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- Beatty K., Bieth J., Travis J. Kinetics of association of serine proteinases with native and oxidized alpha-1-proteinase inhibitor and alpha-1-antichymotrypsin. J Biol Chem. 1980 May 10;255(9):3931–3934. [PubMed] [Google Scholar]
- Brantly M., Nukiwa T., Crystal R. G. Molecular basis of alpha-1-antitrypsin deficiency. Am J Med. 1988 Jun 24;84(6A):13–31. doi: 10.1016/0002-9343(88)90154-4. [DOI] [PubMed] [Google Scholar]
- Bruce D., Perry D. J., Borg J. Y., Carrell R. W., Wardell M. R. Thromboembolic disease due to thermolabile conformational changes of antithrombin Rouen-VI (187 Asn-->Asp) J Clin Invest. 1994 Dec;94(6):2265–2274. doi: 10.1172/JCI117589. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Carp H., Miller F., Hoidal J. R., Janoff A. Potential mechanism of emphysema: alpha 1-proteinase inhibitor recovered from lungs of cigarette smokers contains oxidized methionine and has decreased elastase inhibitory capacity. Proc Natl Acad Sci U S A. 1982 Mar;79(6):2041–2045. doi: 10.1073/pnas.79.6.2041. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Carrell R. W., Jeppsson J. O., Laurell C. B., Brennan S. O., Owen M. C., Vaughan L., Boswell D. R. Structure and variation of human alpha 1-antitrypsin. Nature. 1982 Jul 22;298(5872):329–334. doi: 10.1038/298329a0. [DOI] [PubMed] [Google Scholar]
- Carrell R. W., Lomas D. A. Conformational disease. Lancet. 1997 Jul 12;350(9071):134–138. doi: 10.1016/S0140-6736(97)02073-4. [DOI] [PubMed] [Google Scholar]
- Carrell R. W., Stein P. E., Fermi G., Wardell M. R. Biological implications of a 3 A structure of dimeric antithrombin. Structure. 1994 Apr 15;2(4):257–270. doi: 10.1016/s0969-2126(00)00028-9. [DOI] [PubMed] [Google Scholar]
- Courtney M., Jallat S., Tessier L. H., Benavente A., Crystal R. G., Lecocq J. P. Synthesis in E. coli of alpha 1-antitrypsin variants of therapeutic potential for emphysema and thrombosis. Nature. 1985 Jan 10;313(5998):149–151. doi: 10.1038/313149a0. [DOI] [PubMed] [Google Scholar]
- Eldering E., Verpy E., Roem D., Meo T., Tosi M. COOH-terminal substitutions in the serpin C1 inhibitor that cause loop overinsertion and subsequent multimerization. J Biol Chem. 1995 Feb 10;270(6):2579–2587. doi: 10.1074/jbc.270.6.2579. [DOI] [PubMed] [Google Scholar]
- Elliott P. R., Abrahams J. P., Lomas D. A. Wild-type alpha 1-antitrypsin is in the canonical inhibitory conformation. J Mol Biol. 1998 Jan 23;275(3):419–425. doi: 10.1006/jmbi.1997.1458. [DOI] [PubMed] [Google Scholar]
- Elliott P. R., Lomas D. A., Carrell R. W., Abrahams J. P. Inhibitory conformation of the reactive loop of alpha 1-antitrypsin. Nat Struct Biol. 1996 Aug;3(8):676–681. doi: 10.1038/nsb0896-676. [DOI] [PubMed] [Google Scholar]
- Elliott P. R., Stein P. E., Bilton D., Carrell R. W., Lomas D. A. Structural explanation for the deficiency of S alpha 1-antitrypsin. Nat Struct Biol. 1996 Nov;3(11):910–911. doi: 10.1038/nsb1196-910. [DOI] [PubMed] [Google Scholar]
