scispace - formally typeset
P

Patrick A. Eyers

Researcher at University of Liverpool

Publications -  124
Citations -  8284

Patrick A. Eyers is an academic researcher from University of Liverpool. The author has contributed to research in topics: Protein kinase A & Phosphorylation. The author has an hindex of 39, co-authored 111 publications receiving 6173 citations. Previous affiliations of Patrick A. Eyers include University of Sheffield & University of Manchester.

Papers
More filters
Journal ArticleDOI

Drug repurposing: progress, challenges and recommendations

TL;DR: Approaches used for drug repurposing (also known as drug repositioning) are presented, the challenges faced by the repurpose community are discussed, and innovative ways by which these challenges could be addressed are recommended to help realize the full potential of drugRepurposing.
Journal ArticleDOI

A novel mechanism for activation of the protein kinase Aurora A.

TL;DR: The finding that a known binding protein, and not a conventional protein kinase, is the relevant activator for Aurora A suggests a biochemical model in which the dynamic localization of TPX2 on mitotic structures directly modulates the activity of Aurora A for spindle assembly.
Journal ArticleDOI

Conversion of SB 203580-insensitive MAP kinase family members to drug-sensitive forms by a single amino-acid substitution

TL;DR: These findings explain how drugs that target the ATP-binding site can inhibit protein kinases specifically, and show that the presence of threonine or a smaller amino acid at the position equivalent to Thr106 of SAPK 2a/p38 and SAPK2b/ p38 beta 2 is diagnostic of whether a protein kinase is sensitive to the pyridinyl imidazole class of inhibitor.
Journal ArticleDOI

Validating Aurora B as an anti-cancer drug target.

TL;DR: Observations indicate that the Auroras may present two avenues for anti-cancer drug discovery, as small molecule-mediated inhibition of Aurora A and Aurora B yields distinct phenotypes.
Journal ArticleDOI

Stress-induced phosphorylation of STAT1 at Ser727 requires p38 mitogen-activated protein kinase whereas IFN-gamma uses a different signaling pathway.

TL;DR: The data suggest that STAT1 is phosphorylated at Ser727 by a stress-activated signaling pathway either through p38 MAPK directly or through an unidentified kinase downstream of p38MAPK.