213 related articles for article (PubMed ID: 17017802)
1. 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; 128(40):13224-8. PubMed ID: 17017802
[TBL] [Abstract][Full Text] [Related]
2. 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; 10(10):1657-65. PubMed ID: 19504509
[TBL] [Abstract][Full Text] [Related]
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; 129(16):5117-30. PubMed ID: 17397156
[TBL] [Abstract][Full Text] [Related]
4. 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; 319(5869):1523-6. PubMed ID: 18339938
[TBL] [Abstract][Full Text] [Related]
5. 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; 405(3):765-72. PubMed ID: 21094164
[TBL] [Abstract][Full Text] [Related]
6. The molecular organization of the fungal prion HET-s in its amyloid form.
Wasmer C; Schütz A; Loquet A; Buhtz C; Greenwald J; Riek R; Böckmann A; Meier BH
J Mol Biol; 2009 Nov; 394(1):119-27. PubMed ID: 19748509
[TBL] [Abstract][Full Text] [Related]
7. 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; 114(10):3457-65. PubMed ID: 20155963
[TBL] [Abstract][Full Text] [Related]
8. Structural similarity between the prion domain of HET-s and a homologue can explain amyloid cross-seeding in spite of limited sequence identity.
Wasmer C; Zimmer A; Sabaté R; Soragni A; Saupe SJ; Ritter C; Meier BH
J Mol Biol; 2010 Sep; 402(2):311-25. PubMed ID: 20600104
[TBL] [Abstract][Full Text] [Related]
9. 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; 378(5):1142-54. PubMed ID: 18423487
[TBL] [Abstract][Full Text] [Related]
10. 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; 16(18):5492-9. PubMed ID: 20358555
[TBL] [Abstract][Full Text] [Related]
11. High-resolution solid-state NMR spectroscopy of the prion protein HET-s in its amyloid conformation.
Siemer AB; Ritter C; Ernst M; Riek R; Meier BH
Angew Chem Int Ed Engl; 2005 Apr; 44(16):2441-4. PubMed ID: 15770629
[No Abstract] [Full Text] [Related]
12. Solid-state NMR spectroscopy reveals that E. coli inclusion bodies of HET-s(218-289) are amyloids.
Wasmer C; Benkemoun L; Sabaté R; Steinmetz MO; Coulary-Salin B; Wang L; Riek R; Saupe SJ; Meier BH
Angew Chem Int Ed Engl; 2009; 48(26):4858-60. PubMed ID: 19472238
[TBL] [Abstract][Full Text] [Related]
13. Conformational transition occurring upon amyloid aggregation of the HET-s prion protein of Podospora anserina analyzed by hydrogen/deuterium exchange and mass spectrometry.
Nazabal A; Dos Reis S; Bonneu M; Saupe SJ; Schmitter JM
Biochemistry; 2003 Jul; 42(29):8852-61. PubMed ID: 12873146
[TBL] [Abstract][Full Text] [Related]
14. The sequences appended to the amyloid core region of the HET-s prion protein determine higher-order aggregate organization in vivo.
Balguerie A; Dos Reis S; Coulary-Salin B; Chaignepain S; Sabourin M; Schmitter JM; Saupe SJ
J Cell Sci; 2004 May; 117(Pt 12):2599-610. PubMed ID: 15159455
[TBL] [Abstract][Full Text] [Related]
15. Characterization of beta-sheet structure in Ure2p1-89 yeast prion fibrils by solid-state nuclear magnetic resonance.
Baxa U; Wickner RB; Steven AC; Anderson DE; Marekov LN; Yau WM; Tycko R
Biochemistry; 2007 Nov; 46(45):13149-62. PubMed ID: 17953455
[TBL] [Abstract][Full Text] [Related]
16. Energy barriers for HET-s prion forming domain amyloid formation.
Sabaté R; Castillo V; Espargaró A; Saupe SJ; Ventura S
FEBS J; 2009 Sep; 276(18):5053-64. PubMed ID: 19682303
[TBL] [Abstract][Full Text] [Related]
17. Domain organization and structure-function relationship of the HET-s prion protein of Podospora anserina.
Balguerie A; Dos Reis S; Ritter C; Chaignepain S; Coulary-Salin B; Forge V; Bathany K; Lascu I; Schmitter JM; Riek R; Saupe SJ
EMBO J; 2003 May; 22(9):2071-81. PubMed ID: 12727874
[TBL] [Abstract][Full Text] [Related]
18. Absolute structural constraints on amyloid fibrils from solid-state NMR spectroscopy of partially oriented samples.
Oyler NA; Tycko R
J Am Chem Soc; 2004 Apr; 126(14):4478-9. PubMed ID: 15070340
[TBL] [Abstract][Full Text] [Related]
19. Core structure of amyloid fibrils formed by residues 106-126 of the human prion protein.
Walsh P; Simonetti K; Sharpe S
Structure; 2009 Mar; 17(3):417-26. PubMed ID: 19278656
[TBL] [Abstract][Full Text] [Related]
20. High-resolution H/D exchange studies on the HET-s218-295 prion protein.
Nazabal A; Bonneu M; Saupe SJ; Schmitter JM
J Mass Spectrom; 2005 May; 40(5):580-90. PubMed ID: 15856424
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
