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Michael Forte

Researcher at Oregon Health & Science University

Publications -  152
Citations -  12979

Michael Forte is an academic researcher from Oregon Health & Science University. The author has contributed to research in topics: Mitochondrial permeability transition pore & Voltage-dependent anion channel. The author has an hindex of 57, co-authored 135 publications receiving 12215 citations. Previous affiliations of Michael Forte include University of Connecticut & University of Maryland, College Park.

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Dimers of mitochondrial ATP synthase form the permeability transition pore

TL;DR: It is shown that CyPD binds the oligomycin sensitivity-conferring protein subunit of the enzyme at the same site as the ATP synthase inhibitor benzodiazepine 423 (Bz-423), which sensitizes the PTP to Ca2+.
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Properties of the Permeability Transition Pore in Mitochondria Devoid of Cyclophilin D

TL;DR: The experiments demonstrate that the PTP can form and open, that CyP-D represents the target for PTP inhibition by CsA, and that Cyp-D modulates the sensitivity of the P TP to Ca2+ but not its regulation by the proton electrochemical gradient, adenine nucleotides, and oxidative stress.
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The mitochondrial permeability transition from in vitro artifact to disease target

TL;DR: Evidence indicating that the permeability transition pore plays a role in pathophysiology, with specific emphasis on in vivo models of disease is discussed, including results based on genetic inactivation of putative permeability Transition pore components.
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Associative learning disrupted by impaired Gs signaling in Drosophila mushroom bodies

TL;DR: Olfactory learning depends on regulated Gs signaling in Drosophila MBs, and the ability to associate odors with electroshock was abolished when Gαs* was targeted to MB, but not CC, structures, whereas sensorimotor responses to these stimuli remained normal.
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The Mitochondrial Permeability Transition Pore: Channel Formation by F-ATP Synthase, Integration in Signal Transduction, and Role in Pathophysiology

TL;DR: Structural and functional features of F-ATP synthases are discussed that may provide clues to its transition from an energy-conserving into anEnergy-dissipating device as well as recent advances on signal transduction to the PTP and on its role in cellular pathophysiology.