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”. 276 (36), s. 33293–6, September 2001. DOI: 10.1074/jbc.R100016200. PMID: 11435447.
Silverman GA, Whisstock JC, Bottomley SP, Huntington JA, Kaiserman D, Luke CJ, Pak SC, Reichhart JM, Bird PI. Serpins flex their muscle: I. Putting the clamps on proteolysis in diverse biological systems. „The Journal of Biological Chemistry”. 285 (32), s. 24299–305, August 2010. DOI: 10.1074/jbc.R110.112771. PMID: 20498369. PMCID: PMC2915665.
Whisstock JC, Silverman GA, Bird PI, Bottomley SP, Kaiserman D, Luke CJ, Pak SC, Reichhart JM, Huntington JA. Serpins flex their muscle: II. Structural insights into target peptidase recognition, polymerization, and transport functions. „The Journal of Biological Chemistry”. 285 (32), s. 24307–12, August 2010. DOI: 10.1074/jbc.R110.141408. PMID: 20498368. PMCID: PMC2915666.
Gettins PG. Serpin structure, mechanism, and function. „Chemical Reviews”. 102 (12), s. 4751–804, December 2002. DOI: 10.1021/cr010170. PMID: 12475206.
Whisstock JC, Bottomley SP. Molecular gymnastics: serpin structure, folding and misfolding. „Current Opinion in Structural Biology”. 16 (6), s. 761–8, December 2006. DOI: 10.1016/j.sbi.2006.10.005. PMID: 17079131.
Law RH, Zhang Q, McGowan S, Buckle AM, Silverman GA, Wong W, Rosado CJ, Langendorf CG, Pike RN, Bird PI, Whisstock JC. An overview of the serpin superfamily. „Genome Biology”. 7 (5), s. 216, 2006. DOI: 10.1186/gb-2006-7-5-216. PMID: 16737556. PMCID: PMC1779521.
Stein PE, Carrell RW. What do dysfunctional serpins tell us about molecular mobility and disease?. „Nature Structural Biology”. 2 (2), s. 96–113, 1995. DOI: 10.1038/nsb0295-96. PMID: 7749926.
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”. 105 (8), s. 1129–39, 2011. DOI: 10.1016/j.rmed.2011.02.002. PMID: 21367592.
Laurell CB, Eriksson S. The electrophoretic α1-globulin pattern of serum in α1-antitrypsin deficiency. 1963. „Copd”. 10 Suppl 1, s. 3–8, 2013. DOI: 10.3109/15412555.2013.771956. PMID: 23527532.
Frederick J. de Serres. Worldwide Racial and Ethnic Distribution of α-Antitrypsin Deficiency. „CHEST Journal”. 122 (5), s. 1818, 1 November 2002. 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”. 95 (2), s. 864–71, July 1980. DOI: 10.1016/0006-291X(80)90867-0. PMID: 6968211.
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”. 177 (3), s. 531–57, August 1984. DOI: 10.1016/0022-2836(84)90298-5. PMID: 6332197.
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”. 347 (6288), s. 99–102, September 1990. DOI: 10.1038/347099a0. PMID: 2395463.
Irving JA, Pike RN, Lesk AM, Whisstock JC. Phylogeny of the serpin superfamily: implications of patterns of amino acid conservation for structure and function. „Genome Research”. 10 (12), s. 1845–64, December 2000. DOI: 10.1101/gr.GR-1478R. PMID: 11116082.
Irving JA, Steenbakkers PJ, Lesk AM, Op den Camp HJ, Pike RN, Whisstock JC. Serpins in prokaryotes. „Molecular Biology and Evolution”. 19 (11), s. 1881–90, 2002. DOI: 10.1093/oxfordjournals.molbev.a004012. PMID: 12411597.
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”. 112 (Pt 8), s. 999–1006, August 2008. DOI: 10.1016/j.mycres.2008.01.021. PMID: 18539447.
Rawlings ND, Tolle DP, Barrett AJ. Evolutionary families of peptidase inhibitors. „The Biochemical Journal”. 378 (Pt 3), s. 705–16, March 2004. DOI: 10.1042/BJ20031825. PMID: 14705960. PMCID: PMC1224039.
Barrett AJ, Rawlings ND. Families and clans of serine peptidases. „Archives of Biochemistry and Biophysics”. 318 (2), s. 247–50, April 1995. DOI: 10.1006/abbi.1995.1227. PMID: 7733651.
Huntington JA, Read RJ, Carrell RW. Structure of a serpin-protease complex shows inhibition by deformation. „Nature”. 407 (6806), s. 923–6, October 2000. DOI: 10.1038/35038119. PMID: 11057674.
Barrett AJ, Rawlings ND. Evolutionary lines of cysteine peptidases. „Biological Chemistry”. 382 (5), s. 727–33, May 2001. DOI: 10.1515/BC.2001.088. PMID: 11517925.
Irving JA, Pike RN, Dai W, Brömme D, Worrall DM, Silverman GA, Coetzer TH, Dennison C, Bottomley SP, Whisstock JC. Evidence that serpin architecture intrinsically supports papain-like cysteine protease inhibition: engineering alpha(1)-antitrypsin to inhibit cathepsin proteases. „Biochemistry”. 41 (15), s. 4998–5004, April 2002. DOI: 10.1021/bi0159985. PMID: 11939796.
Schick C, Brömme D, Bartuski AJ, Uemura Y, Schechter NM, Silverman GA. The reactive site loop of the serpin SCCA1 is essential for cysteine proteinase inhibition. „Proceedings of the National Academy of Sciences of the United States of America”. 95 (23), s. 13465–70, November 1998. DOI: 10.1073/pnas.95.23.13465. PMID: 9811823. PMCID: PMC24842.
McGowan S, Buckle AM, Irving JA, Ong PC, Bashtannyk-Puhalovich TA, Kan WT, Henderson KN, Bulynko YA, Popova EY, Smith AI, Bottomley SP, Rossjohn J, Grigoryev SA, Pike RN, Whisstock JC. X-ray crystal structure of MENT: evidence for functional loop-sheet polymers in chromatin condensation. „The EMBO Journal”. 25 (13), s. 3144–55, July 2006. DOI: 10.1038/sj.emboj.7601201. PMID: 16810322. PMCID: PMC1500978.
Ong PC, McGowan S, Pearce MC, Irving JA, Kan WT, Grigoryev SA, Turk B, Silverman GA, Brix K, Bottomley SP, Whisstock JC, Pike RN. DNA accelerates the inhibition of human cathepsin V by serpins. „The Journal of Biological Chemistry”. 282 (51), s. 36980–6, December 2007. DOI: 10.1074/jbc.M706991200. PMID: 17923478.
Acosta H, Iliev D, Grahn TH, Gouignard N, Maccarana M, Griesbach J, Herzmann S, Sagha M, Climent M, Pera EM. The serpin PN1 is a feedback regulator of FGF signaling in germ layer and primary axis formation. „Development”. 142 (6), s. 1146–58, March 2015. DOI: 10.1242/dev.113886. PMID: 25758225.
Hashimoto C, Kim DR, Weiss LA, Miller JW, Morisato D. Spatial regulation of developmental signaling by a serpin. „Developmental Cell”. 5 (6), s. 945–50, December 2003. DOI: 10.1016/S1534-5807(03)00338-1. PMID: 14667416.
Bird PI. Regulation of pro-apoptotic leucocyte granule serine proteinases by intracellular serpins. „Immunology and Cell Biology”. 77 (1), s. 47–57, February 1999. DOI: 10.1046/j.1440-1711.1999.00787.x. PMID: 10101686.
Bird CH, Sutton VR, Sun J, Hirst CE, Novak A, Kumar S, Trapani JA, Bird PI. Selective regulation of apoptosis: the cytotoxic lymphocyte serpin proteinase inhibitor 9 protects against granzyme B-mediated apoptosis without perturbing the Fas cell death pathway. „Molecular and Cellular Biology”. 18 (11), s. 6387–98, November 1998. DOI: 10.1128/mcb.18.11.6387. PMID: 9774654.
Ray CA, Black RA, Kronheim SR, Greenstreet TA, Sleath PR, Salvesen GS, Pickup DJ. Viral inhibition of inflammation: cowpox virus encodes an inhibitor of the interleukin-1 beta converting enzyme. „Cell”. 69 (4), s. 597–604, May 1992. DOI: 10.1016/0092-8674(92)90223-Y. PMID: 1339309.
Vercammen D, Belenghi B, van de Cotte B, Beunens T, Gavigan JA, De Rycke R, Brackenier A, Inzé D, Harris JL, Van Breusegem F. Serpin1 of Arabidopsis thaliana is a suicide inhibitor for metacaspase 9. „Journal of Molecular Biology”. 364 (4), s. 625–36, December 2006. DOI: 10.1016/j.jmb.2006.09.010. PMID: 17028019.
Lampl N, Budai-Hadrian O, Davydov O, Joss TV, Harrop SJ, Curmi PM, Roberts TH, Fluhr R. Arabidopsis AtSerpin1, crystal structure and in vivo interaction with its target protease responsive to desiccation (RD21). „The Journal of Biological Chemistry”. 285 (18), s. 13550–60, April 2010. DOI: 10.1074/jbc.M109.095075. PMID: 20181955. PMCID: PMC2859516.
Klieber MA, Underhill C, Hammond GL, Muller YA. Corticosteroid-binding globulin, a structural basis for steroid transport and proteinase-triggered release. „The Journal of Biological Chemistry”. 282 (40), s. 29594–603, October 2007. DOI: 10.1074/jbc.M705014200. PMID: 17644521.
Zhou A, Wei Z, Read RJ, Carrell RW. Structural mechanism for the carriage and release of thyroxine in the blood. „Proceedings of the National Academy of Sciences of the United States of America”. 103 (36), s. 13321–6, September 2006. DOI: 10.1073/pnas.0604080103. PMID: 16938877. PMCID: PMC1557382.
Huntington JA, Stein PE. Structure and properties of ovalbumin. „Journal of Chromatography. B, Biomedical Sciences and Applications”. 756 (1-2), s. 189–98, May 2001. DOI: 10.1016/S0378-4347(01)00108-6. PMID: 11419711.
Mala JG, Rose C. Interactions of heat shock protein 47 with collagen and the stress response: an unconventional chaperone model?. „Life Sciences”. 87 (19-22), s. 579–86, November 2010. DOI: 10.1016/j.lfs.2010.09.024. PMID: 20888348.
Grigoryev SA, Bednar J, Woodcock CL. MENT, a heterochromatin protein that mediates higher order chromatin folding, is a new serpin family member. „The Journal of Biological Chemistry”. 274 (9), s. 5626–36, February 1999. DOI: 10.1074/jbc.274.9.5626. PMID: 10026180.
Elliott PR, Lomas DA, Carrell RW, Abrahams JP. Inhibitory conformation of the reactive loop of alpha 1-antitrypsin. „Nature Structural Biology”. 3 (8), s. 676–81, August 1996. DOI: 10.1038/nsb0896-676. PMID: 8756325.
Horvath AJ, Irving JA, Rossjohn J, Law RH, Bottomley SP, Quinsey NS, Pike RN, Coughlin PB, Whisstock JC. The murine orthologue of human antichymotrypsin: a structural paradigm for clade A3 serpins. „The Journal of Biological Chemistry”. 280 (52), s. 43168–78, December 2005. DOI: 10.1074/jbc.M505598200. PMID: 16141197.
Whisstock JC, Skinner R, Carrell RW, Lesk AM. Conformational changes in serpins: I. The native and cleaved conformations of alpha(1)-antitrypsin. „Journal of Molecular Biology”. 296 (2), s. 685–99, February 2000. DOI: 10.1006/jmbi.1999.3520. PMID: 10669617.
Huntington JA. Shape-shifting serpins--advantages of a mobile mechanism. „Trends in Biochemical Sciences”. 31 (8), s. 427–35, August 2006. DOI: 10.1016/j.tibs.2006.06.005. PMID: 16820297.
