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• W2048148224 endingPage "1065" @default.
• W2048148224 startingPage "1047" @default.
• W2048148224 abstract "Misfolding and conformational diseases are increasing in prominence and prevalence. Both misfolding and 'postfolding' conformational mechanisms can contribute to pathogenesis and can coexist. The different contexts of folding and native state behavior may have implications for the development of therapeutic strategies. α1-antitrypsin deficiency illustrates how these issues can be addressed with therapeutic approaches to rescue folding, ameliorate downstream consequences of aberrant polymerization and/or maintain physiological function. Small-molecule strategies have successfully targeted structural features of the native conformer. Recent developments include the capability to follow solution behavior of α1-antitrypsin in the context of disease mutations and interactions with drug-like compounds. Moreover, preclinical studies in cells and organisms support the potential of manipulating cellular response repertoires to process misfolded and polymer states." @default.
• W2048148224 created "2016-06-24" @default.
• W2048148224 creator A5008435984 @default.
• W2048148224 creator A5011754804 @default.
• W2048148224 date "2014-06-01" @default.
• W2048148224 modified "2023-09-25" @default.
• W2048148224 title "Therapeutic targeting of misfolding and conformational change in α₁-antitrypsin deficiency" @default.
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