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Metodi V. Metodiev

Researcher at University of Essex

Publications -  56
Citations -  1697

Metodi V. Metodiev is an academic researcher from University of Essex. The author has contributed to research in topics: Cancer & Breast cancer. The author has an hindex of 21, co-authored 56 publications receiving 1434 citations. Previous affiliations of Metodi V. Metodiev include Bulgarian Academy of Sciences & University of Illinois at Chicago.

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Genomic modelling of the ESR1 Y537S mutation for evaluating function and new therapeutic approaches for metastatic breast cancer

TL;DR: The functional importance of ER mutations in endocrine resistance, the utility of knock-in mutational models for investigating alternative therapeutic approaches and CDK7 inhibition as a potential therapy for endocrine-resistant breast cancer mediated by ER mutations are confirmed.
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Pheromone-induced polarization is dependent on the Fus3p MAPK acting through the formin Bni1p

TL;DR: A model wherein activated Fus3p is recruited back to the cortex, where it activates Bni1p to promote polarization and cell fusion is suggested.
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Regulation of MAPK function by direct interaction with the mating-specific Gα in yeast

TL;DR: This work has found that Gα binds directly to the mating-specific MAPK in yeast cells responding to pheromone, and it demonstrates direct communication between the top and bottom of a Gα-MAPK pathway.
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Stat1 and CD74 overexpression is co-dependent and linked to increased invasion and lymph node metastasis in triple-negative breast cancer.

TL;DR: The results show that Stat1/CD74 positive triple-negative tumors are more aggressive and suggest an approach for development of better diagnostics and more targeted therapies for triple negative breast cancer.
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Thioredoxin-mediated reversible dissociation of a stromal multiprotein complex in response to changes in light availability

TL;DR: It is shown here that both PRK and GAPDH are present in the reduced form in leaves in the dark, but are inactive, demonstrating the role of the PRK/GAPDH/CP12 complex in deactivating these enzymes in response to reductions in light intensity.