Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Daniel Y Dubois"'
Autor:
W Edward C Bradley, John V Raelson, Daniel Y Dubois, Eric Godin, Hélène Fournier, Charles Privé, René Allard, Vadym Pinchuk, Micheline Lapalme, René J A Paulussen, Abdelmajid Belouchi
Publikováno v:
PLoS ONE, Vol 5, Iss 2, p e9401 (2010)
BACKGROUND: We have examined the genomic distribution of large rare autosomal deletions in a sample of 440 parent-parent-child trios from the Quebec founder population (QFP) which was recruited for a study of Attention Deficit Hyperactivity Disorder.
Externí odkaz:
https://doaj.org/article/c391641ddd8a43aa9dc15d8dd5870873
Autor:
Daniel Y. Dubois, Daniel Kern, Valérie Campanacci, Jacques Lapointe, Christian Cambillau, Hubert Dominique Becker, Mickaël Blaise, Richard Giegé, Gérard Keith
Publikováno v:
Dubois, D Y, Blaise, M, Becker, H D, Campanacci, V, Keith, G, Giege, R, Cambillau, C, Lapointe, J & Kern, D 2004, ' An aminoacyl-tRNA synthetase-like protein encoded by the Escherichia coli yadB gene glutamylates specifically tRNAAsp. ', Proceeding of the National Academy of Sciences USA .
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 the stem-contact fold. This GluRS-like protein, which
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::553cc4cb5f21f889c163909187acea6c
https://doi.org/10.1073/pnas.0401634101
https://doi.org/10.1073/pnas.0401634101
Autor:
Sheng-Xiang Lin, Sabita Roy, Daniel Y. Dubois, Jacques Lapointe, Joelle Gauthier, Rajat Banerjee
Publikováno v:
European Journal of Biochemistry. 271:724-733
In its tRNA acceptor end binding domain, the glutamyl-tRNA synthetase (GluRS) of Escherichia coli contains one atom of zinc that holds the extremities of a segment (Cys98-x-Cys100-x24-Cys125-x-His127) homologous to the Escherichia coli glutaminyl-tRN
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::0fe9913ec56d7c736466f338670a32ef
https://doi.org/10.1111/j.1432-1033.2003.03976.x
https://doi.org/10.1111/j.1432-1033.2003.03976.x
Autor:
Rajat, Banerjee, Daniel Y, Dubois, Joelle, Gauthier, Sheng-Xiang, Lin, Siddhartha, Roy, Jacques, Lapointe
Publikováno v:
European journal of biochemistry. 271(4)
In its tRNA acceptor end binding domain, the glutamyl-tRNA synthetase (GluRS) of Escherichia coli contains one atom of zinc that holds the extremities of a segment (Cys98-x-Cys100-x24-Cys125-x-His127) homologous to the Escherichia coli glutaminyl-tRN
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::50a91ed3c675dc47930d3a7b5c3e2fdf
https://pubmed.ncbi.nlm.nih.gov/14764088
https://pubmed.ncbi.nlm.nih.gov/14764088
Autor:
Christian Cambillau, Christophe Bignon, Daniel Y. Dubois, Renaud Vincentelli, Sacha Grisel, Silvia Spinelli, Jacques Lapointe, Valérie Campanacci, Daniel Kern, F. Pagot, Richard Giegé, Christel Valencia, Hubert Dominique Becker, Aurelia Salomoni
Publikováno v:
Journal of Molecular Biology
Journal of Molecular Biology, Elsevier, 2004, 337 (2), pp.273-283. ⟨10.1016/j.jmb.2004.01.027⟩
Journal of Molecular Biology, Elsevier, 2004, 337 (2), pp.273-283. ⟨10.1016/j.jmb.2004.01.027⟩
In the course of a structural genomics program aiming at solving the structures of Escherichia coli open reading frame products of unknown function, we have determined the structure of YadB at 1.5Å using molecular replacement. The YadB protein is 29
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::85ed1ecb92abedb7329b3cc09013f454
https://pubmed.ncbi.nlm.nih.gov/15003446
https://pubmed.ncbi.nlm.nih.gov/15003446
Autor:
Shigeyuki Yokoyama, Robert Chênevert, Stéphane Bernier, Osamu Nureki, Shun-ichi Sekine, Dmitry G. Vassylyev, Jacques Lapointe, Daniel Y. Dubois
Publikováno v:
The EMBO journal. 22(3)
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 glutamyl-tRNA synthetase (GluRS), have a regulation mechanism
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::51597cf6295bfc46e189c9c73d9b3b17
https://pubmed.ncbi.nlm.nih.gov/12554668
https://pubmed.ncbi.nlm.nih.gov/12554668
Publikováno v:
Bioorganicmedicinal chemistry letters. 10(21)
Glutaminol adenylate 5 is a competitive inhibitor of glutaminyl-tRNA synthetase with respect to glutamine ( K i =280 nM) and to ATP ( K i =860 nM). The corresponding methyl phosphate ester 4 is a weaker inhibitor ( K i ∼10 μM) with respect to glut
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::073ea47f6c34de7836db9afba0655324
https://pubmed.ncbi.nlm.nih.gov/11078196
https://pubmed.ncbi.nlm.nih.gov/11078196
Publikováno v:
Biochemistry. 48:7352-7352
Faithful translation of the genetic code is mainly based on the specificity of tRNA aminoacylation catalyzed by aminoacyl-tRNA synthetases. These enzymes are comprised of a catalytic core and several appended domains. Bacterial glutamyl-tRNA syntheta
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d2b956e2c6f580f9b1693d7b676bc870
https://doi.org/10.1021/bi901013h
https://doi.org/10.1021/bi901013h