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Maxence V. Nachury

Researcher at University of California, San Francisco

Publications -  72
Citations -  9983

Maxence V. Nachury is an academic researcher from University of California, San Francisco. The author has contributed to research in topics: Cilium & BBSome. The author has an hindex of 39, co-authored 68 publications receiving 8455 citations. Previous affiliations of Maxence V. Nachury include Stanford University & University of California, Berkeley.

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A Core Complex of BBS Proteins Cooperates with the GTPase Rab8 to Promote Ciliary Membrane Biogenesis

TL;DR: The data reveal that BBS may be caused by defects in vesicular transport to the cilium, and a complex composed of seven highly conserved BBS proteins is identified, the BBSome, which localizes to nonmembranous centriolar satellites in the cytoplasm but also to the membrane of the cILium.
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The Conserved Bardet-Biedl Syndrome Proteins Assemble a Coat that Traffics Membrane Proteins to Cilia

TL;DR: The BBSome constitutes a coat complex that sorts membrane proteins to primary cilia and it is proposed that trafficking of BBSome cargoes to cilia entails the coupling ofBBSome coat polymerization to the recognition of sorting signals by the BBSome.
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A Septin Diffusion Barrier at the Base of the Primary Cilium Maintains Ciliary Membrane Protein Distribution

TL;DR: Septin 2 (SEPT2), a member of the septin family of guanosine triphosphatases that form a diffusion barrier in budding yeast, localized at the base of the ciliary membrane and is essential for retaining receptor-signaling pathways in the primary cilium.
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Trafficking to the Ciliary Membrane: How to Get Across the Periciliary Diffusion Barrier?

TL;DR: The stage is now set to dissect the interplay between signaling and regulated trafficking to and from cilia.
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The major α-tubulin K40 acetyltransferase αTAT1 promotes rapid ciliogenesis and efficient mechanosensation

TL;DR: It is concluded that αTAT1 is the major and possibly the sole α-tubulin K40 acetyltransferase in mammals and nematodes, and that tubulin acetylation plays a conserved role in several microtubule-based processes.