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Volumn 299, Issue 5607, 2003, Pages 713-716

Prevention of transthyretin arnyloid disease by changing protein misfolding energetics

Author keywords

[No Author keywords available]

Indexed keywords

AGGLOMERATION; GENES; PROTEINS;

EID: 0037473750     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.1079589     Document Type: Article
Times cited : (471)

References (34)
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    • Supporting material is available on Science Online.
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    • Small-molecule inhibitors 6 and 8 through 10 do not inhibit TTR amyloidosis when a monomeric variant of TTR (M-TTR) (24) is employed for acid-mediated amyloid fibril formation studies (Fig. 2F), demonstrating that the inhibitors mediate amyloid inhibition through tetramer binding (Fig. 2, E and F). Inhibitor 7 slightly inhibits fibril formation from M-TTR because it drives a small fraction of M-TTR into a tetrameric quaternary structure (Fig. 2F).
  • 18
    • 0346523628 scopus 로고    scopus 로고
    • note
    • 2) ligands were all evaluated under physiological conditions (Fig. 1B), and the experiments described here were carried out in 6 M urea.
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    • note
    • d2)}.
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    • note
    • Sc).
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    • published online 17 October 2002 (10.1126/science. 1073619)
    • J. Ma, S. Lindquist, Science 298, 1785 (2002); published online 17 October 2002 (10.1126/science. 1073619).
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    • Ma, J.1    Lindquist, S.2
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    • note
    • We thank NIH (grant DK 46335), The Skaggs Institute of Chemical Biology, and the Lita Annenberg Hazen Foundation for financial support; R. A. Lerner and I. Wilson for useful suggestions; and the Wenner-Gren Foundation for a postdoctoral fellowship (P.H.).


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.