Year |
Citation |
Score |
2017 |
Audet-Walsh É, Dufour CR, Yee T, Zouanat FZ, Yan M, Kalloghlian G, Vernier M, Caron M, Bourque G, Scarlata E, Hamel L, Brimo F, Aprikian AG, Lapointe J, Chevalier S, et al. Nuclear mTOR acts as a transcriptional integrator of the androgen signaling pathway in prostate cancer. Genes & Development. PMID 28724614 DOI: 10.1101/Gad.299958.117 |
0.314 |
|
2016 |
Pham VH, Maaroufi H, Christian B, Blais SP, Messier N, Roy PH, Otis F, Voyer N, Lapointe J, Chênevert R. Inhibition of Helicobacter pylori Glu-tRNA(G) (ln) amidotransferase by novel analogues of the putative transamidation intermediates. Febs Letters. PMID 27586694 DOI: 10.1002/1873-3468.12380 |
0.337 |
|
2016 |
Pham VH, Maaroufi H, Levesque RC, Lapointe J. Cyclic peptides identified by phage display are competitive inhibitors of the tRNA-dependent amidotransferase of Helicobacter pylori. Peptides. PMID 26976271 DOI: 10.1016/J.Peptides.2016.03.001 |
0.333 |
|
2015 |
Blais SP, Kornblatt JA, Barbeau X, Bonnaure G, Lagüe P, Chênevert R, Lapointe J. 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. Plos One. 10: e0130238. PMID 26039673 DOI: 10.1371/Journal.Pone.0130238 |
0.396 |
|
2013 |
Lapointe J. Mechanism and evolution of multidomain aminoacyl-tRNA synthetases revealed by their inhibition by analogues of a reaction intermediate, and by properties of truncated forms Journal of Biomedical Science and Engineering. 6: 943-946. DOI: 10.4236/Jbise.2013.610115 |
0.393 |
|
2012 |
Choucair KA, Guérard KP, Ejdelman J, Chevalier S, Yoshimoto M, Scarlata E, Fazli L, Sircar K, Squire JA, Brimo F, Cunha IW, Aprikian A, Gleave M, Lapointe J. The 16p13.3 (PDPK1) Genomic Gain in Prostate Cancer: A Potential Role in Disease Progression. Translational Oncology. 5: 453-60. PMID 23401739 DOI: 10.1593/Tlo.12286 |
0.303 |
|
2012 |
Choucair K, Ejdelman J, Brimo F, Aprikian A, Chevalier S, Lapointe J. PTEN genomic deletion predicts prostate cancer recurrence and is associated with low AR expression and transcriptional activity. Bmc Cancer. 12: 543. PMID 23171135 DOI: 10.1186/1471-2407-12-543 |
0.33 |
|
2012 |
Akochy PM, Lapointe J, Roy PH. Natural insertion of the bro-1 β-lactamase gene into the gatCAB operon affects Moraxella catarrhalis aspartyl-tRNA(Asn) amidotransferase activity. Microbiology (Reading, England). 158: 2363-71. PMID 22745266 DOI: 10.1099/Mic.0.060095-0 |
0.397 |
|
2012 |
Huang S, Gulzar ZG, Salari K, Lapointe J, Brooks JD, Pollack JR. Recurrent deletion of CHD1 in prostate cancer with relevance to cell invasiveness. Oncogene. 31: 4164-4170. PMID 22179824 DOI: 10.1038/Onc.2011.590 |
0.341 |
|
2011 |
Malhotra S, Lapointe J, Salari K, Higgins JP, Ferrari M, Montgomery K, van de Rijn M, Brooks JD, Pollack JR. A tri-marker proliferation index predicts biochemical recurrence after surgery for prostate cancer. Plos One. 6: e20293. PMID 21629784 DOI: 10.1371/Journal.Pone.0020293 |
0.307 |
|
2010 |