Jin L, Abrahams JP, Skinner R, Petitou M, Pike RN, Carrell RW. The anticoagulant activation of antithrombin by heparin. „Proceedings of the National Academy of Sciences of the United States of America”. 94 (26), s. 14683–8, December 1997. DOI: 10.1073/pnas.94.26.14683. PMID: 9405673. PMCID: PMC25092.
Whisstock JC, Pike RN, Jin L, Skinner R, Pei XY, Carrell RW, Lesk AM. Conformational changes in serpins: II. The mechanism of activation of antithrombin by heparin. „Journal of Molecular Biology”. 301 (5), s. 1287–305, September 2000. DOI: 10.1006/jmbi.2000.3982. PMID: 10966821.
Li W, Johnson DJ, Esmon CT, Huntington JA. Structure of the antithrombin-thrombin-heparin ternary complex reveals the antithrombotic mechanism of heparin. „Nature Structural & Molecular Biology”. 11 (9), s. 857–62, September 2004. DOI: 10.1038/nsmb811. PMID: 15311269.
Johnson DJ, Li W, Adams TE, Huntington JA. Antithrombin-S195A factor Xa-heparin structure reveals the allosteric mechanism of antithrombin activation. „The EMBO Journal”. 25 (9), s. 2029–37, May 2006. DOI: 10.1038/sj.emboj.7601089. PMID: 16619025. PMCID: PMC1456925.
Walenga JM, Jeske WP, Samama MM, Frapaise FX, Bick RL, Fareed J. Fondaparinux: a synthetic heparin pentasaccharide as a new antithrombotic agent. „Expert Opinion on Investigational Drugs”. 11 (3), s. 397–407, March 2002. DOI: 10.1517/13543784.11.3.397. PMID: 11866668.
Petitou M, van Boeckel CA. A synthetic antithrombin III binding pentasaccharide is now a drug! What comes next?. „Angewandte Chemie”. 43 (24), s. 3118–33, June 2004. DOI: 10.1002/anie.200300640. PMID: 15199558.
Mushunje A, Evans G, Brennan SO, Carrell RW, Zhou A. Latent antithrombin and its detection, formation and turnover in the circulation. „Journal of Thrombosis and Haemostasis”. 2 (12), s. 2170–7, 2004-23. DOI: 10.1111/j.1538-7836.2004.01047.x. PMID: 15613023.
Zhang Q, Buckle AM, Law RH, Pearce MC, Cabrita LD, Lloyd GJ, Irving JA, Smith AI, Ruzyla K, Rossjohn J, Bottomley SP, Whisstock JC. The N terminus of the serpin, tengpin, functions to trap the metastable native state. „EMBO Reports”. 8 (7), s. 658–63, July 2007. DOI: 10.1038/sj.embor.7400986. PMID: 17557112. PMCID: PMC1905895.
Zhang Q, Law RH, Bottomley SP, Whisstock JC, Buckle AM. A structural basis for loop C-sheet polymerization in serpins. „Journal of Molecular Biology”. 376 (5), s. 1348–59, 2008-03. DOI: 10.1016/j.jmb.2007.12.050. PMID: 18234218.
Pemberton PA, Stein PE, Pepys MB, Potter JM, Carrell RW. Hormone binding globulins undergo serpin conformational change in inflammation. „Nature”. 336 (6196), s. 257–8, 1988-11. DOI: 10.1038/336257a0. PMID: 3143075.
Cao C, Lawrence DA, Li Y, Von Arnim CA, Herz J, Su EJ, Makarova A, Hyman BT, Strickland DK, Zhang L. Endocytic receptor LRP together with tPA and PAI-1 coordinates Mac-1-dependent macrophage migration. „The EMBO Journal”. 25 (9), s. 1860–70, 2006-05. DOI: 10.1038/sj.emboj.7601082. PMID: 16601674. PMCID: PMC1456942.
Jensen JK, Dolmer K, Gettins PG. Specificity of binding of the low density lipoprotein receptor-related protein to different conformational states of the clade E serpins plasminogen activator inhibitor-1 and proteinase nexin-1. „The Journal of Biological Chemistry”. 284 (27), s. 17989–97, 2009-07. DOI: 10.1074/jbc.M109.009530. PMID: 19439404. PMCID: PMC2709341.
Eric Rulifson. Uptake of the necrotic serpin in Drosophila melanogaster via the lipophorin receptor-1. „PLoS Genetics”. 5 (6), s. e1000532, 2009-06. DOI: 10.1371/journal.pgen.1000532. PMID: 19557185. PMCID: PMC2694266.Sprawdź autora:1.
Kaiserman D, Whisstock JC, Bird PI. Mechanisms of serpin dysfunction in disease. „Expert Reviews in Molecular Medicine”. 8 (31), s. 1–19, 2006-01-01. DOI: 10.1017/S1462399406000184. PMID: 17156576.
Hopkins PC, Carrell RW, Stone SR. Effects of mutations in the hinge region of serpins. „Biochemistry”. 32 (30), s. 7650–7, 1993-08. DOI: 10.1021/bi00081a008. PMID: 8347575.
Gooptu B, Hazes B, Chang WS, Dafforn TR, Carrell RW, Read RJ, Lomas DA. Inactive conformation of the serpin alpha(1)-antichymotrypsin indicates two-stage insertion of the reactive loop: implications for inhibitory function and conformational disease. „Proceedings of the National Academy of Sciences of the United States of America”. 97 (1), s. 67–72, 2000-01. DOI: 10.1073/pnas.97.1.67. PMID: 10618372. PMCID: PMC26617.
Homan EP, Rauch F, Grafe I, Lietman C, Doll JA, Dawson B, Bertin T, Napierala D, Morello R, Gibbs R, White L, Miki R, Cohn DH, Crawford S, Travers R, Glorieux FH, Lee B. Mutations in SERPINF1 cause osteogenesis imperfecta type VI. „Journal of Bone and Mineral Research”. 26 (12), s. 2798–803, December 2011. DOI: 10.1002/jbmr.487. PMID: 21826736. PMCID: PMC3214246.
Heit C, Jackson BC, McAndrews M, Wright MW, Thompson DC, Silverman GA, Nebert DW, Vasiliou V. Update of the human and mouse SERPIN gene superfamily. „Human Genomics”. 7, s. 22, 30 October 2013. DOI: 10.1186/1479-7364-7-22. PMID: 24172014. PMCID: PMC3880077.
Owen MC, Brennan SO, Lewis JH, Carrell RW. Mutation of antitrypsin to antithrombin. alpha 1-antitrypsin Pittsburgh (358 Met leads to Arg), a fatal bleeding disorder. „The New England Journal of Medicine”. 309 (12), s. 694–8, September 1983. DOI: 10.1056/NEJM198309223091203. PMID: 6604220.
Lomas DA, Evans DL, Finch JT, Carrell RW. The mechanism of Z alpha 1-antitrypsin accumulation in the liver. „Nature”. 357 (6379), s. 605–7, 1992. DOI: 10.1038/357605a0. PMID: 1608473.
Kroeger H, Miranda E, MacLeod I, Pérez J, Crowther DC, Marciniak SJ, Lomas DA. Endoplasmic reticulum-associated degradation (ERAD) and autophagy cooperate to degrade polymerogenic mutant serpins. „The Journal of Biological Chemistry”. 284 (34), s. 22793–802, 2009. DOI: 10.1074/jbc.M109.027102. PMID: 19549782. PMCID: PMC2755687.
Yamasaki M, Li W, Johnson DJ, Huntington JA. Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization. „Nature”. 455 (7217), s. 1255–8, 2008. DOI: 10.1038/nature07394. PMID: 18923394.
Yamasaki M, Sendall TJ, Pearce MC, Whisstock JC, Huntington JA. Molecular basis of α1-antitrypsin deficiency revealed by the structure of a domain-swapped trimer. „EMBO Reports”. 12 (10), s. 1011–7, October 2011. DOI: 10.1038/embor.2011.171. PMID: 21909074. PMCID: PMC3185345.
Chang WS, Whisstock J, Hopkins PC, Lesk AM, Carrell RW, Wardell MR. Importance of the release of strand 1C to the polymerization mechanism of inhibitory serpins. „Protein Science”. 6 (1), s. 89–98, January 1997. DOI: 10.1002/pro.5560060110. PMID: 9007980. PMCID: PMC2143506.
Miranda E, Pérez J, Ekeowa UI, Hadzic N, Kalsheker N, Gooptu B, Portmann B, Belorgey D, Hill M, Chambers S, Teckman J, Alexander GJ, Marciniak SJ, Lomas DA. A novel monoclonal antibody to characterize pathogenic polymers in liver disease associated with alpha1-antitrypsin deficiency. „Hepatology”. 52 (3), s. 1078–88, September 2010. DOI: 10.1002/hep.23760. PMID: 20583215.
Sandhaus RA. alpha1-Antitrypsin deficiency . 6: new and emerging treatments for alpha1-antitrypsin deficiency. „Thorax”. 59 (10), s. 904–9, October 2004. DOI: 10.1136/thx.2003.006551. PMID: 15454659. PMCID: PMC1746849.
Fregonese L, Stolk J. Hereditary alpha-1-antitrypsin deficiency and its clinical consequences. „Orphanet Journal of Rare Diseases”. 3, s. 16, 2008. DOI: 10.1186/1750-1172-3-16. PMID: 18565211. PMCID: PMC2441617.
Yusa K, Rashid ST, Strick-Marchand H, Varela I, Liu PQ, Paschon DE, Miranda E, Ordóñez A, Hannan NR, Rouhani FJ, Darche S, Alexander G, Marciniak SJ, Fusaki N, Hasegawa M, Holmes MC, Di Santo JP, Lomas DA, Bradley A, Vallier L. Targeted gene correction of α1-antitrypsin deficiency in induced pluripotent stem cells. „Nature”. 478 (7369), s. 391–4, 2011. DOI: 10.1038/nature10424. PMID: 21993621. PMCID: PMC3198846.
Mallya M, Phillips RL, Saldanha SA, Gooptu B, Brown SC, Termine DJ, Shirvani AM, Wu Y, Sifers RN, Abagyan R, Lomas DA. Small molecules block the polymerization of Z alpha1-antitrypsin and increase the clearance of intracellular aggregates. „Journal of Medicinal Chemistry”. 50 (22), s. 5357–63, 2007. DOI: 10.1021/jm070687z. PMID: 17918823. PMCID: PMC2631427.
Gosai SJ, Kwak JH, Luke CJ, Long OS, King DE, Kovatch KJ, Johnston PA, Shun TY, Lazo JS, Perlmutter DH, Silverman GA, Pak SC. Automated high-content live animal drug screening using C. elegans expressing the aggregation prone serpin α1-antitrypsin Z. „PloS One”. 5 (11), s. e15460, 2010. DOI: 10.1371/journal.pone.0015460. PMID: 21103396. PMCID: PMC2980495.
Cabrita LD, Irving JA, Pearce MC, Whisstock JC, Bottomley SP. Aeropin from the extremophile Pyrobaculum aerophilum bypasses the serpin misfolding trap. „The Journal of Biological Chemistry”. 282 (37), s. 26802–9, 2007. DOI: 10.1074/jbc.M705020200. PMID: 17635906.
Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. „Cell”. 129 (2), s. 263–75, April 2007. DOI: 10.1016/j.cell.2007.02.042. PMID: 17448989.
Gooptu B, Dickens JA, Lomas DA. The molecular and cellular pathology of α₁-antitrypsin deficiency. „Trends in Molecular Medicine”. 20 (2), s. 116–27, 2014. DOI: 10.1016/j.molmed.2013.10.007. PMID: 24374162.
Seixas S, Suriano G, Carvalho F, Seruca R, Rocha J, Di Rienzo A. Sequence diversity at the proximal 14q32.1 SERPIN subcluster: evidence for natural selection favoring the pseudogenization of SERPINA2. „Molecular Biology and Evolution”. 24 (2), s. 587–98, February 2007. DOI: 10.1093/molbev/msl187. PMID: 17135331.
