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Soc."},{"key":"10.1016\/j.chembiol.2022.12.004_bib100","series-title":"Geostatistics: Modeling Spatial Uncertainty","first-page":"497","author":"Chiles","year":"2009"},{"key":"10.1016\/j.chembiol.2022.12.004_bib101","doi-asserted-by":"crossref","DOI":"10.1371\/journal.pone.0038405","article-title":"Three new alpha1-antitrypsin deficiency variants help to define a C-terminal region regulating conformational change and polymerization","volume":"7","author":"Fra","year":"2012","journal-title":"PLoS One"},{"key":"10.1016\/j.chembiol.2022.12.004_bib102","doi-asserted-by":"crossref","first-page":"13133","DOI":"10.1021\/bi970664u","article-title":"Preparative induction and characterization of L-antithrombin: a structural homologue of latent plasminogen activator inhibitor-1","volume":"36","author":"Wardell","year":"1997","journal-title":"Biochemistry"},{"key":"10.1016\/j.chembiol.2022.12.004_bib103","doi-asserted-by":"crossref","first-page":"89","DOI":"10.1002\/pro.5560060110","article-title":"Importance of the release of strand 1C to the polymerization mechanism of inhibitory serpins","volume":"6","author":"Chang","year":"1997","journal-title":"Protein Sci."},{"key":"10.1016\/j.chembiol.2022.12.004_bib104","doi-asserted-by":"crossref","first-page":"244","DOI":"10.1186\/s12931-021-01842-5","article-title":"Association between circulating alpha-1 antitrypsin polymers and lung and liver disease","volume":"22","author":"N\u00fa\u00f1ez","year":"2021","journal-title":"Respir. 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