메뉴 건너뛰기




Volumn 113, Issue 37, 2009, Pages 12447-12455

Cross-β-Sheet structure in amyloid fiber formation

Author keywords

[No Author keywords available]

Indexed keywords

AGGREGATES; AMINES; ATOMIC FORCE MICROSCOPY; ENERGY MANAGEMENT; FIBERS; GLYCOPROTEINS; MONOMERS; SPHERES; TRANSMISSION ELECTRON MICROSCOPY; X RAY DIFFRACTION; X RAY DIFFRACTION ANALYSIS;

EID: 70349160466     PISSN: 15206106     EISSN: None     Source Type: Journal    
DOI: 10.1021/jp903106x     Document Type: Article
Times cited : (36)

References (23)
  • 1
    • 34250779284 scopus 로고    scopus 로고
    • Aggregation drives misfolding in protein amyloid fiber formation
    • Xu, S. Aggregation drives "misfolding" in protein amyloid fiber formation. Amyloid. 2007, 14 (2), 119-131
    • (2007) Amyloid. , vol.14 , Issue.2 , pp. 119-131
    • Xu, S.1
  • 2
    • 0034951056 scopus 로고    scopus 로고
    • The assembly of amyloidogenic yeast sup35 as assessed by scanning (atomic) force microscopy: An analogy to linear colloidal aggregation
    • Xu, S.; Bevis, B.; Arnsdorf, M. F. The assembly of amyloidogenic yeast sup35 as assessed by scanning (atomic) force microscopy: an analogy to linear colloidal aggregation. Biophys. J. 2001, 87 (1), 446-454
    • (2001) Biophys. J. , vol.87 , Issue.1 , pp. 446-454
    • Xu, S.1    Bevis, B.2    Arnsdorf, M.F.3
  • 3
    • 0000134186 scopus 로고
    • Theory of the stability of strongly charged lyophobic sols and of the adhesion of strongly charged particles in solutions of electrolytes
    • URSS.
    • Derjaguin, B.; Landau., L. Theory of the stability of strongly charged lyophobic sols and of the adhesion of strongly charged particles in solutions of electrolytes. Acta Phisicochim. URSS. 1941, 14633-14662
    • (1941) Acta Phisicochim. , pp. 14633-14662
    • Derjaguin, B.1    Landau, L.2
  • 5
    • 0033170904 scopus 로고    scopus 로고
    • Formation of magnetosomes in magnetotactic bacteria
    • Schueler, D. Formation of Magnetosomes in Magnetotactic Bacteria. J. Mol. Microbiol. Biotechnol. 1999, 7 (1), 79-86.
    • (1999) J. Mol. Microbiol. Biotechnol. , vol.7 , Issue.1 , pp. 79-86
    • Schueler, D.1
  • 6
    • 4143067019 scopus 로고    scopus 로고
    • Pauling and corey's a-pleated sheet structure may define the prefibrillar amyloidogenic intermediate in amyloid disease
    • Armen, R. S.; DeMarco, M. L.; Alonso, D. O. V.; Daggett, V. Pauling and Corey's a-pleated sheet structure may define the prefibrillar amyloidogenic intermediate in amyloid disease. Proc. Natl. Acad. Sci. U.S.A. 2004, 101 (32), 11622-11627.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , Issue.32 , pp. 11622-11627
    • Armen, R.S.1    Demarco, M.L.2    Alonso, D.O.V.3    Daggett, V.4
  • 7
    • 33749857843 scopus 로고    scopus 로고
    • The toxic conformer in amyloid diseases
    • Daggett, V. Alpha-sheet: The toxic conformer in amyloid diseases. Ace. Chem. Res. 2006, 39 (9), 594-602.
    • (2006) Ace. Chem. Res. , vol.39 , Issue.9 , pp. 594-602
    • Alpha-sheet, D.V.1
  • 8
    • 0030586945 scopus 로고    scopus 로고
    • Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix
    • DOI 10.1016/S0969-2126(96)00104-9
    • (8) Blake, C.; Serpell, L. Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous beta-sheet helix. Structure. 1996, 4 (8), 989-998 (Pubitemid 26324709)
    • (1996) Structure , vol.4 , Issue.8 , pp. 989-998
    • Blake, C.1    Serpell, L.2
  • 9
    • 18844387881 scopus 로고    scopus 로고
    • A cylinder-shaped double ribbon structure formed by an amyloid hairpin peptide derived from the β-sheet of murine PrP: An X-ray and molecular dynamics simulation study
