
Chemistry and Physics of Lipids. 166:12-17
When giant unilamellar vesicles (GUVs) composed of sphingomyelin, phosphatidylcholine, phosphatidylethanolamine, and cholesterol are treated with PlcHR(2), a phospholipase C/sphingomyelinase from Pseudomonas aeruginosa, the initial stages of lipid hy
Autor:
Yuxin Chen, Michael T. Guarnieri, Colin T. Mant, Adriana I. Vasil, Robert S. Hodges, Michael L. Vasil
Publikováno v:
Antimicrobial Agents and Chemotherapy. 51:1398-1406
In the present study, the 26-residue amphipathic α-helical antimicrobial peptide V13KL(Y. Chen et al., J. Biol. Chem. 2005, 280:12316-12329, 2005) was used as the framework to study the effects of peptide hydrophobicity on the mechanism of action of
Autor:
Paula J. Wilderman, Adriana I. Vasil, Alain Filloux, Geneviève Ball, Michael L. Vasil, Adam P. Barker
Publikováno v:
Molecular Microbiology. 53:1089-1098
Pseudomonas aeruginosa and other bacterial pathogens express one or more homologous extracellular phospholipases C (PLC) that are secreted through the inner membrane via the twin arginine translocase (TAT) pathway. Analysis of TAT mutants of P. aerug
Autor:
Norma Marchesini, Adriana I. Vasil, Martin J. Stonehouse, Yusuf A. Hannun, Elizabeth A. Collins, Samer El-Bawab, Chiara Luberto, Michael L. Vasil
Publikováno v:
Journal of Biological Chemistry. 278:32733-32743
Sphingomyelin synthase is the enzyme that synthesizes sphingomyelin (SM) in mammalian cells by transferring a phosphorylcholine moiety from phosphatidylcholine to ceramide. Despite its importance, the gene and/or the protein responsible for this acti