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Items: 1 to 20 of 311

1.

Vertebrate food products as a potential source of prion-like α-synuclein.

Killinger BA, Labrie V.

NPJ Parkinsons Dis. 2017 Nov 24;3:33. doi: 10.1038/s41531-017-0035-z. eCollection 2017. Review.

2.

Real-Time Observation of the Interaction between Thioflavin T and an Amyloid Protein by Using High-Sensitivity Rheo-NMR.

Iwakawa N, Morimoto D, Walinda E, Kawata Y, Shirakawa M, Sugase K.

Int J Mol Sci. 2017 Oct 28;18(11). pii: E2271. doi: 10.3390/ijms18112271.

3.

Modulation of the extent of structural heterogeneity in α-synuclein fibrils by the small molecule thioflavin T.

Kumar H, Singh J, Kumari P, Udgaonkar JB.

J Biol Chem. 2017 Oct 13;292(41):16891-16903. doi: 10.1074/jbc.M117.795617. Epub 2017 Jul 31.

PMID:
28760825
4.

Nanobodies raised against monomeric ɑ-synuclein inhibit fibril formation and destabilize toxic oligomeric species.

Iljina M, Hong L, Horrocks MH, Ludtmann MH, Choi ML, Hughes CD, Ruggeri FS, Guilliams T, Buell AK, Lee JE, Gandhi S, Lee SF, Bryant CE, Vendruscolo M, Knowles TPJ, Dobson CM, De Genst E, Klenerman D.

BMC Biol. 2017 Jul 3;15(1):57. doi: 10.1186/s12915-017-0390-6.

5.

Functional Amyloids in Reproduction.

Hewetson A, Do HQ, Myers C, Muthusubramanian A, Sutton RB, Wylie BJ, Cornwall GA.

Biomolecules. 2017 Jun 29;7(3). pii: E46. doi: 10.3390/biom7030046. Review.

6.

Structure, Distribution, and Genetic Profile of α-Synuclein and Their Potential Clinical Application in Parkinson's Disease.

Si X, Pu J, Zhang B.

J Mov Disord. 2017 May;10(2):69-79. doi: 10.14802/jmd.16061. Epub 2017 May 8.

7.

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.

PMID:
28373279
8.

Dementia with Lewy Bodies: Molecular Pathology in the Frontal Cortex in Typical and Rapidly Progressive Forms.

Garcia-Esparcia P, López-González I, Grau-Rivera O, García-Garrido MF, Konetti A, Llorens F, Zafar S, Carmona M, Del Rio JA, Zerr I, Gelpi E, Ferrer I.

Front Neurol. 2017 Mar 13;8:89. doi: 10.3389/fneur.2017.00089. eCollection 2017.

9.

Extracellular α-synuclein induces sphingosine 1-phosphate receptor subtype 1 uncoupled from inhibitory G-protein leaving β-arrestin signal intact.

Zhang L, Okada T, Badawy SM, Hirai C, Kajimoto T, Nakamura SI.

Sci Rep. 2017 Mar 16;7:44248. doi: 10.1038/srep44248.

10.

High-Throughput Screening Methodology to Identify Alpha-Synuclein Aggregation Inhibitors.

Pujols J, Peña-Díaz S, Conde-Giménez M, Pinheiro F, Navarro S, Sancho J, Ventura S.

Int J Mol Sci. 2017 Mar 2;18(3). pii: E478. doi: 10.3390/ijms18030478.

11.

Formation of covalent di-tyrosine dimers in recombinant α-synuclein.

van Maarschalkerweerd A, Pedersen MN, Peterson H, Nilsson M, Nguyen T, Skamris T, Rand K, Vetri V, Langkilde AE, Vestergaard B.

Intrinsically Disord Proteins. 2015 Oct 19;3(1):e1071302. doi: 10.1080/21690707.2015.1071302. eCollection 2015.

12.

RNA Interference of Human α-Synuclein in Mouse.

Kim YC, Miller A, Lins LC, Han SW, Keiser MS, Boudreau RL, Davidson BL, Narayanan NS.

Front Neurol. 2017 Jan 31;8:13. doi: 10.3389/fneur.2017.00013. eCollection 2017.

13.

α-Synuclein increases β-amyloid secretion by promoting β-/γ-secretase processing of APP.

Roberts HL, Schneider BL, Brown DR.

PLoS One. 2017 Feb 10;12(2):e0171925. doi: 10.1371/journal.pone.0171925. eCollection 2017.

14.

Endosulfine-alpha inhibits membrane-induced α-synuclein aggregation and protects against α-synuclein neurotoxicity.

Ysselstein D, Dehay B, Costantino IM, McCabe GP, Frosch MP, George JM, Bezard E, Rochet JC.

Acta Neuropathol Commun. 2017 Jan 10;5(1):3. doi: 10.1186/s40478-016-0403-7.

15.

Calcium: Alpha-Synuclein Interactions in Alpha-Synucleinopathies.

Rcom-H'cheo-Gauthier AN, Osborne SL, Meedeniya AC, Pountney DL.

Front Neurosci. 2016 Dec 20;10:570. doi: 10.3389/fnins.2016.00570. eCollection 2016. Review.

16.

Mapping of Surface-Exposed Epitopes of In Vitro and In Vivo Aggregated Species of Alpha-Synuclein.

Almandoz-Gil L, Lindström V, Sigvardson J, Kahle PJ, Lannfelt L, Ingelsson M, Bergström J.

Cell Mol Neurobiol. 2017 Oct;37(7):1217-1226. doi: 10.1007/s10571-016-0454-0. Epub 2016 Dec 27.

17.
18.

Nanomolar oligomerization and selective co-aggregation of α-synuclein pathogenic mutants revealed by single-molecule fluorescence.

Sierecki E, Giles N, Bowden Q, Polinkovsky ME, Steinbeck J, Arrioti N, Rahman D, Bhumkar A, Nicovich PR, Ross I, Parton RG, Böcking T, Gambin Y.

Sci Rep. 2016 Nov 28;6:37630. doi: 10.1038/srep37630.

19.

Impairment of PDGF-induced chemotaxis by extracellular α-synuclein through selective inhibition of Rac1 activation.

Okada T, Hirai C, Badawy SM, Zhang L, Kajimoto T, Nakamura SI.

Sci Rep. 2016 Nov 25;6:37810. doi: 10.1038/srep37810.

20.

Arachidonic acid mediates the formation of abundant alpha-helical multimers of alpha-synuclein.

Iljina M, Tosatto L, Choi ML, Sang JC, Ye Y, Hughes CD, Bryant CE, Gandhi S, Klenerman D.

Sci Rep. 2016 Sep 27;6:33928. doi: 10.1038/srep33928.

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