메뉴 건너뛰기




Volumn 1345, Issue , 2016, Pages 299-312

Preparation of amyloid fibrils seeded from brain and meninges

Author keywords

Alzheimer s disease; Cerebral amyloid angiopathy; Fibril polymorphism; Fibril structure; Neuritic plaques; Protein aggregation; Protein aggregation diseases; Solid state NMR; Amyloid

Indexed keywords

AMYLOID; AMYLOID BETA PROTEIN; AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42];

EID: 84943737492     PISSN: 10643745     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4939-2978-8_20     Document Type: Chapter
Times cited : (10)

References (21)
  • 1
    • 12244249201 scopus 로고    scopus 로고
    • Self-propagating, molecular-level polymorphism in Alzheimer’s β-amyloid fibrils
    • Petkova AT, Leapman RD, Guo ZH, Yau WM, Mattson MP, Tycko R (2005) Self-propagating, molecular-level polymorphism in Alzheimer’s β-amyloid fibrils. Science 307:262-265
    • (2005) Science , vol.307 , pp. 262-265
    • Petkova, A.T.1    Leapman, R.D.2    Guo, Z.H.3    Yau, W.M.4    Mattson, M.P.5    Tycko, R.6
  • 3
    • 84908675131 scopus 로고    scopus 로고
    • Physical and structural basis for polymorphism in amyloid fibrils
    • Tycko R (2014) Physical and structural basis for polymorphism in amyloid fibrils. Protein Sci 23:1528-1539
    • (2014) Protein Sci , vol.23 , pp. 1528-1539
    • Tycko, R.1
  • 4
    • 79953765150 scopus 로고    scopus 로고
    • Solid-state NMR studies of amyloid fi bril structure
    • Tycko R (2011) Solid-state NMR studies of amyloid fi bril structure. Annu Rev Phys Chem 62:279-299
    • (2011) Annu Rev Phys Chem , vol.62 , pp. 279-299
    • Tycko, R.1
  • 5
    • 30744433878 scopus 로고    scopus 로고
    • Experimental constraints on quaternary structure in Alzheimer’s β-amyloid fibrils
    • Petkova AT, Yau WM, Tycko R (2006) Experimental constraints on quaternary structure in Alzheimer’s β-amyloid fibrils. Biochemistry 45:498-512
    • (2006) Biochemistry , vol.45 , pp. 498-512
    • Petkova, A.T.1    Yau, W.M.2    Tycko, R.3
  • 7
    • 57449091884 scopus 로고    scopus 로고
    • Molecular structural basis for polymorphism in Alzheimer’s β-amyloid fibrils
    • Paravastu AK, Leapman RD, Yau WM, Tycko R (2008) Molecular structural basis for polymorphism in Alzheimer’s β-amyloid fibrils. Proc Natl Acad Sci U S A 105: 18349-18354
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 18349-18354
    • Paravastu, A.K.1    Leapman, R.D.2    Yau, W.M.3    Tycko, R.4
  • 8
    • 24644447303 scopus 로고    scopus 로고
    • Seeding-dependent propagation and maturation of amyloid fibril conformation
    • Yamaguchi K, Takahashi S, Kawai T, Naiki H, Goto Y (2005) Seeding-dependent propagation and maturation of amyloid fibril conformation. J Mol Biol 352:952-960
    • (2005) J Mol Biol , vol.352 , pp. 952-960
    • Yamaguchi, K.1    Takahashi, S.2    Kawai, T.3    Naiki, H.4    Goto, Y.5
  • 9
    • 84888594143 scopus 로고    scopus 로고
    • Biology and genetics of prions causing neurodegeneration
    • Prusiner SB (2013) Biology and genetics of prions causing neurodegeneration. Annu Rev Genet 47:601-623
    • (2013) Annu Rev Genet , vol.47 , pp. 601-623
    • Prusiner, S.B.1
  • 10
    • 79953245314 scopus 로고    scopus 로고
    • Amyloid structure: Conformational diversity and consequences
    • Toyama BH, Weissman JS (2011) Amyloid structure: conformational diversity and consequences. Annu Rev Biochem 80:557-585
    • (2011) Annu Rev Biochem , vol.80 , pp. 557-585
    • Toyama, B.H.1    Weissman, J.S.2
  • 11
    • 84874639389 scopus 로고    scopus 로고
    • Molecular structures of amyloid and prion fibrils: Consensus versus controversy