- Eriksson S., Carlson J., Velez R. Risk of cirrhosis and primary liver cancer in alpha 1-antitrypsin deficiency. N Engl J Med. 1986 Mar 20;314(12):736–739. doi: 10.1056/NEJM198603203141202. [DOI] [PubMed] [Google Scholar]
- Faber J. P., Poller W., Olek K., Baumann U., Carlson J., Lindmark B., Eriksson S. The molecular basis of alpha 1-antichymotrypsin deficiency in a heterozygote with liver and lung disease. J Hepatol. 1993 Jul;18(3):313–321. doi: 10.1016/s0168-8278(05)80275-2. [DOI] [PubMed] [Google Scholar]
- Griffith M. E., Lovegrove J. U., Gaskin G., Whitehouse D. B., Pusey C. D. C-antineutrophil cytoplasmic antibody positivity in vasculitis patients is associated with the Z allele of alpha-1-antitrypsin, and P-antineutrophil cytoplasmic antibody positivity with the S allele. Nephrol Dial Transplant. 1996 Mar;11(3):438–443. [PubMed] [Google Scholar]
- Huber R., Carrell R. W. Implications of the three-dimensional structure of alpha 1-antitrypsin for structure and function of serpins. Biochemistry. 1989 Nov 14;28(23):8951–8966. doi: 10.1021/bi00449a001. [DOI] [PubMed] [Google Scholar]
- Jaffe H. A., Danel C., Longenecker G., Metzger M., Setoguchi Y., Rosenfeld M. A., Gant T. W., Thorgeirsson S. S., Stratford-Perricaudet L. D., Perricaudet M. Adenovirus-mediated in vivo gene transfer and expression in normal rat liver. Nat Genet. 1992 Aug;1(5):372–378. doi: 10.1038/ng0892-372. [DOI] [PubMed] [Google Scholar]
- Janus E. D., Phillips N. T., Carrell R. W. Smoking, lung function, and alpha 1-antitrypsin deficiency. Lancet. 1985 Jan 19;1(8421):152–154. doi: 10.1016/s0140-6736(85)91916-6. [DOI] [PubMed] [Google Scholar]
- Jeppsson J. O. Amino acid substitution Glu leads to Lys alpha1-antitrypsin PiZ. FEBS Lett. 1976 Jun 1;65(2):195–197. doi: 10.1016/0014-5793(76)80478-4. [DOI] [PubMed] [Google Scholar]
- Kay M. A., Baley P., Rothenberg S., Leland F., Fleming L., Ponder K. P., Liu T., Finegold M., Darlington G., Pokorny W. Expression of human alpha 1-antitrypsin in dogs after autologous transplantation of retroviral transduced hepatocytes. Proc Natl Acad Sci U S A. 1992 Jan 1;89(1):89–93. doi: 10.1073/pnas.89.1.89. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Kim J., Lee K. N., Yi G. S., Yu M. H. A thermostable mutation located at the hydrophobic core of alpha 1-antitrypsin suppresses the folding defect of the Z-type variant. J Biol Chem. 1995 Apr 14;270(15):8597–8601. doi: 10.1074/jbc.270.15.8597. [DOI] [PubMed] [Google Scholar]
- King M. A., Stone J. A., Diaz P. T., Mueller C. F., Becker W. J., Gadek J. E. Alpha 1-antitrypsin deficiency: evaluation of bronchiectasis with CT. Radiology. 1996 Apr;199(1):137–141. doi: 10.1148/radiology.199.1.8633137. [DOI] [PubMed] [Google Scholar]
- Kwon K. S., Kim J., Shin H. S., Yu M. H. Single amino acid substitutions of alpha 1-antitrypsin that confer enhancement in thermal stability. J Biol Chem. 1994 Apr 1;269(13):9627–9631. [PubMed] [Google Scholar]
- Larsson C. Natural history and life expectancy in severe alpha1-antitrypsin deficiency, Pi Z. Acta Med Scand. 1978;204(5):345–351. doi: 10.1111/j.0954-6820.1978.tb08452.x. [DOI] [PubMed] [Google Scholar]
