메뉴 건너뛰기




Volumn 149, Issue 2, 2005, Pages 213-218

Association of thin filaments into thick filaments revealing the structural hierarchy of amyloid fibrils

Author keywords

2 Microglobulin; Amyloid fibril; Atomic force microscopy; Trifluoroethanol

Indexed keywords

AMYLOID; SOLVENT;

EID: 12844260879     PISSN: 10478477     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jsb.2004.11.008     Document Type: Article
Times cited : (18)

References (21)
  • 2
    • 0347357617 scopus 로고    scopus 로고
    • Protein folding and misfolding
    • C.M. Dobson Protein folding and misfolding Nature 426 2003 884 889
    • (2003) Nature , vol.426 , pp. 884-889
    • Dobson, C.M.1
  • 3
    • 0035187228 scopus 로고    scopus 로고
    • Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from HypF N-terminal domain
    • F. Chiti, M. Bucciantini, C. Apanni, N. Taddei, C.M. Dobson, and M. Stefani Solution conditions can promote formation of either amyloid protofilaments or mature fibrils from HypF N-terminal domain J. Protein Sci. 10 2001 2541 2547
    • (2001) J. Protein Sci. , vol.10 , pp. 2541-2547
    • Chiti, F.1    Bucciantini, M.2    Apanni, C.3    Taddei, N.4    Dobson, C.M.5    Stefani, M.6
  • 4
    • 0037020259 scopus 로고    scopus 로고
    • Kinetic studies of amyloid β-protein fibril assembly. Differential effects of α-helix stabilization
    • Y. Fezoui, and D.B. Teplow Kinetic studies of amyloid β-protein fibril assembly. Differential effects of α-helix stabilization J. Biol. Chem. 277 2002 36948 36954
    • (2002) J. Biol. Chem. , vol.277 , pp. 36948-36954
    • Fezoui, Y.1    Teplow, D.B.2
  • 5
    • 0031444010 scopus 로고    scopus 로고
    • Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-β protein
    • J.D. Harper, C.M. Lieber, and P.T. Lansbury Jr. Atomic force microscopic imaging of seeded fibril formation and fibril branching by the Alzheimer's disease amyloid-β protein Chem. Biol. 4 1997 951 959
    • (1997) Chem. Biol. , vol.4 , pp. 951-959
    • Harper, J.D.1    Lieber, C.M.2    Lansbury Jr., P.T.3
  • 6
    • 0032536194 scopus 로고    scopus 로고
    • Group additive contributions to the alcohol-induced α-helix formation of melittin: Implication for the mechanism of the alcohol effects on proteins
    • N. Hirota, K. Mizuno, and Y. Goto Group additive contributions to the alcohol-induced α-helix formation of melittin: implication for the mechanism of the alcohol effects on proteins J. Mol. Biol. 275 1998 365 378
    • (1998) J. Mol. Biol. , vol.275 , pp. 365-378
    • Hirota, N.1    Mizuno, K.2    Goto, Y.3
  • 7
    • 0042821622 scopus 로고    scopus 로고
    • Dissolution of β2-microglobulin amyloid fibrils by dimethyl sulfoxide
    • N. Hirota-Nakaoka, K. Hasegawa, H. Naiki, and Y. Goto Dissolution of β2-microglobulin amyloid fibrils by dimethyl sulfoxide J. Biochem. 134 2003 159 164
    • (2003) J. Biochem. , vol.134 , pp. 159-164
    • Hirota-Nakaoka, N.1    Hasegawa, K.2    Naiki, H.3    Goto, Y.4
  • 13
    • 0000079910 scopus 로고    scopus 로고
    • Establishment of a kinetic model of dialysis-related amyloid fibril extension in vitro
    • H. Naiki, N. Hashimoto, S. Suzuki, H. Kimura, K. Nakakuki, and F. Gejyo Establishment of a kinetic model of dialysis-related amyloid fibril extension in vitro Amyloid 4 1997 223 232
    • (1997) Amyloid , vol.4 , pp. 223-232
    • Naiki, H.1    Hashimoto, N.2    Suzuki, S.3    Kimura, H.4    Nakakuki, K.5    Gejyo, F.6
  • 15
    • 0034636976 scopus 로고    scopus 로고
    • Solution conformation and amyloid-like fibril formation of a polar peptide derived from a beta-hairpin in the OspA single-layer beta-sheet
    • S. Ohnishi, A. Koide, and S. Koide Solution conformation and amyloid-like fibril formation of a polar peptide derived from a beta-hairpin in the OspA single-layer beta-sheet J. Mol. Biol. 301 2000 477 489
    • (2000) J. Mol. Biol. , vol.301 , pp. 477-489
    • Ohnishi, S.1    Koide, A.2    Koide, S.3
  • 18
    • 0038043276 scopus 로고    scopus 로고
    • Amyloid-like fibril formation in an all β-barrel protein. Partially structured intermediate state(s) is a precursor for fibril formation
    • S. Srisailam, T.K. Kumar, D. Rajalingam, K.M. Kathir, H.S. Sheu, F.J. Jan, P.C. Chao, and C. Yu Amyloid-like fibril formation in an all β-barrel protein. Partially structured intermediate state(s) is a precursor for fibril formation J. Biol. Chem. 278 2003 17701 17709
    • (2003) J. Biol. Chem. , vol.278 , pp. 17701-17709
    • Srisailam, S.1    Kumar, T.K.2    Rajalingam, D.3    Kathir, K.M.4    Sheu, H.S.5    Jan, F.J.6    Chao, P.C.7    Yu, C.8
  • 19
    • 0037465708 scopus 로고    scopus 로고
    • Insight into the amyloid folding problem from solid-state NMR
    • R. Tycko Insight into the amyloid folding problem from solid-state NMR Biochemistry 42 2003 3151 3159
    • (2003) Biochemistry , vol.42 , pp. 3151-3159
    • Tycko, R.1
  • 20
    • 2342569618 scopus 로고    scopus 로고
    • Conformational constraints for amyloid fibrillation: The importance of being unfolded
    • V.N. Uversky, and A.L. Fink Conformational constraints for amyloid fibrillation: the importance of being unfolded Biochim. Biophys. Acta 1698 2004 131 153
    • (2004) Biochim. Biophys. Acta , vol.1698 , pp. 131-153
    • Uversky, V.N.1    Fink, A.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.