Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Consuelo Marín-Vicente"'
Autor:
Emilio M. Serrano-López, Teresa Coronado-Parra, Consuelo Marín-Vicente, Zoltan Szallasi, Victoria Gómez-Abellán, María José López-Andreo, Marcos Gragera, Juan C. Gómez-Fernández, Rubén López-Nicolás, Senena Corbalán-García
Publikováno v:
International Journal of Molecular Sciences, Vol 23, Iss 22, p 14023 (2022)
Protein kinase C (PKC) comprises a family of highly related serine/threonine protein kinases involved in multiple signaling pathways, which control cell proliferation, survival, and differentiation. The role of PKCα in cancer has been studied for ma
Externí odkaz:
https://doaj.org/article/15c72ba2bbc944ce927569469619fa53
Autor:
Consuelo Marín-Vicente, Vivian de los Ríos, Ma Jesús Fernández-Aceñero, J. Ignacio Casal, Marta Mendes
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
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10 p.-5 fig.
PURPOSE:Successful prevention of colorectal cancer (CRC) would benefit from a rapid serum screening for early detection. Here, a novel strategy for CRC biomarker discovery and validation exclusively based on MS procedures is reporte
PURPOSE:Successful prevention of colorectal cancer (CRC) would benefit from a rapid serum screening for early detection. Here, a novel strategy for CRC biomarker discovery and validation exclusively based on MS procedures is reporte
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::abdd62be9452d2e190f280e8415ea03c
https://doi.org/10.1002/prca.201900052
https://doi.org/10.1002/prca.201900052
Autor:
Consuelo Marín-Vicente, Francisco E. Nicolás, Senena Corbalán-García, Juan C. Gómez-Fernández
Publikováno v:
Journal of Molecular Biology. 377:1038-1052
Rapamycin-triggered heterodimerization strategy is becoming an excellent tool for rapidly modifying phosphatidylinositol(4,5)-bisphosphate [PtdIns(4,5)P2] levels at the plasma membrane and for studying their influence in different processes. In this
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::097a00ab34c4b9f03969dd310036eb38
https://doi.org/10.1016/j.jmb.2007.12.011
https://doi.org/10.1016/j.jmb.2007.12.011
Autor:
Juan C. Gómez-Fernández, Senena Corbalán-García, Marta Guerrero-Valero, Consuelo Marín-Vicente
Publikováno v:
Journal of Molecular Biology. 371:608-621
C2 domains are conserved protein modules in many eukaryotic signaling proteins, including the protein kinase (PKCs). The C2 domains of classical PKCs bind to membranes in a Ca(2+)-dependent manner and thereby act as cellular Ca(2+) effectors. Recent
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ccab7d98ec867251c8d4762a9a1b1ab8
https://doi.org/10.1016/j.jmb.2007.05.086
https://doi.org/10.1016/j.jmb.2007.05.086
Autor:
Senena Corbalán-García, M. José López-Andreo, Consuelo Marín-Vicente, Rubén López-Nicolás, Juan C. Gómez-Fernández
Publikováno v:
Journal of Molecular Biology. 357:1105-1120
Arachidonic acid, one of the major unsaturated fatty acids released during cell stimulation, participates in the signaling necessary for activation of different enzymes, including protein kinase C (PKC). Here, we demonstrate that arachidonic acid is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce8c88653e3572f7240f01402fa0eff4
https://doi.org/10.1016/j.jmb.2006.01.018
https://doi.org/10.1016/j.jmb.2006.01.018
Autor:
Núria Verdaguer, Consuelo Marín-Vicente, Cristina Ferrer-Orta, Jordi Querol-Audí, Senena Corbalán-García, Ignacio Fita, Marta Guerrero-Valero, Juan C. Gómez-Fernández
Publikováno v:
The FASEB Journal. 23
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::56a9d1056b87eeedb5648737ef5a5465
https://doi.org/10.1096/fasebj.23.1_supplement.520.5
https://doi.org/10.1096/fasebj.23.1_supplement.520.5
Autor:
Cristina Ferrer-Orta, Juan C. Gómez-Fernández, Ignacio Fita, Núria Verdaguer, Consuelo Marín-Vicente, Jordi Querol-Audí, Marta Guerrero-Valero, Senena Corbalán-García
Publikováno v:
Digital.CSIC. Repositorio Institucional del CSIC
instname
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C2 domains are widely-spread protein signaling motifs that in classical PKCs act as Ca2+-binding modules. However, the molecular mechanisms of their targeting process at the plasma membrane remain poorly understood. Here, the crystal structure of PKC
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a5051d89050bd6413995802fb7753462
http://hdl.handle.net/10261/110200
http://hdl.handle.net/10261/110200
Autor:
Juan C. Gómez-Fernández, Senena Corbalán-García, Marta Guerrero-Valero, Consuelo Marín-Vicente
Publikováno v:
Biochemical Society transactions. 35(Pt 5)
The C2 domains of cPKCs [classical/conventional PKCs (protein kinase Cs)] bind to membranes in a Ca 2+ -dependent manner and thereby act as cellular Ca 2+ effectors. Recent findings have demonstrated that the C2 domain of cPKCs interacts specifically
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::965acdadd76bcd04a7a663a4d22b5e5b
https://pubmed.ncbi.nlm.nih.gov/17956275
https://pubmed.ncbi.nlm.nih.gov/17956275
Autor:
Senena Corbalán-García, Juan C. Gómez-Fernández, Consuelo Marín-Vicente, Sonia Sánchez-Bautista
Publikováno v:
Journal of molecular biology. 362(5)
The C2 domain is a targeting domain that responds to intracellular Ca 2+ signals in classical protein kinases (PKCs) and mediates the translocation of its host protein to membranes. Recent studies have revealed a new motif in the C2 domain, named the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::02fb09c7db5903b813986fd4c25d0ca0
https://pubmed.ncbi.nlm.nih.gov/16949603
https://pubmed.ncbi.nlm.nih.gov/16949603
Publikováno v:
Molecular biology of the cell. 16(6)
Signal transduction through protein kinase Cs (PKCs) strongly depends on their subcellular localization. Here, we investigate the molecular determinants of PKCα localization by using a model system of neural growth factor (NGF)-differentiated pheoch
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::85f9c9258ff3b52e91f5912a04baafa8
https://pubmed.ncbi.nlm.nih.gov/15814842
https://pubmed.ncbi.nlm.nih.gov/15814842