- Le A., Ferrell G. A., Dishon D. S., Le Q. Q., Sifers R. N. Soluble aggregates of the human PiZ alpha 1-antitrypsin variant are degraded within the endoplasmic reticulum by a mechanism sensitive to inhibitors of protein synthesis. J Biol Chem. 1992 Jan 15;267(2):1072–1080. [PubMed] [Google Scholar]
- Lindo V. S., Kakkar V. V., Learmonth M., Melissari E., Zappacosta F., Panico M., Morris H. R. Antithrombin-TRI (Ala382 to Thr) causing severe thromboembolic tendency undergoes the S-to-R transition and is associated with a plasma-inactive high-molecular-weight complex of aggregated antithrombin. Br J Haematol. 1995 Mar;89(3):589–601. doi: 10.1111/j.1365-2141.1995.tb08368.x. [DOI] [PubMed] [Google Scholar]
- Llewellyn-Jones C. G., Lomas D. A., Carrell R. W., Stockley R. A. The effect of the Z mutation on the ability of alpha 1-antitrypsin to prevent neutrophil mediated tissue damage. Biochim Biophys Acta. 1994 Nov 29;1227(3):155–160. doi: 10.1016/0925-4439(94)90089-2. [DOI] [PubMed] [Google Scholar]
- Lomas D. A., Elliott P. R., Chang W. S., Wardell M. R., Carrell R. W. Preparation and characterization of latent alpha 1-antitrypsin. J Biol Chem. 1995 Mar 10;270(10):5282–5288. doi: 10.1074/jbc.270.10.5282. [DOI] [PubMed] [Google Scholar]
- Lomas D. A., Elliott P. R., Sidhar S. K., Foreman R. C., Finch J. T., Cox D. W., Whisstock J. C., Carrell R. W. alpha 1-Antitrypsin Mmalton (Phe52-deleted) forms loop-sheet polymers in vivo. Evidence for the C sheet mechanism of polymerization. J Biol Chem. 1995 Jul 14;270(28):16864–16870. doi: 10.1074/jbc.270.28.16864. [DOI] [PubMed] [Google Scholar]
- Lomas D. A., Evans D. L., Finch J. T., Carrell R. W. The mechanism of Z alpha 1-antitrypsin accumulation in the liver. Nature. 1992 Jun 18;357(6379):605–607. doi: 10.1038/357605a0. [DOI] [PubMed] [Google Scholar]
- Lomas D. A., Evans D. L., Stone S. R., Chang W. S., Carrell R. W. Effect of the Z mutation on the physical and inhibitory properties of alpha 1-antitrypsin. Biochemistry. 1993 Jan 19;32(2):500–508. doi: 10.1021/bi00053a014. [DOI] [PubMed] [Google Scholar]
- Lomas D. A., Finch J. T., Seyama K., Nukiwa T., Carrell R. W. Alpha 1-antitrypsin Siiyama (Ser53-->Phe). Further evidence for intracellular loop-sheet polymerization. J Biol Chem. 1993 Jul 25;268(21):15333–15335. [PubMed] [Google Scholar]
- Massaro G. D., Massaro D. Retinoic acid treatment abrogates elastase-induced pulmonary emphysema in rats. Nat Med. 1997 Jun;3(6):675–677. doi: 10.1038/nm0697-675. [DOI] [PubMed] [Google Scholar]
- Mast A. E., Enghild J. J., Pizzo S. V., Salvesen G. Analysis of the plasma elimination kinetics and conformational stabilities of native, proteinase-complexed, and reactive site cleaved serpins: comparison of alpha 1-proteinase inhibitor, alpha 1-antichymotrypsin, antithrombin III, alpha 2-antiplasmin, angiotensinogen, and ovalbumin. Biochemistry. 1991 Feb 12;30(6):1723–1730. doi: 10.1021/bi00220a039. [DOI] [PubMed] [Google Scholar]
