Thèse (M. Sc.)--Université du Québec, 1976.
Monographie de l'Industrielle, cie d'assurance-vie / (1950)
Thèse (Maîtrise) - École de commerce de l'Université Laval de Québec.
ATP binding by glutamyl-tRNA synthetase is switched to the productive mode by tRNA binding
Sekine, Shun-ichi, Nureki, Osamu, Dubois, Daniel Y., Bernier, Stéphane, Chênevert, Robert, Lapointe, Jacques, ...
Aminoacyl-tRNA synthetases catalyze the formation of an aminoacyl-AMP from an amino acid and ATP, prior to the aminoacyl transfer to tRNA. A subset of aminoacyl-tRNA synthetases, including...
Akochy, Pierre-Marie, Bernard, Dominic, Roy, Paul H., Lapointe, Jacques
The genomic sequence of Pseudomonas aeruginosa PAO1 was searched for the presence of open reading frames (ORFs) encoding enzymes potentially involved in the formation of Gln-tRNA and of Asn-tRNA. We...
Gene expression profiling identifies clinically relevant subtypes of prostate cancer
Lapointe, Jacques, Li, Chunde, Higgins, John P., Van De Rijn, Matt, Bair, Eric, Montgomery, Kelli, ...
Prostate cancer, a leading cause of cancer death, displays a broad range of clinical behavior from relatively indolent to aggressive metastatic disease. To explore potential molecular variation...
A minimalist glutamyl-tRNA synthetase dedicated to aminoacylation of the tRNAAsp QUC anticodon
Blaise, Mickaël, Becker, Hubert Dominique, Keith, Gérard, Cambillau, Christian, Lapointe, Jacques, Giegé, Richard, ...
Escherichia coli encodes YadB, a protein displaying 34% identity with the catalytic core of glutamyl-tRNA synthetase but lacking the anticodon-binding domain. We show that YadB is a tRNA modifying...
Dubois, Daniel Y., Blaise, Mickaël, Becker, Hubert D., Campanacci, Valérie, Keith, Gérard, Giegé, Richard, ...
The product of the Escherichia coli yadB gene is homologous to the N-terminal part of bacterial glutamyl-tRNA synthetases (GluRSs), including the Rossmann fold with the acceptor-binding domain and...
Bernard, Dominic, Akochy, Pierre-Marie, Beaulieu, David, Lapointe, Jacques, Roy, Paul H.
In many organisms, the formation of asparaginyl-tRNA is not done by direct aminoacylation of tRNAAsn but by specific tRNA-dependent transamidation of aspartyl-tRNAAsn. This transamidation pathway...
ATP binding by glutamyl-tRNA synthetase is switched to the productive mode by tRNA binding
Sekine, Shun-ichi, Nureki, Osamu, Dubois, Daniel Y., Bernier, Stéphane, Chênevert, Robert, Lapointe, Jacques, ...
Aminoacyl-tRNA synthetases catalyze the formation of an aminoacyl-AMP from an amino acid and ATP, prior to the aminoacyl transfer to tRNA. A subset of aminoacyl-tRNA synthetases, including...
Akochy, Pierre-Marie, Bernard, Dominic, Roy, Paul H., Lapointe, Jacques
The genomic sequence of Pseudomonas aeruginosa PAO1 was searched for the presence of open reading frames (ORFs) encoding enzymes potentially involved in the formation of Gln-tRNA and of Asn-tRNA. We...
Gene expression profiling identifies clinically relevant subtypes of prostate cancer
Lapointe, Jacques, Li, Chunde, Higgins, John P., Van De Rijn, Matt, Bair, Eric, Montgomery, Kelli, ...
Prostate cancer, a leading cause of cancer death, displays a broad range of clinical behavior from relatively indolent to aggressive metastatic disease. To explore potential molecular variation...
A minimalist glutamyl-tRNA synthetase dedicated to aminoacylation of the tRNAAsp QUC anticodon
Blaise, Mickaël, Becker, Hubert Dominique, Keith, Gérard, Cambillau, Christian, Lapointe, Jacques, Giegé, Richard, ...
Escherichia coli encodes YadB, a protein displaying 34% identity with the catalytic core of glutamyl-tRNA synthetase but lacking the anticodon-binding domain. We show that YadB is a tRNA modifying...
Dubois, Daniel Y., Blaise, Mickaël, Becker, Hubert D., Campanacci, Valérie, Keith, Gérard, Giegé, Richard, ...
The product of the Escherichia coli yadB gene is homologous to the N-terminal part of bacterial glutamyl-tRNA synthetases (GluRSs), including the Rossmann fold with the acceptor-binding domain and...
Bernard, Dominic, Akochy, Pierre-Marie, Beaulieu, David, Lapointe, Jacques, Roy, Paul H.
In many organisms, the formation of asparaginyl-tRNA is not done by direct aminoacylation of tRNAAsn but by specific tRNA-dependent transamidation of aspartyl-tRNAAsn. This transamidation pathway...