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Small molecules block the polymerisation of Z α(1)-antitrypsin and increase the clearance of intracellular aggregates
The Z mutant of α(1)-antitrypsin (Glu342Lys) causes a domain-swap and the formation of intrahepatic polymers that aggregate as inclusions and predispose the homozygote to cirrhosis. We have identified an allosteric cavity that is distinct from the interface involved in polymerisation for rational st...
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| Hoofdauteurs: | , , , , , , , , , , |
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| Formaat: | Artigo |
| Taal: | Inglês |
| Gepubliceerd in: |
2007
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| Onderwerpen: | |
| Online toegang: | https://ncbi.nlm.nih.gov/pmc/articles/PMC2631427/ https://ncbi.nlm.nih.gov/pubmed/17918823 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/jm070687z |
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