Jacques Lapointe

ATP binding by glutamyl-tRNA synthetase is switched to the productive mode by tRNA binding.

Gene expression profiling identifies clinically relevant subtypes of prostate cancer.

Direct glutaminyl-tRNA biosynthesis and indirect asparaginyl-tRNA biosynthesis in Pseudomonas aeruginosa PAO1.

The zinc-binding site of a class I aminoacyl-tRNA synthetase is a SWIM domain that modulates amino acid binding via the tRNA acceptor arm.

The Escherichia coli YadB gene product reveals a novel aminoacyl-tRNA synthetase like activity.

An aminoacyl-tRNA synthetase-like protein encoded by the Escherichia coli yadB gene glutamylates specifically tRNAAsp.

A minimalist glutamyl-tRNA synthetase dedicated to aminoacylation of the tRNAAsp QUC anticodon.

Crystal structure of chloramphenicol acetyltransferase B2 encoded by the multiresistance transposon Tn2424.

Genome-wide characterization of gene expression variations and DNA copy number changes in prostate cancer cell lines.

Synthesis and aminoacyl-tRNA synthetase inhibitory activity of aspartyl adenylate analogs.

Glutamylsulfamoyladenosine and pyroglutamylsulfamoyladenosine are competitive inhibitors of E. coli glutamyl-tRNA synthetase.

Glu-Q-tRNA(Asp) synthetase coded by the yadB gene, a new paralog of aminoacyl-tRNA synthetase that glutamylates tRNA(Asp) anticodon.

The retinoic acid synthesis gene ALDH1a2 is a candidate tumor suppressor in prostate cancer.

Two residues in the anticodon recognition domain of the aspartyl-tRNA synthetase from Pseudomonas aeruginosa are individually implicated in the recognition of tRNAAsn.

Synthesis of beta-ketophosphonate analogs of glutamyl and glutaminyl adenylate, and selective inhibition of the corresponding bacterial aminoacyl-tRNA synthetases.

Application of genomic technologies to human prostate cancer.

Structural bases of transfer RNA-dependent amino acid recognition and activation by glutamyl-tRNA synthetase.

A variant TMPRSS2 isoform and ERG fusion product in prostate cancer with implications for molecular diagnosis.

Inhibition by L-aspartol adenylate of a nondiscriminating aspartyl-tRNA synthetase reveals differences between the interactions of its active site with tRNA(Asp) and tRNA(Asn).

E. coli glutamyl-tRNA synthetase is inhibited by anticodon stem-loop domains and a minihelix.

Genomic profiling reveals alternative genetic pathways of prostate tumorigenesis.

Mechanism of a GatCAB amidotransferase: aspartyl-tRNA synthetase increases its affinity for Asp-tRNA(Asn) and novel aminoacyl-tRNA analogues are competitive inhibitors.

hCAP-D3 expression marks a prostate cancer subtype with favorable clinical behavior and androgen signaling signature.

Inhibition of Helicobacter pylori aminoacyl-tRNA amidotransferase by puromycin analogues.

Identification of candidate prostate cancer genes through comparative expression-profiling of seminal vesicle.

Peculiar inhibition of human mitochondrial aspartyl-tRNA synthetase by adenylate analogs.

A C-truncated glutamyl-tRNA synthetase specific for tRNA(Glu) is stimulated by its free complementary distal domain: mechanistic and evolutionary implications.

Inhibition of Helicobacter pylori aminoacyl-tRNA amidotransferase by chloramphenicol analogs.

A tri-marker proliferation index predicts biochemical recurrence after surgery for prostate cancer.

Gln-tRNAGln synthesis in a dynamic transamidosome from Helicobacter pylori, where GluRS2 hydrolyzes excess Glu-tRNAGln.

The asparagine-transamidosome from Helicobacter pylori: a dual-kinetic mode in non-discriminating aspartyl-tRNA synthetase safeguards the genetic code.

Natural insertion of the bro-1 β-lactamase gene into the gatCAB operon affects Moraxella catarrhalis aspartyl-tRNA(Asn) amidotransferase activity.

PTEN genomic deletion predicts prostate cancer recurrence and is associated with low AR expression and transcriptional activity.

Magnetic interference of cardiac pacemakers from a surgical magnetic drape.

The 16p13.3 (PDPK1) Genomic Gain in Prostate Cancer: A Potential Role in Disease Progression.

tRNAGlu increases the affinity of glutamyl-tRNA synthetase for its inhibitor glutamyl-sulfamoyl-adenosine, an analogue of the aminoacylation reaction intermediate glutamyl-AMP: mechanistic and evolutionary implications.

Correction: tRNAGlu Increases the Affinity of Glutamyl-tRNA Synthetase for Its Inhibitor Glutamyl-Sulfamoyl-Adenosine, an Analogue of the Aminoacylation Reaction Intermediate Glutamyl-AMP: Mechanistic and Evolutionary Implications.

Cyclic peptides identified by phage display are competitive inhibitors of the tRNA-dependent amidotransferase of Helicobacter pylori.

Interference between surgical magnetic drapes and pacemakers: an observational study comparing commercially available devices and a new magnetically isolated drape.