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Items: 1 to 20 of 235

1.
2.

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
3.

Inhibition of fibrillization and accumulation of prefibrillar oligomers in mixtures of human and mouse alpha-synuclein.

Rochet JC, Conway KA, Lansbury PT Jr.

Biochemistry. 2000 Sep 5;39(35):10619-26.

PMID:
10978144
4.
6.

Both familial Parkinson's disease mutations accelerate alpha-synuclein aggregation.

Narhi L, Wood SJ, Steavenson S, Jiang Y, Wu GM, Anafi D, Kaufman SA, Martin F, Sitney K, Denis P, Louis JC, Wypych J, Biere AL, Citron M.

J Biol Chem. 1999 Apr 2;274(14):9843-6. Erratum in: J Biol Chem 1999 May 7;274(19):13728.

7.

Alpha-synuclein, especially the Parkinson's disease-associated mutants, forms pore-like annular and tubular protofibrils.

Lashuel HA, Petre BM, Wall J, Simon M, Nowak RJ, Walz T, Lansbury PT Jr.

J Mol Biol. 2002 Oct 4;322(5):1089-102.

PMID:
12367530
8.
9.

Vesicle permeabilization by protofibrillar alpha-synuclein: implications for the pathogenesis and treatment of Parkinson's disease.

Volles MJ, Lee SJ, Rochet JC, Shtilerman MD, Ding TT, Kessler JC, Lansbury PT Jr.

Biochemistry. 2001 Jul 3;40(26):7812-9.

PMID:
11425308
10.
11.

Defective membrane interactions of familial Parkinson's disease mutant A30P alpha-synuclein.

Jo E, Fuller N, Rand RP, St George-Hyslop P, Fraser PE.

J Mol Biol. 2002 Jan 25;315(4):799-807.

PMID:
11812148
12.
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14.

Residual structure and dynamics in Parkinson's disease-associated mutants of alpha-synuclein.

Bussell R Jr, Eliezer D.

J Biol Chem. 2001 Dec 7;276(49):45996-6003. Epub 2001 Oct 4.

16.

Fibrillization of alpha-synuclein and tau in familial Parkinson's disease caused by the A53T alpha-synuclein mutation.

Kotzbauer PT, Giasson BI, Kravitz AV, Golbe LI, Mark MH, Trojanowski JQ, Lee VM.

Exp Neurol. 2004 Jun;187(2):279-88.

PMID:
15144854
17.
19.

Zeroing in on the pathogenic form of alpha-synuclein and its mechanism of neurotoxicity in Parkinson's disease.

Volles MJ, Lansbury PT Jr.

Biochemistry. 2003 Jul 8;42(26):7871-8. Review.

PMID:
12834338
20.

Dissociation of amyloid fibrils of alpha-synuclein and transthyretin by pressure reveals their reversible nature and the formation of water-excluded cavities.

Foguel D, Suarez MC, Ferrão-Gonzales AD, Porto TC, Palmieri L, Einsiedler CM, Andrade LR, Lashuel HA, Lansbury PT, Kelly JW, Silva JL.

Proc Natl Acad Sci U S A. 2003 Aug 19;100(17):9831-6. Epub 2003 Aug 4.

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