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Volumn 256, Issue 19-20, 2012, Pages 2175-2187

Coordination of redox active metal ions to the amyloid precursor protein and to amyloid-β peptides involved in Alzheimer disease. Part 2: Dependence of Cu(II) binding sites with Aβ sequences

Author keywords

Amyloid; Copper bioinorganic chemistry; EPR HYSCORE NMR; Mutations; Truncations

Indexed keywords


EID: 84864564804     PISSN: 00108545     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ccr.2012.03.034     Document Type: Review
Times cited : (130)

References (94)
  • 2
    • 84864560360 scopus 로고    scopus 로고
    • Coord. Chem. Rev., in this issue
    • C. Hureau, Coord. Chem. Rev., in this issue.
    • Hureau, C.1
  • 74
    • 84864534503 scopus 로고    scopus 로고
    • Note. Proportions between components I and II are modified between the Cu complexes of the unlabeled Aβ1-16 and the 15N and 13C labeled peptides varying for approximately 70:30 in the case of Aβ1-16 to 50:50 in the case of the (15N-His6,13,14)Aβ peptide [48]. This is inconsistent. Indeed, labeling should no
    • Note. Proportions between components I and II are modified between the Cu complexes of the unlabeled Aβ1-16 and the 15N and 13C labeled peptides varying for approximately 70:30 in the case of Aβ1-16 to 50:50 in the case of the (15N-His6,13,14)Aβ peptide [48]. This is inconsistent. Indeed, labeling should not affect the proportion between I and II. Neither could the recording frequency. However, it is also observed that the proportion between I and II is modified between the EPR spectra recorded at S-band and X-band. Such changes may be linked to freezing procedure.


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.