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Close inspection of our SNIP1-P-SF3B1 interaction model also indicates that E366 is in close proximity to the binding interface and its mutation to glycine (E366G) induces most likely local conformational changes in the FHA domain leading to suboptimal P-SF3B1 binding (Fig

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EGCG post-treatment significantly rescued 1-methyl-4-phenyl-1,2,3,6-tetrahydropyridine (MPTP)-induced neurotoxicity by increasing the rotational latency and increasing dopamine [178181]

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