메뉴 건너뛰기




Volumn 79, Issue 1, 2011, Pages 92-98

Asymmetric amyloid fibril elongation: A new perspective on a symmetric world

Author keywords

Alzheimer's disease; Fluorescent tags; Insulin; Nucleus; Unidirectional growth

Indexed keywords

AMYLOID; INSULIN;

EID: 78649796520     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.22861     Document Type: Article
Times cited : (26)

References (30)
  • 1
    • 33750361540 scopus 로고    scopus 로고
    • A century-old debate on protein aggregation and neurodegeneration enters the clinic
    • Lansbury PT, Lashuel A. A century-old debate on protein aggregation and neurodegeneration enters the clinic. Nature 2006; 443: 774-779.
    • (2006) Nature , vol.443 , pp. 774-779
    • Lansbury, P.T.1    Lashuel, A.2
  • 2
    • 0035918550 scopus 로고    scopus 로고
    • Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism
    • Nielsen L, Khurana R, Coats A, Frokjaer S, Brange J, Vyas S, Uversky VN, Fink AL. Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism. Biochemistry 2001; 40: 6036-6046.
    • (2001) Biochemistry , vol.40 , pp. 6036-6046
    • Nielsen, L.1    Khurana, R.2    Coats, A.3    Frokjaer, S.4    Brange, J.5    Vyas, S.6    Uversky, V.N.7    Fink, A.L.8
  • 3
    • 70349318348 scopus 로고    scopus 로고
    • Time-dependent insulin oligomer reaction pathway prior to fibril formation: cooling and seeding
    • Sorci M, Grassucci RA, Hahn I, Frank J, Belfort G. Time-dependent insulin oligomer reaction pathway prior to fibril formation: cooling and seeding. Proteins 2009; 77: 62-73.
    • (2009) Proteins , vol.77 , pp. 62-73
    • Sorci, M.1    Grassucci, R.A.2    Hahn, I.3    Frank, J.4    Belfort, G.5
  • 6
    • 40849130157 scopus 로고    scopus 로고
    • Surface-enhanced nucleation of insulin amyloid fibrillation
    • Nayak A, Dutta AK, Belfort G. Surface-enhanced nucleation of insulin amyloid fibrillation. Biochem Biophys Res Commun 2008; 369: 303-307.
    • (2008) Biochem Biophys Res Commun , vol.369 , pp. 303-307
    • Nayak, A.1    Dutta, A.K.2    Belfort, G.3
  • 7
    • 70350191425 scopus 로고    scopus 로고
    • Osmolyte controlled fibrillation kinetics of insulin: new insight into fibrillation using the preferential exclusion principle
    • Nayak A, Lee CC, McRae G, Belfort G. Osmolyte controlled fibrillation kinetics of insulin: new insight into fibrillation using the preferential exclusion principle. Biotechnol Prog 2009; 25: 1508-1514.
    • (2009) Biotechnol Prog , vol.25 , pp. 1508-1514
    • Nayak, A.1    Lee, C.C.2    McRae, G.3    Belfort, G.4
  • 10
    • 59849109485 scopus 로고    scopus 로고
    • A universal pathway for amyloid nucleus and precursor formation for insulin
    • Nayak A, Sorci M, Krueger S, Belfort G. A universal pathway for amyloid nucleus and precursor formation for insulin. Proteins 2009; 74: 556-565.
    • (2009) Proteins , vol.74 , pp. 556-565
    • Nayak, A.1    Sorci, M.2    Krueger, S.3    Belfort, G.4
  • 12
    • 33646199155 scopus 로고    scopus 로고
    • Early events in insulin fibrillization studied by time-lapse atomic force microscopy
    • Podesta A, Tiana G, Milani P, Manno M. Early events in insulin fibrillization studied by time-lapse atomic force microscopy. Biophys J 2006; 90: 589-597.
    • (2006) Biophys J , vol.90 , pp. 589-597
    • Podesta, A.1    Tiana, G.2    Milani, P.3    Manno, M.4
  • 17
    • 63849293323 scopus 로고    scopus 로고
    • Interprotofilament interactions between Alzheimer's Ab1-42 peptides in amyloid fibrils revealed by cryoEM
    • Zhang R, Hu X, Khant H, Ludtke SJ, Chiu W, Schmid MF, Frieden C, Lee J-M. Interprotofilament interactions between Alzheimer's Ab1-42 peptides in amyloid fibrils revealed by cryoEM. Proc Natl Acad Sci USA 2009; 106: 4653-4658.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 4653-4658
    • Zhang, R.1    Hu, X.2    Khant, H.3    Ludtke, S.J.4    Chiu, W.5    Schmid, M.F.6    Frieden, C.7    Lee, J.8
  • 19
    • 70349466557 scopus 로고    scopus 로고
    • Effect of maghemite nanoparticles on insulin amyloid fibril formation: selective labeling, kinetics, and fibril removal by a magnetic field
    • Skaat H, Sorci M, Belfort G, Margel S. Effect of maghemite nanoparticles on insulin amyloid fibril formation: selective labeling, kinetics, and fibril removal by a magnetic field. J Biomed Mater Res A 2009: 91: 342-351.
