Inhibiting transthyretin conformational changes that lead to amyloid fibril formation (Q27765742)

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T Klabunde

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H Purkey

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J C Sacchettini

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J W Kelly

Proceedings of the National Academy of Sciences of the United States of America

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language of work or name

English

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publication date

27 October 1998

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published in

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volume

95

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issue

22

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page(s)

12956-60

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cites work

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Inhibiting transthyretin amyloid fibril formation via protein stabilization

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The acid-mediated denaturation pathway of transthyretin yields a conformational intermediate that can self-assemble into amyloid

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Synchrotron X-ray studies suggest that the core of the transthyretin amyloid fibril is a continuous β-sheet helix

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Guanidine Hydrochloride-Induced Denaturation and Refolding of Transthyretin Exhibits a Marked Hysteresis: Equilibria with High Kinetic Barriers

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Evidence that the amyloid fibril protein in senile systemic amyloidosis is derived from normal prealbumin

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Discovering transthyretin amyloid fibril inhibitors by limited screening

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Drug competition for thyroxine binding to transthyretin (prealbumin): comparison with effects on thyroxine-binding globulin

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