Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Zoila M. Estrada-Tobar"'
Autor:
Peter Bartels, Ian Salveson, Andrea M. Coleman, David E. Anderson, Grace Jeng, Zoila M. Estrada-Tobar, Kwun Nok Mimi Man, Qinhong Yu, Elza Kuzmenkina, Madeline Nieves-Cintron, Manuel F. Navedo, Mary C. Horne, Johannes W. Hell, James B. Ames
Publikováno v:
The Journal of biological chemistry, vol 298, iss 12
The L-type Ca2+ channel CaV1.2 controls gene expression, cardiac contraction, and neuronal activity. Calmodulin (CaM) governs CaV1.2 open probability (Po) and Ca2+-dependent inactivation (CDI) but the mechanisms remain unclear. Here, we present elect
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f051a5dc802d62dbb779f0a8225b2a42
https://escholarship.org/uc/item/06t096dz
https://escholarship.org/uc/item/06t096dz
Autor:
Peter, Bartels, Ian, Salveson, Andrea M, Coleman, David E, Anderson, Grace, Jeng, Zoila M, Estrada-Tobar, Kwun Nok, Mimi Man, Qinhong, Yu, Elza, Kuzmenkina, Madeline, Nieves-Cintron, Manuel F, Navedo, Mary C, Horne, Johannes W, Hell, James B, Ames
Publikováno v:
The Journal of biological chemistry.
The L-type Ca
Autor:
Peter Bartels, Ian Salveson, Andrea M. Coleman, David E. Anderson, Grace Jeng, Zoila M. Estrada-Tobar, Kwun Nok Mimi Man, Qinhong Yu, Elza Kuzmenkina, Madeline Nieves-Cintron, Manuel F. Navedo, Mary C. Horne, Johannes W. Hell, James B. Ames
The L-type Ca2+ channel CaV1.2 controls gene expression, cardiac contraction, and neuronal activity. Calmodulin (CaM) governs CaV1.2 open probability (Po) and Ca2+-dependent inactivation (CDI) but the mechanisms remain unclear. We identified a half C
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::47b3129855c74710ca7ee907bee1418c
https://doi.org/10.1101/2022.06.24.497440
https://doi.org/10.1101/2022.06.24.497440
Autor:
Mariel Mendoza, Juan A. Leal, Paul S. Nerenberg, Zoila M. Estrada-Tobar, Frederick Wade, Alexander Meza, Cecilia Zurita-Lopez, Aron Judd P. Mendiola
Publikováno v:
Archives of biochemistry and biophysics. 698
The effects of phosphorylation of histone H3 at serine 10 have been studied in the context of other posttranslational modifications such as lysine methylation. We set out to investigate the impact of phosphoserine-10 on arginine-8 methylation. We per
Publikováno v:
The FASEB Journal. 32