Kalsheker NA. Alpha 1-antichymotrypsin. „The International Journal of Biochemistry & Cell Biology”. 28 (9), s. 961–4, September 1996. DOI: 10.1016/1357-2725(96)00032-5. PMID: 8930118.
Santamaria M, Pardo-Saganta A, Alvarez-Asiain L, Di Scala M, Qian C, Prieto J, Avila MA. Nuclear α1-antichymotrypsin promotes chromatin condensation and inhibits proliferation of human hepatocellular carcinoma cells. „Gastroenterology”. 144 (4), s. 818–828.e4, April 2013. DOI: 10.1053/j.gastro.2012.12.029. PMID: 23295442.
Chao J, Stallone JN, Liang YM, Chen LM, Wang DZ, Chao L. Kallistatin is a potent new vasodilator. „The Journal of Clinical Investigation”. 100 (1), s. 11–7, July 1997. DOI: 10.1172/JCI119502. PMID: 9202051. PMCID: PMC508159.
Miao RQ, Agata J, Chao L, Chao J. Kallistatin is a new inhibitor of angiogenesis and tumor growth. „Blood”. 100 (9), s. 3245–52, November 2002. DOI: 10.1182/blood-2002-01-0185. PMID: 12384424.
Liu Y, Bledsoe G, Hagiwara M, Shen B, Chao L, Chao J. Depletion of endogenous kallistatin exacerbates renal and cardiovascular oxidative stress, inflammation, and organ remodeling. „American Journal of Physiology. Renal Physiology”. 303 (8), s. F1230-8, October 2012. DOI: 10.1152/ajprenal.00257.2012. PMID: 22811485.
Geiger M. Protein C inhibitor, a serpin with functions in- and outside vascular biology. „Thrombosis and Haemostasis”. 97 (3), s. 343–7, March 2007. DOI: 10.1160/th06-09-0488. PMID: 17334499.
Baumgärtner P, Geiger M, Zieseniss S, Malleier J, Huntington JA, Hochrainer K, Bielek E, Stoeckelhuber M, Lauber K, Scherfeld D, Schwille P, Wäldele K, Beyer K, Engelmann B. Phosphatidylethanolamine critically supports internalization of cell-penetrating protein C inhibitor. „The Journal of Cell Biology”. 179 (4), s. 793–804, November 2007. DOI: 10.1083/jcb.200707165. PMID: 18025309. PMCID: PMC2080921.
Uhrin P, Dewerchin M, Hilpert M, Chrenek P, Schöfer C, Zechmeister-Machhart M, Krönke G, Vales A, Carmeliet P, Binder BR, Geiger M. Disruption of the protein C inhibitor gene results in impaired spermatogenesis and male infertility. „The Journal of Clinical Investigation”. 106 (12), s. 1531–9, December 2000. DOI: 10.1172/JCI10768. PMID: 11120760. PMCID: PMC381472.
Han MH, Hwang SI, Roy DB, Lundgren DH, Price JV, Ousman SS, Fernald GH, Gerlitz B, Robinson WH, Baranzini SE, Grinnell BW, Raine CS, Sobel RA, Han DK, Steinman L. Proteomic analysis of active multiple sclerosis lesions reveals therapeutic targets. „Nature”. 451 (7182), s. 1076–81, 2008. DOI: 10.1038/nature06559. PMID: 18278032.
Torpy DJ, Ho JT. Corticosteroid-binding globulin gene polymorphisms: clinical implications and links to idiopathic chronic fatigue disorders. „Clinical Endocrinology”. 67 (2), s. 161–7, August 2007. DOI: 10.1111/j.1365-2265.2007.02890.x. PMID: 17547679.
Bartalena L, Robbins J. Variations in thyroid hormone transport proteins and their clinical implications. „Thyroid”. 2 (3), s. 237–45, 1992. DOI: 10.1089/thy.1992.2.237. PMID: 1422238.
Persani L. Clinical review: Central hypothyroidism: pathogenic, diagnostic, and therapeutic challenges. „The Journal of Clinical Endocrinology and Metabolism”. 97 (9), s. 3068–78, September 2012. DOI: 10.1210/jc.2012-1616. PMID: 22851492.
Kumar R, Singh VP, Baker KM. The intracellular renin-angiotensin system: a new paradigm. „Trends in Endocrinology and Metabolism”. 18 (5), s. 208–14, 2007. DOI: 10.1016/j.tem.2007.05.001. PMID: 17509892.
Jeunemaitre X, Gimenez-Roqueplo AP, Célérier J, Corvol P. Angiotensinogen variants and human hypertension. „Current Hypertension Reports”. 1 (1), s. 31–41, 1999. DOI: 10.1007/s11906-999-0071-0. PMID: 10981040.
Sethi AA, Nordestgaard BG, Tybjaerg-Hansen A. Angiotensinogen gene polymorphism, plasma angiotensinogen, and risk of hypertension and ischemic heart disease: a meta-analysis. „Arteriosclerosis, Thrombosis, and Vascular Biology”. 23 (7), s. 1269–75, 2003. DOI: 10.1161/01.ATV.0000079007.40884.5C. PMID: 12805070.
Frazer JK, Jackson DG, Gaillard JP, Lutter M, Liu YJ, Banchereau J, Capra JD, Pascual V. Identification of centerin: a novel human germinal center B cell-restricted serpin. „European Journal of Immunology”. 30 (10), s. 3039–48, October 2000. DOI: 10.1002/1521-4141(200010)30:10<3039::AID-IMMU3039>3.0.CO;2-H. PMID: 11069088.
Paterson MA, Horvath AJ, Pike RN, Coughlin PB. Molecular characterization of centerin, a germinal centre cell serpin. „The Biochemical Journal”. 405 (3), s. 489–94, August 2007. DOI: 10.1042/BJ20070174. PMID: 17447896. PMCID: PMC2267310.
Paterson MA, Hosking PS, Coughlin PB. Expression of the serpin centerin defines a germinal center phenotype in B-cell lymphomas. „American Journal of Clinical Pathology”. 130 (1), s. 117–26, July 2008. DOI: 10.1309/9QKE68QU7B825A3U. PMID: 18550480.
Ashton-Rickardt PG. An emerging role for Serine Protease Inhibitors in T lymphocyte immunity and beyond. „Immunology Letters”. 152 (1), s. 65–76, April 2013. DOI: 10.1016/j.imlet.2013.04.004. PMID: 23624075.
Hida K, Wada J, Eguchi J, Zhang H, Baba M, Seida A, Hashimoto I, Okada T, Yasuhara A, Nakatsuka A, Shikata K, Hourai S, Futami J, Watanabe E, Matsuki Y, Hiramatsu R, Akagi S, Makino H, Kanwar YS. Visceral adipose tissue-derived serine protease inhibitor: a unique insulin-sensitizing adipocytokine in obesity. „Proceedings of the National Academy of Sciences of the United States of America”. 102 (30), s. 10610–5, July 2005. DOI: 10.1073/pnas.0504703102. PMID: 16030142. PMCID: PMC1180799.
Feng R, Li Y, Wang C, Luo C, Liu L, Chuo F, Li Q, Sun C. Higher vaspin levels in subjects with obesity and type 2 diabetes mellitus: a meta-analysis. „Diabetes Research and Clinical Practice”. 106 (1), s. 88–94, October 2014. DOI: 10.1016/j.diabres.2014.07.026. PMID: 25151227.
Remold-O'Donnell E, Chin J, Alberts M. Sequence and molecular characterization of human monocyte/neutrophil elastase inhibitor. „Proceedings of the National Academy of Sciences of the United States of America”. 89 (12), s. 5635–9, June 1992. DOI: 10.1073/pnas.89.12.5635. PMID: 1376927. PMCID: PMC49347.
Benarafa C, Priebe GP, Remold-O'Donnell E. The neutrophil serine protease inhibitor serpinb1 preserves lung defense functions in Pseudomonas aeruginosa infection. „The Journal of Experimental Medicine”. 204 (8), s. 1901–9, August 2007. DOI: 10.1084/jem.20070494. PMID: 17664292. PMCID: PMC2118684.
Antalis TM, La Linn M, Donnan K, Mateo L, Gardner J, Dickinson JL, Buttigieg K, Suhrbier A. The serine proteinase inhibitor (serpin) plasminogen activation inhibitor type 2 protects against viral cytopathic effects by constitutive interferon alpha/beta priming. „The Journal of Experimental Medicine”. 187 (11), s. 1799–811, June 1998. DOI: 10.1084/jem.187.11.1799. PMID: 9607921. PMCID: PMC2212304.
Zhao A, Yang Z, Sun R, Grinchuk V, Netzel-Arnett S, Anglin IE, Driesbaugh KH, Notari L, Bohl JA, Madden KB, Urban JF, Antalis TM, Shea-Donohue T. SerpinB2 is critical to Th2 immunity against enteric nematode infection. „Journal of Immunology”. 190 (11), s. 5779–87, June 2013. DOI: 10.4049/jimmunol.1200293. PMID: 23630350.
Dougherty KM, Pearson JM, Yang AY, Westrick RJ, Baker MS, Ginsburg D. The plasminogen activator inhibitor-2 gene is not required for normal murine development or survival. „Proceedings of the National Academy of Sciences of the United States of America”. 96 (2), s. 686–91, 1999. DOI: 10.1073/pnas.96.2.686. PMID: 9892694. PMCID: PMC15197.
Turato C, Pontisso P. SERPINB3 (serpin peptidase inhibitor, clade B (ovalbumin), member 3). „Atlas of Genetics and Cytogenetics in Oncology and Haematology”. 19 (3), s. 202–209, March 2015. DOI: 10.4267/2042/56413. PMID: 25984243.
Sivaprasad U, Askew DJ, Ericksen MB, Gibson AM, Stier MT, Brandt EB, Bass SA, Daines MO, Chakir J, Stringer KF, Wert SE, Whitsett JA, Le Cras TD, Wills-Karp M, Silverman GA, Khurana Hershey GK. A nonredundant role for mouse Serpinb3a in the induction of mucus production in asthma. „The Journal of Allergy and Clinical Immunology”. 127 (1), s. 254–61, 261.e1-6, 2011. DOI: 10.1016/j.jaci.2010.10.009. PMID: 21126757. PMCID: PMC3058372.
Schick C, Kamachi Y, Bartuski AJ, Cataltepe S, Schechter NM, Pemberton PA, Silverman GA. Squamous cell carcinoma antigen 2 is a novel serpin that inhibits the chymotrypsin-like proteinases cathepsin G and mast cell chymase. „The Journal of Biological Chemistry”. 272 (3), s. 1849–55, January 1997. DOI: 10.1074/jbc.272.3.1849. PMID: 8999871.
Teoh SS, Whisstock JC, Bird PI. Maspin (SERPINB5) is an obligate intracellular serpin. „The Journal of Biological Chemistry”. 285 (14), s. 10862–9, April 2010. DOI: 10.1074/jbc.M109.073171. PMID: 20123984. PMCID: PMC2856292.
Zou Z, Anisowicz A, Hendrix MJ, Thor A, Neveu M, Sheng S, Rafidi K, Seftor E, Sager R. Maspin, a serpin with tumor-suppressing activity in human mammary epithelial cells. „Science”. 263 (5146), s. 526–9, 1994. DOI: 10.1126/science.8290962. PMID: 8290962.
Teoh SS, Vieusseux J, Prakash M, Berkowicz S, Luu J, Bird CH, Law RH, Rosado C, Price JT, Whisstock JC, Bird PI. Maspin is not required for embryonic development or tumour suppression. „Nature Communications”. 5, s. 3164, 2014. DOI: 10.1038/ncomms4164. PMID: 24445777. PMCID: PMC3905777.
