Paul M. Joyce

Montreal, QC, Canada

Last Updated: 09/26/2026

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Found 8 publications

The oral pathogen Porphyromonas gingivalis gains tolerance to the antimicrobial peptide DGL13K by synonymous mutations in hagA.

The oral pathogen Porphyromonas gingivalis gains tolerance to the antimicrobial peptide DGL13K by synonymous mutations in hagA.

Journal: PloS one
Published: December 20, 2023

Analysis of the pathogenic I326T variant of human tRNA nucleotidyltransferase reveals reduced catalytic activity and thermal stability in vitro linked to a conformational change.

Analysis of the pathogenic I326T variant of human tRNA nucleotidyltransferase reveals reduced catalytic activity and thermal stability in vitro linked to a conformational change.

Journal: Biochimica et biophysica acta. Proteins and proteomics
Published: October 12, 2018

Schizosaccharomyces pombe contains separate CC- and A-adding tRNA nucleotidyltransferases.

Schizosaccharomyces pombe contains separate CC- and A-adding tRNA nucleotidyltransferases.

Journal: Biochemical and biophysical research communications
Published: October 03, 2018

In vitro studies of disease-linked variants of human tRNA nucleotidyltransferase reveal decreased thermal stability and altered catalytic activity.

In vitro studies of disease-linked variants of human tRNA nucleotidyltransferase reveal decreased thermal stability and altered catalytic activity.

Journal: Biochimica et biophysica acta. Proteins and proteomics
Published: November 17, 2017

Mutations in TRNT1 cause congenital sideroblastic anemia with immunodeficiency, fevers, and developmental delay (SIFD).

Mutations in TRNT1 cause congenital sideroblastic anemia with immunodeficiency, fevers, and developmental delay (SIFD).

Journal: Blood
Published: September 07, 2014

The folding capacity of the mature domain of the dual-targeted plant tRNA nucleotidyltransferase influences organelle selection.

The folding capacity of the mature domain of the dual-targeted plant tRNA nucleotidyltransferase influences organelle selection.

Journal: The Biochemical journal
Published: May 30, 2013

The ability of an arginine to tryptophan substitution in Saccharomyces cerevisiae tRNA nucleotidyltransferase to alleviate a temperature-sensitive phenotype suggests a role for motif C in active site organization.

The ability of an arginine to tryptophan substitution in Saccharomyces cerevisiae tRNA nucleotidyltransferase to alleviate a temperature-sensitive phenotype suggests a role for motif C in active site organization.

Journal: Biochimica et biophysica acta
Published: January 18, 2013

The Saccharomyces cerevisiae enolase-related regions encode proteins that are active enolases.

The Saccharomyces cerevisiae enolase-related regions encode proteins that are active enolases.

Journal: Yeast (Chichester, England)
Published: October 09, 2012
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Last Updated: 09/26/2026