Balg C, De Mieri M, Huot JL, Blais SP, Lapointe J, Chênevert R. Inhibition of Helicobacter pylori aminoacyl-tRNA amidotransferase by chloramphenicol analogs. Bioorganic & Medicinal Chemistry. 18: 7868-72. PMID 20943400 DOI: 10.1016/J.Bmc.2010.09.045 |
0.357 |
|
2009 |
Dubois DY, Blais SP, Huot JL, Lapointe J. A C-truncated glutamyl-tRNA synthetase specific for tRNA(Glu) is stimulated by its free complementary distal domain: mechanistic and evolutionary implications. Biochemistry. 48: 6012-21. PMID 19496540 DOI: 10.1021/Bi801690F |
0.325 |
|
2009 |
Messmer M, Blais SP, Balg C, Chênevert R, Grenier L, Lagüe P, Sauter C, Sissler M, Giegé R, Lapointe J, Florentz C. Peculiar inhibition of human mitochondrial aspartyl-tRNA synthetase by adenylate analogs. Biochimie. 91: 596-603. PMID 19254750 DOI: 10.1016/J.Biochi.2009.02.005 |
0.363 |
|
2008 |
Thompson M, Lapointe J, Choi YL, Ong DE, Higgins JP, Brooks JD, Pollack JR. Identification of candidate prostate cancer genes through comparative expression-profiling of seminal vesicle. The Prostate. 68: 1248-56. PMID 18500686 DOI: 10.1002/Pros.20792 |
0.319 |
|
2008 |
Balg C, Huot JL, Lapointe J, Chênevert R. Inhibition of Helicobacter pylori aminoacyl-tRNA amidotransferase by puromycin analogues. Journal of the American Chemical Society. 130: 3264-5. PMID 18293984 DOI: 10.1021/Ja7100714 |
0.366 |
|
2008 |
Lapointe J, Malhotra S, Higgins JP, Bair E, Thompson M, Salari K, Giacomini CP, Ferrari M, Montgomery K, Tibshirani R, van de Rijn M, Brooks JD, Pollack JR. hCAP-D3 expression marks a prostate cancer subtype with favorable clinical behavior and androgen signaling signature. The American Journal of Surgical Pathology. 32: 205-9. PMID 18223322 DOI: 10.1097/Pas.0B013E318124A865 |
0.31 |
|
2007 |
Huot JL, Balg C, Jahn D, Moser J, Emond A, Blais SP, Chênevert R, Lapointe J. Mechanism of a GatCAB amidotransferase: aspartyl-tRNA synthetase increases its affinity for Asp-tRNA(Asn) and novel aminoacyl-tRNA analogues are competitive inhibitors. Biochemistry. 46: 13190-8. PMID 17929881 DOI: 10.1021/Bi700602N |
0.396 |
|
2007 |
Lapointe J, Li C, Giacomini CP, Salari K, Huang S, Wang P, Ferrari M, Hernandez-Boussard T, Brooks JD, Pollack JR. Genomic profiling reveals alternative genetic pathways of prostate tumorigenesis. Cancer Research. 67: 8504-10. PMID 17875689 DOI: 10.1158/0008-5472.Can-07-0673 |
0.318 |
|
2007 |
Gustilo EM, Dubois DY, Lapointe J, Agris PF. E. coli glutamyl-tRNA synthetase is inhibited by anticodon stem-loop domains and a minihelix. Rna Biology. 4: 85-92. PMID 17671438 DOI: 10.4161/Rna.4.2.4736 |
0.338 |
|
2007 |
Bernard D, Akochy PM, Bernier S, Fisette O, Brousseau OC, Chênevert R, Roy PH, Lapointe J. 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). Journal of Enzyme Inhibition and Medicinal Chemistry. 22: 77-82. PMID 17373551 DOI: 10.1080/14756360600952316 |
0.387 |
|
2007 |