Gao F, Shi HY, Daughty C, Cella N, Zhang M. Maspin plays an essential role in early embryonic development. „Development”. 131 (7), s. 1479–89, 2004. DOI: 10.1242/dev.01048. PMID: 14985257.
Tan J, Prakash MD, Kaiserman D, Bird PI. Absence of SERPINB6A causes sensorineural hearing loss with multiple histopathologies in the mouse inner ear. „The American Journal of Pathology”. 183 (1), s. 49–59, July 2013. DOI: 10.1016/j.ajpath.2013.03.009. PMID: 23669344.
Scarff KL, Ung KS, Nandurkar H, Crack PJ, Bird CH, Bird PI. Targeted disruption of SPI3/Serpinb6 does not result in developmental or growth defects, leukocyte dysfunction, or susceptibility to stroke. „Molecular and Cellular Biology”. 24 (9), s. 4075–82, May 2004. DOI: 10.1128/MCB.24.9.4075-4082.2004. PMID: 15082799. PMCID: PMC387772.
Miyata T, Inagi R, Nangaku M, Imasawa T, Sato M, Izuhara Y, Suzuki D, Yoshino A, Onogi H, Kimura M, Sugiyama S, Kurokawa K. Overexpression of the serpin megsin induces progressive mesangial cell proliferation and expansion. „The Journal of Clinical Investigation”. 109 (5), s. 585–93, March 2002. DOI: 10.1172/JCI14336. PMID: 11877466. PMCID: PMC150894.
Miyata T, Li M, Yu X, Hirayama N. Megsin gene: its genomic analysis, pathobiological functions, and therapeutic perspectives. „Current Genomics”. 8 (3), s. 203–8, 2007. DOI: 10.2174/138920207780833856. PMID: 18645605. PMCID: PMC2435355.
Kubo A. Nagashima-type palmoplantar keratosis: a common Asian type caused by SERPINB7 protease inhibitor deficiency. „The Journal of Investigative Dermatology”. 134 (8), s. 2076–9, 2014. DOI: 10.1038/jid.2014.156. PMID: 25029323.
Dahlen JR, Jean F, Thomas G, Foster DC, Kisiel W. Inhibition of soluble recombinant furin by human proteinase inhibitor 8. „The Journal of Biological Chemistry”. 273 (4), s. 1851–4, 1998. DOI: 10.1074/jbc.273.4.1851. PMID: 9442015.
Sun J, Bird CH, Sutton V, McDonald L, Coughlin PB, De Jong TA, Trapani JA, Bird PI. A cytosolic granzyme B inhibitor related to the viral apoptotic regulator cytokine response modifier A is present in cytotoxic lymphocytes. „The Journal of Biological Chemistry”. 271 (44), s. 27802–9, 1996. DOI: 10.1074/jbc.271.44.27802. PMID: 8910377.
Zhang M, Park SM, Wang Y, Shah R, Liu N, Murmann AE, Wang CR, Peter ME, Ashton-Rickardt PG. Serine protease inhibitor 6 protects cytotoxic T cells from self-inflicted injury by ensuring the integrity of cytotoxic granules. „Immunity”. 24 (4), s. 451–61, April 2006. DOI: 10.1016/j.immuni.2006.02.002. PMID: 16618603.
Rizzitelli A, Meuter S, Vega Ramos J, Bird CH, Mintern JD, Mangan MS, Villadangos J, Bird PI. Serpinb9 (Spi6)-deficient mice are impaired in dendritic cell-mediated antigen cross-presentation. „Immunology and Cell Biology”. 90 (9), s. 841–51, 2012. DOI: 10.1038/icb.2012.29. PMID: 22801574.
Askew DJ, Cataltepe S, Kumar V, Edwards C, Pace SM, Howarth RN, Pak SC, Askew YS, Brömme D, Luke CJ, Whisstock JC, Silverman GA. SERPINB11 is a new noninhibitory intracellular serpin. Common single nucleotide polymorphisms in the scaffold impair conformational change. „The Journal of Biological Chemistry”. 282 (34), s. 24948–60, August 2007. DOI: 10.1074/jbc.M703182200. PMID: 17562709.
Finno CJ, Stevens C, Young A, Affolter V, Joshi NA, Ramsay S, Bannasch DL. SERPINB11 frameshift variant associated with novel hoof specific phenotype in Connemara ponies. „PLoS Genetics”. 11 (4), s. e1005122, 2015. DOI: 10.1371/journal.pgen.1005122. PMID: 25875171.
Askew YS, Pak SC, Luke CJ, Askew DJ, Cataltepe S, Mills DR, Kato H, Lehoczky J, Dewar K, Birren B, Silverman GA. SERPINB12 is a novel member of the human ov-serpin family that is widely expressed and inhibits trypsin-like serine proteinases. „The Journal of Biological Chemistry”. 276 (52), s. 49320–30, December 2001. DOI: 10.1074/jbc.M108879200. PMID: 11604408.
Welss T, Sun J, Irving JA, Blum R, Smith AI, Whisstock JC, Pike RN, von Mikecz A, Ruzicka T, Bird PI, Abts HF. Hurpin is a selective inhibitor of lysosomal cathepsin L and protects keratinocytes from ultraviolet-induced apoptosis. „Biochemistry”. 42 (24), s. 7381–9, 2003. DOI: 10.1021/bi027307q. PMID: 12809493.
Ishiguro K, Kojima T, Kadomatsu K, Nakayama Y, Takagi A, Suzuki M, Takeda N, Ito M, Yamamoto K, Matsushita T, Kusugami K, Muramatsu T, Saito H. Complete antithrombin deficiency in mice results in embryonic lethality. „The Journal of Clinical Investigation”. 106 (7), s. 873–8, October 2000. DOI: 10.1172/JCI10489. PMID: 11018075. PMCID: PMC517819.
Vicente CP, He L, Pavão MS, Tollefsen DM. Antithrombotic activity of dermatan sulfate in heparin cofactor II-deficient mice. „Blood”. 104 (13), s. 3965–70, December 2004. DOI: 10.1182/blood-2004-02-0598. PMID: 15315969.
Aihara K, Azuma H, Akaike M, Ikeda Y, Sata M, Takamori N, Yagi S, Iwase T, Sumitomo Y, Kawano H, Yamada T, Fukuda T, Matsumoto T, Sekine K, Sato T, Nakamichi Y, Yamamoto Y, Yoshimura K, Watanabe T, Nakamura T, Oomizu A, Tsukada M, Hayashi H, Sudo T, Kato S, Matsumoto T. Strain-dependent embryonic lethality and exaggerated vascular remodeling in heparin cofactor II-deficient mice. „The Journal of Clinical Investigation”. 117 (6), s. 1514–26, June 2007. DOI: 10.1172/JCI27095. PMID: 17549254. PMCID: PMC1878511.
Cale JM, Lawrence DA. Structure-function relationships of plasminogen activator inhibitor-1 and its potential as a therapeutic agent. „Current Drug Targets”. 8 (9), s. 971–81, September 2007. DOI: 10.2174/138945007781662337. PMID: 17896949.
Lino MM, Atanasoski S, Kvajo M, Fayard B, Moreno E, Brenner HR, Suter U, Monard D. Mice lacking protease nexin-1 show delayed structural and functional recovery after sciatic nerve crush. „The Journal of Neuroscience”. 27 (14), s. 3677–85, April 2007. DOI: 10.1523/JNEUROSCI.0277-07.2007. PMID: 17409231.
Murer V, Spetz JF, Hengst U, Altrogge LM, de Agostini A, Monard D. Male fertility defects in mice lacking the serine protease inhibitor protease nexin-1. „Proceedings of the National Academy of Sciences of the United States of America”. 98 (6), s. 3029–33, March 2001. DOI: 10.1073/pnas.051630698. PMID: 11248026. PMCID: PMC30601.
Doll JA, Stellmach VM, Bouck NP, Bergh AR, Lee C, Abramson LP, Cornwell ML, Pins MR, Borensztajn J, Crawford SE. Pigment epithelium-derived factor regulates the vasculature and mass of the prostate and pancreas. „Nature Medicine”. 9 (6), s. 774–80, June 2003. DOI: 10.1038/nm870. PMID: 12740569.
Becerra SP, Perez-Mediavilla LA, Weldon JE, Locatelli-Hoops S, Senanayake P, Notari L, Notario V, Hollyfield JG. Pigment epithelium-derived factor binds to hyaluronan. Mapping of a hyaluronan binding site. „The Journal of Biological Chemistry”. 283 (48), s. 33310–20, November 2008. DOI: 10.1074/jbc.M801287200. PMID: 18805795. PMCID: PMC2586245.
Andreu-Agulló C, Morante-Redolat JM, Delgado AC, Fariñas I. Vascular niche factor PEDF modulates Notch-dependent stemness in the adult subependymal zone. „Nature Neuroscience”. 12 (12), s. 1514–23, December 2009. DOI: 10.1038/nn.2437. PMID: 19898467.
Carpenter SL, Mathew P. Alpha2-antiplasmin and its deficiency: fibrinolysis out of balance. „Haemophilia”. 14 (6), s. 1250–4, November 2008. DOI: 10.1111/j.1365-2516.2008.01766.x. PMID: 19141165.
R. Favier, N. Aoki, P. De Moerloose. Congenital α2-plasmin inhibitor deficiencies: a review. „British Journal of Haematology”. 114 (1), s. 4–10, 1 July 2001. DOI: 10.1046/j.1365-2141.2001.02845.x. ISSN1365-2141.
Beinrohr L, Harmat V, Dobó J, Lörincz Z, Gál P, Závodszky P. C1 inhibitor serpin domain structure reveals the likely mechanism of heparin potentiation and conformational disease. „The Journal of Biological Chemistry”. 282 (29), s. 21100–9, July 2007. DOI: 10.1074/jbc.M700841200. PMID: 17488724.
Mollnes TE, Jokiranta TS, Truedsson L, Nilsson B, Rodriguez de Cordoba S, Kirschfink M. Complement analysis in the 21st century. „Molecular Immunology”. 44 (16), s. 3838–49, September 2007. DOI: 10.1016/j.molimm.2007.06.150. PMID: 17768101.
Triggianese P, Chimenti MS, Toubi E, Ballanti E, Guarino MD, Perricone C, Perricone R. The autoimmune side of hereditary angioedema: insights on the pathogenesis. „Autoimmunity Reviews”. 14 (8), s. 665–9, August 2015. DOI: 10.1016/j.autrev.2015.03.006. PMID: 25827463.
Nagai N, Hosokawa M, Itohara S, Adachi E, Matsushita T, Hosokawa N, Nagata K. Embryonic lethality of molecular chaperone hsp47 knockout mice is associated with defects in collagen biosynthesis. „The Journal of Cell Biology”. 150 (6), s. 1499–506, September 2000. DOI: 10.1083/jcb.150.6.1499. PMID: 10995453. PMCID: PMC2150697.
Marini JC, Reich A, Smith SM. Osteogenesis imperfecta due to mutations in non-collagenous genes: lessons in the biology of bone formation. „Current Opinion in Pediatrics”. 26 (4), s. 500–7, August 2014. DOI: 10.1097/MOP.0000000000000117. PMID: 25007323. PMCID: PMC4183132.
Osterwalder T, Cinelli P, Baici A, Pennella A, Krueger SR, Schrimpf SP, Meins M, Sonderegger P. The axonally secreted serine proteinase inhibitor, neuroserpin, inhibits plasminogen activators and plasmin but not thrombin. „The Journal of Biological Chemistry”. 273 (4), s. 2312–21, January 1998. DOI: 10.1074/jbc.273.4.2312. PMID: 9442076.
Crowther DC. Familial conformational diseases and dementias. „Human Mutation”. 20 (1), s. 1–14, July 2002. DOI: 10.1002/humu.10100. PMID: 12112652.
