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Volumn 83, Issue 3, 2002, Pages 1268-1280

Exploring the propensities of helices in PrPC to form β sheet using NMR structures and sequence alignments

Author keywords

[No Author keywords available]

Indexed keywords

PRION PROTEIN;

EID: 0036708438     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(02)73899-X     Document Type: Article
Times cited : (94)

References (49)
  • 21
    • 0031973966 scopus 로고    scopus 로고
    • Folding type-specific secondary structure propensities of amino acids, derived from α-helical, β-sheet, α/β, and α+β proteins of known structures
    • (1998) Biopolymers , vol.45 , pp. 35-49
    • Jiang, B.1    Guo, T.2    Peng, L.W.3    Sun, Z.R.4
  • 24
    • 0033574161 scopus 로고    scopus 로고
    • Influence of amino acid substitutions related to inherited human prion diseases on the thermodynamic stability of the cellular prion protein
    • (1999) Biochemistry , vol.38 , pp. 3258-3267
    • Liemann, S.1    Glockshuber, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.