Lapointe J, Kim YH, Miller MA, Li C, Kaygusuz G, van de Rijn M, Huntsman DG, Brooks JD, Pollack JR. A variant TMPRSS2 isoform and ERG fusion product in prostate cancer with implications for molecular diagnosis. Modern Pathology : An Official Journal of the United States and Canadian Academy of Pathology, Inc. 20: 467-73. PMID 17334351 DOI: 10.1038/Modpathol.3800759 |
0.33 |
|
2007 |
Balg C, Blais SP, Bernier S, Huot JL, Couture M, Lapointe J, Chênevert R. Synthesis of beta-ketophosphonate analogs of glutamyl and glutaminyl adenylate, and selective inhibition of the corresponding bacterial aminoacyl-tRNA synthetases. Bioorganic & Medicinal Chemistry. 15: 295-304. PMID 17049867 DOI: 10.1016/J.Bmc.2006.09.056 |
0.347 |
|
2006 |
Sekine S, Shichiri M, Bernier S, Chênevert R, Lapointe J, Yokoyama S. Structural bases of transfer RNA-dependent amino acid recognition and activation by glutamyl-tRNA synthetase. Structure (London, England : 1993). 14: 1791-9. PMID 17161369 DOI: 10.1016/J.Str.2006.10.005 |
0.351 |
|
2006 |
Li S, Bhamre S, Lapointe J, Pollack JR, Brooks JD. Application of genomic technologies to human prostate cancer. Omics : a Journal of Integrative Biology. 10: 261-75. PMID 17069507 DOI: 10.1089/Omi.2006.10.261 |
0.304 |
|
2006 |
Bernard D, Akochy PM, Beaulieu D, Lapointe J, Roy PH. Two residues in the anticodon recognition domain of the aspartyl-tRNA synthetase from Pseudomonas aeruginosa are individually implicated in the recognition of tRNAAsn. Journal of Bacteriology. 188: 269-74. PMID 16352843 DOI: 10.1128/Jb.188.1.269-274.2006 |
0.343 |
|
2005 |
Kim H, Lapointe J, Kaygusuz G, Ong DE, Li C, van de Rijn M, Brooks JD, Pollack JR. The retinoic acid synthesis gene ALDH1a2 is a candidate tumor suppressor in prostate cancer. Cancer Research. 65: 8118-24. PMID 16166285 DOI: 10.1158/0008-5472.Can-04-4562 |
0.343 |
|
2005 |
Blaise M, Becker HD, Lapointe J, Cambillau C, Giegé R, Kern D. Glu-Q-tRNA(Asp) synthetase coded by the yadB gene, a new paralog of aminoacyl-tRNA synthetase that glutamylates tRNA(Asp) anticodon. Biochimie. 87: 847-61. PMID 16164993 DOI: 10.1016/J.Biochi.2005.03.007 |
0.403 |
|
2005 |
Bernier S, Dubois DY, Habegger-Polomat C, Gagnon LP, Lapointe J, Chênevert R. Glutamylsulfamoyladenosine and pyroglutamylsulfamoyladenosine are competitive inhibitors of E. coli glutamyl-tRNA synthetase. Journal of Enzyme Inhibition and Medicinal Chemistry. 20: 61-7. PMID 15895686 DOI: 10.1080/14756360400002007 |
0.343 |
|
2005 |
Bernier S, Akochy PM, Lapointe J, Chênevert R. Synthesis and aminoacyl-tRNA synthetase inhibitory activity of aspartyl adenylate analogs. Bioorganic & Medicinal Chemistry. 13: 69-75. PMID 15582453 DOI: 10.1016/J.Bmc.2004.09.055 |
0.323 |
|
2005 |
Zhao H, Kim Y, Wang P, Lapointe J, Tibshirani R, Pollack JR, Brooks JD. Genome-wide characterization of gene expression variations and DNA copy number changes in prostate cancer cell lines. The Prostate. 63: 187-97. PMID 15486987 DOI: 10.1002/Pros.20158 |
0.315 |
|
2004 |
