메뉴 건너뛰기




Volumn 11, Issue 10, 2002, Pages 2417-2426

A kinetic study of β-lactoglobulin amyloid fibril formation promoted by urea

Author keywords

lactoglobulin; Amyloid fibril; Electron microscope; Kinetics; MALDI TOF mass; Thioflavin T

Indexed keywords

AMYLOID; BETA LACTOGLOBULIN; THIOFLAVINE; UREA;

EID: 0036784667     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0217702     Document Type: Article
Times cited : (246)

References (69)
  • 2
    • 0031846139 scopus 로고    scopus 로고
    • Protein stability function relations: β-lactoglobulin - A sulphydryl group reactivity and its relationship to protein unfolding stability
    • (1998) Int. J. Biol. Macromol. , vol.23 , pp. 19-25
    • Apenten, R.K.O.1
  • 15
    • 0035961329 scopus 로고    scopus 로고
    • The structural basis of protein folding and its links with human disease
    • (2001) Philos. Trans. Biol. Sci. , vol.356 , pp. 133-145
  • 24
  • 30
    • 0027195933 scopus 로고
    • Seeding "one-dimensional crystallization" of amyloid: A pathogenic mechanism in Alzheimer's disease and scrapie?
    • (1993) Cell , vol.73 , pp. 1055-1058
    • Jarrett, J.T.1    Lansbury P.T., Jr.2
  • 37
    • 0030582679 scopus 로고    scopus 로고
    • The burst-phase intermediate in the refolding of β-lactoglobulin studied by stopped-flow circular dichroism and absorption spectroscopy
    • (1996) J. Mol. Biol. , vol.264 , pp. 806-822
    • Kuwajima, K.1    Yamaya, H.2    Sugai, S.3
  • 52
    • 0035849879 scopus 로고    scopus 로고
    • Cause of neural death in neurodegenerative diseases attributable to expansion of glutamine repeats
    • (2001) Nature , vol.412 , pp. 143-144
    • Perutz, M.F.1    Windle, A.H.2
  • 65
    • 34447595268 scopus 로고
    • Über eine im gehirn und rückenmark des menschen aufgefundene substanz mit der chemischen reaktion der cellulose
    • (1853) Virchows Arch. , vol.6 , pp. 135-138
    • Virchow, R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.