Format
Sort by
Items per page

Send to

Choose Destination

Links from PubMed

Items: 1 to 20 of 172

1.

Substrate specificity and inhibitors of LRRK2, a protein kinase mutated in Parkinson's disease.

Nichols RJ, Dzamko N, Hutti JE, Cantley LC, Deak M, Moran J, Bamborough P, Reith AD, Alessi DR.

Biochem J. 2009 Oct 23;424(1):47-60. doi: 10.1042/BJ20091035.

2.

Inhibition of LRRK2 kinase activity leads to dephosphorylation of Ser(910)/Ser(935), disruption of 14-3-3 binding and altered cytoplasmic localization.

Dzamko N, Deak M, Hentati F, Reith AD, Prescott AR, Alessi DR, Nichols RJ.

Biochem J. 2010 Sep 15;430(3):405-13. doi: 10.1042/BJ20100784.

3.

Identification of compounds that inhibit the kinase activity of leucine-rich repeat kinase 2.

Covy JP, Giasson BI.

Biochem Biophys Res Commun. 2009 Jan 16;378(3):473-7. doi: 10.1016/j.bbrc.2008.11.048. Epub 2008 Nov 21. Erratum in: Biochem Biophys Res Commun. 2009 Sep 18;387(2):419-20.

4.

Kinetic mechanistic studies of wild-type leucine-rich repeat kinase 2: characterization of the kinase and GTPase activities.

Liu M, Dobson B, Glicksman MA, Yue Z, Stein RL.

Biochemistry. 2010 Mar 9;49(9):2008-17. doi: 10.1021/bi901851y.

5.

Characterization of a selective inhibitor of the Parkinson's disease kinase LRRK2.

Deng X, Dzamko N, Prescott A, Davies P, Liu Q, Yang Q, Lee JD, Patricelli MP, Nomanbhoy TK, Alessi DR, Gray NS.

Nat Chem Biol. 2011 Apr;7(4):203-5. doi: 10.1038/nchembio.538. Epub 2011 Mar 6.

6.

ATP-competitive LRRK2 inhibitors interfere with monoclonal antibody binding to the kinase domain of LRRK2 under native conditions. A method to directly monitor the active conformation of LRRK2?

Gillardon F, Kremmer E, Froehlich T, Ueffing M, Hengerer B, Gloeckner CJ.

J Neurosci Methods. 2013 Mar 30;214(1):62-8. doi: 10.1016/j.jneumeth.2012.12.015. Epub 2013 Jan 12.

PMID:
23318290
7.

Phosphorylation of LRRK2: from kinase to substrate.

Lobbestael E, Baekelandt V, Taymans JM.

Biochem Soc Trans. 2012 Oct;40(5):1102-10. Review.

PMID:
22988873
8.

LRRK2 phosphorylates moesin at threonine-558: characterization of how Parkinson's disease mutants affect kinase activity.

Jaleel M, Nichols RJ, Deak M, Campbell DG, Gillardon F, Knebel A, Alessi DR.

Biochem J. 2007 Jul 15;405(2):307-17.

10.

The Parkinson disease-linked LRRK2 protein mutation I2020T stabilizes an active state conformation leading to increased kinase activity.

Ray S, Bender S, Kang S, Lin R, Glicksman MA, Liu M.

J Biol Chem. 2014 May 9;289(19):13042-53. doi: 10.1074/jbc.M113.537811. Epub 2014 Apr 2.

11.

Small molecule kinase inhibitors for LRRK2 and their application to Parkinson's disease models.

Kramer T, Lo Monte F, Göring S, Okala Amombo GM, Schmidt B.

ACS Chem Neurosci. 2012 Mar 21;3(3):151-60. doi: 10.1021/cn200117j. Epub 2012 Jan 18. Review.

12.

Leucine-rich repeat kinase 2 inhibitors: a patent review (2006 - 2011).

Deng X, Choi HG, Buhrlage SJ, Gray NS.

Expert Opin Ther Pat. 2012 Dec;22(12):1415-26. doi: 10.1517/13543776.2012.729041. Epub 2012 Nov 6. Review.

PMID:
23126385
13.

Leucine-rich repeat kinase 2 (LRRK2) cellular biology: a review of recent advances in identifying physiological substrates and cellular functions.

Drolet RE, Sanders JM, Kern JT.

J Neurogenet. 2011 Dec;25(4):140-51. doi: 10.3109/01677063.2011.627072. Epub 2011 Nov 11. Review.

PMID:
22077787
14.

Measuring the activity of leucine-rich repeat kinase 2: a kinase involved in Parkinson's disease.

Lee BD, Li X, Dawson TM, Dawson VL.

Methods Mol Biol. 2012;795:45-54. doi: 10.1007/978-1-61779-337-0_3.

15.

Identification of chemicals to inhibit the kinase activity of leucine-rich repeat kinase 2 (LRRK2), a Parkinson's disease-associated protein.

Yun H, Heo HY, Kim HH, DooKim N, Seol W.

Bioorg Med Chem Lett. 2011 May 15;21(10):2953-7. doi: 10.1016/j.bmcl.2011.03.061. Epub 2011 Mar 21.

PMID:
21474311
16.

New biochemical approaches towards understanding the Parkinson's disease-associated kinase, LRRK2.

Liou GY, Gallo KA.

Biochem J. 2009 Oct 23;424(1):e1-3. doi: 10.1042/BJ20091540. Review.

PMID:
19839940
17.
19.

Current understanding of LRRK2 in Parkinson's disease: biochemical and structural features and inhibitor design.

Ray S, Liu M.

Future Med Chem. 2012 Sep;4(13):1701-13. doi: 10.4155/fmc.12.110. Review.

20.

14-3-3 binding to LRRK2 is disrupted by multiple Parkinson's disease-associated mutations and regulates cytoplasmic localization.

Nichols RJ, Dzamko N, Morrice NA, Campbell DG, Deak M, Ordureau A, Macartney T, Tong Y, Shen J, Prescott AR, Alessi DR.

Biochem J. 2010 Sep 15;430(3):393-404. doi: 10.1042/BJ20100483.

Supplemental Content

Support Center