Blaise M, Becker HD, Keith G, Cambillau C, Lapointe J, Giegé R, Kern D. A minimalist glutamyl-tRNA synthetase dedicated to aminoacylation of the tRNAAsp QUC anticodon. Nucleic Acids Research. 32: 2768-75. PMID 15150343 DOI: 10.1093/Nar/Gkh608 |
0.408 |
|
2004 |
Dubois DY, Blaise M, Becker HD, Campanacci V, Keith G, Giegé R, Cambillau C, Lapointe J, Kern D. An aminoacyl-tRNA synthetase-like protein encoded by the Escherichia coli yadB gene glutamylates specifically tRNAAsp. Proceedings of the National Academy of Sciences of the United States of America. 101: 7530-5. PMID 15096594 DOI: 10.1073/Pnas.0401634101 |
0.375 |
|
2004 |
Campanacci V, Dubois DY, Becker HD, Kern D, Spinelli S, Valencia C, Pagot F, Salomoni A, Grisel S, Vincentelli R, Bignon C, Lapointe J, Giegé R, Cambillau C. The Escherichia coli YadB gene product reveals a novel aminoacyl-tRNA synthetase like activity. Journal of Molecular Biology. 337: 273-83. PMID 15003446 DOI: 10.1016/J.Jmb.2004.01.027 |
0.393 |
|
2004 |
Banerjee R, Dubois DY, Gauthier J, Lin SX, Roy S, Lapointe J. 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. European Journal of Biochemistry / Febs. 271: 724-33. PMID 14764088 DOI: 10.1111/J.1432-1033.2003.03976.X |
0.34 |
|
2004 |
Akochy PM, Bernard D, Roy PH, Lapointe J. Direct glutaminyl-tRNA biosynthesis and indirect asparaginyl-tRNA biosynthesis in Pseudomonas aeruginosa PAO1. Journal of Bacteriology. 186: 767-76. PMID 14729703 DOI: 10.1128/Jb.186.3.767-776.2004 |
0.391 |
|
2003 |
Sekine S, Nureki O, Dubois DY, Bernier S, Chênevert R, Lapointe J, Vassylyev DG, Yokoyama S. ATP binding by glutamyl-tRNA synthetase is switched to the productive mode by tRNA binding. The Embo Journal. 22: 676-88. PMID 12554668 DOI: 10.1093/Emboj/Cdg053 |
0.329 |
|
2001 |
Lapointe J, Labrie C. Role of the Cyclin-Dependent Kinase Inhibitor p27Kip1 in Androgen-Induced Inhibition of CAMA-1 Breast Cancer Cell Proliferation. Endocrinology. 142: 4331-4338. PMID 28204441 DOI: 10.1210/endo.142.10.8417 |
0.54 |
|
2001 |
Lapointe J, Labrie C. Role of the cyclin-dependent kinase inhibitor p27kip1 in androgen-induced inhibition of CAMA-1 breast cancer cell proliferation Endocrinology. 142: 4331-4338. PMID 11564693 DOI: 10.1210/Endo.142.10.8417 |
0.581 |
|
2000 |
Bernier S, Dubois DY, Therrien M, Lapointe J, Chênevert R. Synthesis of glutaminyl adenylate analogues that are inhibitors of glutaminyl-tRNA synthetase. Bioorganic & Medicinal Chemistry Letters. 10: 2441-4. PMID 11078196 DOI: 10.1016/S0960-894X(00)00478-9 |
0.311 |
|
2000 |
Madore E, Lipman RSA, Hou Y, Lapointe J. Evidence for unfolding of the single-stranded GCCA 3'-End of a tRNA on its aminoacyl-tRNA synthetase from a stacked helical to a foldback conformation. Biochemistry. 39: 6791-6798. PMID 10841758 DOI: 10.1021/Bi992477X |
0.371 |
|
1999 |