Ozaki K, Nagata M, Suzuki M, Fujiwara T, Miyoshi Y, Ishikawa O, Ohigashi H, Imaoka S, Takahashi E, Nakamura Y. Isolation and characterization of a novel human pancreas-specific gene, pancpin, that is down-regulated in pancreatic cancer cells. „Genes, Chromosomes & Cancer”. 22 (3), s. 179–85, July 1998. DOI: 10.1002/(SICI)1098-2264(199807)22:3<179::AID-GCC3>3.0.CO;2-T. PMID: 9624529.
Loftus SK, Cannons JL, Incao A, Pak E, Chen A, Zerfas PM, Bryant MA, Biesecker LG, Schwartzberg PL, Pavan WJ. Acinar cell apoptosis in Serpini2-deficient mice models pancreatic insufficiency. „PLoS Genetics”. 1 (3), s. e38, September 2005. DOI: 10.1371/journal.pgen.0010038. PMID: 16184191. PMCID: PMC1231717.
Padua MB, Kowalski AA, Cañas MY, Hansen PJ. The molecular phylogeny of uterine serpins and its relationship to evolution of placentation. „FASEB Journal”. 24 (2), s. 526–37, February 2010. DOI: 10.1096/fj.09-138453. PMID: 19825977.
Padua MB, Hansen PJ. Evolution and function of the uterine serpins (SERPINA14). „American Journal of Reproductive Immunology”. 64 (4), s. 265–74, October 2010. DOI: 10.1111/j.1600-0897.2010.00901.x. PMID: 20678169.
Reichhart JM. Tip of another iceberg: Drosophila serpins. „Trends in Cell Biology”. 15 (12), s. 659–65, December 2005. DOI: 10.1016/j.tcb.2005.10.001. PMID: 16260136.
Tang H, Kambris Z, Lemaitre B, Hashimoto C. A serpin that regulates immune melanization in the respiratory system of Drosophila. „Developmental Cell”. 15 (4), s. 617–26, October 2008. DOI: 10.1016/j.devcel.2008.08.017. PMID: 18854145. PMCID: PMC2671232.
Scherfer C, Tang H, Kambris Z, Lhocine N, Hashimoto C, Lemaitre B. Drosophila Serpin-28D regulates hemolymph phenoloxidase activity and adult pigmentation. „Developmental Biology”. 323 (2), s. 189–96, November 2008. DOI: 10.1016/j.ydbio.2008.08.030. PMID: 18801354.
Rushlow C. Dorsoventral patterning: a serpin pinned down at last. „Current Biology”. 14 (1), s. R16-8, January 2004. DOI: 10.1016/j.cub.2003.12.015. PMID: 14711428.
Ligoxygakis P, Roth S, Reichhart JM. A serpin regulates dorsal-ventral axis formation in the Drosophila embryo. „Current Biology”. 13 (23), s. 2097–102, December 2003. DOI: 10.1016/j.cub.2003.10.062. PMID: 14654000.
Jiang R, Zhang B, Kurokawa K, So YI, Kim EH, Hwang HO, Lee JH, Shiratsuchi A, Zhang J, Nakanishi Y, Lee HS, Lee BL. 93-kDa twin-domain serine protease inhibitor (Serpin) has a regulatory function on the beetle Toll proteolytic signaling cascade. „The Journal of Biological Chemistry”. 286 (40), s. 35087–95, October 2011. DOI: 10.1074/jbc.M111.277343. PMID: 21862574. PMCID: PMC3186399.
Pak SC, Kumar V, Tsu C, Luke CJ, Askew YS, Askew DJ, Mills DR, Brömme D, Silverman GA. SRP-2 is a cross-class inhibitor that participates in postembryonic development of the nematode Caenorhabditis elegans: initial characterization of the clade L serpins. „The Journal of Biological Chemistry”. 279 (15), s. 15448–59, April 2004. DOI: 10.1074/jbc.M400261200. PMID: 14739286.
Luke CJ, Pak SC, Askew YS, Naviglia TL, Askew DJ, Nobar SM, Vetica AC, Long OS, Watkins SC, Stolz DB, Barstead RJ, Moulder GL, Brömme D, Silverman GA. An intracellular serpin regulates necrosis by inhibiting the induction and sequelae of lysosomal injury. „Cell”. 130 (6), s. 1108–19, September 2007. DOI: 10.1016/j.cell.2007.07.013. PMID: 17889653. PMCID: PMC2128786.
Hejgaard J, Rasmussen SK, Brandt A, SvendsenI. Sequence homology between barley endosperm protein Z and protease inhibitors of the alpha-1-antitrypsin family. „FEBS Lett.”. 180 (1), s. 89–94, 1985. DOI: 10.1016/0014-5793(85)80238-6.
Dahl SW, Rasmussen SK, Petersen LC, Hejgaard J. Inhibition of coagulation factors by recombinant barley serpin BSZx. „FEBS Letters”. 394 (2), s. 165–8, September 1996. DOI: 10.1016/0014-5793(96)00940-4. PMID: 8843156.
Hejgaard J. Inhibitory serpins from rye grain with glutamine as P1 and P2 residues in the reactive center. „FEBS Letters”. 488 (3), s. 149–53, January 2001. DOI: 10.1016/S0014-5793(00)02425-X. PMID: 11163762.
Ostergaard H, Rasmussen SK, Roberts TH, Hejgaard J. Inhibitory serpins from wheat grain with reactive centers resembling glutamine-rich repeats of prolamin storage proteins. Cloning and characterization of five major molecular forms. „The Journal of Biological Chemistry”. 275 (43), s. 33272–9, October 2000. DOI: 10.1074/jbc.M004633200. PMID: 10874043.
Yoo BC, Aoki K, Xiang Y, Campbell LR, Hull RJ, Xoconostle-Cázares B, Monzer J, Lee JY, Ullman DE, Lucas WJ. Characterization of cucurbita maxima phloem serpin-1 (CmPS-1). A developmentally regulated elastase inhibitor. „The Journal of Biological Chemistry”. 275 (45), s. 35122–8, November 2000. DOI: 10.1074/jbc.M006060200. PMID: 10960478.
la Cour Petersen M, Hejgaard J, Thompson GA, Schulz A. Cucurbit phloem serpins are graft-transmissible and appear to be resistant to turnover in the sieve element-companion cell complex. „Journal of Experimental Botany”. 56 (422), s. 3111–20, December 2005. DOI: 10.1093/jxb/eri308. PMID: 16246856.
Roberts TH, Hejgaard J. Serpins in plants and green algae. „Functional & Integrative Genomics”. 8 (1), s. 1–27, February 2008. DOI: 10.1007/s10142-007-0059-2. PMID: 18060440.
Lampl N, Alkan N, Davydov O, Fluhr R. Set-point control of RD21 protease activity by AtSerpin1 controls cell death in Arabidopsis. „The Plant Journal”. 74 (3), s. 498–510, May 2013. DOI: 10.1111/tpj.12141. PMID: 23398119.
Ahn JW, Atwell BJ, Roberts TH. Serpin genes AtSRP2 and AtSRP3 are required for normal growth sensitivity to a DNA alkylating agent in Arabidopsis. „BMC Plant Biology”. 9, s. 52, 2009. DOI: 10.1186/1471-2229-9-52. PMID: 19426562. PMCID: PMC2689219.
Kang S, Barak Y, Lamed R, Bayer EA, Morrison M. The functional repertoire of prokaryote cellulosomes includes the serpin superfamily of serine proteinase inhibitors. „Molecular Microbiology”. 60 (6), s. 1344–54, June 2006. DOI: 10.1111/j.1365-2958.2006.05182.x. PMID: 16796673.
Irving JA, Cabrita LD, Rossjohn J, Pike RN, Bottomley SP, Whisstock JC. The 1.5 A crystal structure of a prokaryote serpin: controlling conformational change in a heated environment. „Structure”. 11 (4), s. 387–97, April 2003. DOI: 10.1016/S0969-2126(03)00057-1. PMID: 12679017.
Fulton KF, Buckle AM, Cabrita LD, Irving JA, Butcher RE, Smith I, Reeve S, Lesk AM, Bottomley SP, Rossjohn J, Whisstock JC. The high resolution crystal structure of a native thermostable serpin reveals the complex mechanism underpinning the stressed to relaxed transition. „The Journal of Biological Chemistry”. 280 (9), s. 8435–42, March 2005. DOI: 10.1074/jbc.M410206200. PMID: 15590653.
Turner PC, Moyer RW. Poxvirus immune modulators: functional insights from animal models. „Virus Research”. 88 (1-2), s. 35–53, September 2002. DOI: 10.1016/S0168-1702(02)00119-3. PMID: 12297326.
Richardson J, Viswanathan K, Lucas A. Serpins, the vasculature, and viral therapeutics. „Frontiers in Bioscience”. 11, s. 1042–56, 2006. DOI: 10.2741/1862. PMID: 16146796.
Jiang J, Arp J, Kubelik D, Zassoko R, Liu W, Wise Y, Macaulay C, Garcia B, McFadden G, Lucas AR, Wang H. Induction of indefinite cardiac allograft survival correlates with toll-like receptor 2 and 4 downregulation after serine protease inhibitor-1 (Serp-1) treatment. „Transplantation”. 84 (9), s. 1158–67, November 2007. DOI: 10.1097/01.tp.0000286099.50532.b0. PMID: 17998872.
Dai E, Guan H, Liu L, Little S, McFadden G, Vaziri S, Cao H, Ivanova IA, Bocksch L, Lucas A. Serp-1, a viral anti-inflammatory serpin, regulates cellular serine proteinase and serpin responses to vascular injury. „The Journal of Biological Chemistry”. 278 (20), s. 18563–72, May 2003. DOI: 10.1074/jbc.M209683200. PMID: 12637546.
Munuswamy-Ramanujam G, Khan KA, Lucas AR. Viral anti-inflammatory reagents: the potential for treatment of arthritic and vasculitic disorders. „Endocrine, Metabolic & Immune Disorders Drug Targets”. 6 (4), s. 331–43, December 2006. DOI: 10.2174/187153006779025720. PMID: 17214579.
Renatus M, Zhou Q, Stennicke HR, Snipas SJ, Turk D, Bankston LA, Liddington RC, Salvesen GS. Crystal structure of the apoptotic suppressor CrmA in its cleaved form. „Structure”. 8 (7), s. 789–97, 2000. DOI: 10.1016/S0969-2126(00)00165-9. PMID: 10903953.
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”. 276 (36), s. 33293–6, September 2001. DOI: 10.1074/jbc.R100016200. PMID: 11435447.
Silverman GA, Whisstock JC, Bottomley SP, Huntington JA, Kaiserman D, Luke CJ, Pak SC, Reichhart JM, Bird PI. Serpins flex their muscle: I. Putting the clamps on proteolysis in diverse biological systems. „The Journal of Biological Chemistry”. 285 (32), s. 24299–305, August 2010. DOI: 10.1074/jbc.R110.112771. PMID: 20498369. PMCID: PMC2915665.
Whisstock JC, Silverman GA, Bird PI, Bottomley SP, Kaiserman D, Luke CJ, Pak SC, Reichhart JM, Huntington JA. Serpins flex their muscle: II. Structural insights into target peptidase recognition, polymerization, and transport functions. „The Journal of Biological Chemistry”. 285 (32), s. 24307–12, August 2010. DOI: 10.1074/jbc.R110.141408. PMID: 20498368. PMCID: PMC2915666.
Gettins PG. Serpin structure, mechanism, and function. „Chemical Reviews”. 102 (12), s. 4751–804, December 2002. DOI: 10.1021/cr010170. PMID: 12475206.
Whisstock JC, Bottomley SP. Molecular gymnastics: serpin structure, folding and misfolding. „Current Opinion in Structural Biology”. 16 (6), s. 761–8, December 2006. DOI: 10.1016/j.sbi.2006.10.005. PMID: 17079131.
