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Volumn 752, Issue , 2011, Pages 121-136

Diagnostics for Amyloid Fibril Formation: Where to Begin?

Author keywords

Aggregation; Amyloid; Birefringence; Congo red; Fibril; Method; Procedures; Protein misfolding; Protocol; Thioflavin T

Indexed keywords

AMYLOID; CONGO RED; THIAZOLE DERIVATIVE; THIOFLAVINE;

EID: 79960999902     PISSN: 10643745     EISSN: 19406029     Source Type: Book Series    
DOI: 10.1007/978-1-60327-223-0_8     Document Type: Chapter
Times cited : (9)

References (23)
  • 1
    • 34447595268 scopus 로고
    • Ueber eine im gehirn und ruckenmark des menschen aufgefunde sub-stanz mit der chemishen reaction der cellulose
    • Virchow R. (1854) Ueber eine im gehirn und ruckenmark des menschen aufgefunde sub-stanz mit der chemishen reaction der cellulose. Virchows Arch Path Anat 6, 135–138.
    • (1854) Virchows Arch Path Anat , vol.6 , pp. 135-138
    • Virchow, R.1
  • 4
    • 0008358896 scopus 로고
    • Polarisationsoptische untersuchungen an der amyloidsubstanz
    • Missmahl H. P., and Hartwig M. (1953) Polarisationsoptische untersuchungen an der amyloidsubstanz. Virchows Archiv 324, 489–508.
    • (1953) Virchows Archiv , vol.324 , pp. 489-508
    • Missmahl, H.P.1    Hartwig, M.2
  • 6
    • 0001611370 scopus 로고
    • Electron microscopic observations on a fibrous component in amyloid of diverse origins
    • Cohen A. S., and Calkins E. (1959) Electron microscopic observations on a fibrous component in amyloid of diverse origins. Nature 183, 1202–1203.
    • (1959) Nature , vol.183 , pp. 1202-1203
    • Cohen, A.S.1    Calkins, E.2
  • 7
    • 33746377894 scopus 로고    scopus 로고
    • Protein misfolding, functional amyloid, and human disease
    • Chiti F., and Dobson C. M. (2006) Protein misfolding, functional amyloid, and human disease. Ann. Rev. Biochem. 75, 333–366.
    • (2006) Ann. Rev. Biochem. , vol.75 , pp. 333-366
    • Chiti, F.1    Dobson, C.M.2
  • 8
    • 0033849738 scopus 로고    scopus 로고
    • Review: History of the amyloid fibril
    • Sipe J. D., and Cohen A. S. (2000) Review: History of the amyloid fibril. J. Struct. Biol. 130, 88–98.
    • (2000) J. Struct. Biol. , vol.130 , pp. 88-98
    • Sipe, J.D.1    Cohen, A.S.2
  • 9
    • 0034718157 scopus 로고    scopus 로고
    • Alzheimer’s amyloid fibrils: Structure and assembly
    • Serpell L. C. (2000) Alzheimer’s amyloid fibrils: Structure and assembly. Biochim. Biophys. Acta 1502, 16–30.
    • (2000) Biochim. Biophys. Acta , vol.1502 , pp. 16-30
    • Serpell, L.C.1
  • 10
    • 0030801746 scopus 로고    scopus 로고
    • The structure of amyloid fibrils by electron microscopy and x-ray diffraction
    • Sunde M., and Blake C. (1997) The structure of amyloid fibrils by electron microscopy and x-ray diffraction. Adv. Protein Chem. 50, 123–159.
    • (1997) Adv. Protein Chem. , vol.50 , pp. 123-159
    • Sunde, M.1    Blake, C.2
  • 12
    • 0035826234 scopus 로고    scopus 로고
    • Amyloid fibrils from muscle myo-globin
    • Fandrich M., Fletcher M. A., and Dobson C. M. (2001) Amyloid fibrils from muscle myo-globin. Nature 410, 165–166.
    • (2001) Nature , vol.410 , pp. 165-166
    • Fandrich, M.1    Fletcher, M.A.2    Dobson, C.M.3
  • 14
    • 33746932145 scopus 로고    scopus 로고
    • Amino-terminal domain stability mediates apolipoprotein E aggregation into neurotoxic fibrils
    • Hatters D. M., Zhong N., Rutenber E., and Weisgraber K. H. (2006) Amino-terminal domain stability mediates apolipoprotein E aggregation into neurotoxic fibrils. J. Mol. Biol. 361, 932–944.
    • (2006) J. Mol. Biol. , vol.361 , pp. 932-944
    • Hatters, D.M.1    Zhong, N.2    Rutenber, E.3    Weisgraber, K.H.4
  • 15
    • 0032899322 scopus 로고    scopus 로고
    • Quantifying amyloid b-peptide (Ab) aggregation using the congo red-Ab (CR-Ab) spectrophotometric assay
    • Klunk W. E., Jacob R. F., and Mason R. P. (1999) Quantifying amyloid b-peptide (Ab) aggregation using the congo red-Ab (CR-Ab) spectrophotometric assay. Anal Biochem 266, 66–76.
    • (1999) Anal Biochem , vol.266 , pp. 66-76
    • Klunk, W.E.1    Jacob, R.F.2    Mason, R.P.3
  • 16
    • 0000464103 scopus 로고
    • Fluorescent stains, with special reference to amyloid and connective tissues
    • Vassar P. S., and Culling C. F. (1959) Fluorescent stains, with special reference to amyloid and connective tissues. Arch. Pathol. 68, 487–498.
    • (1959) Arch. Pathol. , vol.68 , pp. 487-498
    • Vassar, P.S.1    Culling, C.F.2
  • 17
    • 0014060419 scopus 로고
    • On the histochemistry of azo group-free thiazole dyes
    • Kelenyi G. (1967) On the histochemistry of azo group-free thiazole dyes. J Histochem. Cytochem. 15, 172–180.
    • (1967) J Histochem. Cytochem. , vol.15 , pp. 172-180
    • Kelenyi, G.1
  • 18
    • 0027502784 scopus 로고
    • Thioflavine T interaction with synthetic alzheimer’s disease b-amyloid peptides: Detection of amyloid aggregation in solution
    • LeVine H., 3rd. (1993) Thioflavine T interaction with synthetic alzheimer’s disease b-amyloid peptides: Detection of amyloid aggregation in solution. Protein Sci. 2, 404–410.
    • (1993) Protein Sci , vol.2 , pp. 404-410
    • Levine, H.1
  • 21
    • 0034727077 scopus 로고    scopus 로고
    • A yeast prion provides a mechanism for genetic variation and phenotypic diversity
    • True H. L., and Lindquist S. L. (2000) A yeast prion provides a mechanism for genetic variation and phenotypic diversity. Nature 407, 477–483.
    • (2000) Nature , vol.407 , pp. 477-483
    • True, H.L.1    Lindquist, S.L.2
  • 22
    • 0034682559 scopus 로고    scopus 로고
    • Human apolipoprotein C-II forms twisted amyloid ribbons and closed loops
    • Hatters D. M., MacPhee C. E., Lawrence L. J., Sawyer W. H., and Howlett G. J. (2000) Human apolipoprotein C-II forms twisted amyloid ribbons and closed loops. Biochemistry 39, 8276–8283.
    • (2000) Biochemistry , vol.39 , pp. 8276-8283
    • Hatters, D.M.1    Macphee, C.E.2    Lawrence, L.J.3    Sawyer, W.H.4    Howlett, G.J.5
  • 23
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72, 248–254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.