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2012 1
2014 2
2015 1
2016 1
2020 0
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Page 1
Phosphoproteomics reveals that Parkinson's disease kinase LRRK2 regulates a subset of Rab GTPases.
Steger M, Tonelli F, Ito G, Davies P, Trost M, Vetter M, Wachter S, Lorentzen E, Duddy G, Wilson S, Baptista MA, Fiske BK, Fell MJ, Morrow JA, Reith AD, Alessi DR, Mann M. Steger M, et al. Elife. 2016 Jan 29;5:e12813. doi: 10.7554/eLife.12813. Elife. 2016. PMID: 26824392 Free PMC article.
Structural Characterization of LRRK2 Inhibitors.
Gilsbach BK, Messias AC, Ito G, Sattler M, Alessi DR, Wittinghofer A, Kortholt A. Gilsbach BK, et al. J Med Chem. 2015 May 14;58(9):3751-6. doi: 10.1021/jm5018779. Epub 2015 May 1. J Med Chem. 2015. PMID: 25897865
Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser65.
Kazlauskaite A, Kondapalli C, Gourlay R, Campbell DG, Ritorto MS, Hofmann K, Alessi DR, Knebel A, Trost M, Muqit MM. Kazlauskaite A, et al. Biochem J. 2014 May 15;460(1):127-39. doi: 10.1042/BJ20140334. Biochem J. 2014. PMID: 24660806 Free PMC article.
Phosphorylation of Parkin at Serine65 is essential for activation: elaboration of a Miro1 substrate-based assay of Parkin E3 ligase activity.
Kazlauskaite A, Kelly V, Johnson C, Baillie C, Hastie CJ, Peggie M, Macartney T, Woodroof HI, Alessi DR, Pedrioli PG, Muqit MM. Kazlauskaite A, et al. Open Biol. 2014 Mar 19;4(3):130213. doi: 10.1098/rsob.130213. Open Biol. 2014. PMID: 24647965 Free PMC article.
PINK1 is activated by mitochondrial membrane potential depolarization and stimulates Parkin E3 ligase activity by phosphorylating Serine 65.
Kondapalli C, Kazlauskaite A, Zhang N, Woodroof HI, Campbell DG, Gourlay R, Burchell L, Walden H, Macartney TJ, Deak M, Knebel A, Alessi DR, Muqit MM. Kondapalli C, et al. Open Biol. 2012 May;2(5):120080. doi: 10.1098/rsob.120080. Open Biol. 2012. PMID: 22724072 Free PMC article.
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