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Items: 1 to 20 of 122

1.

Structural intermediates during α-synuclein fibrillogenesis on phospholipid vesicles.

Comellas G, Lemkau LR, Zhou DH, George JM, Rienstra CM.

J Am Chem Soc. 2012 Mar 21;134(11):5090-9. doi: 10.1021/ja209019s.

2.

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.

3.

Membrane lipid co-aggregation with α-synuclein fibrils.

Hellstrand E, Nowacka A, Topgaard D, Linse S, Sparr E.

PLoS One. 2013 Oct 11;8(10):e77235. doi: 10.1371/journal.pone.0077235.

4.

Structural comparison of mouse and human α-synuclein amyloid fibrils by solid-state NMR.

Lv G, Kumar A, Giller K, Orcellet ML, Riedel D, Fernández CO, Becker S, Lange A.

J Mol Biol. 2012 Jun 29;420(1-2):99-111. doi: 10.1016/j.jmb.2012.04.009.

PMID:
22516611
5.

Multiple tight phospholipid-binding modes of alpha-synuclein revealed by solution NMR spectroscopy.

Bodner CR, Dobson CM, Bax A.

J Mol Biol. 2009 Jul 24;390(4):775-90. doi: 10.1016/j.jmb.2009.05.066.

6.

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.

7.

Solid-state NMR reveals structural differences between fibrils of wild-type and disease-related A53T mutant alpha-synuclein.

Heise H, Celej MS, Becker S, Riedel D, Pelah A, Kumar A, Jovin TM, Baldus M.

J Mol Biol. 2008 Jul 11;380(3):444-50. doi: 10.1016/j.jmb.2008.05.026.

PMID:
18539297
8.

Yet another polymorph of α-synuclein: solid-state sequential assignments.

Gath J, Bousset L, Habenstein B, Melki R, Meier BH, Böckmann A.

Biomol NMR Assign. 2014 Oct;8(2):395-404. doi: 10.1007/s12104-013-9526-y.

PMID:
24114178
9.

Mechanistic insight into the relationship between N-terminal acetylation of α-synuclein and fibril formation rates by NMR and fluorescence.

Kang L, Janowska MK, Moriarty GM, Baum J.

PLoS One. 2013 Sep 18;8(9):e75018. doi: 10.1371/journal.pone.0075018.

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.

Site-specific perturbations of alpha-synuclein fibril structure by the Parkinson's disease associated mutations A53T and E46K.

Lemkau LR, Comellas G, Lee SW, Rikardsen LK, Woods WS, George JM, Rienstra CM.

PLoS One. 2013;8(3):e49750. doi: 10.1371/journal.pone.0049750.

12.

Charge neutralization and collapse of the C-terminal tail of alpha-synuclein at low pH.

McClendon S, Rospigliosi CC, Eliezer D.

Protein Sci. 2009 Jul;18(7):1531-40. doi: 10.1002/pro.149.

13.

Solid-state NMR spectroscopy reveals that water is nonessential to the core structure of alpha-synuclein fibrils.

Kloepper KD, Hartman KL, Ladror DT, Rienstra CM.

J Phys Chem B. 2007 Nov 29;111(47):13353-6.

14.

Structure based aggregation studies reveal the presence of helix-rich intermediate during α-Synuclein aggregation.

Ghosh D, Singh PK, Sahay S, Jha NN, Jacob RS, Sen S, Kumar A, Riek R, Maji SK.

Sci Rep. 2015 Mar 18;5:9228. doi: 10.1038/srep09228.

15.

A study of the regional effects of alpha-synuclein on the organization and stability of phospholipid bilayers.

Madine J, Doig AJ, Middleton DA.

Biochemistry. 2006 May 9;45(18):5783-92.

PMID:
16669622
16.

Besides fibrillization: putative role of the peptide fragment 71-82 on the structural and assembly behavior of α-synuclein.

Bédard L, Lefèvre T, Morin-Michaud É, Auger M.

Biochemistry. 2014 Oct 21;53(41):6463-72. doi: 10.1021/bi5008707.

PMID:
25255476
17.

The impact of the E46K mutation on the properties of alpha-synuclein in its monomeric and oligomeric states.

Fredenburg RA, Rospigliosi C, Meray RK, Kessler JC, Lashuel HA, Eliezer D, Lansbury PT Jr.

Biochemistry. 2007 Jun 19;46(24):7107-18.

PMID:
17530780
19.

Molecular-level secondary structure, polymorphism, and dynamics of full-length alpha-synuclein fibrils studied by solid-state NMR.

Heise H, Hoyer W, Becker S, Andronesi OC, Riedel D, Baldus M.

Proc Natl Acad Sci U S A. 2005 Nov 1;102(44):15871-6.

20.

Conformation-specific binding of alpha-synuclein to novel protein partners detected by phage display and NMR spectroscopy.

Woods WS, Boettcher JM, Zhou DH, Kloepper KD, Hartman KL, Ladror DT, Qi Z, Rienstra CM, George JM.

J Biol Chem. 2007 Nov 23;282(47):34555-67.

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