G
Gloria Reyes
Researcher at University of California, San Diego
Publications - 7
Citations - 460
Gloria Reyes is an academic researcher from University of California, San Diego. The author has contributed to research in topics: Phosphorylation & Kinase. The author has an hindex of 7, co-authored 7 publications receiving 420 citations. Previous affiliations of Gloria Reyes include Max F. Perutz Laboratories.
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Journal ArticleDOI
A Mek1-Mek2 heterodimer determines the strength and duration of the Erk signal.
Federica Catalanotti,Gloria Reyes,Gloria Reyes,Veronika Jesenberger,Gergana Galabova-Kovacs,Ricardo De Matos Simoes,Oliviero Carugo,Manuela Baccarini +7 more
TL;DR: The role of Mek1 and Mek2 in growth factor–induced Erk phosphorylation is not interchangeable, and Mek1 is established as the crucial modulator of Mek and Erk signaling.
Journal ArticleDOI
MEK1 is required for PTEN membrane recruitment, AKT regulation, and the maintenance of peripheral tolerance.
Katarina Zmajkovicova,Veronika Jesenberger,Federica Catalanotti,Christian Baumgartner,Gloria Reyes,Manuela Baccarini +5 more
TL;DR: This work identifies MEK1 as an essential regulator of lipid/protein phosphatase PTEN, through which it controls phosphatidylinositol-3-phosphate accumulation and AKT signaling and offers a conceptual framework for the observation that activation of the PI3K pathway frequently mediate resistance to MEK inhibitors and for the promising results obtained by combined MEK/PI3K inhibition in preclinical cancer models.
Journal ArticleDOI
Essential role of B-Raf in oligodendrocyte maturation and myelination during postnatal central nervous system development
Gergana Galabova-Kovacs,Federica Catalanotti,Dana Matzen,Gloria Reyes,Jürgen Zezula,Ruth Herbst,Alcino Silva,Ingrid Walter,Manuela Baccarini +8 more
TL;DR: In this paper, B-Raf is shown to be a rate-limiting MEK/ERK activator in oligodendrocyte differentiation and myelination.
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Active site inhibitors protect protein kinase C from dephosphorylation and stabilize its mature form
Christine M. Gould,Corina E. Antal,Gloria Reyes,Maya T. Kunkel,Ryan A. Adams,Ahdad Ziyar,Tania Riveros,Alexandra C. Newton +7 more
TL;DR: Using homogeneously pure PKC, it is shown that the active site inhibitor Gö 6983 prevents the dephosphorylation by pure protein phosphatase 1 (PP1) or the hydrophobic motifosphatase, pleckstrin homology domain leucine-rich repeat protein phosph atase (PHLPP).
Journal ArticleDOI
Common Polymorphism in the Phosphatase PHLPP2 Results in Reduced Regulation of Akt and Protein Kinase C
TL;DR: A functional polymorphism is identified that impairs the activity of PHLPP2 and correlates with elevated Akt phosphorylation and increased PKC levels and results in reduced apoptosis.