Lapointe J, Fournier AA, Richard V, Labrie C. Androgens Down-Regulate bcl-2 Protooncogene Expression in ZR-75-1 Human Breast Cancer Cells* * This work was supported by a grant from the Canadian Breast Cancer Research Initiative (to C.L.), scholarships from the Fonds de la Recherche en Santé du Québec (to C.L. and J.L.). Additional financial support was provided by Endorecherche. Endocrinology. 140: 416-421. PMID 28200729 DOI: 10.1210/endo.140.1.6410 |
0.528 |
|
1999 |
Lapointe J, Labrie C. Identification and Cloning of a Novel Androgen-Responsive Gene, Uridine Diphosphoglucose Dehydrogenase, in Human Breast Cancer Cells1. Endocrinology. 140: 4486-4493. PMID 28200594 DOI: 10.1210/endo.140.10.7071 |
0.554 |
|
1999 |
Madore E, Florentz C, Giegé R, Sekine S, Yokoyama S, Lapointe J. Effect of modified nucleotides on Escherichia coli tRNAGlu structure and on its aminoacylation by glutamyl-tRNA synthetase. Predominant and distinct roles of the mnm5 and s2 modifications of U34. European Journal of Biochemistry / Febs. 266: 1128-35. PMID 10583410 DOI: 10.1046/J.1432-1327.1999.00965.X |
0.38 |
|
1999 |
Lapointe J, Labrie C. Identification and cloning of a novel androgen-Responsive gene, uridine diphosphoglucose dehydrogenase, in human breast cancer cells Endocrinology. 140: 4486-4493. PMID 10499502 DOI: 10.1210/Endo.140.10.7071 |
0.623 |
|
1999 |
Madore E, Florentz C, Giegé R, Lapointe J. Magnesium-dependent alternative foldings of active and inactive Escherichia coli tRNA(Glu) revealed by chemical probing. Nucleic Acids Research. 27: 3583-8. PMID 10446250 DOI: 10.1093/Nar/27.17.3583 |
0.32 |
|
1999 |
Pelchat M, Gagnon Y, Laberge S, Lapointe J. Co-transcription of Rhizobium meliloti lysyl-tRNA synthetase and glutamyl-tRNA synthetase genes. Febs Letters. 449: 23-7. PMID 10225420 DOI: 10.1016/S0014-5793(99)00385-3 |
0.353 |
|
1999 |
Pelchat M, Lapointe J. In vivo and in vitro processing of the Bacillus subtilis transcript coding for glutamyl-tRNA synthetase, serine acetyltransferase, and cysteinyl-tRNA synthetase. Rna (New York, N.Y.). 5: 281-9. PMID 10024179 DOI: 10.1017/S1355838299980858 |
0.364 |
|
1999 |
Lapointe J, Fournier A, Richard V, Labrie C. Androgens down-regulate bcl-2 protooncogene expression in ZR-75-1 human breast cancer cells Endocrinology. 140: 416-421. PMID 9886853 DOI: 10.1210/Endo.140.1.6410 |
0.588 |
|
1999 |
Pelchat M, Lapointe J. In vivo and in vitro processing of the Bacillus subtilis transcript coding for glutamyl-tRNA synthetase, serine acetyltransferase, and cysteinyl-tRNA synthetase Biochemistry and Cell Biology. 77: 403. DOI: 10.1139/O99-903Z |
0.319 |
|
1999 |
Pelchat M, Lapointe J. Aminoacyl-tRNA synthetase genes of Bacillus subtilis: organization and regulation. Biochemistry and Cell Biology. 77: 343-347. DOI: 10.1139/O99-040 |
0.329 |
|
1998 |
Pope AJ, Lapointe J, Mensah L, Benson N, Brown MJ, Moore KJ. Characterization of isoleucyl-tRNA synthetase from Staphylococcus aureus. I: Kinetic mechanism of the substrate activation reaction studied by transient and steady-state techniques. The Journal of Biological Chemistry. 273: 31680-90. PMID 9822629 DOI: 10.1074/Jbc.273.48.31680 |