Law RH, Zhang Q, McGowan S, Buckle AM, Silverman GA, Wong W, Rosado CJ, Langendorf CG, Pike RN, Bird PI, Whisstock JC. An overview of the serpin superfamily. „Genome Biology”. 7 (5), s. 216, 2006. DOI: 10.1186/gb-2006-7-5-216. PMID: 16737556. PMCID: PMC1779521.
Stein PE, Carrell RW. What do dysfunctional serpins tell us about molecular mobility and disease?. „Nature Structural Biology”. 2 (2), s. 96–113, 1995. DOI: 10.1038/nsb0295-96. PMID: 7749926.
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”. 105 (8), s. 1129–39, 2011. DOI: 10.1016/j.rmed.2011.02.002. PMID: 21367592.
Laurell CB, Eriksson S. The electrophoretic α1-globulin pattern of serum in α1-antitrypsin deficiency. 1963. „Copd”. 10 Suppl 1, s. 3–8, 2013. DOI: 10.3109/15412555.2013.771956. PMID: 23527532.
Egeberg O. Inherited antithrombin deficiency causing thrombophilia. „Thrombosis Et Diathesis Haemorrhagica”. 13, s. 516–30, June 1965. PMID: 14347873.
Hunt LT, Dayhoff MO. A surprising new protein superfamily containing ovalbumin, antithrombin-III, and alpha 1-proteinase inhibitor. „Biochemical and Biophysical Research Communications”. 95 (2), s. 864–71, July 1980. DOI: 10.1016/0006-291X(80)90867-0. PMID: 6968211.
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”. 177 (3), s. 531–57, August 1984. DOI: 10.1016/0022-2836(84)90298-5. PMID: 6332197.
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”. 347 (6288), s. 99–102, September 1990. DOI: 10.1038/347099a0. PMID: 2395463.
Irving JA, Pike RN, Lesk AM, Whisstock JC. Phylogeny of the serpin superfamily: implications of patterns of amino acid conservation for structure and function. „Genome Research”. 10 (12), s. 1845–64, December 2000. DOI: 10.1101/gr.GR-1478R. PMID: 11116082.
Irving JA, Steenbakkers PJ, Lesk AM, Op den Camp HJ, Pike RN, Whisstock JC. Serpins in prokaryotes. „Molecular Biology and Evolution”. 19 (11), s. 1881–90, 2002. DOI: 10.1093/oxfordjournals.molbev.a004012. PMID: 12411597.
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”. 112 (Pt 8), s. 999–1006, August 2008. DOI: 10.1016/j.mycres.2008.01.021. PMID: 18539447.
Rawlings ND, Tolle DP, Barrett AJ. Evolutionary families of peptidase inhibitors. „The Biochemical Journal”. 378 (Pt 3), s. 705–16, March 2004. DOI: 10.1042/BJ20031825. PMID: 14705960. PMCID: PMC1224039.
Barrett AJ, Rawlings ND. Families and clans of serine peptidases. „Archives of Biochemistry and Biophysics”. 318 (2), s. 247–50, April 1995. DOI: 10.1006/abbi.1995.1227. PMID: 7733651.
Huntington JA, Read RJ, Carrell RW. Structure of a serpin-protease complex shows inhibition by deformation. „Nature”. 407 (6806), s. 923–6, October 2000. DOI: 10.1038/35038119. PMID: 11057674.
Barrett AJ, Rawlings ND. Evolutionary lines of cysteine peptidases. „Biological Chemistry”. 382 (5), s. 727–33, May 2001. DOI: 10.1515/BC.2001.088. PMID: 11517925.
Irving JA, Pike RN, Dai W, Brömme D, Worrall DM, Silverman GA, Coetzer TH, Dennison C, Bottomley SP, Whisstock JC. Evidence that serpin architecture intrinsically supports papain-like cysteine protease inhibition: engineering alpha(1)-antitrypsin to inhibit cathepsin proteases. „Biochemistry”. 41 (15), s. 4998–5004, April 2002. DOI: 10.1021/bi0159985. PMID: 11939796.
Schick C, Brömme D, Bartuski AJ, Uemura Y, Schechter NM, Silverman GA. The reactive site loop of the serpin SCCA1 is essential for cysteine proteinase inhibition. „Proceedings of the National Academy of Sciences of the United States of America”. 95 (23), s. 13465–70, November 1998. DOI: 10.1073/pnas.95.23.13465. PMID: 9811823. PMCID: PMC24842.
McGowan S, Buckle AM, Irving JA, Ong PC, Bashtannyk-Puhalovich TA, Kan WT, Henderson KN, Bulynko YA, Popova EY, Smith AI, Bottomley SP, Rossjohn J, Grigoryev SA, Pike RN, Whisstock JC. X-ray crystal structure of MENT: evidence for functional loop-sheet polymers in chromatin condensation. „The EMBO Journal”. 25 (13), s. 3144–55, July 2006. DOI: 10.1038/sj.emboj.7601201. PMID: 16810322. PMCID: PMC1500978.
Ong PC, McGowan S, Pearce MC, Irving JA, Kan WT, Grigoryev SA, Turk B, Silverman GA, Brix K, Bottomley SP, Whisstock JC, Pike RN. DNA accelerates the inhibition of human cathepsin V by serpins. „The Journal of Biological Chemistry”. 282 (51), s. 36980–6, December 2007. DOI: 10.1074/jbc.M706991200. PMID: 17923478.
Acosta H, Iliev D, Grahn TH, Gouignard N, Maccarana M, Griesbach J, Herzmann S, Sagha M, Climent M, Pera EM. The serpin PN1 is a feedback regulator of FGF signaling in germ layer and primary axis formation. „Development”. 142 (6), s. 1146–58, March 2015. DOI: 10.1242/dev.113886. PMID: 25758225.
Hashimoto C, Kim DR, Weiss LA, Miller JW, Morisato D. Spatial regulation of developmental signaling by a serpin. „Developmental Cell”. 5 (6), s. 945–50, December 2003. DOI: 10.1016/S1534-5807(03)00338-1. PMID: 14667416.
Bird PI. Regulation of pro-apoptotic leucocyte granule serine proteinases by intracellular serpins. „Immunology and Cell Biology”. 77 (1), s. 47–57, February 1999. DOI: 10.1046/j.1440-1711.1999.00787.x. PMID: 10101686.
Bird CH, Sutton VR, Sun J, Hirst CE, Novak A, Kumar S, Trapani JA, Bird PI. Selective regulation of apoptosis: the cytotoxic lymphocyte serpin proteinase inhibitor 9 protects against granzyme B-mediated apoptosis without perturbing the Fas cell death pathway. „Molecular and Cellular Biology”. 18 (11), s. 6387–98, November 1998. DOI: 10.1128/mcb.18.11.6387. PMID: 9774654.
Ray CA, Black RA, Kronheim SR, Greenstreet TA, Sleath PR, Salvesen GS, Pickup DJ. Viral inhibition of inflammation: cowpox virus encodes an inhibitor of the interleukin-1 beta converting enzyme. „Cell”. 69 (4), s. 597–604, May 1992. DOI: 10.1016/0092-8674(92)90223-Y. PMID: 1339309.
Vercammen D, Belenghi B, van de Cotte B, Beunens T, Gavigan JA, De Rycke R, Brackenier A, Inzé D, Harris JL, Van Breusegem F. Serpin1 of Arabidopsis thaliana is a suicide inhibitor for metacaspase 9. „Journal of Molecular Biology”. 364 (4), s. 625–36, December 2006. DOI: 10.1016/j.jmb.2006.09.010. PMID: 17028019.
Lampl N, Budai-Hadrian O, Davydov O, Joss TV, Harrop SJ, Curmi PM, Roberts TH, Fluhr R. Arabidopsis AtSerpin1, crystal structure and in vivo interaction with its target protease responsive to desiccation (RD21). „The Journal of Biological Chemistry”. 285 (18), s. 13550–60, April 2010. DOI: 10.1074/jbc.M109.095075. PMID: 20181955. PMCID: PMC2859516.
Klieber MA, Underhill C, Hammond GL, Muller YA. Corticosteroid-binding globulin, a structural basis for steroid transport and proteinase-triggered release. „The Journal of Biological Chemistry”. 282 (40), s. 29594–603, October 2007. DOI: 10.1074/jbc.M705014200. PMID: 17644521.
Zhou A, Wei Z, Read RJ, Carrell RW. Structural mechanism for the carriage and release of thyroxine in the blood. „Proceedings of the National Academy of Sciences of the United States of America”. 103 (36), s. 13321–6, September 2006. DOI: 10.1073/pnas.0604080103. PMID: 16938877. PMCID: PMC1557382.
Huntington JA, Stein PE. Structure and properties of ovalbumin. „Journal of Chromatography. B, Biomedical Sciences and Applications”. 756 (1-2), s. 189–98, May 2001. DOI: 10.1016/S0378-4347(01)00108-6. PMID: 11419711.
Mala JG, Rose C. Interactions of heat shock protein 47 with collagen and the stress response: an unconventional chaperone model?. „Life Sciences”. 87 (19-22), s. 579–86, November 2010. DOI: 10.1016/j.lfs.2010.09.024. PMID: 20888348.
Grigoryev SA, Bednar J, Woodcock CL. MENT, a heterochromatin protein that mediates higher order chromatin folding, is a new serpin family member. „The Journal of Biological Chemistry”. 274 (9), s. 5626–36, February 1999. DOI: 10.1074/jbc.274.9.5626. PMID: 10026180.
Elliott PR, Lomas DA, Carrell RW, Abrahams JP. Inhibitory conformation of the reactive loop of alpha 1-antitrypsin. „Nature Structural Biology”. 3 (8), s. 676–81, August 1996. DOI: 10.1038/nsb0896-676. PMID: 8756325.
Horvath AJ, Irving JA, Rossjohn J, Law RH, Bottomley SP, Quinsey NS, Pike RN, Coughlin PB, Whisstock JC. The murine orthologue of human antichymotrypsin: a structural paradigm for clade A3 serpins. „The Journal of Biological Chemistry”. 280 (52), s. 43168–78, December 2005. DOI: 10.1074/jbc.M505598200. PMID: 16141197.
Whisstock JC, Skinner R, Carrell RW, Lesk AM. Conformational changes in serpins: I. The native and cleaved conformations of alpha(1)-antitrypsin. „Journal of Molecular Biology”. 296 (2), s. 685–99, February 2000. DOI: 10.1006/jmbi.1999.3520. PMID: 10669617.
Huntington JA. Shape-shifting serpins--advantages of a mobile mechanism. „Trends in Biochemical Sciences”. 31 (8), s. 427–35, August 2006. DOI: 10.1016/j.tibs.2006.06.005. PMID: 16820297.
Jin L, Abrahams JP, Skinner R, Petitou M, Pike RN, Carrell RW. The anticoagulant activation of antithrombin by heparin. „Proceedings of the National Academy of Sciences of the United States of America”. 94 (26), s. 14683–8, December 1997. DOI: 10.1073/pnas.94.26.14683. PMID: 9405673. PMCID: PMC25092.
Whisstock JC, Pike RN, Jin L, Skinner R, Pei XY, Carrell RW, Lesk AM. Conformational changes in serpins: II. The mechanism of activation of antithrombin by heparin. „Journal of Molecular Biology”. 301 (5), s. 1287–305, September 2000. DOI: 10.1006/jmbi.2000.3982. PMID: 10966821.
Li W, Johnson DJ, Esmon CT, Huntington JA. Structure of the antithrombin-thrombin-heparin ternary complex reveals the antithrombotic mechanism of heparin. „Nature Structural & Molecular Biology”. 11 (9), s. 857–62, September 2004. DOI: 10.1038/nsmb811. PMID: 15311269.
Johnson DJ, Li W, Adams TE, Huntington JA. Antithrombin-S195A factor Xa-heparin structure reveals the allosteric mechanism of antithrombin activation. „The EMBO Journal”. 25 (9), s. 2029–37, May 2006. DOI: 10.1038/sj.emboj.7601089. PMID: 16619025. PMCID: PMC1456925.
