Effects of glycosylation on the folding and stability of human, recombinant and cleaved α1-antitrypsin
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Structural Biology
Reference27 articles.
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2. Plasma serine proteinase inhibitors (serpins) exhibit major conformational changes and a large increase in conformational stability upon cleavage at their reactive sites;Bruch;J. Biol. Chem,1988
3. Reactive-centre variants of α1-antitrypsin. A new range of anti-inflammatory agents;Carrell;Biotechnol. Genet. Eng. Rev,1986
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5. Human α1-antitrypsin: carbohydrate attachment and sequence homology;Carrell;FEBS Letters,1981
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