ORCID Profile
0000-0001-8920-3522
Current Organisation
The University of Edinburgh
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Publisher: American Chemical Society (ACS)
Date: 11-07-2023
Publisher: Cold Spring Harbor Laboratory
Date: 04-12-2022
DOI: 10.1101/2022.12.04.519019
Abstract: Antimicrobial resistance has emerged as an urgent global public health threat, and development of novel therapeutics for treating infections caused by multi-drug resistant bacteria is urgent. Staphylococcus aureus is a major human and animal pathogen, responsible for high levels of morbidity and mortality worldwide. The intracellular survival of S. aureus in macrophages contributes to immune evasion, dissemination, and resilience to antibiotic treatment. Here, we present a confocal fluorescence imaging assay for monitoring macrophage infection by GFP-tagged Staphylococcus aureus as a front-line tool to identify antibiotic leads. The assay was employed in combination with nanoscaled chemical analyses to facilitate the discovery of a novel, active rifamycin analogue. Our findings indicate a promising new approach to the identification of anti-microbial compounds with macrophage intracellular activity. The novel antibiotic identified here may represent a useful addition to our armoury in tackling the silent pandemic of antimicrobial resistance.
Publisher: Public Library of Science (PLoS)
Date: 13-06-2017
Publisher: Elsevier BV
Date: 10-1998
Abstract: We have developed a baculovirus expression system for the rapid and efficient production of large quantities (>10 mg/l) of VP16. The recombinant VP16 binds to a complex of host cell transcription factors and TAATGARAT motif. Secondary structure calculations from circular dichroism measurements indicate a content of 32.0 % alpha-helix and 17.5 % beta-sheet. This is the first structural CD analysis of VP16 which will be very useful for high-throughput assay development and mechanistic studies.
Publisher: Elsevier BV
Date: 06-1999
Abstract: We have developed a baculovirus expression system for the rapid and efficient production of large quantities (>5 mg/10(8) cells) of ICP8. The recombinant ICP8 is fully functional and binds to single-stranded DNA. Secondary structure calculations from circular dichroism measurements indicate a content of 34.5% alpha-helix and 15.4% beta-sheet. This is the first structural report for ICP8 using CD analysis, which will be very useful for high-throughput assay development and mechanistic studies.
Publisher: Springer Science and Business Media LLC
Date: 24-01-2020
DOI: 10.1038/S41467-019-14224-9
Abstract: Protein-protein-interaction networks (PPINs) organize fundamental biological processes, but how oncogenic mutations impact these interactions and their functions at a network-level scale is poorly understood. Here, we analyze how a common oncogenic KRAS mutation (KRAS G13D ) affects PPIN structure and function of the Epidermal Growth Factor Receptor (EGFR) network in colorectal cancer (CRC) cells. Mapping PPIs shows that this network is extensively rewired in cells expressing transforming levels of KRAS G13D (mtKRAS). The factors driving PPIN rewiring are multifactorial including changes in protein expression and phosphorylation. Mathematical modelling also suggests that the binding dynamics of low and high affinity KRAS interactors contribute to rewiring. PPIN rewiring substantially alters the composition of protein complexes, signal flow, transcriptional regulation, and cellular phenotype. These changes are validated by targeted and global experimental analysis. Importantly, genetic alterations in the most extensively rewired PPIN nodes occur frequently in CRC and are prognostic of poor patient outcomes.
Location: United Kingdom of Great Britain and Northern Ireland
Location: United Kingdom of Great Britain and Northern Ireland
No related grants have been discovered for Manfred Auer.