Walenga JM, Jeske WP, Samama MM, Frapaise FX, Bick RL, Fareed J. Fondaparinux: a synthetic heparin pentasaccharide as a new antithrombotic agent. „Expert Opinion on Investigational Drugs”. 11 (3), s. 397–407, March 2002. DOI: 10.1517/13543784.11.3.397. PMID: 11866668.
Petitou M, van Boeckel CA. A synthetic antithrombin III binding pentasaccharide is now a drug! What comes next?. „Angewandte Chemie”. 43 (24), s. 3118–33, June 2004. DOI: 10.1002/anie.200300640. PMID: 15199558.
Lindahl TL, Sigurdardottir O, Wiman B. Stability of plasminogen activator inhibitor 1 (PAI-1). „Thrombosis and Haemostasis”. 62 (2), s. 748–51, September 1989. PMID: 2479113.
Mushunje A, Evans G, Brennan SO, Carrell RW, Zhou A. Latent antithrombin and its detection, formation and turnover in the circulation. „Journal of Thrombosis and Haemostasis”. 2 (12), s. 2170–7, 2004-23. DOI: 10.1111/j.1538-7836.2004.01047.x. PMID: 15613023.
Zhang Q, Buckle AM, Law RH, Pearce MC, Cabrita LD, Lloyd GJ, Irving JA, Smith AI, Ruzyla K, Rossjohn J, Bottomley SP, Whisstock JC. The N terminus of the serpin, tengpin, functions to trap the metastable native state. „EMBO Reports”. 8 (7), s. 658–63, July 2007. DOI: 10.1038/sj.embor.7400986. PMID: 17557112. PMCID: PMC1905895.
Zhang Q, Law RH, Bottomley SP, Whisstock JC, Buckle AM. A structural basis for loop C-sheet polymerization in serpins. „Journal of Molecular Biology”. 376 (5), s. 1348–59, 2008-03. DOI: 10.1016/j.jmb.2007.12.050. PMID: 18234218.
Pemberton PA, Stein PE, Pepys MB, Potter JM, Carrell RW. Hormone binding globulins undergo serpin conformational change in inflammation. „Nature”. 336 (6196), s. 257–8, 1988-11. DOI: 10.1038/336257a0. PMID: 3143075.
Cao C, Lawrence DA, Li Y, Von Arnim CA, Herz J, Su EJ, Makarova A, Hyman BT, Strickland DK, Zhang L. Endocytic receptor LRP together with tPA and PAI-1 coordinates Mac-1-dependent macrophage migration. „The EMBO Journal”. 25 (9), s. 1860–70, 2006-05. DOI: 10.1038/sj.emboj.7601082. PMID: 16601674. PMCID: PMC1456942.
Jensen JK, Dolmer K, Gettins PG. Specificity of binding of the low density lipoprotein receptor-related protein to different conformational states of the clade E serpins plasminogen activator inhibitor-1 and proteinase nexin-1. „The Journal of Biological Chemistry”. 284 (27), s. 17989–97, 2009-07. DOI: 10.1074/jbc.M109.009530. PMID: 19439404. PMCID: PMC2709341.
Eric Rulifson. Uptake of the necrotic serpin in Drosophila melanogaster via the lipophorin receptor-1. „PLoS Genetics”. 5 (6), s. e1000532, 2009-06. DOI: 10.1371/journal.pgen.1000532. PMID: 19557185. PMCID: PMC2694266.Sprawdź autora:1.
Kaiserman D, Whisstock JC, Bird PI. Mechanisms of serpin dysfunction in disease. „Expert Reviews in Molecular Medicine”. 8 (31), s. 1–19, 2006-01-01. DOI: 10.1017/S1462399406000184. PMID: 17156576.
Hopkins PC, Carrell RW, Stone SR. Effects of mutations in the hinge region of serpins. „Biochemistry”. 32 (30), s. 7650–7, 1993-08. DOI: 10.1021/bi00081a008. PMID: 8347575.
Beauchamp NJ, Pike RN, Daly M, Butler L, Makris M, Dafforn TR, Zhou A, Fitton HL, Preston FE, Peake IR, Carrell RW. Antithrombins Wibble and Wobble (T85M/K): archetypal conformational diseases with in vivo latent-transition, thrombosis, and heparin activation. „Blood”. 92 (8), s. 2696–706, 1998-10. PMID: 9763552.
Gooptu B, Hazes B, Chang WS, Dafforn TR, Carrell RW, Read RJ, Lomas DA. Inactive conformation of the serpin alpha(1)-antichymotrypsin indicates two-stage insertion of the reactive loop: implications for inhibitory function and conformational disease. „Proceedings of the National Academy of Sciences of the United States of America”. 97 (1), s. 67–72, 2000-01. DOI: 10.1073/pnas.97.1.67. PMID: 10618372. PMCID: PMC26617.
Homan EP, Rauch F, Grafe I, Lietman C, Doll JA, Dawson B, Bertin T, Napierala D, Morello R, Gibbs R, White L, Miki R, Cohn DH, Crawford S, Travers R, Glorieux FH, Lee B. Mutations in SERPINF1 cause osteogenesis imperfecta type VI. „Journal of Bone and Mineral Research”. 26 (12), s. 2798–803, December 2011. DOI: 10.1002/jbmr.487. PMID: 21826736. PMCID: PMC3214246.
Fay WP, Parker AC, Condrey LR, Shapiro AD. Human plasminogen activator inhibitor-1 (PAI-1) deficiency: characterization of a large kindred with a null mutation in the PAI-1 gene. „Blood”. 90 (1), s. 204–8, 1997-07. PMID: 9207454.
Heit C, Jackson BC, McAndrews M, Wright MW, Thompson DC, Silverman GA, Nebert DW, Vasiliou V. Update of the human and mouse SERPIN gene superfamily. „Human Genomics”. 7, s. 22, 30 October 2013. DOI: 10.1186/1479-7364-7-22. PMID: 24172014. PMCID: PMC3880077.
Owen MC, Brennan SO, Lewis JH, Carrell RW. Mutation of antitrypsin to antithrombin. alpha 1-antitrypsin Pittsburgh (358 Met leads to Arg), a fatal bleeding disorder. „The New England Journal of Medicine”. 309 (12), s. 694–8, September 1983. DOI: 10.1056/NEJM198309223091203. PMID: 6604220.
Lomas DA, Evans DL, Finch JT, Carrell RW. The mechanism of Z alpha 1-antitrypsin accumulation in the liver. „Nature”. 357 (6379), s. 605–7, 1992. DOI: 10.1038/357605a0. PMID: 1608473.
Kroeger H, Miranda E, MacLeod I, Pérez J, Crowther DC, Marciniak SJ, Lomas DA. Endoplasmic reticulum-associated degradation (ERAD) and autophagy cooperate to degrade polymerogenic mutant serpins. „The Journal of Biological Chemistry”. 284 (34), s. 22793–802, 2009. DOI: 10.1074/jbc.M109.027102. PMID: 19549782. PMCID: PMC2755687.
Yamasaki M, Li W, Johnson DJ, Huntington JA. Crystal structure of a stable dimer reveals the molecular basis of serpin polymerization. „Nature”. 455 (7217), s. 1255–8, 2008. DOI: 10.1038/nature07394. PMID: 18923394.
Yamasaki M, Sendall TJ, Pearce MC, Whisstock JC, Huntington JA. Molecular basis of α1-antitrypsin deficiency revealed by the structure of a domain-swapped trimer. „EMBO Reports”. 12 (10), s. 1011–7, October 2011. DOI: 10.1038/embor.2011.171. PMID: 21909074. PMCID: PMC3185345.
Chang WS, Whisstock J, Hopkins PC, Lesk AM, Carrell RW, Wardell MR. Importance of the release of strand 1C to the polymerization mechanism of inhibitory serpins. „Protein Science”. 6 (1), s. 89–98, January 1997. DOI: 10.1002/pro.5560060110. PMID: 9007980. PMCID: PMC2143506.
Miranda E, Pérez J, Ekeowa UI, Hadzic N, Kalsheker N, Gooptu B, Portmann B, Belorgey D, Hill M, Chambers S, Teckman J, Alexander GJ, Marciniak SJ, Lomas DA. A novel monoclonal antibody to characterize pathogenic polymers in liver disease associated with alpha1-antitrypsin deficiency. „Hepatology”. 52 (3), s. 1078–88, September 2010. DOI: 10.1002/hep.23760. PMID: 20583215.
Sandhaus RA. alpha1-Antitrypsin deficiency . 6: new and emerging treatments for alpha1-antitrypsin deficiency. „Thorax”. 59 (10), s. 904–9, October 2004. DOI: 10.1136/thx.2003.006551. PMID: 15454659. PMCID: PMC1746849.
Fregonese L, Stolk J. Hereditary alpha-1-antitrypsin deficiency and its clinical consequences. „Orphanet Journal of Rare Diseases”. 3, s. 16, 2008. DOI: 10.1186/1750-1172-3-16. PMID: 18565211. PMCID: PMC2441617.
Yusa K, Rashid ST, Strick-Marchand H, Varela I, Liu PQ, Paschon DE, Miranda E, Ordóñez A, Hannan NR, Rouhani FJ, Darche S, Alexander G, Marciniak SJ, Fusaki N, Hasegawa M, Holmes MC, Di Santo JP, Lomas DA, Bradley A, Vallier L. Targeted gene correction of α1-antitrypsin deficiency in induced pluripotent stem cells. „Nature”. 478 (7369), s. 391–4, 2011. DOI: 10.1038/nature10424. PMID: 21993621. PMCID: PMC3198846.
Mallya M, Phillips RL, Saldanha SA, Gooptu B, Brown SC, Termine DJ, Shirvani AM, Wu Y, Sifers RN, Abagyan R, Lomas DA. Small molecules block the polymerization of Z alpha1-antitrypsin and increase the clearance of intracellular aggregates. „Journal of Medicinal Chemistry”. 50 (22), s. 5357–63, 2007. DOI: 10.1021/jm070687z. PMID: 17918823. PMCID: PMC2631427.
Gosai SJ, Kwak JH, Luke CJ, Long OS, King DE, Kovatch KJ, Johnston PA, Shun TY, Lazo JS, Perlmutter DH, Silverman GA, Pak SC. Automated high-content live animal drug screening using C. elegans expressing the aggregation prone serpin α1-antitrypsin Z. „PloS One”. 5 (11), s. e15460, 2010. DOI: 10.1371/journal.pone.0015460. PMID: 21103396. PMCID: PMC2980495.
Cabrita LD, Irving JA, Pearce MC, Whisstock JC, Bottomley SP. Aeropin from the extremophile Pyrobaculum aerophilum bypasses the serpin misfolding trap. „The Journal of Biological Chemistry”. 282 (37), s. 26802–9, 2007. DOI: 10.1074/jbc.M705020200. PMID: 17635906.
Münch J, Ständker L, Adermann K, Schulz A, Schindler M, Chinnadurai R, Pöhlmann S, Chaipan C, Biet T, Peters T, Meyer B, Wilhelm D, Lu H, Jing W, Jiang S, Forssmann WG, Kirchhoff F. Discovery and optimization of a natural HIV-1 entry inhibitor targeting the gp41 fusion peptide. „Cell”. 129 (2), s. 263–75, April 2007. DOI: 10.1016/j.cell.2007.02.042. PMID: 17448989.
Gooptu B, Dickens JA, Lomas DA. The molecular and cellular pathology of α₁-antitrypsin deficiency. „Trends in Molecular Medicine”. 20 (2), s. 116–27, 2014. DOI: 10.1016/j.molmed.2013.10.007. PMID: 24374162.
Seixas S, Suriano G, Carvalho F, Seruca R, Rocha J, Di Rienzo A. Sequence diversity at the proximal 14q32.1 SERPIN subcluster: evidence for natural selection favoring the pseudogenization of SERPINA2. „Molecular Biology and Evolution”. 24 (2), s. 587–98, February 2007. DOI: 10.1093/molbev/msl187. PMID: 17135331.