    • DOI 10.1016/j.jsb.2005.03.003, PII S1047847705000638
    • (9) Croixmarie, V.; Briki, F.; David, G; Coïc, Y.; Ovtracht, L.; Doucet, J.; Jamin, N.; Sanson, A. A cylinder-shaped double ribbon structure formed by an amyloid hairpin peptide derived from the [beta]-sheet of murine PrP: An X-ray and molecular dynamics simulation study. J. Struct. Biol. 2005, 150 (3), 284-299. (Pubitemid 40693679)
    • (2005) Journal of Structural Biology , vol.150 , Issue.3 , pp. 284-299
    • Croixmarie, V.1    Briki, F.2    David, G.3    Coic, Y.-M.4    Ovtracht, L.5    Doucet, J.6    Jamin, N.7    Sanson, A.8
  • 10
    • 0034494233 scopus 로고    scopus 로고
    • Fibers of tau fragments, but not full length tau, exhibit a cross β-structure: Implications for the formation of paired helical filaments
    • (10) Gianetti, A.; Lindwall, G.; Chau, M.; Radeke, M.; Feinstein, S.; Kohlstaedt, L. Fibers of Tau Fragments, but Not Full Length Tau, Exhibit a Cross [beta]-Structure: Implications for the Formation of Paired Helical Filaments. Protein Science 2000, 9 (12), 2427-2435. (Pubitemid 32105725)
    • (2000) Protein Science , vol.9 , Issue.12 , pp. 2427-2435
    • Giannetti, A.M.1    Lindwall, G.2    Chau, M.-F.3    Radeke, M.J.4    Feinstein, S.C.5    Kohlstaedt, L.A.6
  • 13
    • 76549238253 scopus 로고
    • The pleated sheet, a new layer configuration of polypeptide chains
    • Pauling, L.; Corey, R. The pleated sheet, a new layer configuration of polypeptide chains. Proc. Natl. Acad. Sci. U.S. A. 1951, 37251-37256
    • (1951) Proc. Natl. Acad. Sci. U.S. A. , pp. 37251-37256
    • Pauling, L.1    Corey, R.2
  • 14
    • 0036289154 scopus 로고    scopus 로고
    • The conformations of polypeptide chains where the main-chain parts of successive residues are enantiomeric. Their occurrence in cation and anion-binding regions of proteins
    • DOI 10.1006/jmbi.2001.5228
    • (14) Watson, J. D.; Milner-White, E. The conformations of polypeptide chains where the main-chain parts of successive residues are enantiomeric. Their occurrence in cation and anion-binding regions of proteins. J. Mol. Biol. 2002, 315 (2), 183-191. (Pubitemid 34722121)
    • (2002) Journal of Molecular Biology , vol.315 , Issue.2 , pp. 183-191
    • Watson, J.D.1    Milner-White, E.J.2
  • 15
    • 0035499892 scopus 로고    scopus 로고
    • Chemistry of ion coordination and hydration revealed by a K+ channelFab complex at 2.0 angstrom resolution
    • Zhou, Y.; Morais-Cabral, J. H.; Kaufman, A.; MacKinnon, R. Chemistry of ion coordination and hydration revealed by a K+ channelFab complex at 2.0 angstrom resolution. Nature. 2001, 414 (6859), 43-48.
    • (2001) Nature. , vol.414 , Issue.6859 , pp. 43-48
    • Zhou, Y.1    Morais-Cabral, J.H.2    Kaufman, A.3    MacKinnon, R.4
  • 16
    • 0035924329 scopus 로고    scopus 로고
    • Structural basis of water-specific transport through the AQP1 water channel
    • Sui, H.; Han, B.; Lee, J. K.; Walian, P.; Jap, B. K. Structural basis of water-specific transport through the AQP1 water channel. Nature. 2001, 414 (6866), 872-878.
    • (2001) Nature. , vol.414 , Issue.6866 , pp. 872-878
    • Sui, H.1    Han, B.2    Lee, J.K.3    Walian, P.4    Jap, B.K.5
  • 20
    • 0000888138 scopus 로고
    • Single crystals of poly-L-glutamic acid
    • Keith, H. Single crystals of poly-L-glutamic acid. Biopolymers. 1969, 7775-7792
    • (1969) Biopolymers. , pp. 7775-7792
    • Keith, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.