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Items: 1 to 20 of 254

1.

Molecular structure of amyloid fibrils formed by residues 127 to 147 of the human prion protein.

Lin NS, Chao JC, Cheng HM, Chou FC, Chang CF, Chen YR, Chang YJ, Huang SJ, Chan JC.

Chemistry. 2010 May 10;16(18):5492-9. doi: 10.1002/chem.200903290.

PMID:
20358555
2.
3.

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
4.

Multiple quantum solid-state NMR indicates a parallel, not antiparallel, organization of beta-sheets in Alzheimer's beta-amyloid fibrils.

Antzutkin ON, Balbach JJ, Leapman RD, Rizzo NW, Reed J, Tycko R.

Proc Natl Acad Sci U S A. 2000 Nov 21;97(24):13045-50.

5.

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.

PMID:
18423487
6.

Mapping abeta amyloid fibril secondary structure using scanning proline mutagenesis.

Williams AD, Portelius E, Kheterpal I, Guo JT, Cook KD, Xu Y, Wetzel R.

J Mol Biol. 2004 Jan 16;335(3):833-42.

PMID:
14687578
7.

Solid state NMR reveals a pH-dependent antiparallel beta-sheet registry in fibrils formed by a beta-amyloid peptide.

Petkova AT, Buntkowsky G, Dyda F, Leapman RD, Yau WM, Tycko R.

J Mol Biol. 2004 Jan 2;335(1):247-60.

PMID:
14659754
8.

Core structure of amyloid fibrils formed by residues 106-126 of the human prion protein.

Walsh P, Simonetti K, Sharpe S.

Structure. 2009 Mar 11;17(3):417-26. doi: 10.1016/j.str.2008.12.018.

10.

Spatial separation of beta-sheet domains of beta-amyloid: disruption of each beta-sheet by N-methyl amino acids.

Sciarretta KL, Boire A, Gordon DJ, Meredith SC.

Biochemistry. 2006 Aug 8;45(31):9485-95.

PMID:
16878983
11.
12.

beta Sheet structure in amyloid beta fibrils and vibrational dipolar coupling.

Paul C, Axelsen PH.

J Am Chem Soc. 2005 Apr 27;127(16):5754-5.

PMID:
15839650
13.

Amyloid fibrils of the HET-s(218-289) prion form a beta solenoid with a triangular hydrophobic core.

Wasmer C, Lange A, Van Melckebeke H, Siemer AB, Riek R, Meier BH.

Science. 2008 Mar 14;319(5869):1523-6. doi: 10.1126/science.1151839. Erratum in: Science. 2008 Apr 4;320(5872):50.

14.

Hydrogen-deuterium (H/D) exchange mapping of Abeta 1-40 amyloid fibril secondary structure using nuclear magnetic resonance spectroscopy.

Whittemore NA, Mishra R, Kheterpal I, Williams AD, Wetzel R, Serpersu EH.

Biochemistry. 2005 Mar 22;44(11):4434-41.

PMID:
15766273
15.

Prolines and amyloidogenicity in fragments of the Alzheimer's peptide beta/A4.

Wood SJ, Wetzel R, Martin JD, Hurle MR.

Biochemistry. 1995 Jan 24;34(3):724-30.

PMID:
7827029
17.

Two-dimensional structure of beta-amyloid(10-35) fibrils.

Benzinger TL, Gregory DM, Burkoth TS, Miller-Auer H, Lynn DG, Botto RE, Meredith SC.

Biochemistry. 2000 Mar 28;39(12):3491-9.

PMID:
10727245
18.

Hydrogen/deuterium exchange mass spectrometry identifies two highly protected regions in recombinant full-length prion protein amyloid fibrils.

Nazabal A, Hornemann S, Aguzzi A, Zenobi R.

J Mass Spectrom. 2009 Jun;44(6):965-77. doi: 10.1002/jms.1572.

PMID:
19283723
19.

HRMAS 1H NMR conformational study of the resin-bound amyloid-forming peptide GNNQQNY from the yeast prion Sup35.

Andrey SB, Chan ML, Power WP.

J Phys Chem A. 2010 Mar 18;114(10):3457-65. doi: 10.1021/jp909899w.

PMID:
20155963
20.

Assembling amyloid fibrils from designed structures containing a significant amyloid beta-peptide fragment.

Tjernberg LO, Tjernberg A, Bark N, Shi Y, Ruzsicska BP, Bu Z, Thyberg J, Callaway DJ.

Biochem J. 2002 Aug 15;366(Pt 1):343-51.

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