B
Brendan Gilmore
Researcher at Queen's University Belfast
Publications - 138
Citations - 7378
Brendan Gilmore is an academic researcher from Queen's University Belfast. The author has contributed to research in topics: Biofilm & Antimicrobial. The author has an hindex of 38, co-authored 130 publications receiving 5866 citations.
Papers
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Journal ArticleDOI
Proteases as Selective Activators of Triggered Drug Release: A Potential Answer to the Problem of Biomaterial-Associated Infections?
TL;DR: Proteases as Selective Activators of Triggered Drug Release: A Potential Answer to the Problem of Biomaterial-Associated Infections?
Journal ArticleDOI
Profiling the activity of edible European macroalgae towards pharmacological targets for type 2 diabetes mellitus
Danielle Calderwood,EP Rafferty,Ciaran Fitzgerald,Velizara Stoilova,A.R.G. Wylie,Brendan Gilmore,Francisco Castaneda,Alvaro Israel,Christine A. Maggs,Brian D. Green +9 more
TL;DR: Future potential for common edible seaweeds to be used as medicinal foods or bio-therapeutics to tackle type 2 diabetes mellitus by targeting GLP-1 secretion, DPP-4 activity or alpha-glucosidase activity is demonstrated.
A Bioadhesive Patch Containing 5-Aminolevulinic acid for Photodynamic Therapy of Vulval Pathologies
Ryan F. Donnelly,Paul A. McCarron,David Woolfson,Agnieszka Zawislak,J.H. Price,Brendan Gilmore +5 more
Book ChapterDOI
Models for the assessment of biofilm and encrustation formation on urological materials
TL;DR: This chapter examines the in vitro encrustation models available for evaluation and preliminary assessment of new biomaterials, coatings and drug-eluting devices for use in the urinary tract, aimed at resisting surface Encrustation and microbial biofilm formation.
Journal ArticleDOI
The inactivation of bovine cathepsin B by novel N-chloro-acetyl-dipeptides: Application of the Houghten ‘tea bag’ methodology to inhibitor synthesis
TL;DR: This preliminary study has highlighted a number of interesting features about the specificity requirements of the bovine proteinase and it is believed that this approach has great potential for the rapid delineation of the subsite specificities of cathepsin B-like proteases from various species.