M
Makrina Totsika
Researcher at Queensland University of Technology
Publications - 141
Citations - 7187
Makrina Totsika is an academic researcher from Queensland University of Technology. The author has contributed to research in topics: Escherichia coli & Bacterial adhesin. The author has an hindex of 46, co-authored 119 publications receiving 6056 citations. Previous affiliations of Makrina Totsika include University of Queensland & University of Edinburgh.
Papers
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Journal ArticleDOI
Global dissemination of a multidrug resistant Escherichia coli clone
Nicola K. Petty,Nouri L. Ben Zakour,Mitchell Stanton-Cook,Elizabeth Skippington,Makrina Totsika,Brian M. Forde,Minh-Duy Phan,Danilo Gomes Moriel,Kate M. Peters,Mark R. Davies,Mark R. Davies,Benjamin A. Rogers,Gordon Dougan,Jesús Rodríguez-Baño,Álvaro Pascual,Johann D. D. Pitout,Mathew Upton,David L. Paterson,Timothy R. Walsh,Mark A. Schembri,Scott A. Beatson +20 more
TL;DR: This study confirms the global dispersal of a single E. coli ST131 clone and demonstrates the role of MGEs and recombination in the evolution of this important MDR pathogen.
Journal ArticleDOI
Host–pathogen checkpoints and population bottlenecks in persistent and intracellular uropathogenic Escherichia coli bladder infection
Thomas J. Hannan,Makrina Totsika,Kylie J Mansfield,Kate H. Moore,Mark A. Schembri,Scott J. Hultgren +5 more
TL;DR: In this paper, the authors proposed a putative host-pathogen mucosal checkpoint that contributes to susceptibility to Uropathogenic Escherichia coli (UPEC) infection.
Journal ArticleDOI
Bacterial Biofilm Eradication Agents: A Current Review.
TL;DR: The current understanding of biofilm antibiotic tolerance mechanisms is reviewed and an overview ofBiofilm remediation strategies is provided, focusing primarily on the most promising biofilm eradication agents and approaches.
Journal ArticleDOI
DSB proteins and bacterial pathogenicity
Begoña Heras,Stephen R. Shouldice,Makrina Totsika,Martin J. Scanlon,Mark A. Schembri,Jennifer L. Martin +5 more
TL;DR: A key step in the protein-folding pathway is the introduction of disulphide bonds between cysteine residues in a process called oxidative protein folding as discussed by the authors, which is a process that is essential for cell integrity and to produce virulence factors.
DSB proteins and bacterial pathogenicity
Begoña Heras,Stephen R. Shouldice,Makrina Totsika,Martin J. Scanlon,Mark A. Schembri,Jennifer L. Martin +5 more
TL;DR: This view of protein-folding machinery must now be adjusted to encompass the wider range of disulphide catalytic systems present in bacteria.