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2. Distinct morphological and electrophysiological properties of an elk prion peptide. Glaves JP; Gorski PA; Alier K; Ma L; Renault L; Primeau JO; Jhamandas JH; Young HS Peptides; 2013 Feb; 40():49-56. PubMed ID: 23262353 [TBL] [Abstract][Full Text] [Related]
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8. Ab initio structure determination from prion nanocrystals at atomic resolution by MicroED. Sawaya MR; Rodriguez J; Cascio D; Collazo MJ; Shi D; Reyes FE; Hattne J; Gonen T; Eisenberg DS Proc Natl Acad Sci U S A; 2016 Oct; 113(40):11232-11236. PubMed ID: 27647903 [TBL] [Abstract][Full Text] [Related]
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11. Molecular dynamics studies on the NMR and X-ray structures of rabbit prion proteins. Zhang J; Zhang Y J Theor Biol; 2014 Feb; 342():70-82. PubMed ID: 24184221 [TBL] [Abstract][Full Text] [Related]
12. X-ray diffraction and far-UV CD studies of filaments formed by a leucine-rich repeat peptide: structural similarity to the amyloid fibrils of prions and Alzheimer's disease beta-protein. Symmons MF; Buchanan SG; Clarke DT; Jones G; Gay NJ FEBS Lett; 1997 Jul; 412(2):397-403. PubMed ID: 9256259 [TBL] [Abstract][Full Text] [Related]
14. A cylinder-shaped double ribbon structure formed by an amyloid hairpin peptide derived from the beta-sheet of murine PrP: an X-ray and molecular dynamics simulation study. Croixmarie V; Briki F; David G; Coïc YM; Ovtracht L; Doucet J; Jamin N; Sanson A J Struct Biol; 2005 Jun; 150(3):284-99. PubMed ID: 15890277 [TBL] [Abstract][Full Text] [Related]
15. Cryo-EM structure of anchorless RML prion reveals variations in shared motifs between distinct strains. Hoyt F; Standke HG; Artikis E; Schwartz CL; Hansen B; Li K; Hughson AG; Manca M; Thomas OR; Raymond GJ; Race B; Baron GS; Caughey B; Kraus A Nat Commun; 2022 Jul; 13(1):4005. PubMed ID: 35831291 [TBL] [Abstract][Full Text] [Related]
16. 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]
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20. Secondary-structure prediction revisited: Theoretical β-sheet propensity and coil propensity represent structures of amyloids and aid in elucidating phenomena involved in interspecies transmission of prions. Taguchi Y; Nishida N PLoS One; 2017; 12(2):e0171974. PubMed ID: 28199368 [TBL] [Abstract][Full Text] [Related] [Next] [New Search]