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- W2008040462 abstract "Emphysema and liver cirrhosis can be caused by the Z mutation (Glu342Lys) in the serine protease inhibitor α1-antitrypsin (α1AT), which is found in more than 4% of the Northern European population. Homozygotes experience deficiency in the lung concomitantly with a massive accumulation of polymers within hepatocytes, causing their destruction. Recently, it was proposed that Z-α1AT polymerizes by a C-terminal domain swap. In this study, small-angle x-ray scattering (SAXS) was used to characterize Z-α1AT polymers in solution. The data show that the Z-α1AT trimer, tetramer, and pentamer all form ring-like structures in strong support of a common domain-swap polymerization mechanism that can lead to self-terminating polymers." @default.
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- W2008040462 date "2014-10-01" @default.
- W2008040462 modified "2023-09-28" @default.
- W2008040462 title "The Shapes of Z- α 1 -Antitrypsin Polymers in Solution Support the C-Terminal Domain-Swap Mechanism of Polymerization" @default.
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- W2008040462 doi "https://doi.org/10.1016/j.bpj.2014.08.030" @default.
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