Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Sylvain Lanouette"'
Publikováno v:
Molecular Systems Biology, Vol 10, Iss 4, Pp 1-26 (2014)
Abstract Large‐scale characterization of post‐translational modifications (PTMs), such as phosphorylation, acetylation and ubiquitination, has highlighted their importance in the regulation of a myriad of signaling events. While high‐throughput
Externí odkaz:
https://doaj.org/article/3bde2bd8de554055bd9f038d74c6e7d8
Autor:
PETER V DICPINIGAITIS, LORCAN MCGARVEY, JACLYN A SMITH, MICHAEL BLAISS, VIVEK N IYER, SYLVAIN LANOUETTE, RONGHUA YANG, MARGARET GARIN, CATHERINE M BONUCCELLI
Publikováno v:
Chest. 162:A2487-A2488
Autor:
Laurent Harvey, Mandel Sher, James H. Hull, Sylvain Lanouette, Surinder S. Birring, Catherine M. Bonuccelli, Alyn H. Morice, Alan B. Goldsobel, Jaclyn A. Smith, Ella Li
Publikováno v:
Airway pharmacology and treatment.
Autor:
Sylvain Lanouette, James A. Davey, Fred Elisma, Daniel Figeys, Zhibin Ning, Roberto A. Chica, Jean-François Couture
Publikováno v:
Structure. 23:206-215
SummaryCharacterization of lysine methylation has proven challenging despite its importance in biological processes such as gene transcription, protein turnover, and cytoskeletal organization. In contrast to other key posttranslational modifications,
Autor:
Daniel Figeys, Sylvain Lanouette, Jean-François Couture, Janice Mayne, Zhibin Ning, Anna S. Mierzwa, Alexandra Therese Star
Publikováno v:
Chemical communications (Cambridge, England). 52(31)
Methylation of arginine and lysine (RK) residues play essential roles in epigenetics and the regulation of gene expression. However, research in this area is often hindered by the lack of effective tools for probing the protein methylation. Here, we
Since its initial discovery by Allfrey and colleagues, methylation of histone proteins on lysine residues has emerged as an important posttranslational modification controlling a myriad of nuclear events, such as DNA damage repair, transcription, and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::84d54dad74fb53423044936e6af5416d
https://doi.org/10.1016/b978-0-12-802389-1.00002-2
https://doi.org/10.1016/b978-0-12-802389-1.00002-2
Autor:
Kim Barroso, Olivier Binda, Maria Victoria Botuyan, Anna L. Chambers, Eric Chevet, Jocelyn Côté, Florence Couteau, Jean-François Couture, Jessica A. Downs, Joel C. Eissenberg, Maite G. Fernandez-Barrena, Martin Ernesto Fernandez-Zapico, Raquel Fueyo, María Alejandra García, Alexandre Gaspar-Maia, John Haddad, Nasim Haghandish, Elisabeth Hessmann, Jonathan M.G. Higgins, Ryan A. Hlady, Timothy C. Humphrey, Steven A. Johnsen, Alexander Koenig, María Julia Lamberti, Sylvain Lanouette, Andrew Liss, Gwen A. Lomberk, Frédérick A. Mallette, Sridhar Mani, Marian A. Martínez-Balbás, Georges Mer, Emma A. Morrison, Catherine A. Musselman, Sankari Nagarajan, Christopher L. Pin, Keith D. Robertson, Andrea Ropolo, María Roqué, Natalia Belén Rumie Vittar, Güenter Schneider, Ana Sevilla, Steven G. Smith, Maria Carolina Touz, Raul Urrutia, Laura Vargas-Roig, Renzo Emanuel Vera, Nikolaus A. Watson, Xiang-Jiao Yang, Pamela Zhang, Ming-Ming Zhou
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6266738ca1055879469c712948b274e6
https://doi.org/10.1016/b978-0-12-802389-1.01002-9
https://doi.org/10.1016/b978-0-12-802389-1.01002-9
Autor:
Daniel Figeys, Jean-François Couture, Véronique Tremblay, Fred Elisma, Jeffery Butson, Sylvain Lanouette, Mohamed Abu-Farha
Publikováno v:
Journal of Molecular Cell Biology. 3:301-308
The SMYD (SET and MYND domain) family of lysine methyltransferases (KMTs) plays pivotal roles in various cellular processes, including gene expression regulation and DNA damage response. Initially identified as genuine histone methyltransferases, spe
Autor:
Jean-François Couture, Sylvain Lanouette, Adam F. Groulx, Pamela Zhang, Joseph S. Brunzelle, Véronique Tremblay, Vanja Avdic
Publikováno v:
Structure. 19(1):101-108
SummaryHistone H3 Lys-4 methylation is predominantly catalyzed by a family of methyltransferases whose enzymatic activity depends on their interaction with a three-subunit complex composed of WDR5, RbBP5, and Ash2L. Here, we report that a segment of
Fine‐tuning the stimulation of MLL1 methyltransferase activity by a histone H3‐based peptide mimetic
Autor:
Sylvain Lanouette, Vanja Avdic, Pamela Zhang, Anastassia Voronova, Jean-François Couture, Ilona S. Skerjanc
Publikováno v:
The FASEB Journal. 25:960-967
The SET1 family of methyltransferases carries out the bulk of histone H3 Lys-4 methylation in vivo. One of the common features of this family is the regulation of their methyltransferase activity by a tripartite complex composed of WDR5, RbBP5, and A