0.302 |
|
1998 |
Champagne N, Lapointe J. Influence of FIS on the transcription from closely spaced and non- overlapping divergent promoters for an aminoacyl-tRNA synthetase gene (gltX) and a tRNA operon (valU) in Escherichia coil Molecular Microbiology. 27: 1141-1156. PMID 9570400 DOI: 10.1046/J.1365-2958.1998.00745.X |
0.325 |
|
1998 |
Pelchat M, Lacoste L, Yang F, Lapointe J. Overproduction of the Bacillus subtilis glutamyl-tRNA synthetase in its host and its toxicity to Escherichia coli. Canadian Journal of Microbiology. 44: 378-381. DOI: 10.1139/W98-014 |
0.369 |
|
1998 |
Desjardins M, Garneau S, Desgagnés J, Lacoste L, Yang F, Lapointe J, Chênevert R. Glutamyl Adenylate Analogues Are Inhibitors of Glutamyl-tRNA Synthetase Bioorganic Chemistry. 26: 1-13. DOI: 10.1006/Bioo.1998.1082 |
0.345 |
|
1996 |
Gagnonl Y, Lacoste L, Champagne N, Lapointe J. Widespread use of the glu-tRNAGln transamidation pathway among bacteria: A member of the α purple bacteria lacks glutaminyl-tRNA synthetase Journal of Biological Chemistry. 271: 14856-14863. PMID 8662929 DOI: 10.1074/Jbc.271.25.14856 |
0.384 |
|
1996 |
Sekine S, Nureki O, Sakamoto K, Niimi T, Tateno M, Go M, Kohno T, Brisson A, Lapointe J, Yokoyama S. Major Identity Determinants in the ''Augmented D Helix'' of tRNA Glu from Escherichia coli Journal of Molecular Biology. 256: 685-700. PMID 8642591 DOI: 10.1006/Jmbi.1996.0118 |
0.323 |
|
1995 |
Liu J, Gagnon Y, Gauthier J, Furenlid L, L'Heureux PJ, Auger M, Nureki O, Yokoyama S, Lapointe J. The zinc-binding site of Escherichia coli glutamyl-tRNA synthetase is located in the acceptor-binding domain: Studies by extended X-ray absorption fine structure, molecular modeling, and site-directed mutagenesis Journal of Biological Chemistry. 270: 15162-15169. PMID 7797500 DOI: 10.1074/Jbc.270.25.15162 |
0.349 |
|
1993 |
Dorion C, Chênevert R, Lacoste L, Lapointe J. Synthesis of an inhibitor of glutamyl-tRNA synthetase Bioorganic and Medicinal Chemistry Letters. 3: 2699-2702. DOI: 10.1016/S0960-894X(01)80745-9 |
0.327 |
|
1992 |
Gendron N, Breton R, Champagne N, Lapointe J. Adenylosuccinate lyase of Bacillus subtilis regulates the activity of the glutamyl-tRNA synthetase. Proceedings of the National Academy of Sciences of the United States of America. 89: 5389-92. PMID 1608947 DOI: 10.1073/Pnas.89.12.5389 |
0.405 |
|
1992 |
Lin S, Brisson A, Liu J, Roy PH, Lapointe J. Higher specific activity of the Escherichia coli glutamylt-RNA synthetase purified to homogeneity by a six-hour procedure Protein Expression and Purification. 3: 71-74. PMID 1384858 DOI: 10.1016/1046-5928(92)90058-5 |
0.319 |
|
1990 |
Brun YV, Sanfaçon H, Breton R, Lapointe J. Closely spaced and divergent promoters for an aminoacyl-tRNA synthetase gene and a tRNA operon in Escherichia coli. Transcriptional and post-transcriptional regulation of gltX, valU and alaW Journal of Molecular Biology. 214: 845-864. PMID 2201777 DOI: 10.1016/0022-2836(90)90340-R |
