Publications / No. 2

Research

Published articles by the Nichols Lab staff are listed below. Click to access the Pubmed abstract or free full article where available.

Recent Publications

LRRK2 levels and phosphorylation in Parkinson’s disease brain and cases with restricted Lewy bodies.. Dzamko N, Gysbers AM, Bandopadhyay R, Bolliger MF, Uchino A, Zhao Y, Takao M, Wauters S, van de Berg WD, Takahashi-Fujigasaki J, Nichols RJ, Holton JL, Murayama S, Halliday GM. Movement disorders : official journal of the Movement Disorder Society. 2016; PubMed [journal]PMID: 27911006 Multisystem Lewy body disease and the other parkinsonian disorders.. Langston JW, Schüle B, Rees L, Nichols RJ, Barlow C. Nature genetics. 2015; 47(12):1378-84. PubMed [journal]PMID: 26620112 LRRK2 dephosphorylation increases its ubiquitination.. Zhao J, Molitor TP, Langston JW, Nichols RJ. The Biochemical journal. 2015; 469(1):107-20. PubMed [journal]PMID: 25939886 PMCID: PMC4613513 LRRK2 kinase activity and biology are not uniformly predicted by its autophosphorylation and cellular phosphorylation site status.. Reynolds A, Doggett EA, Riddle SM, Lebakken CS, Nichols RJ. Frontiers in molecular neuroscience. 2014; 7:54. PubMed [journal]PMID: 25009464 PMCID: PMC4068021 Parkinson disease-associated mutation R1441H in LRRK2 prolongs the “active state” of its GTPase domain.. Liao J, Wu CX, Burlak C, Zhang S, Sahm H, Wang M, Zhang ZY, Vogel KW, Federici M, Riddle SM, Nichols RJ, Liu D, Cookson MR, Stone TA, Hoang QQ. Proceedings of the National Academy of Sciences of the United States of America. 2014; 111(11):4055-60. PubMed [journal]PMID: 24591621 PMCID: PMC3964117 Identification of protein phosphatase 1 as a regulator of the LRRK2 phosphorylation cycle.. Lobbestael E, Zhao J, Rudenko IN, Beylina A, Gao F, Wetter J, Beullens M, Bollen M, Cookson MR, Baekelandt V, Nichols RJ, Taymans JM. The Biochemical journal. 2013; 456(1):119-28. NIHMSID: NIHMS739070 PubMed [journal]PMID: 23937259 PMCID: PMC5141581 Pharmacological inhibition of LRRK2 cellular phosphorylation sites provides insight into LRRK2 biology. Zhao J, Hermanson SB, Carlson CB, Riddle SM, Vogel KW, Bi K, Nichols RJ. Biochem Soc Trans. 2012 Oct;40(5):1158-62. Review. PMID: 22988882 http://www.ncbi.nlm.nih.gov/pubmed/22988882 Screening for novel LRRK2 inhibitors using a high-throughput TR-FRET cellular assay for LRRK2 Ser935 phosphorylation. Hermanson SB, Carlson CB, Riddle SM, Zhao J, Vogel KW, Nichols RJ, Bi K. PLoS One. 2012;7(8):e43580. doi: 10.1371/journal.pone.0043580. Epub 2012 Aug 28. PMID: 22952710 http://www.ncbi.nlm.nih.gov/pubmed/22952710 Phosphorylation of LRRK2 serines 955 and 973 is disrupted by Parkinson’s disease mutations and LRRK2 pharmacological inhibition. Doggett EA, Zhao J, Mork CN, Hu D, Nichols RJ. Biochem Soc Trans. 2012 Oct;40(5):1158-62. PMID: 22004453 http://www.ncbi.nlm.nih.gov/pubmed/22004453 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. PMID: 20659021 http://www.ncbi.nlm.nih.gov/pubmed/20659021 14-3-3 binding to LRRK2 is disrupted by multiple Parkinson’s disease associated mutations and regulates cytoplasmic localisation. Nichols RJ*, Dzamko N, Morrice NA, Campbell DG, Deak M, Ordureau A, Macartney T, Tong Y, Shen J, Prescott A, Alessi DR*. Biochem J. 2010 Sep 15;430(3):393-404 PMID: 20642453 [PubMed – indexed for MEDLINE] http://www.ncbi.nlm.nih.gov/pubmed/20642453 Mice deficient in the serine/threonine protein kinase VRK1 are infertile due to a progressive loss of spermatogonia. Wiebe MS, Nichols RJ, Molitor TP, Lindgren JK, Traktman P. Biol Reprod. 2010 Jan;82(1):182-93. Epub 2009 Aug 19. PMID: 19696012 http://www.ncbi.nlm.nih.gov/pubmed/19696012 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. PMID: 19740074 http://www.ncbi.nlm.nih.gov/pubmed/19740074 Functional characterization of the vaccinia virus I5 protein. Unger B, Nichols RJ, Stanitsa ES, Traktman P. Virol J. 2008 Dec 15;5:148. PMID: 19077320 http://www.ncbi.nlm.nih.gov/pubmed/19077320 The vaccinia virus gene I2L encodes a membrane protein with an essential role in virion entry. Nichols RJ, Stanitsa E, Unger B, Traktman P. J Virol. 2008 Oct;82(20):10247-61. Epub 2008 Aug 13. PMID: 18701587 http://www.ncbi.nlm.nih.gov/pubmed/18701587 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. PMID: 17447891 http://www.ncbi.nlm.nih.gov/pubmed/17447891 The vaccinia-related kinases phosphorylate the N’ terminus of BAF, regulating its interaction with DNA and its retention in the nucleus. Nichols RJ, Wiebe MS, Traktman P. Mol Biol Cell. 2006 May;17(5):2451-64. Epub 2006 Feb 22. PMID: 16495336 http://www.ncbi.nlm.nih.gov/pubmed/16495336 Characterization of three paralogous members of the Mammalian vaccinia related kinase family. Nichols RJ, Traktman P. J Biol Chem. 2004 Feb 27;279(9):7934-46. Epub 2003 Nov 25. PMID: 14645249 http://www.ncbi.nlm.nih.gov/pubmed/14645249 *indicates corresponding authors

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The Parkinson’s Institute and Clinical Center is designated as one of 45 worldwide Centers of Excellence for Parkinson’s treatment and research. This is a distinction awarded by the Parkinson’s Foundation.

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