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Items: 1 to 20 of 120

1.

Structural complexity of a composite amyloid fibril.

Lewandowski JR, van der Wel PC, Rigney M, Grigorieff N, Griffin RG.

J Am Chem Soc. 2011 Sep 21;133(37):14686-98. doi: 10.1021/ja203736z. Epub 2011 Aug 23.

2.

Structural characterization of GNNQQNY amyloid fibrils by magic angle spinning NMR.

van der Wel PC, Lewandowski JR, Griffin RG.

Biochemistry. 2010 Nov 9;49(44):9457-69. doi: 10.1021/bi100077x.

3.

Solid-state NMR study of amyloid nanocrystals and fibrils formed by the peptide GNNQQNY from yeast prion protein Sup35p.

van der Wel PC, Lewandowski JR, Griffin RG.

J Am Chem Soc. 2007 Apr 25;129(16):5117-30. Epub 2007 Mar 31.

PMID:
17397156
4.

Molecular structures of amyloid and prion fibrils: consensus versus controversy.

Tycko R, Wickner RB.

Acc Chem Res. 2013 Jul 16;46(7):1487-96. doi: 10.1021/ar300282r. Epub 2013 Jan 7. Review.

5.

The architecture of amyloid-like peptide fibrils revealed by X-ray scattering, diffraction and electron microscopy.

Langkilde AE, Morris KL, Serpell LC, Svergun DI, Vestergaard B.

Acta Crystallogr D Biol Crystallogr. 2015 Apr;71(Pt 4):882-95. doi: 10.1107/S1399004715001674. Epub 2015 Mar 27.

6.
7.

Steric zipper of the amyloid fibrils formed by residues 109-122 of the Syrian hamster prion protein.

Lee SW, Mou Y, Lin SY, Chou FC, Tseng WH, Chen CH, Lu CY, Yu SS, Chan JC.

J Mol Biol. 2008 May 16;378(5):1142-54. doi: 10.1016/j.jmb.2008.03.035. Epub 2008 Mar 26.

PMID:
18423487
8.

Molecular structure of amyloid fibrils: insights from solid-state NMR.

Tycko R.

Q Rev Biophys. 2006 Feb;39(1):1-55. Epub 2006 Jun 13. Review.

PMID:
16772049
9.

Structures of amyloid fibrils formed by the prion protein derived peptides PrP(244-249) and PrP(245-250).

Yau J, Sharpe S.

J Struct Biol. 2012 Nov;180(2):290-302. doi: 10.1016/j.jsb.2012.08.002. Epub 2012 Aug 21.

PMID:
22929126
10.

Effects of randomizing the Sup35NM prion domain sequence on formation of amyloid fibrils in vitro.

Liu Y, Wei H, Wang J, Qu J, Zhao W, Tao H.

Biochem Biophys Res Commun. 2007 Feb 2;353(1):139-46. Epub 2006 Dec 6.

PMID:
17166483
11.

Probing water accessibility in HET-s(218-289) amyloid fibrils by solid-state NMR.

Van Melckebeke H, Schanda P, Gath J, Wasmer C, Verel R, Lange A, Meier BH, Böckmann A.

J Mol Biol. 2011 Jan 21;405(3):765-72. doi: 10.1016/j.jmb.2010.11.004. Epub 2010 Nov 19.

PMID:
21094164
12.

Atomic structures of amyloid cross-beta spines reveal varied steric zippers.

Sawaya MR, Sambashivan S, Nelson R, Ivanova MI, Sievers SA, Apostol MI, Thompson MJ, Balbirnie M, Wiltzius JJ, McFarlane HT, Madsen AØ, Riekel C, Eisenberg D.

Nature. 2007 May 24;447(7143):453-7. Epub 2007 Apr 29.

PMID:
17468747
13.

Conformational flexibility of Y145Stop human prion protein amyloid fibrils probed by solid-state nuclear magnetic resonance spectroscopy.

Helmus JJ, Surewicz K, Surewicz WK, Jaroniec CP.

J Am Chem Soc. 2010 Feb 24;132(7):2393-403. doi: 10.1021/ja909827v.

14.

Amyloid fibril formation by A beta 16-22, a seven-residue fragment of the Alzheimer's beta-amyloid peptide, and structural characterization by solid state NMR.

Balbach JJ, Ishii Y, Antzutkin ON, Leapman RD, Rizzo NW, Dyda F, Reed J, Tycko R.

Biochemistry. 2000 Nov 14;39(45):13748-59.

PMID:
11076514
15.

Observation of highly flexible residues in amyloid fibrils of the HET-s prion.

Siemer AB, Arnold AA, Ritter C, Westfeld T, Ernst M, Riek R, Meier BH.

J Am Chem Soc. 2006 Oct 11;128(40):13224-8.

PMID:
17017802
16.

A combined solid-state NMR and MD characterization of the stability and dynamics of the HET-s(218-289) prion in its amyloid conformation.

Lange A, Gattin Z, Van Melckebeke H, Wasmer C, Soragni A, van Gunsteren WF, Meier BH.

Chembiochem. 2009 Jul 6;10(10):1657-65. doi: 10.1002/cbic.200900019.

PMID:
19504509
17.

Magic angle spinning NMR analysis of beta2-microglobulin amyloid fibrils in two distinct morphologies.

Debelouchina GT, Platt GW, Bayro MJ, Radford SE, Griffin RG.

J Am Chem Soc. 2010 Aug 4;132(30):10414-23. doi: 10.1021/ja102775u.

18.

High-resolution MAS NMR analysis of PI3-SH3 amyloid fibrils: backbone conformation and implications for protofilament assembly and structure .

Bayro MJ, Maly T, Birkett NR, Macphee CE, Dobson CM, Griffin RG.

Biochemistry. 2010 Sep 7;49(35):7474-84. doi: 10.1021/bi100864t.

19.
20.

Amyloid of the prion domain of Sup35p has an in-register parallel beta-sheet structure.

Shewmaker F, Wickner RB, Tycko R.

Proc Natl Acad Sci U S A. 2006 Dec 26;103(52):19754-9. Epub 2006 Dec 14.

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