https://ogma.newcastle.edu.au/vital/access/ /manager/Index en-au 5 https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:45054 Escherichia coli and Pseudomonas aeruginosa, with a clear delineation of the outer and inner membrane as well as the peptidoglycan layer. We suggest that the use of ultrathin cryo-sectioning can be used to better visualize and understand drug interaction mechanisms on the bacterial cell membrane.]]> Wed 26 Oct 2022 11:36:12 AEDT ]]> https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:42541 Wed 24 Aug 2022 16:53:29 AEST ]]> https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:17083 a, R_d and R_e rough LPS mutants. The SAR analysis enabled by the binding data suggested that, in addition to the important role played by the lipid A and core components of LPS, it is predominately the unique species- and strain-specific carbohydrate structure of the O-antigen polysaccharide that largely determines the binding affinity for AGP. Together, these data are consistent with the role of AGP in the binding and transport of LPS in plasma during acute-phase inflammatory responses to invading Gram-negative bacteria.]]> Wed 11 Apr 2018 11:39:50 AEST ]]> https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:53705 Wed 10 Jan 2024 11:03:27 AEDT ]]> https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:54519 Tue 27 Feb 2024 15:46:23 AEDT ]]>