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Ana M. Mata
Researcher at University of Extremadura
Publications - 74
Citations - 1820
Ana M. Mata is an academic researcher from University of Extremadura. The author has contributed to research in topics: Endoplasmic reticulum & Plasma membrane Ca2+ ATPase. The author has an hindex of 24, co-authored 66 publications receiving 1652 citations. Previous affiliations of Ana M. Mata include Spanish National Research Council & University of Southampton.
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Journal ArticleDOI
Distribution of two distinct Ca2+-ATPase-like proteins and their relationships to the agonist-sensitive calcium store in adrenal chromaffin cells.
Robert D. Burgoyne,Timothy R. Cheek,Alan Morgan,Antony J. O'Sullivan,Roger B. Moreton,Michael J. Berridge,Ana M. Mata,John Colyer,Anthony G. Lee,J. Malcolm East +9 more
TL;DR: It is shown that bovine adrenal chromaffin cells contain two calcium stores with distinct Ca2+-ATPase-like proteins with distinct subcellular distributions and that the organelle with the 100K Ca2-atPase is not the Ins(l,4,5)P3-sensitive store.
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Glycogen synthase kinase-3 plays a crucial role in tau exon 10 splicing and intranuclear distribution of SC35. Implications for Alzheimer's disease.
TL;DR: It is demonstrated that GSK-3 plays a crucial role in tau exon 10 splicing, raising the possibility that Gsk3 could contribute to tauopathies via aberrant tau splicing.
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Reversible inactivation of Saccharomyces cerevisiae glutathione reductase under reducing conditions
TL;DR: The enzyme was protected against redox inactivation by low concentrations of GSSG, ferricyanide, GSH, or dithiothreitol, and high concentrations of NAD(P)+; oxidized glutathione effectively protected the enzyme at concentrations even lower than GSH.
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The plasma membrane Ca2+-ATPase isoform 4 is localized in lipid rafts of cerebellum synaptic plasma membranes.
TL;DR: By providing an ordered membrane microenvironment, lipid rafts may contribute to the interaction of PMCA4 with proteins involved in Ca2+ signaling at discrete functional positions on the synaptic nerve terminals.
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Ca2+ Transport by Reconstituted Synaptosomal ATPase Is Associated with H+ Countertransport and Net Charge Displacement
TL;DR: Calmodulin stimulated ATPase activity, Ca2+ uptake, and H+ ejection, demonstrating that these parameters are linked by the same mechanism of PMCA regulation.