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Sebastien Lavoie, Ph.D. - Publications

Affiliations: 
2003 Universite Laval (Canada) 
Area:
Molecular Biology
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6 high-probability publications. We are testing a new system for linking publications to authors. You can help! If you notice any inaccuracies, please sign in and mark papers as correct or incorrect matches. If you identify any major omissions or other inaccuracies in the publication list, please let us know.

Year Citation  Score
2008 Michaud S, Lavoie S, Guimond MO, Tanguay RM. The nuclear localization of Drosophila Hsp27 is dependent on a monopartite arginine-rich NLS and is uncoupled from its association to nuclear speckles. Biochimica Et Biophysica Acta. 1783: 1200-10. PMID 18339325 DOI: 10.1016/J.Bbamcr.2008.01.031  0.309
2005 Proteau A, Blier S, Albert AL, Lavoie SB, Traish AM, Vincent M. The multifunctional nuclear protein p54nrb is multiphosphorylated in mitosis and interacts with the mitotic regulator Pin1. Journal of Molecular Biology. 346: 1163-72. PMID 15701524 DOI: 10.1016/J.Jmb.2004.12.034  0.508
2004 Albert AL, Lavoie SB, Vincent M. Multisite phosphorylation of Pin1-associated mitotic phosphoproteins revealed by monoclonal antibodies MPM-2 and CC-3. Bmc Cell Biology. 5: 22. PMID 15171797 DOI: 10.1186/1471-2121-5-22  0.334
2001 Lavoie SB, Albert AL, Handa H, Vincent M, Bensaude O. The peptidyl-prolyl isomerase Pin1 interacts with hSpt5 phosphorylated by Cdk9. Journal of Molecular Biology. 312: 675-85. PMID 11575923 DOI: 10.1006/Jmbi.2001.4991  0.451
1999 Lavoie S, Albert A, Vincent M. Heat-shock-induced variations in phosphorylation levels of the RNA polymerase II largest subunit may regulate its interaction with the peptidyl-prolyl-isomerase Pin1 Biochemistry and Cell Biology. 77: 401. DOI: 10.1139/O99-903V  0.522
1996 Vincent M, Lauriault P, Dubois MF, Lavoie S, Bensaude O, Chabot B. The nuclear matrix protein p255 is a highly phosphorylated form of RNA polymerase II largest subunit which associates with spliceosomes. Nucleic Acids Research. 24: 4649-52. PMID 8972849 DOI: 10.1093/Nar/24.23.4649  0.42
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