    • Tycko R, Wickner RB (2013) Molecular structures of amyloid and prion fibrils: consensus versus controversy. Acc Chem Res 46:1487-1496
    • (2013) Acc Chem Res , vol.46 , pp. 1487-1496
    • Tycko, R.1    Wickner, R.B.2
  • 12
    • 66149140617 scopus 로고    scopus 로고
    • Seeded growth of β-amyloid fibrils from Alzheimer's brainderived fibrils produces a distinct fibril structure
    • Paravastu AK, Qahwash I, Leapman RD, Meredith SC, Tycko R (2009) Seeded growth of β-amyloid fibrils from Alzheimer's brainderived fibrils produces a distinct fibril structure. Proc Natl Acad Sci U S A 106:7443-7448
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 7443-7448
    • Paravastu, A.K.1    Qahwash, I.2    Leapman, R.D.3    Meredith, S.C.4    Tycko, R.5
  • 13
    • 84884217594 scopus 로고    scopus 로고
    • Molecular structure of β-amyloid fibrils in Alzheimer's disease brain tissue
    • Lu JX, Qiang W, Yau WM, Schwieters CD, Meredith SC, Tycko R (2013) Molecular structure of β-amyloid fibrils in Alzheimer's disease brain tissue. Cell 154:1257-1268
    • (2013) Cell , vol.154 , pp. 1257-1268
    • Lu, J.X.1    Qiang, W.2    Yau, W.M.3    Schwieters, C.D.4    Meredith, S.C.5    Tycko, R.6
  • 14
    • 0032879666 scopus 로고    scopus 로고
    • Isolation of amyloid deposits from brain
    • Roher AE, Kuo YM (1999) Isolation of amyloid deposits from brain. Methods Enzymol 309:58-67
    • (1999) Methods Enzymol , vol.309 , pp. 58-67
    • Roher, A.E.1    Kuo, Y.M.2
  • 17
    • 17644397372 scopus 로고    scopus 로고
    • Aβ40-lactam(D23/ K28) models a conformation highly favorable for nucleation of amyloid
    • Sciarretta KL, Gordon DJ, Petkova AT, Tycko R, Meredith SC (2005) Aβ40-lactam(D23/ K28) models a conformation highly favorable for nucleation of amyloid. Biochemistry 44:6003-6014
    • (2005) Biochemistry , vol.44 , pp. 6003-6014
    • Sciarretta, K.L.1    Gordon, D.J.2    Petkova, A.T.3    Tycko, R.4    Meredith, S.C.5
  • 18
    • 0032849874 scopus 로고    scopus 로고
    • Quantifi cation of β-sheet amyloid fibril structures with thiofl avin T
    • LeVine H 3rd (1999) Quantifi cation of β-sheet amyloid fibril structures with thiofl avin T. Methods Enzymol 309:274-284
    • (1999) Methods Enzymol , vol.309 , pp. 274-284
    • Levine, H.1
  • 19
    • 0021312893 scopus 로고
    • Amino acid analysis by reverse-phase high-performance liquid chromatography: Precolumn derivatization with phenylisothiocyanate
    • Heinrikson RL, Meredith SC (1984) Amino acid analysis by reverse-phase high-performance liquid chromatography: precolumn derivatization with phenylisothiocyanate. Anal Biochem 136:65-74
    • (1984) Anal Biochem , vol.136 , pp. 65-74
    • Heinrikson, R.L.1    Meredith, S.C.2
  • 20
    • 0023688448 scopus 로고
    • Quantitation of aspartate and glutamate in HPLC analysis of phenylthiocarbamyl amino acids
    • Mora R, Berndt KD, Tsai H, Meredith SC (1988) Quantitation of aspartate and glutamate in HPLC analysis of phenylthiocarbamyl amino acids. Anal Biochem 172:368-376
    • (1988) Anal Biochem , vol.172 , pp. 368-376
    • Mora, R.1    Berndt, K.D.2    Tsai, H.3    Meredith, S.C.4
  • 21
    • 0029033319 scopus 로고
    • Practice guidelines for autopsy pathology: Autopsy procedures for brain, spinal cord, and neuromuscular system
    • Powers, JM (1995) Practice guidelines for autopsy pathology: autopsy procedures for brain, spinal cord, and neuromuscular system. Arch Path Lab Man 119:777-783
    • (1995) Arch Path Lab Man , vol.119 , pp. 777-783
    • Powers, J.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.