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Polo-like kinase 2 regulates selective autophagic α-synuclein clearance and suppresses its toxicity in vivo.

Oueslati A, Schneider BL, Aebischer P, Lashuel HA.

Proc Natl Acad Sci U S A. 2013 Oct 8;110(41):E3945-54. doi: 10.1073/pnas.1309991110.


In vivo modulation of polo-like kinases supports a key role for PLK2 in Ser129 α-synuclein phosphorylation in mouse brain.

Bergeron M, Motter R, Tanaka P, Fauss D, Babcock M, Chiou SS, Nelson S, San Pablo F, Anderson JP.

Neuroscience. 2014 Jan 3;256:72-82. doi: 10.1016/j.neuroscience.2013.09.061.


Polo-like kinase 2 (PLK2) phosphorylates alpha-synuclein at serine 129 in central nervous system.

Inglis KJ, Chereau D, Brigham EF, Chiou SS, Schöbel S, Frigon NL, Yu M, Caccavello RJ, Nelson S, Motter R, Wright S, Chian D, Santiago P, Soriano F, Ramos C, Powell K, Goldstein JM, Babcock M, Yednock T, Bard F, Basi GS, Sham H, Chilcote TJ, McConlogue L, Griswold-Prenner I, Anderson JP.

J Biol Chem. 2009 Jan 30;284(5):2598-602. doi: 10.1074/jbc.C800206200.


Silencing synuclein at the synapse with PLK2.

Looyenga BD, Brundin P.

Proc Natl Acad Sci U S A. 2013 Oct 8;110(41):16293-4. doi: 10.1073/pnas.1315622110. No abstract available.


Pharmacological inhibition of polo like kinase 2 (PLK2) does not cause chromosomal damage or result in the formation of micronuclei.

Fitzgerald K, Bergeron M, Willits C, Bowers S, Aubele DL, Goldbach E, Tonn G, Ness D, Olaharski A.

Toxicol Appl Pharmacol. 2013 May 15;269(1):1-7. doi: 10.1016/j.taap.2013.02.012.


Mimicking phosphorylation at serine 87 inhibits the aggregation of human α-synuclein and protects against its toxicity in a rat model of Parkinson's disease.

Oueslati A, Paleologou KE, Schneider BL, Aebischer P, Lashuel HA.

J Neurosci. 2012 Feb 1;32(5):1536-44. doi: 10.1523/JNEUROSCI.3784-11.2012.


Ser129 phosphorylation of endogenous α-synuclein induced by overexpression of polo-like kinases 2 and 3 in nigral dopamine neurons is not detrimental to their survival and function.

Buck K, Landeck N, Ulusoy A, Majbour NK, El-Agnaf OM, Kirik D.

Neurobiol Dis. 2015 Jun;78:100-14. doi: 10.1016/j.nbd.2015.03.008.


Dissecting the Molecular Pathway Involved in PLK2 Kinase-mediated α-Synuclein-selective Autophagic Degradation.

Dahmene M, Bérard M, Oueslati A.

J Biol Chem. 2017 Mar 3;292(9):3919-3928. doi: 10.1074/jbc.M116.759373.


Phosphorylation of synucleins by members of the Polo-like kinase family.

Mbefo MK, Paleologou KE, Boucharaba A, Oueslati A, Schell H, Fournier M, Olschewski D, Yin G, Zweckstetter M, Masliah E, Kahle PJ, Hirling H, Lashuel HA.

J Biol Chem. 2010 Jan 22;285(4):2807-22. doi: 10.1074/jbc.M109.081950.


α-Synuclein disrupts stress signaling by inhibiting polo-like kinase Cdc5/Plk2.

Wang S, Xu B, Liou LC, Ren Q, Huang S, Luo Y, Zhang Z, Witt SN.

Proc Natl Acad Sci U S A. 2012 Oct 2;109(40):16119-24. doi: 10.1073/pnas.1206286109.


Tenuigenin attenuates α-synuclein-induced cytotoxicity by down-regulating polo-like kinase 3.

Zhou JX, Zhang HB, Huang Y, He Y, Zheng Y, Anderson JP, Gai WP, Liang ZG, Wang Y, Ren XM, Wang Q, Gong XL, Yang J, Wang X, Halliday G, Wang XM.

CNS Neurosci Ther. 2013 Sep;19(9):688-94. doi: 10.1111/cns.12124.


Parkinson's disease and alpha synuclein: is Parkinson's disease a prion-like disorder?

Olanow CW, Brundin P.

Mov Disord. 2013 Jan;28(1):31-40. doi: 10.1002/mds.25373. Review.


Progressive neurodegenerative and behavioural changes induced by AAV-mediated overexpression of α-synuclein in midbrain dopamine neurons.

Decressac M, Mattsson B, Lundblad M, Weikop P, Björklund A.

Neurobiol Dis. 2012 Mar;45(3):939-53. doi: 10.1016/j.nbd.2011.12.013.


Casein kinase II-mediated phosphorylation regulates alpha-synuclein/synphilin-1 interaction and inclusion body formation.

Lee G, Tanaka M, Park K, Lee SS, Kim YM, Junn E, Lee SH, Mouradian MM.

J Biol Chem. 2004 Feb 20;279(8):6834-9.


TFEB-mediated autophagy rescues midbrain dopamine neurons from α-synuclein toxicity.

Decressac M, Mattsson B, Weikop P, Lundblad M, Jakobsson J, Björklund A.

Proc Natl Acad Sci U S A. 2013 May 7;110(19):E1817-26. doi: 10.1073/pnas.1305623110.


Pathological biochemistry of alpha-synucleinopathy.

Iwatsubo T.

Neuropathology. 2007 Oct;27(5):474-8. Retraction in: Neuropathology. 2012 Jun;32(3):318.


Cyclin-G-associated kinase modifies α-synuclein expression levels and toxicity in Parkinson's disease: results from the GenePD Study.

Dumitriu A, Pacheco CD, Wilk JB, Strathearn KE, Latourelle JC, Goldwurm S, Pezzoli G, Rochet JC, Lindquist S, Myers RH.

Hum Mol Genet. 2011 Apr 15;20(8):1478-87. doi: 10.1093/hmg/ddr026.


c-Abl phosphorylates α-synuclein and regulates its degradation: implication for α-synuclein clearance and contribution to the pathogenesis of Parkinson's disease.

Mahul-Mellier AL, Fauvet B, Gysbers A, Dikiy I, Oueslati A, Georgeon S, Lamontanara AJ, Bisquertt A, Eliezer D, Masliah E, Halliday G, Hantschel O, Lashuel HA.

Hum Mol Genet. 2014 Jun 1;23(11):2858-79. doi: 10.1093/hmg/ddt674.


Phosphorylation does not prompt, nor prevent, the formation of alpha-synuclein toxic species in a rat model of Parkinson's disease.

Azeredo da Silveira S, Schneider BL, Cifuentes-Diaz C, Sage D, Abbas-Terki T, Iwatsubo T, Unser M, Aebischer P.

Hum Mol Genet. 2009 Mar 1;18(5):872-87. doi: 10.1093/hmg/ddn417.


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