LRRK2 phosphorylates pre-synaptic N-ethylmaleimide sensitive fusion (NSF) protein enhancing its ATPase activity and SNARE complex disassembling rate-Reference-Cited by-同舟云学术

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LRRK2 phosphorylates pre-synaptic N-ethylmaleimide sensitive fusion (NSF) protein enhancing its ATPase activity and SNARE complex disassembling rate

Published:2016-01-13 Issue:1 Volume:11 Page:
ISSN:1750-1326
Container-title:Molecular Neurodegeneration
language:en
Short-container-title:Mol Neurodegeneration

Author:

Belluzzi Elisa,Gonnelli Adriano,Cirnaru Maria-Daniela,Marte Antonella,Plotegher Nicoletta,Russo Isabella,Civiero Laura,Cogo Susanna,Carrion Maria Perèz,Franchin Cinzia,Arrigoni Giorgio,Beltramini Mariano,Bubacco Luigi,Onofri Franco,Piccoli Giovanni,Greggio Elisa

Funder

Michael J. Fox Foundation for Parkinson's Research (US)

Fondazione Telethon (IT)

Progetto di Ateneo CPDA University pf Padova

Regione Lombardia

Publisher

Springer Science and Business Media LLC

Subject

Cellular and Molecular Neuroscience,Neurology (clinical),Molecular Biology

Link

http://link.springer.com/content/pdf/10.1186/s13024-015-0066-z

Reference50 articles.

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2. Taymans JM. The GTPase function of LRRK2. Biochem Soc Trans. 2012;40(5):1063–9. doi: 10.1042/BST20120133 .

3. Greggio E. Role of LRRK2 kinase activity in the pathogenesis of Parkinson’s disease. Biochem Soc Trans. 2012;40(5):1058–62. doi: 10.1042/BST20120054 .

4. Paisan-Ruiz C, Jain S, Evans EW, Gilks WP, Simon J, van der Brug M, et al. Cloning of the gene containing mutations that cause PARK8-linked Parkinson’s disease. Neuron. 2004;44(4):595–600. doi: 10.1016/j.neuron.2004.10.023 .

5. Zimprich A, Biskup S, Leitner P, Lichtner P, Farrer M, Lincoln S, et al. Mutations in LRRK2 cause autosomal-dominant parkinsonism with pleomorphic pathology. Neuron. 2004;44(4):601–7. doi: 10.1016/j.neuron.2004.11.005 .

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