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Additionally, tyrosines play an important role in aSyn-vesicle binding while nitration impairs this interaction (making the charge more negative at the N-terminal domain, or causing a conformational change when the C-terminal domain is nitrated) thereby increasing the amount of aSyn in a random coil or beta-sheet conformation and thus shifting equilibrium toward oligomer formation 105,106,109

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Collectively, HDL has multiple biological mechanisms that inhibit thrombus formation, and thus, contribute to HDLs anti-atherogenic properties

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