Silverman GA, Bird PI, Carrell RW, Church FC, Coughlin PB, Gettins PG, Irving JA, Lomas DA, Luke CJ, Moyer RW, Pemberton PA, Remold-O'Donnell E, Salvesen GS, Travis J, Whisstock JC. The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature. The Journal of Biological Chemistry. September 2001, 276 (36): 33293–6. PMID 11435447. doi:10.1074/jbc.R100016200.
Gettins PG. Serpin structure, mechanism, and function. Chemical Reviews. December 2002, 102 (12): 4751–804. PMID 12475206. doi:10.1021/cr010170.
Whisstock JC, Bottomley SP. Molecular gymnastics: serpin structure, folding and misfolding. Current Opinion in Structural Biology. December 2006, 16 (6): 761–8. PMID 17079131. doi:10.1016/j.sbi.2006.10.005.
Stein PE, Carrell RW. What do dysfunctional serpins tell us about molecular mobility and disease?. Nature Structural Biology. February 1995, 2 (2): 96–113. PMID 7749926. doi:10.1038/nsb0295-96.
Janciauskiene SM, Bals R, Koczulla R, Vogelmeier C, Köhnlein T, Welte T. The discovery of α1-antitrypsin and its role in health and disease. Respiratory Medicine. August 2011, 105 (8): 1129–39. PMID 21367592. doi:10.1016/j.rmed.2011.02.002.
Laurell CB, Eriksson S. The electrophoretic α1-globulin pattern of serum in α1-antitrypsin deficiency. 1963. Copd. 2013,. 10 Suppl 1: 3–8. PMID 23527532. doi:10.3109/15412555.2013.771956.
de Serres FJ. Worldwide Racial and Ethnic Distribution of α-Antitrypsin Deficiency. CHEST Journal. 1 November 2002, 122 (5): 1818–1829. doi:10.1378/chest.122.5.1818.
Hunt LT, Dayhoff MO. A surprising new protein superfamily containing ovalbumin, antithrombin-III, and alpha 1-proteinase inhibitor. Biochemical and Biophysical Research Communications. July 1980, 95 (2): 864–71. PMID 6968211. doi:10.1016/0006-291X(80)90867-0.
Loebermann H, Tokuoka R, Deisenhofer J, Huber R. Human alpha 1-proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function. Journal of Molecular Biology. August 1984, 177 (3): 531–57. PMID 6332197. doi:10.1016/0022-2836(84)90298-5.
Stein PE, Leslie AG, Finch JT, Turnell WG, McLaughlin PJ, Carrell RW. Crystal structure of ovalbumin as a model for the reactive centre of serpins. Nature. September 1990, 347 (6288): 99–102. PMID 2395463. doi:10.1038/347099a0.
Stein PE, Leslie AG, Finch JT, Turnell WG, McLaughlin PJ, Carrell RW. Crystal structure of ovalbumin as a model for the reactive centre of serpins. Nature. September 1990, 347 (6288): 99–102. PMID 2395463. doi:10.1038/347099a0.
Stein PE, Leslie AG, Finch JT, Turnell WG, McLaughlin PJ, Carrell RW. Crystal structure of ovalbumin as a model for the reactive centre of serpins. Nature. September 1990, 347 (6288): 99–102. PMID 2395463. doi:10.1038/347099a0.
Steenbakkers PJ, Irving JA, Harhangi HR, Swinkels WJ, Akhmanova A, Dijkerman R, Jetten MS, van der Drift C, Whisstock JC, Op den Camp HJ. A serpin in the cellulosome of the anaerobic fungus Piromyces sp. strain E2. Mycological Research. August 2008, 112 (Pt 8): 999–1006. PMID 18539447. doi:10.1016/j.mycres.2008.01.021.
Silverman GA, Bird PI, Carrell RW, Church FC, Coughlin PB, Gettins PG, Irving JA, Lomas DA, Luke CJ, Moyer RW, Pemberton PA, Remold-O'Donnell E, Salvesen GS, Travis J, Whisstock JC. The serpins are an expanding superfamily of structurally similar but functionally diverse proteins. Evolution, mechanism of inhibition, novel functions, and a revised nomenclature. The Journal of Biological Chemistry. September 2001, 276 (36): 33293–6. PMID 11435447. doi:10.1074/jbc.R100016200.
Gettins PG. Serpin structure, mechanism, and function. Chemical Reviews. December 2002, 102 (12): 4751–804. PMID 12475206. doi:10.1021/cr010170.
Whisstock JC, Bottomley SP. Molecular gymnastics: serpin structure, folding and misfolding. Current Opinion in Structural Biology. December 2006, 16 (6): 761–8. PMID 17079131. doi:10.1016/j.sbi.2006.10.005.
Stein PE, Carrell RW. What do dysfunctional serpins tell us about molecular mobility and disease?. Nature Structural Biology. February 1995, 2 (2): 96–113. PMID 7749926. doi:10.1038/nsb0295-96.
Janciauskiene SM, Bals R, Koczulla R, Vogelmeier C, Köhnlein T, Welte T. The discovery of α1-antitrypsin and its role in health and disease. Respiratory Medicine. August 2011, 105 (8): 1129–39. PMID 21367592. doi:10.1016/j.rmed.2011.02.002.
Hunt LT, Dayhoff MO. A surprising new protein superfamily containing ovalbumin, antithrombin-III, and alpha 1-proteinase inhibitor. Biochemical and Biophysical Research Communications. July 1980, 95 (2): 864–71. PMID 6968211. doi:10.1016/0006-291X(80)90867-0.
Loebermann H, Tokuoka R, Deisenhofer J, Huber R. Human alpha 1-proteinase inhibitor. Crystal structure analysis of two crystal modifications, molecular model and preliminary analysis of the implications for function. Journal of Molecular Biology. August 1984, 177 (3): 531–57. PMID 6332197. doi:10.1016/0022-2836(84)90298-5.
Stein PE, Leslie AG, Finch JT, Turnell WG, McLaughlin PJ, Carrell RW. Crystal structure of ovalbumin as a model for the reactive centre of serpins. Nature. September 1990, 347 (6288): 99–102. PMID 2395463. doi:10.1038/347099a0.
Stein PE, Leslie AG, Finch JT, Turnell WG, McLaughlin PJ, Carrell RW. Crystal structure of ovalbumin as a model for the reactive centre of serpins. Nature. September 1990, 347 (6288): 99–102. PMID 2395463. doi:10.1038/347099a0.
Stein PE, Leslie AG, Finch JT, Turnell WG, McLaughlin PJ, Carrell RW. Crystal structure of ovalbumin as a model for the reactive centre of serpins. Nature. September 1990, 347 (6288): 99–102. PMID 2395463. doi:10.1038/347099a0.
Steenbakkers PJ, Irving JA, Harhangi HR, Swinkels WJ, Akhmanova A, Dijkerman R, Jetten MS, van der Drift C, Whisstock JC, Op den Camp HJ. A serpin in the cellulosome of the anaerobic fungus Piromyces sp. strain E2. Mycological Research. August 2008, 112 (Pt 8): 999–1006. PMID 18539447. doi:10.1016/j.mycres.2008.01.021.