메뉴 건너뛰기




Volumn 736, Issue , 2011, Pages 81-95

Atomic force microscopy of ex vivo amyloid fibrils

Author keywords

AFM; Aggregation; Amyloid; Fibrillogenesis

Indexed keywords

AMYLOID; APOLIPOPROTEIN A1; BETA 2 MICROGLOBULIN; COLLAGEN; LEUCINE; SERINE; ALUMINUM SILICATE; APOLIPOPROTEIN; MICA; RECOMBINANT PROTEIN;

EID: 80054835218     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-61779-105-5_6     Document Type: Chapter
Times cited : (4)

References (25)
  • 1
    • 0035237310 scopus 로고    scopus 로고
    • Protein folding and its links with human disease
    • Dobson, C.M. (2001) Protein folding and its links with human disease. Biochem. Soc. Symp. 68, 1–26.
    • (2001) Biochem. Soc. Symp. , vol.68 , pp. 1-26
    • Dobson, C.M.1
  • 2
    • 0031056829 scopus 로고    scopus 로고
    • Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis
    • Booth, D. R., Sunde, M., Bellotti, V., Robinson, C. V., Hutchinson, W. L., Fraser, P. E. (1997) Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis. Nature 385, 787–793.
    • (1997) Nature , vol.385 , pp. 787-793
    • Booth, D.R.1    Sunde, M.2    Bellotti, V.3    Robinson, C.V.4    Hutchinson, W.L.5    Fraser, P.E.6
  • 3
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti, F. and Dobson, C.M. (2006) Protein misfolding, functional amyloid, and human disease. Annu Rev Biochem 75, 333–366.
    • (2006) Annu Rev Biochem , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 9
    • 34249041646 scopus 로고    scopus 로고
    • Metal ions differentially influence the aggregation and deposition of Alzheimer’s β-amyloid on a solid template
    • Ha, C., Ryu, J. and Park, C.B. (2007) Metal ions differentially influence the aggregation and deposition of Alzheimer’s β-amyloid on a solid template. Biochemistry 46, 6118–6125.
    • (2007) Biochemistry , vol.46 , pp. 6118-6125
    • Ha, C.1    Ryu, J.2    Park, C.B.3
  • 12
    • 4344678675 scopus 로고    scopus 로고
    • Ultrastructural organization of ex vivo amyloid fibrils formed by the apolipoprotein A-I Leu174Ser variant: An atomic force microscopy study
    • Relini, A., Rolandi, R., Bolognesi, M., Aboudan, M., Merlini, G., Bellotti, V., Gliozzi, A. (2004) Ultrastructural organization of ex vivo amyloid fibrils formed by the apolipoprotein A-I Leu174Ser variant: an atomic force microscopy study. Biochim. Biophys. Acta 1690, 33–41.
    • (2004) Biochim. Biophys. Acta , vol.1690 , pp. 33-41
    • Relini, A.1    Rolandi, R.2    Bolognesi, M.3    Aboudan, M.4    Merlini, G.5    Bellotti, V.6    Gliozzi, A.7
  • 14
    • 0035367287 scopus 로고    scopus 로고
    • Kidney dialysis-associated amyloidosis: A molecular role for copper in fiber formation
    • Morgan, C. J., Gelfand, M., Atreya, C., and Miranker, A. D. (2001) Kidney dialysis-associated amyloidosis: a molecular role for copper in fiber formation. J. Mol. Biol. 309, 339–345.
    • (2001) J. Mol. Biol. , vol.309 , pp. 339-345
    • Morgan, C.J.1    Gelfand, M.2    Atreya, C.3    Miranker, A.D.4
  • 15
    • 27744454828 scopus 로고    scopus 로고
    • Historical background and clinical treatment of dialysis-related amyloidosis
    • Yamamoto, S, Gejyo, F. (2005) Historical background and clinical treatment of dialysis-related amyloidosis. Biochim. Biophys. Acta 1753, 4–10.
    • (2005) Biochim. Biophys. Acta , vol.1753 , pp. 4-10
    • Yamamoto, S.1    Gejyo, F.2
  • 16
    • 15744386870 scopus 로고    scopus 로고
    • Seeding-dependent maturation of beta2-microglobulin amyloid fibrils at neutral pH
    • Kihara, M., Chatani, E., Sakai, M., Hasegawa, K., Naiki, H., and Goto, Y. (2005) Seeding-dependent maturation of beta2-microglobulin amyloid fibrils at neutral pH. J. Biol. Chem. 280, 12012–12018.
    • (2005) J. Biol. Chem. , vol.280 , pp. 12012-12018
    • Kihara, M.1    Chatani, E.2    Sakai, M.3    Hasegawa, K.4    Naiki, H.5    Goto, Y.6
  • 17
  • 18
    • 0030050003 scopus 로고    scopus 로고
    • Beta-2-microglobulin-associated amyloidosis
    • Floege,J, and Ehlerding, G. (1996) Beta-2-microglobulin-associated amyloidosis. Nephron. 72, 9–26.
    • (1996) Nephron , vol.72 , pp. 9-26
    • Floege, J.1    Ehlerding, G.2
  • 21
    • 0032048837 scopus 로고    scopus 로고
    • Tip characterization from AFM images of nanometric spherical particles
    • Ramirez-Aguilar, K.A., Rowlen, K.L. (1998) Tip characterization from AFM images of nanometric spherical particles, Langmuir 14, 2562–2566.
    • (1998) Langmuir , vol.14 , pp. 2562-2566
    • Ramirez-Aguilar, K.A.1    Rowlen, K.L.2
  • 25
    • 85059868153 scopus 로고    scopus 로고
    • Markiewicz, P. http://www.weizmann.ac.il/Chemical_Research_Support/surflab/peter/standard/index.htm.
    • Markiewicz, P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.