- Mast A. E., Enghild J. J., Salvesen G. Conformation of the reactive site loop of alpha 1-proteinase inhibitor probed by limited proteolysis. Biochemistry. 1992 Mar 17;31(10):2720–2728. doi: 10.1021/bi00125a012. [DOI] [PubMed] [Google Scholar]
- Morrison H. M., Kramps J. A., Burnett D., Stockley R. A. Lung lavage fluid from patients with alpha 1-proteinase inhibitor deficiency or chronic obstructive bronchitis: anti-elastase function and cell profile. Clin Sci (Lond) 1987 Mar;72(3):373–381. doi: 10.1042/cs0720373. [DOI] [PubMed] [Google Scholar]
- Ogushi F., Fells G. A., Hubbard R. C., Straus S. D., Crystal R. G. Z-type alpha 1-antitrypsin is less competent than M1-type alpha 1-antitrypsin as an inhibitor of neutrophil elastase. J Clin Invest. 1987 Nov;80(5):1366–1374. doi: 10.1172/JCI113214. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Patston P. A., Hauert J., Michaud M., Schapira M. Formation and properties of C1-inhibitor polymers. FEBS Lett. 1995 Jul 24;368(3):401–404. doi: 10.1016/0014-5793(95)00694-5. [DOI] [PubMed] [Google Scholar]
- Poller W., Faber J. P., Weidinger S., Tief K., Scholz S., Fischer M., Olek K., Kirchgesser M., Heidtmann H. H. A leucine-to-proline substitution causes a defective alpha 1-antichymotrypsin allele associated with familial obstructive lung disease. Genomics. 1993 Sep;17(3):740–743. doi: 10.1006/geno.1993.1396. [DOI] [PubMed] [Google Scholar]
- Potempa J., Korzus E., Travis J. The serpin superfamily of proteinase inhibitors: structure, function, and regulation. J Biol Chem. 1994 Jun 10;269(23):15957–15960. [PubMed] [Google Scholar]
- Roberts E. A., Cox D. W., Medline A., Wanless I. R. Occurrence of alpha-1-antitrypsin deficiency in 155 patients with alcoholic liver disease. Am J Clin Pathol. 1984 Oct;82(4):424–427. doi: 10.1093/ajcp/82.4.424. [DOI] [PubMed] [Google Scholar]
- Rosenfeld M. A., Siegfried W., Yoshimura K., Yoneyama K., Fukayama M., Stier L. E., Päkkö P. K., Gilardi P., Stratford-Perricaudet L. D., Perricaudet M. Adenovirus-mediated transfer of a recombinant alpha 1-antitrypsin gene to the lung epithelium in vivo. Science. 1991 Apr 19;252(5004):431–434. doi: 10.1126/science.2017680. [DOI] [PubMed] [Google Scholar]
- Ryu S. E., Choi H. J., Kwon K. S., Lee K. N., Yu M. H. The native strains in the hydrophobic core and flexible reactive loop of a serine protease inhibitor: crystal structure of an uncleaved alpha1-antitrypsin at 2.7 A. Structure. 1996 Oct 15;4(10):1181–1192. doi: 10.1016/s0969-2126(96)00126-8. [DOI] [PubMed] [Google Scholar]
- Schreuder H. A., de Boer B., Dijkema R., Mulders J., Theunissen H. J., Grootenhuis P. D., Hol W. G. The intact and cleaved human antithrombin III complex as a model for serpin-proteinase interactions. Nat Struct Biol. 1994 Jan;1(1):48–54. doi: 10.1038/nsb0194-48. [DOI] [PubMed] [Google Scholar]
- Schulze A. J., Baumann U., Knof S., Jaeger E., Huber R., Laurell C. B. Structural transition of alpha 1-antitrypsin by a peptide sequentially similar to beta-strand s4A. Eur J Biochem. 1990 Nov 26;194(1):51–56. doi: 10.1111/j.1432-1033.1990.tb19425.x. [DOI] [PubMed] [Google Scholar]
