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Shivaji Rikka

Researcher at University of Montana

Publications -  7
Citations -  1138

Shivaji Rikka is an academic researcher from University of Montana. The author has contributed to research in topics: Mitochondrion & Mitochondrial permeability transition pore. The author has an hindex of 6, co-authored 7 publications receiving 953 citations. Previous affiliations of Shivaji Rikka include University of Missouri.

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Microtubule-associated Protein 1 Light Chain 3 (LC3) Interacts with Bnip3 Protein to Selectively Remove Endoplasmic Reticulum and Mitochondria via Autophagy

TL;DR: The data indicate that Bnip3 regulates the apoptotic balance as an autophagy receptor that induces removal of both mitochondria and ER and that this process significantly reduced both mitophagy and ERphagy.
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Bnip3 impairs mitochondrial bioenergetics and stimulates mitochondrial turnover.

TL;DR: Bnip3-mediated impairment of mitochondrial respiration induces mitochondrial turnover by activating mitochondrial autophagy, and it is found that this effect caused an increase in mitochondrial protease activity, suggesting that Bnip 3 might promote degradation of proteins in the mitochondria.
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Juvenile Exposure to Anthracyclines Impairs Cardiac Progenitor Cell Function and Vascularization Resulting in Greater Susceptibility to Stress-Induced Myocardial Injury in Adult Mice

TL;DR: The data suggest that anthracycline treatment impairs vascular development as well as progenitor cell function in the young heart, resulting in an adult heart that is more susceptible to stress.
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Bnip3 mediates permeabilization of mitochondria and release of cytochrome c via a novel mechanism.

TL;DR: Bnip3 induced mitochondrial matrix remodeling and large amplitude swelling of the inner membrane, which led to disassembly of OPA1 complexes and release from the mitochondria, suggesting that Bh3 mediates mitochondrial permeabilization by a novel mechanism that is different from other BH3-only proteins.
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P2Y2 nucleotide receptors mediate metalloprotease-dependent phosphorylation of epidermal growth factor receptor and ErbB3 in human salivary gland cells.

TL;DR: It is demonstrated that in human salivary gland (HSG) cells, activation of the P2Y2R by its agonist induces phosphorylation of ERK1/2 via two distinct mechanisms, a rapid, protein kinase C-dependent pathway and a slower and prolonged, epidermal growth factor receptor (EGFR)-dependent pathway.