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- W2328487810 startingPage "334" @default.
- W2328487810 abstract "An increasing number of Rab GTPases associated with partial dysfunction has been linked to several human diseases characterized by a diminution in vesicle transport. Due to its direct implication in human disorders, the Rab27 subfamily is considered as a standard for vesicle docking studies. By which mechanism Rab27 effectors distinguish among the pool of Rab GTPases? What is the underneath machinery rendering the interaction of eleven distinct effectors specific of Rab27 when compared to other Rabs of the secretory pathway? By solving the X-ray structures of Rab27, both in its inactive form and active form bound to the effector protein Slp2-a, attempts have been given to unravel the molecular basis of regulation of the delivering process of vesicles to fusion by the Rab27 subfamily." @default.
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- W2328487810 date "2009-01-01" @default.
- W2328487810 modified "2023-10-01" @default.
- W2328487810 title "Structural Insights into Rab27 Recruitment by its Effectors" @default.
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- W2328487810 doi "https://doi.org/10.5940/jcrsj.51.334" @default.
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