0.351 |
|
1990 |
Brun YV, Breton R, Lanouette P, Lapointe J. Precise mapping and comparison of two evolutionarily related regions of the Escherichia coli K-12 chromosome. Evolution of valU and lysT from an ancestral tRNA operon Journal of Molecular Biology. 214: 825-843. PMID 2201776 DOI: 10.1016/0022-2836(90)90339-N |
0.34 |
|
1989 |
Brisson A, Brun YV, Bell AW, Roy PH, Lapointe J. Overproduction and domain structure of the glutamyl-tRNA synthetase of Escherichia coli Biochemistry and Cell Biology. 67: 404-410. PMID 2686721 DOI: 10.1139/O89-065 |
0.387 |
|
1989 |
Laberge S, Gagnon Y, Bordeleau LM, Lapointe J. Cloning and sequencing of the gltX gene, encoding the glutamyl-tRNA synthetase of Rhizobium meliloti A2 Journal of Bacteriology. 171: 3926-3932. PMID 2661539 DOI: 10.1128/Jb.171.7.3926-3932.1989 |
0.361 |
|
1989 |
Laberge S, Belair M, Verreault A, Bell AW, Bordeleau LM, Lapointe J. Purification and partial amino acid sequence of a glutamyl-tRNA synthetase from Rhizobium meliloti. Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire. 67: 674-9. PMID 2590524 DOI: 10.1139/O89-101 |
0.382 |
|
1986 |
Lapointe J, Duplain L, Proulx M. A single glutamyl-tRNA synthetase aminoacylates tRNA(Glu) and tRNA(Gln) in Bacillus subtilis and efficiently misacylates Escherichia coli tRNA1(Gln) in vitro Journal of Bacteriology. 165: 88-93. PMID 3079749 DOI: 10.1128/Jb.165.1.88-93.1986 |
0.415 |
|
1986 |
Lapointe J, Levasseur S, Kern D. Glutamyl-tRNA synthetase from Escherichia coli. Methods in Enzymology. 113: 42-9. PMID 3003503 DOI: 10.1016/S0076-6879(85)13009-0 |
0.396 |
|
1986 |
Tremblay TL, Lapointe J. The so-called tRNA1(Glu) of Escherichia coli is a stable denatured conformer of the major isoacceptor tRNA2(Glu) Biochemistry and Cell Biology. 64: 315-322. PMID 2872905 DOI: 10.1139/O86-044 |
0.325 |
|
1983 |
Sanfaçon H, Levasseur S, Roy PH, Lapointe J. Cloning of the gene for Escherichia coli glutamyl-tRNA synthetase Gene. 22: 175-180. PMID 6307818 DOI: 10.1016/0378-1119(83)90101-4 |
0.344 |
|
1982 |
Lapointe J. Study of the evolution of the genetic code by comparing the structural and catalytic properties of the aminoacyl-tRNA synthetases Canadian Journal of Biochemistry. 60: 471-474. PMID 7104823 DOI: 10.1139/O82-055 |
0.341 |
|
1982 |
Lacoste L, Chaudhary KD, Lapointe J. Derepression of the glutamine synthetase in neuroblastoma cells at low concentrations of glutamine Journal of Neurochemistry. 39: 78-85. PMID 6123553 DOI: 10.1111/J.1471-4159.1982.Tb04703.X |
0.327 |
|
1981 |
KERN D, LAPOINTE J. The Catalytic Mechanism of Glutamyl‐tRNA Synthetase of Escherichia coli A Steady‐State Kinetic Investigation European Journal of Biochemistry. 115: 29-38. PMID 7014220 DOI: 10.1111/J.1432-1033.1981.Tb06193.X |
0.352 |
|
1980 |
