Ontology highlight
ABSTRACT:
INSTRUMENT(S): LTQ Orbitrap, LTQ Orbitrap Velos
ORGANISM(S): Escherichia Coli
SUBMITTER: Christian Ahrens
LAB HEAD: Prof. John Robinson
PROVIDER: PXD002588 | Pride | 2015-12-07
REPOSITORIES: Pride
Items per page: 5 1 - 5 of 300 |
Urfer Matthias M Bogdanovic Jasmina J Lo Monte Fabio F Moehle Kerstin K Zerbe Katja K Omasits Ulrich U Ahrens Christian H CH Pessi Gabriella G Eberl Leo L Robinson John A JA
The Journal of biological chemistry 20151201 4
Increasing antibacterial resistance presents a major challenge in antibiotic discovery. One attractive target in Gram-negative bacteria is the unique asymmetric outer membrane (OM), which acts as a permeability barrier that protects the cell from external stresses, such as the presence of antibiotics. We describe a novel β-hairpin macrocyclic peptide JB-95 with potent antimicrobial activity against Escherichia coli. This peptide exhibits no cellular lytic activity, but electron microscopy and fl ...[more]