P
P. J. Doherty
Researcher at University of Liverpool
Publications - 29
Citations - 1579
P. J. Doherty is an academic researcher from University of Liverpool. The author has contributed to research in topics: Biocompatibility & Surface modification. The author has an hindex of 18, co-authored 29 publications receiving 1499 citations.
Papers
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Journal ArticleDOI
Semisynthetic resorbable materials from hyaluronan esterification.
Davide Campoccia,P. J. Doherty,Marco Radice,Paola Brun,Giovanni Abatangelo,David F. Williams +5 more
TL;DR: This review on the properties of the new materials reports some of their biocompatibility and characterization aspects based on findings from studies conducted on the ethyl and benzyl hyaluronan esters, and is intended to arouse interest in the potential of other, as yet unexplored derivatives.
Journal ArticleDOI
A preliminary assessment of poly(pyrrole) in nerve guide studies
Rachel Williams,P. J. Doherty +1 more
TL;DR: The results demonstrate that the polypyrrole is cytocompatible in vitro if prepared by appropriate extraction techniques and can be an effective medium for carrying current in a biological environment.
Journal ArticleDOI
Biodegradation of hyaluronic acid derivatives by hyaluronidase
Sheng P. Zhong,Davide Campoccia,P. J. Doherty,Rachel Williams,Luca Benedetti,David F. Williams +5 more
TL;DR: Observations tend to suggest that the carboxylic groups in the beta-glucoronic acid unit are the activation centre of this enzyme and the total blockage of these groups can restrict the cleavage of beta (1-->4) glycoside bonds by this enzyme.
Journal ArticleDOI
The effect of silica nanoparticulate coatings on serum protein adsorption and cellular response.
Megan S. Lord,B.G. Cousins,P. J. Doherty,John M. Whitelock,Anne Simmons,Rachel Williams,Bruce Milthorpe +6 more
TL;DR: The conformation of adsorbed proteins on the colloidal silica-coated surfaces was conformationally changed compared with control silica reducing the availability of the cell-binding domain of fibronectin, one of the main extracellular matrix proteins involved in endothelial cell attachment to biomaterial surfaces.