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Natalia Filippova

Researcher at University of Alabama at Birmingham

Publications -  20
Citations -  718

Natalia Filippova is an academic researcher from University of Alabama at Birmingham. The author has contributed to research in topics: Glioma & RNA-binding protein. The author has an hindex of 12, co-authored 17 publications receiving 610 citations. Previous affiliations of Natalia Filippova include French Institute of Health and Medical Research & University of Alabama.

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The rna-binding protein hur promotes glioma growth and treatment resistance

TL;DR: Findings reveal a HuR-dependent mechanism for cancer cell survival and sensitivity to chemotherapeutic drugs suggesting that HuR should be considered as a new therapeutic target.
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Calcium‐dependent inactivation of heteromeric NMDA receptor‐channels expressed in human embryonic kidney cells.

TL;DR: Results show that both NR1‐NR2A and NR1-NR2B recombinant NMDA receptor‐channels expressed in HEK 293 cells can be transiently inhibited by Ca2+ ions in a similar way to that described for hippocampal neurones.
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Kainate-induced inactivation of NMDA currents via an elevation of intracellular Ca2+ in hippocampal neurons.

TL;DR: It is suggested that in the hippocampal neurons kainate produces in activation of NMDA currents via an elevation of [Ca2+]i, and Cadmium, a blocker of voltage-gated channels, prevented development of the depolarization-induced inactivation ofNMDA currents.
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Amyotrophic Lateral Sclerosis-linked Mutant SOD1 Sequesters Hu Antigen R (HuR) and TIA-1-related Protein (TIAR) IMPLICATIONS FOR IMPAIRED POST-TRANSCRIPTIONAL REGULATION OF VASCULAR ENDOTHELIAL GROWTH FACTOR

TL;DR: The findings indicate that mutant SOD1 impairs post-transcriptional regulation by sequestering key regulatory RNA-binding proteins in cells, and the rescue effect of HuR suggests that this impairment, whether related to VEGF or other potential mRNA targets, contributes to cytotoxicity in ALS.
Journal Article

Regulation of recombinant gamma-aminobutyric acid (GABA)(A) and GABA(C) receptors by protein kinase C.

TL;DR: Data suggest internalized receptors can exist in an intracellular compartment that can be delivered back to the plasma membrane, and PKC may play a key role in the regulation of GABA-mediated inhibition.