    • (2009) J Biomed Mater Res A , vol.91 , pp. 342-351
    • Skaat, H.1    Sorci, M.2    Belfort, G.3    Margel, S.4
  • 20
    • 67649148203 scopus 로고    scopus 로고
    • Synthesis and characterization of fluorinated magnetic core-shell nanoparticles for inhibition of insulin amyloid fibril formation
    • 225106:
    • Skaat H, Belfort G, Margel S. Synthesis and characterization of fluorinated magnetic core-shell nanoparticles for inhibition of insulin amyloid fibril formation. Nanotechnology 2009; 20, 225106: 1-9.
    • (2009) Nanotechnology , vol.20 , pp. 1-9
    • Skaat, H.1    Belfort, G.2    Margel, S.3
  • 22
    • 0036233931 scopus 로고    scopus 로고
    • Origins and kinetic consequences of diversity in Sup35 yeast prion fibers
    • DePace AH, Weissman JS. Origins and kinetic consequences of diversity in Sup35 yeast prion fibers. Nat Struct Biol 2002; 9: 389-396.
    • (2002) Nat Struct Biol , vol.9 , pp. 389-396
    • DePace, A.H.1    Weissman, J.S.2
  • 23
    • 0033557842 scopus 로고    scopus 로고
    • A strategy for the generation of sufraces presenting ligands for studies of binding based on an active ester as a common reactive intermediate: a surface plasmon resonance study
    • Lahiri J, Isaacs L, Tien J, Whitesides GM. A strategy for the generation of sufraces presenting ligands for studies of binding based on an active ester as a common reactive intermediate: a surface plasmon resonance study. Anal Chem 1999; 71: 777-790.
    • (1999) Anal Chem , vol.71 , pp. 777-790
    • Lahiri, J.1    Isaacs, L.2    Tien, J.3    Whitesides, G.M.4
  • 24
    • 84860121488 scopus 로고    scopus 로고
    • Alexa Fluor® 568 Protein Labeling Kit (A10238)., Molecular Probes, Carlsbad, CA;
    • Alexa Fluor® 568 Protein Labeling Kit (A10238). Molecular Probes, Carlsbad, CA; 2004.
    • (2004)
  • 25
    • 0041935939 scopus 로고    scopus 로고
    • ImageJ
    • Bethesda, MD, U.S. National Institutes of Health;
    • Rasband WS. ImageJ. Bethesda, MD: U.S. National Institutes of Health; 1997-2009.
    • Rasband, W.S.1
  • 26
    • 66149140617 scopus 로고    scopus 로고
    • Seeded growth of β-amyloid fibrils from Alzheimer's brain-derived fibrils produces a distinct fibril structure
    • Paravastu AK, Qahwash I, Leapman RD, Meredith SC, Tycko R. Seeded growth of β-amyloid fibrils from Alzheimer's brain-derived fibrils produces a distinct fibril structure. Proc Natl Acad Sci USA 2009; 106: 7443-7448.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 7443-7448
    • Paravastu, A.K.1    Qahwash, I.2    Leapman, R.D.3    Meredith, S.C.4    Tycko, R.5
  • 27
    • 67650079178 scopus 로고    scopus 로고
    • Structurally distinct amyloid protofibrils form on separate pathways of aggregation of a small protein
    • Kumar S, Udgaonkar JB. Structurally distinct amyloid protofibrils form on separate pathways of aggregation of a small protein. Biochemistry 2009; 48: 6441-6449.
    • (2009) Biochemistry , vol.48 , pp. 6441-6449
    • Kumar, S.1    Udgaonkar, J.B.2
  • 28
    • 75749107767 scopus 로고    scopus 로고
    • The free-energy landscape of clusters of attractive hard spheres
    • Meng G, Arkus N, Brenner MP, Manoharan VN. The free-energy landscape of clusters of attractive hard spheres. Science 2010; 327: 560-563.
    • (2010) Science , vol.327 , pp. 560-563
    • Meng, G.1    Arkus, N.2    Brenner, M.P.3    Manoharan, V.N.4
  • 29
    • 33749836310 scopus 로고    scopus 로고
    • Direct observation of amyloid fibril growth, propagation, and adaptation
    • Ban T, Yamaguchi K, Goto Y. Direct observation of amyloid fibril growth, propagation, and adaptation. Acc Chem Res 2006; 39: 663-670.
    • (2006) Acc Chem Res , vol.39 , pp. 663-670
    • Ban, T.1    Yamaguchi, K.2    Goto, Y.3
  • 30
    • 77749308383 scopus 로고    scopus 로고
    • Amyloid oligomers: spectroscopic characterization of amyloidogenic protein states
    • Lindgren M, Hammarstrom P. Amyloid oligomers: spectroscopic characterization of amyloidogenic protein states. FEBS J 2010; 277: 1380-1388.
    • (2010) FEBS J , vol.277 , pp. 1380-1388
    • Lindgren, M.1    Hammarstrom, P.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.