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Anne Marie Quinn

Researcher at University Hospital Galway

Publications -  32
Citations -  7297

Anne Marie Quinn is an academic researcher from University Hospital Galway. The author has contributed to research in topics: Diacylglycerol kinase & G protein-coupled receptor. The author has an hindex of 15, co-authored 27 publications receiving 7023 citations. Previous affiliations of Anne Marie Quinn include Howard Hughes Medical Institute & Salk Institute for Biological Studies.

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Journal ArticleDOI

The protein kinase family: conserved features and deduced phylogeny of the catalytic domains.

TL;DR: Phylogenetic mapping of the conserved protein kinase catalytic domains can serve as a useful first step in the functional characterization of these newly identified family members.
Book ChapterDOI

Protein kinase catalytic domain sequence database: identification of conserved features of primary structure and classification of family members

TL;DR: The catalytic domain database (PKINASES) as mentioned in this paper is a large-scale database of protein kinase amino acid sequences, which is used for the initial classification of novel protein kinases and for other studies that require extensive sequence comparisons.
Journal ArticleDOI

Dual-specificity protein kinases: will any hydroxyl do?

TL;DR: Several new protein kinases have been discovered that, by the criterion of primary structure, would be classified as protein-serine/threonine kinases but which, surprisingly, are able to phosphorylate tyrosine residues.
Journal ArticleDOI

Human deltex is a conserved regulator of Notch signalling

TL;DR: Evidence linking deltex to the modulation of basic helix-loop-helix (bHLH) transcription factor activity is presented, and results from two different reporter assays allow for the first time to associate deltex with Notch-dependent transcriptional events.
Journal ArticleDOI

Ratiometric biosensors based on dimerization-dependent fluorescent protein exchange

TL;DR: A versatile new class of genetically encoded fluorescent biosensor is developed based on reversible exchange of the heterodimeric partners of green and red dimerization-dependent fluorescent proteins for qualitative imaging of caspase activity, Ca2+ concentration dynamics and other second-messenger signaling activities.