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Alice Kaganovich

Researcher at National Institutes of Health

Publications -  33
Citations -  6466

Alice Kaganovich is an academic researcher from National Institutes of Health. The author has contributed to research in topics: LRRK2 & Kinase activity. The author has an hindex of 16, co-authored 28 publications receiving 5529 citations. Previous affiliations of Alice Kaganovich include University of Padua.

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Journal ArticleDOI

A hexanucleotide repeat expansion in C9ORF72 is the cause of chromosome 9p21-linked ALS-FTD

Alan E. Renton, +85 more
- 20 Oct 2011 - 
TL;DR: The chromosome 9p21 amyotrophic lateral sclerosis-frontotemporal dementia (ALS-FTD) locus contains one of the last major unidentified autosomal-dominant genes underlying these common neurodegenerative diseases, and a large hexanucleotide repeat expansion in the first intron of C9ORF72 is shown.
Journal ArticleDOI

Kinase activity is required for the toxic effects of mutant LRRK2/dardarin.

TL;DR: Manipulating activity by replacing the kinase domain with a 'kinase-dead' version blocks inclusion body formation and strongly delays cell death, predicting that kinase inhibitors will be useful therapeutic agents in patients with LRRK2 mutations and, perhaps, in sporadic PD.
Journal ArticleDOI

Unbiased screen for interactors of leucine-rich repeat kinase 2 supports a common pathway for sporadic and familial Parkinson disease

Alexandra Beilina, +168 more
TL;DR: It is shown, using the specific example of Parkinson disease, that identification of protein–protein interactions can help determine the most likely candidate for several GWAS loci, and proposed that three different genes for PD have a common biological function.
Journal ArticleDOI

The Parkinson Disease-associated Leucine-rich Repeat Kinase 2 (LRRK2) Is a Dimer That Undergoes Intramolecular Autophosphorylation

TL;DR: It is shown that L RRK2 predominantly exists as a dimer under native conditions, a state that appears to be stabilized by multiple domain-domain interactions and it is demonstrated that LRRK2 undergoes intramolecular autophosphorylation.