- Seyama K., Nukiwa T., Takabe K., Takahashi H., Miyake K., Kira S. Siiyama (serine 53 (TCC) to phenylalanine 53 (TTC)). A new alpha 1-antitrypsin-deficient variant with mutation on a predicted conserved residue of the serpin backbone. J Biol Chem. 1991 Jul 5;266(19):12627–12632. [PubMed] [Google Scholar]
- Sidhar S. K., Lomas D. A., Carrell R. W., Foreman R. C. Mutations which impede loop/sheet polymerization enhance the secretion of human alpha 1-antitrypsin deficiency variants. J Biol Chem. 1995 Apr 14;270(15):8393–8396. doi: 10.1074/jbc.270.15.8393. [DOI] [PubMed] [Google Scholar]
- Snider G. L. Emphysema: the first two centuries--and beyond. A historical overview, with suggestions for future research: Part 2. Am Rev Respir Dis. 1992 Dec;146(6):1615–1622. doi: 10.1164/ajrccm/146.6.1615. [DOI] [PubMed] [Google Scholar]
- Stein P. D., Leu J. D., Welch M. H., Guenter C. A. Pathophysiology of the pulmonary circulation in emphysema associated with alpha antitrypsin deficiency. Circulation. 1971 Feb;43(2):227–239. doi: 10.1161/01.cir.43.2.227. [DOI] [PubMed] [Google Scholar]
- Sveger T. Liver disease in alpha1-antitrypsin deficiency detected by screening of 200,000 infants. N Engl J Med. 1976 Jun 10;294(24):1316–1321. doi: 10.1056/NEJM197606102942404. [DOI] [PubMed] [Google Scholar]
- Sveger T. The natural history of liver disease in alpha 1-antitrypsin deficient children. Acta Paediatr Scand. 1988 Nov;77(6):847–851. doi: 10.1111/j.1651-2227.1988.tb10767.x. [DOI] [PubMed] [Google Scholar]
- Teckman J. H., Perlmutter D. H. The endoplasmic reticulum degradation pathway for mutant secretory proteins alpha1-antitrypsin Z and S is distinct from that for an unassembled membrane protein. J Biol Chem. 1996 May 31;271(22):13215–13220. doi: 10.1074/jbc.271.22.13215. [DOI] [PubMed] [Google Scholar]
- Wewers M. D., Casolaro M. A., Sellers S. E., Swayze S. C., McPhaul K. M., Wittes J. T., Crystal R. G. Replacement therapy for alpha 1-antitrypsin deficiency associated with emphysema. N Engl J Med. 1987 Apr 23;316(17):1055–1062. doi: 10.1056/NEJM198704233161704. [DOI] [PubMed] [Google Scholar]
- Wu Y., Whitman I., Molmenti E., Moore K., Hippenmeyer P., Perlmutter D. H. A lag in intracellular degradation of mutant alpha 1-antitrypsin correlates with the liver disease phenotype in homozygous PiZZ alpha 1-antitrypsin deficiency. Proc Natl Acad Sci U S A. 1994 Sep 13;91(19):9014–9018. doi: 10.1073/pnas.91.19.9014. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Yoshida A., Lieberman J., Gaidulis L., Ewing C. Molecular abnormality of human alpha1-antitrypsin variant (Pi-ZZ) associated with plasma activity deficiency. Proc Natl Acad Sci U S A. 1976 Apr;73(4):1324–1328. doi: 10.1073/pnas.73.4.1324. [DOI] [PMC free article] [PubMed] [Google Scholar]
- Yu M. H., Lee K. N., Kim J. The Z type variation of human alpha 1-antitrypsin causes a protein folding defect. Nat Struct Biol. 1995 May;2(5):363–367. doi: 10.1038/nsb0595-363. [DOI] [PubMed] [Google Scholar]