메뉴 건너뛰기




Volumn 106, Issue 49, 2009, Pages 20555-20556

Inconvenient facts about pathological amyloid fibrils

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID;

EID: 73949137636     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0910978107     Document Type: Note
Times cited : (10)

References (20)
  • 1
    • 73949117777 scopus 로고    scopus 로고
    • Comparison of Alzheimer's Aβ(1-40) and Aβ(1-42) amyloid fibrils reveals similar protofilament structures
    • Schmidt M, et al. (2009) Comparison of Alzheimer's Aβ(1-40) and Aβ(1-42) amyloid fibrils reveals similar protofilament structures. Proc Natl Acad Sci USA 106:19813-19818.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 19813-19818
    • Schmidt, M.1
  • 2
    • 33750017513 scopus 로고    scopus 로고
    • Molecular structure of amyloid fibrils: Insights from solid-state NMR
    • Tycko R (2006) Molecular structure of amyloid fibrils: Insights from solid-state NMR. Q Rev Biophys 39:1-55.
    • (2006) Q Rev Biophys , vol.39 , pp. 1-55
    • Tycko, R.1
  • 3
    • 44949250850 scopus 로고    scopus 로고
    • Paired β-sheet structure of an Aβ(1-40) amyloid fibril revealed by electron microscopy
    • Sachse C, Fandrich M, Grigorieff N (2008) Paired β-sheet structure of an Aβ(1-40) amyloid fibril revealed by electron microscopy. Proc Natl Acad Sci USA 105:7462-7466.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 7462-7466
    • Sachse, C.1    Fandrich, M.2    Grigorieff, N.3
  • 4
    • 0001266102 scopus 로고
    • Athree-dimensional model of the myoglobin molecule obtained by X-ray analysis
    • Kendrew JC, et al. (1958)Athree-dimensional model of the myoglobin molecule obtained by X-ray analysis. Nature 181:662-666.
    • (1958) Nature , vol.181 , pp. 662-666
    • Kendrew, J.C.1
  • 5
    • 0001419932 scopus 로고
    • The X-ray interpretation of denaturation of the seed globulins
    • Astbury WT, Dickinson S, Bailey K (1935) The X-ray interpretation of denaturation of the seed globulins. Biochem J 29:2351-2360.
    • (1935) Biochem J , vol.29 , pp. 2351-2360
    • Astbury, W.T.1    Dickinson, S.2    Bailey, K.3
  • 6
    • 0012809642 scopus 로고
    • The silk of the egg stalk of the green lace-wing fly: Structure of the silk of Chrysopa egg stalks
    • RudallKM
    • Parker KD, RudallKM(1957) The silk of the egg stalk of the green lace-wing fly: Structure of the silk of Chrysopa egg stalks. Nature 179:905-906.
    • (1957) Nature , vol.179 , pp. 905-906
    • Parker, K.D.1
  • 7
    • 85085674564 scopus 로고    scopus 로고
    • Geddes AJ, Parker KD, Atkins EDT, Beighton E (1968) Cross-β conformation in proteins. J Mol Biol 32:343-344.
    • Geddes AJ, Parker KD, Atkins EDT, Beighton E (1968) "Cross-β" conformation in proteins. J Mol Biol 32:343-344.
  • 9
    • 70350245040 scopus 로고    scopus 로고
    • Fifty years later: The sequence, structure, and function of lacewing cross-beta silk
    • Weisman S, et al. (2009) Fifty years later: The sequence, structure, and function of lacewing cross-beta silk. J Struct Biol 168:467-475.
    • (2009) J Struct Biol , vol.168 , pp. 467-475
    • Weisman, S.1
  • 10
    • 0014351967 scopus 로고
    • X-ray diffraction studies on amyloid filaments
    • Eanes E, Glenner G (1968) X-ray diffraction studies on amyloid filaments. J Histochem Cytochem 16:673-677.
    • (1968) J Histochem Cytochem , vol.16 , pp. 673-677
    • Eanes, E.1    Glenner, G.2
  • 11
    • 0014578835 scopus 로고
    • Characterization of the amyloid fibril as a cross-β protein
    • SkinnerM
    • Bonnar I, Cohen AS, SkinnerM(1969) Characterization of the amyloid fibril as a cross-β protein. Proc Soc Exp Biol Med 131:1373-1375.
    • (1969) Proc Soc Exp Biol Med , vol.131 , pp. 1373-1375
    • Bonnar, I.1    Cohen, A.S.2
  • 12
    • 0008465437 scopus 로고
    • A mechanism for the formation of fibrils from protein molecules
    • Waugh DF (1957) A mechanism for the formation of fibrils from protein molecules. J Cell Comp Physiol 49:145-164.
    • (1957) J Cell Comp Physiol , vol.49 , pp. 145-164
    • Waugh, D.F.1
  • 13
    • 0000237715 scopus 로고
    • An X-ray diffraction investigation of selected types of insulin fibrils
    • Koltun WL,Waugh DF, Bear RS (1954) An X-ray diffraction investigation of selected types of insulin fibrils. J Am Chem Soc 76:413-417.
    • (1954) J Am Chem Soc , vol.76 , pp. 413-417
    • Koltun, W.L.1    Waugh, D.F.2    Bear, R.S.3
  • 14
    • 0003336652 scopus 로고
    • Self-control of self-assembly
    • Caspar DLD (1991) Self-control of self-assembly. Curr Biol 1:30-32.
    • (1991) Curr Biol , vol.1 , pp. 30-32
    • Caspar, D.L.D.1
  • 15
    • 0014413819 scopus 로고
    • A kinetic study of in vitro polymerization of flagellin
    • Asakura S (1968) A kinetic study of in vitro polymerization of flagellin. J Mol Biol 35:237-239.
    • (1968) J Mol Biol , vol.35 , pp. 237-239
    • Asakura, S.1
  • 16
    • 40849120669 scopus 로고    scopus 로고
    • Amyloid fibrils of the HET-s(218-289) prion form a β solenoid with a triangular hydrophobic core
    • Wasmer C, et al. (2008) Amyloid fibrils of the HET-s(218-289) prion form a β solenoid with a triangular hydrophobic core. Science 319:1523-1526.
    • (2008) Science , vol.319 , pp. 1523-1526
    • Wasmer, C.1
  • 19
    • 70449584579 scopus 로고    scopus 로고
    • 2D IR provides evidence for mobile water molecules in β-amyloid fibrils
    • Kim YS, Liu L, Axelsen PH, Hochstrasser RM (2009) 2D IR provides evidence for mobile water molecules in β-amyloid fibrils. Proc Natl Acad Sci USA 106:17751-17756.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 17751-17756
    • Kim, Y.S.1    Liu, L.2    Axelsen, P.H.3    Hochstrasser, R.M.4
  • 20
    • 49149124343 scopus 로고    scopus 로고
    • Amyloid-β protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory
    • Shankar GM, et al. (2008) Amyloid-β protein dimers isolated directly from Alzheimer's brains impair synaptic plasticity and memory. Nat Med 14:837-842.
    • (2008) Nat Med , vol.14 , pp. 837-842
    • Shankar, G.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.