VADEBONCOEUR C, LAPOINTE J. Slow Diffusion of Glutamate and ATP‐Mg into High‐Molecular‐Weight Complexes Containing the Glutamyl‐tRNA Synthetase from Bovine Brain European Journal of Biochemistry. 109: 581-587. PMID 7408903 DOI: 10.1111/J.1432-1033.1980.Tb04831.X |
0.31 |
|
1980 |
Christian V, Lapointe J. Properties of the cytoplasmic glutamyl-tRNA synthetase in high molecular weight complexes from bovine brain Brain Research. 188: 129-138. PMID 7370748 DOI: 10.1016/0006-8993(80)90562-4 |
0.339 |
|
1980 |
Kern D, Potier S, Lapointe J, Boulanger Y. The glutaminyl-transfer RNA synthetase of Escherichia coli. Purification, structure and function relationship Bba Section Nucleic Acids and Protein Synthesis. 607: 65-80. PMID 6989402 DOI: 10.1016/0005-2787(80)90221-X |
0.398 |
|
1980 |
KERN D, LAPOINTE J. The Catalytic Mechanism of Glutamyl‐tRNA Synthetase of Escherichia coli Evidence for a Two‐step Aminoacylation Pathway, and Study of the Reactivity of the Intermediate Complex European Journal of Biochemistry. 106: 137-150. PMID 6280993 DOI: 10.1111/J.1432-1033.1980.Tb06004.X |
0.3 |
|
1980 |
Kern D, Lapointe J. Catalytic mechanism of glutamyl-tRNA synthetase from Escherichia coli. Reaction pathway in the aminoacylation of tRNAGlu Biochemistry. 19: 3060-3068. PMID 6249345 DOI: 10.1021/Bi00554A035 |
0.345 |
|
1980 |
Kern D, Lapointe J. The twenty aminoacyl-tRNA synthetases from Escherichia coli. General separation procedure, and comparison of the influence of pH and divalent cations on their catalytic activities Biochimie. 61: 1257-1272. PMID 44203 DOI: 10.1016/S0300-9084(80)80285-9 |
0.353 |
|
1979 |
Kern D, Lapointe J. The glutamyl-tRNA synthetase of Escherichia coil: Substrate-induced protection against its thermal inactivation Nucleic Acids Research. 7: 501-515. PMID 386286 DOI: 10.1093/Nar/7.2.501 |
0.34 |
|
1979 |
Kern D, Lapointe J. Glutamyl transfer ribonucleic acid synthetase of escherichia coli. effect of alteration of the 5-(methylaminomethyl)-2-thiouridine in the anticodon of glutamic acid transfer ribonucleic acid on the catalytic mechanism Biochemistry. 18: 5819-5826. PMID 229902 DOI: 10.1021/Bi00593A011 |
0.347 |
|
1979 |
Kern D, Lapointe J. Glutamyl transfer ribonucleic acid synthetase of escherichia coll. Study of the interactions with its substrates Biochemistry. 18: 5809-5818. PMID 229901 DOI: 10.1021/Bi00593A010 |
0.389 |
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1975 |
Lapointe J, Delcuve G. Thermosensitive mutants of Escherichia coli K 12 altered in the catalytic subunit and in a regulatory factor of the glutamyl transfer ribonucleic acid synthetase Journal of Bacteriology. 122: 352-358. PMID 1092645 DOI: 10.1128/Jb.122.2.352-358.1975 |
0.328 |
|
1975 |
Lapointe J, Delcuve G, Duplain L. Derepressed levels of glutamate synthase and glutamine synthetase in Escherichia coli mutants altered in glutamyl transfer ribonucleic acid synthetase Journal of Bacteriology. 123: 843-850. PMID 239924 DOI: 10.1128/Jb.123.3.843-850.1975 |
0.343 |
|
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