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Biochimica Et Biophysica Acta|February 4, 2014
Four structural subclasses of the antivirulence drug target disulfide oxidoreductase DsbA provide a platform for design of subclass-specific inhibitorsRóisín M McMahon, Lakshmanane Premkumar, Jennifer L MartinJournal of Autoimmunity|June 3, 2008
Dissection of the multiple sclerosis associated DR2 haplotypeRuth Etzensperger, Róisín M McMahon, E Yvonne Jones, et al.Critical Reviews in Microbiology|January 22, 2019
Life inside and out: making and breaking protein disulfide bonds in ChlamydiaSigne Christensen, Róisín M McMahon, Jennifer L Martin, et al.Acta Crystallographica. Section D, Biological Crystallography|May 6, 2011
Structure of HLA-A*0301 in complex with a peptide of proteolipid protein: insights into the role of HLA-A alleles in susceptibility to multiple sclerosisRóisín M McMahon, Lone Friis, Christian Siebold, et al.Plos One|July 31, 2015
Virtual Screening of Peptide and Peptidomimetic Fragments Targeted to Inhibit Bacterial Dithiol Oxidase DsbAWilko Duprez, Prabhakar Bachu, Martin J Stoermer, et al.Plos One|September 20, 2019
Oxidoreductase disulfide bond proteins DsbA and DsbB form an active redox pair in Chlamydia trachomatis, a bacterium with disulfide dependent infection and developmentSigne Christensen, Maria A Halili, Natalie Strange, et al.Plos One|December 29, 2016
Structural and Biochemical Characterization of Chlamydia trachomatis DsbA Reveals a Cysteine-Rich and Weakly Oxidising OxidoreductaseSigne Christensen, Morten K Grøftehauge, Karl Byriel, et al.Antioxidants & Redox Signaling|August 2, 2013
Disarming Burkholderia pseudomallei: structural and functional characterization of a disulfide oxidoreductase (DsbA) required for virulence in vivoPhilip M Ireland, Róisín M McMahon, Laura E Marshall, et al.Infection and Immunity|February 15, 2018
Virulence of the Melioidosis Pathogen Burkholderia pseudomallei Requires the Oxidoreductase Membrane Protein DsbBRóisín M McMahon, Philip M Ireland, Derek S Sarovich, et al.Scientific Reports|October 16, 2020
Crystal structure and site-directed mutagenesis of circular bacteriocin plantacyclin B21AG reveals cationic and aromatic residues important for antimicrobial activityMian-Chee Gor, Ben Vezina, Róisín M McMahon, et al.Pageof 2