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Items: 1 to 20 of 107

1.

Modulating α-synuclein fibril formation using DNA tetrahedron nanostructures.

Yoo WK, Ryu BH, Kim KR, Wang Y, Le LTHL, Lee JH, Kim KK, Toth G, Ahn DR, Doohun Kim T.

Biochim Biophys Acta Gen Subj. 2019 Jan;1863(1):73-81. doi: 10.1016/j.bbagen.2018.09.025. Epub 2018 Sep 29.

PMID:
30278239
2.

Single fibril growth kinetics of α-synuclein.

Wördehoff MM, Bannach O, Shaykhalishahi H, Kulawik A, Schiefer S, Willbold D, Hoyer W, Birkmann E.

J Mol Biol. 2015 Mar 27;427(6 Pt B):1428-1435. doi: 10.1016/j.jmb.2015.01.020. Epub 2015 Feb 4.

PMID:
25659910
3.

Stimulation of α-synuclein amyloid formation by phosphatidylglycerol micellar tubules.

Jiang Z, Flynn JD, Teague WE Jr, Gawrisch K, Lee JC.

Biochim Biophys Acta Biomembr. 2018 Mar 1. pii: S0005-2736(18)30066-X. doi: 10.1016/j.bbamem.2018.02.025. [Epub ahead of print]

PMID:
29501608
4.

Amyloid fibril structure of α-synuclein determined by cryo-electron microscopy.

Li Y, Zhao C, Luo F, Liu Z, Gui X, Luo Z, Zhang X, Li D, Liu C, Li X.

Cell Res. 2018 Sep;28(9):897-903. doi: 10.1038/s41422-018-0075-x. Epub 2018 Jul 31.

PMID:
30065316
5.

A sensitive assay reveals structural requirements for α-synuclein fibril growth.

Dhavale DD, Tsai C, Bagchi DP, Engel LA, Sarezky J, Kotzbauer PT.

J Biol Chem. 2017 Jun 2;292(22):9034-9050. doi: 10.1074/jbc.M116.767053. Epub 2017 Apr 3.

6.

The effect of fluorescent labeling on α-synuclein fibril morphology.

Mučibabić M, Apetri MM, Canters GW, Aartsma TJ.

Biochim Biophys Acta. 2016 Oct;1864(10):1419-27. doi: 10.1016/j.bbapap.2016.07.007. Epub 2016 Jul 28.

PMID:
27475048
7.

Intranasal administration of alpha-synuclein aggregates: a Parkinson's disease model with behavioral and neurochemical correlates.

Gruden MA, Davydova TV, Narkevich VB, Fomina VG, Wang C, Kudrin VS, Morozova-Roche LA, Sewell RD.

Behav Brain Res. 2014 Apr 15;263:158-68. doi: 10.1016/j.bbr.2014.01.017. Epub 2014 Jan 27.

PMID:
24480422
8.

Fibril growth and seeding capacity play key roles in α-synuclein-mediated apoptotic cell death.

Mahul-Mellier AL, Vercruysse F, Maco B, Ait-Bouziad N, De Roo M, Muller D, Lashuel HA.

Cell Death Differ. 2015 Dec;22(12):2107-22. doi: 10.1038/cdd.2015.79. Epub 2015 Jul 3.

9.

Comparison of α-Synuclein Fibril Inhibition by Four Different Amyloid Inhibitors.

Jha NN, Kumar R, Panigrahi R, Navalkar A, Ghosh D, Sahay S, Mondal M, Kumar A, Maji SK.

ACS Chem Neurosci. 2017 Dec 20;8(12):2722-2733. doi: 10.1021/acschemneuro.7b00261. Epub 2017 Sep 21.

PMID:
28872299
10.

Fibrils formed in vitro from alpha-synuclein and two mutant forms linked to Parkinson's disease are typical amyloid.

Conway KA, Harper JD, Lansbury PT Jr.

Biochemistry. 2000 Mar 14;39(10):2552-63.

PMID:
10704204
11.

Quantitative characterization of protein nanostructures using atomic force microscopy.

Segers-Nolten I, van der Werf K, van Raaij M, Subramaniam V.

Conf Proc IEEE Eng Med Biol Soc. 2007;2007:6609-12.

PMID:
18003540
12.

Lysosomal enzyme cathepsin B enhances the aggregate forming activity of exogenous α-synuclein fibrils.

Tsujimura A, Taguchi K, Watanabe Y, Tatebe H, Tokuda T, Mizuno T, Tanaka M.

Neurobiol Dis. 2015 Jan;73:244-53. doi: 10.1016/j.nbd.2014.10.011. Epub 2014 Oct 22.

13.
14.

Sensitive fluorescence polarization technique for rapid screening of alpha-synuclein oligomerization/fibrillization inhibitors.

Luk KC, Hyde EG, Trojanowski JQ, Lee VM.

Biochemistry. 2007 Nov 6;46(44):12522-9. Epub 2007 Oct 10.

PMID:
17927212
15.

Structure activity relationship of phenolic acid inhibitors of α-synuclein fibril formation and toxicity.

Ardah MT, Paleologou KE, Lv G, Abul Khair SB, Kazim AS, Minhas ST, Al-Tel TH, Al-Hayani AA, Haque ME, Eliezer D, El-Agnaf OM.

Front Aging Neurosci. 2014 Aug 5;6:197. doi: 10.3389/fnagi.2014.00197. eCollection 2014.

16.

The fold of alpha-synuclein fibrils.

Vilar M, Chou HT, Lührs T, Maji SK, Riek-Loher D, Verel R, Manning G, Stahlberg H, Riek R.

Proc Natl Acad Sci U S A. 2008 Jun 24;105(25):8637-42. doi: 10.1073/pnas.0712179105. Epub 2008 Jun 12.

17.

Biasing the native α-synuclein conformational ensemble towards compact states abolishes aggregation and neurotoxicity.

Carija A, Pinheiro F, Pujols J, Brás IC, Lázaro DF, Santambrogio C, Grandori R, Outeiro TF, Navarro S, Ventura S.

Redox Biol. 2019 Apr;22:101135. doi: 10.1016/j.redox.2019.101135. Epub 2019 Feb 5.

18.

Structure of amyloid oligomers and their mechanisms of toxicities: Targeting amyloid oligomers using novel therapeutic approaches.

Salahuddin P, Fatima MT, Abdelhameed AS, Nusrat S, Khan RH.

Eur J Med Chem. 2016 May 23;114:41-58. doi: 10.1016/j.ejmech.2016.02.065. Epub 2016 Mar 2. Review.

PMID:
26974374
19.

Covalent α-synuclein dimers: chemico-physical and aggregation properties.

Pivato M, De Franceschi G, Tosatto L, Frare E, Kumar D, Aioanei D, Brucale M, Tessari I, Bisaglia M, Samori B, de Laureto PP, Bubacco L.

PLoS One. 2012;7(12):e50027. doi: 10.1371/journal.pone.0050027. Epub 2012 Dec 13.

20.

Pyrroloquinoline quinone (PQQ) prevents fibril formation of alpha-synuclein.

Kobayashi M, Kim J, Kobayashi N, Han S, Nakamura C, Ikebukuro K, Sode K.

Biochem Biophys Res Commun. 2006 Oct 27;349(3):1139-44. Epub 2006 Sep 1.

PMID:
16962995

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