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Volumn 17, Issue 6, 2008, Pages 1102-1105

Distinguishing the cross-β spine arrangements in amyloid fibrils using FRET analysis

Author keywords

Amyloid fibril; Classification; Cross ; FRET; Structure elucidation

Indexed keywords

AMYLOID;

EID: 44349091002     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.083475108     Document Type: Article
Times cited : (12)

References (8)
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  • 2
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  • 5
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    • Solid-state NMR study of amyloid nanocrystals and fibrils formed by the peptide GNNQQNY from yeast prion protein Sup35p
    • van der Wel, P.C., Lewandowski, J.R., and Griffin, R.G. 2007. Solid-state NMR study of amyloid nanocrystals and fibrils formed by the peptide GNNQQNY from yeast prion protein Sup35p. J. Am. Chem. Soc. 129: 5117-5130.
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    • Probing the cross-β core structure of amyloid fibrils by hydrogen-deuterium exchange deep ultraviolet resonance Raman spectroscopy
    • Xu, M., Shashilov, V., and Lednev, I.K. 2007. Probing the cross-β core structure of amyloid fibrils by hydrogen-deuterium exchange deep ultraviolet resonance Raman spectroscopy. J. Am. Chem. Soc. 129: 11002-11003.
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.