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Marta Vieira

Researcher at National Institutes of Health

Publications -  23
Citations -  866

Marta Vieira is an academic researcher from National Institutes of Health. The author has contributed to research in topics: NMDA receptor & Transthyretin. The author has an hindex of 12, co-authored 23 publications receiving 625 citations. Previous affiliations of Marta Vieira include University of Coimbra & Instituto de Biologia Molecular e Celular.

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Streptococcus agalactiae GAPDH Is a Virulence-Associated Immunomodulatory Protein

TL;DR: The results suggest that IL-10 production, which was detected at higher concentrations in the serum of rGAPDH-treated mice, is important in determining the successfulness of the host colonization by S. agalactiae and they highlight the direct role of GAPDH in this process.
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Transthyretin: a multifaceted protein.

TL;DR: The aim of this review is to stress the relevance of TTR, besides its well-known role on transport of thyroxine and retinol-binding protein, in the nervous system, as well as in ischemia and Alzheimer’s disease.
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Ischemic insults induce necroptotic cell death in hippocampal neurons through the up-regulation of endogenous RIP3.

TL;DR: The results highlight that cerebral ischemia activates transcriptional changes that lead to an increase in the endogenous RIP3 protein level which might contribute to the formation of the necrosome complex and to the subsequent component of necroptotic neuronal death that follows ischemic injury.
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The CaMKII/NMDA receptor complex controls hippocampal synaptic transmission by kinase-dependent and independent mechanisms.

TL;DR: Using a series of molecular replacement experiments, the authors show that the kinase function of CaMKII is required for long-term plasticity and basal AMPA receptor-mediated transmission.
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Regulation of NMDA glutamate receptor functions by the GluN2 subunits.

TL;DR: Recent progress made towards understanding the molecular mechanisms that regulate the trafficking of GluN2‐containing N MDARs are reviewed, focusing on the roles of several key synaptic proteins that interact with NMDARs via their carboxyl termini.