Kalsheker NA. Alpha 1-antichymotrypsin. „The International Journal of Biochemistry & Cell Biology”. 28 (9), s. 961–4, September 1996. DOI: 10.1016/1357-2725(96)00032-5. PMID: 8930118.
Santamaria M, Pardo-Saganta A, Alvarez-Asiain L, Di Scala M, Qian C, Prieto J, Avila MA. Nuclear α1-antichymotrypsin promotes chromatin condensation and inhibits proliferation of human hepatocellular carcinoma cells. „Gastroenterology”. 144 (4), s. 818–828.e4, April 2013. DOI: 10.1053/j.gastro.2012.12.029. PMID: 23295442.
Zhang S, Janciauskiene S. Multi-functional capability of proteins: alpha1-antichymotrypsin and the correlation with Alzheimer's disease. „Journal of Alzheimer's Disease”. 4 (2), s. 115–22, April 2002. PMID: 12214135.
Chao J, Stallone JN, Liang YM, Chen LM, Wang DZ, Chao L. Kallistatin is a potent new vasodilator. „The Journal of Clinical Investigation”. 100 (1), s. 11–7, July 1997. DOI: 10.1172/JCI119502. PMID: 9202051. PMCID: PMC508159.
Miao RQ, Agata J, Chao L, Chao J. Kallistatin is a new inhibitor of angiogenesis and tumor growth. „Blood”. 100 (9), s. 3245–52, November 2002. DOI: 10.1182/blood-2002-01-0185. PMID: 12384424.
Liu Y, Bledsoe G, Hagiwara M, Shen B, Chao L, Chao J. Depletion of endogenous kallistatin exacerbates renal and cardiovascular oxidative stress, inflammation, and organ remodeling. „American Journal of Physiology. Renal Physiology”. 303 (8), s. F1230-8, October 2012. DOI: 10.1152/ajprenal.00257.2012. PMID: 22811485.
Geiger M. Protein C inhibitor, a serpin with functions in- and outside vascular biology. „Thrombosis and Haemostasis”. 97 (3), s. 343–7, March 2007. DOI: 10.1160/th06-09-0488. PMID: 17334499.
Baumgärtner P, Geiger M, Zieseniss S, Malleier J, Huntington JA, Hochrainer K, Bielek E, Stoeckelhuber M, Lauber K, Scherfeld D, Schwille P, Wäldele K, Beyer K, Engelmann B. Phosphatidylethanolamine critically supports internalization of cell-penetrating protein C inhibitor. „The Journal of Cell Biology”. 179 (4), s. 793–804, November 2007. DOI: 10.1083/jcb.200707165. PMID: 18025309. PMCID: PMC2080921.
Uhrin P, Dewerchin M, Hilpert M, Chrenek P, Schöfer C, Zechmeister-Machhart M, Krönke G, Vales A, Carmeliet P, Binder BR, Geiger M. Disruption of the protein C inhibitor gene results in impaired spermatogenesis and male infertility. „The Journal of Clinical Investigation”. 106 (12), s. 1531–9, December 2000. DOI: 10.1172/JCI10768. PMID: 11120760. PMCID: PMC381472.
Han MH, Hwang SI, Roy DB, Lundgren DH, Price JV, Ousman SS, Fernald GH, Gerlitz B, Robinson WH, Baranzini SE, Grinnell BW, Raine CS, Sobel RA, Han DK, Steinman L. Proteomic analysis of active multiple sclerosis lesions reveals therapeutic targets. „Nature”. 451 (7182), s. 1076–81, 2008. DOI: 10.1038/nature06559. PMID: 18278032.
Torpy DJ, Ho JT. Corticosteroid-binding globulin gene polymorphisms: clinical implications and links to idiopathic chronic fatigue disorders. „Clinical Endocrinology”. 67 (2), s. 161–7, August 2007. DOI: 10.1111/j.1365-2265.2007.02890.x. PMID: 17547679.
Bartalena L, Robbins J. Variations in thyroid hormone transport proteins and their clinical implications. „Thyroid”. 2 (3), s. 237–45, 1992. DOI: 10.1089/thy.1992.2.237. PMID: 1422238.
Persani L. Clinical review: Central hypothyroidism: pathogenic, diagnostic, and therapeutic challenges. „The Journal of Clinical Endocrinology and Metabolism”. 97 (9), s. 3068–78, September 2012. DOI: 10.1210/jc.2012-1616. PMID: 22851492.
Kumar R, Singh VP, Baker KM. The intracellular renin-angiotensin system: a new paradigm. „Trends in Endocrinology and Metabolism”. 18 (5), s. 208–14, 2007. DOI: 10.1016/j.tem.2007.05.001. PMID: 17509892.
Tanimoto K, Sugiyama F, Goto Y, Ishida J, Takimoto E, Yagami K, Fukamizu A, Murakami K. Angiotensinogen-deficient mice with hypotension. „The Journal of Biological Chemistry”. 269 (50), s. 31334–7, December 1994. PMID: 7989296.
Jeunemaitre X, Gimenez-Roqueplo AP, Célérier J, Corvol P. Angiotensinogen variants and human hypertension. „Current Hypertension Reports”. 1 (1), s. 31–41, 1999. DOI: 10.1007/s11906-999-0071-0. PMID: 10981040.
Sethi AA, Nordestgaard BG, Tybjaerg-Hansen A. Angiotensinogen gene polymorphism, plasma angiotensinogen, and risk of hypertension and ischemic heart disease: a meta-analysis. „Arteriosclerosis, Thrombosis, and Vascular Biology”. 23 (7), s. 1269–75, 2003. DOI: 10.1161/01.ATV.0000079007.40884.5C. PMID: 12805070.
Frazer JK, Jackson DG, Gaillard JP, Lutter M, Liu YJ, Banchereau J, Capra JD, Pascual V. Identification of centerin: a novel human germinal center B cell-restricted serpin. „European Journal of Immunology”. 30 (10), s. 3039–48, October 2000. DOI: 10.1002/1521-4141(200010)30:10<3039::AID-IMMU3039>3.0.CO;2-H. PMID: 11069088.
Paterson MA, Horvath AJ, Pike RN, Coughlin PB. Molecular characterization of centerin, a germinal centre cell serpin. „The Biochemical Journal”. 405 (3), s. 489–94, August 2007. DOI: 10.1042/BJ20070174. PMID: 17447896. PMCID: PMC2267310.
Paterson MA, Hosking PS, Coughlin PB. Expression of the serpin centerin defines a germinal center phenotype in B-cell lymphomas. „American Journal of Clinical Pathology”. 130 (1), s. 117–26, July 2008. DOI: 10.1309/9QKE68QU7B825A3U. PMID: 18550480.
Ashton-Rickardt PG. An emerging role for Serine Protease Inhibitors in T lymphocyte immunity and beyond. „Immunology Letters”. 152 (1), s. 65–76, April 2013. DOI: 10.1016/j.imlet.2013.04.004. PMID: 23624075.
Han X, Fiehler R, Broze GJ. Characterization of the protein Z-dependent protease inhibitor. „Blood”. 96 (9), s. 3049–55, November 2000. PMID: 11049983.
Hida K, Wada J, Eguchi J, Zhang H, Baba M, Seida A, Hashimoto I, Okada T, Yasuhara A, Nakatsuka A, Shikata K, Hourai S, Futami J, Watanabe E, Matsuki Y, Hiramatsu R, Akagi S, Makino H, Kanwar YS. Visceral adipose tissue-derived serine protease inhibitor: a unique insulin-sensitizing adipocytokine in obesity. „Proceedings of the National Academy of Sciences of the United States of America”. 102 (30), s. 10610–5, July 2005. DOI: 10.1073/pnas.0504703102. PMID: 16030142. PMCID: PMC1180799.
Feng R, Li Y, Wang C, Luo C, Liu L, Chuo F, Li Q, Sun C. Higher vaspin levels in subjects with obesity and type 2 diabetes mellitus: a meta-analysis. „Diabetes Research and Clinical Practice”. 106 (1), s. 88–94, October 2014. DOI: 10.1016/j.diabres.2014.07.026. PMID: 25151227.
Remold-O'Donnell E, Chin J, Alberts M. Sequence and molecular characterization of human monocyte/neutrophil elastase inhibitor. „Proceedings of the National Academy of Sciences of the United States of America”. 89 (12), s. 5635–9, June 1992. DOI: 10.1073/pnas.89.12.5635. PMID: 1376927. PMCID: PMC49347.
Benarafa C, Priebe GP, Remold-O'Donnell E. The neutrophil serine protease inhibitor serpinb1 preserves lung defense functions in Pseudomonas aeruginosa infection. „The Journal of Experimental Medicine”. 204 (8), s. 1901–9, August 2007. DOI: 10.1084/jem.20070494. PMID: 17664292. PMCID: PMC2118684.
Antalis TM, La Linn M, Donnan K, Mateo L, Gardner J, Dickinson JL, Buttigieg K, Suhrbier A. The serine proteinase inhibitor (serpin) plasminogen activation inhibitor type 2 protects against viral cytopathic effects by constitutive interferon alpha/beta priming. „The Journal of Experimental Medicine”. 187 (11), s. 1799–811, June 1998. DOI: 10.1084/jem.187.11.1799. PMID: 9607921. PMCID: PMC2212304.
Zhao A, Yang Z, Sun R, Grinchuk V, Netzel-Arnett S, Anglin IE, Driesbaugh KH, Notari L, Bohl JA, Madden KB, Urban JF, Antalis TM, Shea-Donohue T. SerpinB2 is critical to Th2 immunity against enteric nematode infection. „Journal of Immunology”. 190 (11), s. 5779–87, June 2013. DOI: 10.4049/jimmunol.1200293. PMID: 23630350.
Dougherty KM, Pearson JM, Yang AY, Westrick RJ, Baker MS, Ginsburg D. The plasminogen activator inhibitor-2 gene is not required for normal murine development or survival. „Proceedings of the National Academy of Sciences of the United States of America”. 96 (2), s. 686–91, 1999. DOI: 10.1073/pnas.96.2.686. PMID: 9892694. PMCID: PMC15197.
Takeda A, Yamamoto T, Nakamura Y, Takahashi T, Hibino T. Squamous cell carcinoma antigen is a potent inhibitor of cysteine proteinase cathepsin L. „FEBS Letters”. 359 (1), s. 78–80, February 1995. PMID: 7851535.
Turato C, Pontisso P. SERPINB3 (serpin peptidase inhibitor, clade B (ovalbumin), member 3). „Atlas of Genetics and Cytogenetics in Oncology and Haematology”. 19 (3), s. 202–209, March 2015. DOI: 10.4267/2042/56413. PMID: 25984243.
Sivaprasad U, Askew DJ, Ericksen MB, Gibson AM, Stier MT, Brandt EB, Bass SA, Daines MO, Chakir J, Stringer KF, Wert SE, Whitsett JA, Le Cras TD, Wills-Karp M, Silverman GA, Khurana Hershey GK. A nonredundant role for mouse Serpinb3a in the induction of mucus production in asthma. „The Journal of Allergy and Clinical Immunology”. 127 (1), s. 254–61, 261.e1-6, 2011. DOI: 10.1016/j.jaci.2010.10.009. PMID: 21126757. PMCID: PMC3058372.
Schick C, Kamachi Y, Bartuski AJ, Cataltepe S, Schechter NM, Pemberton PA, Silverman GA. Squamous cell carcinoma antigen 2 is a novel serpin that inhibits the chymotrypsin-like proteinases cathepsin G and mast cell chymase. „The Journal of Biological Chemistry”. 272 (3), s. 1849–55, January 1997. DOI: 10.1074/jbc.272.3.1849. PMID: 8999871.
Teoh SS, Whisstock JC, Bird PI. Maspin (SERPINB5) is an obligate intracellular serpin. „The Journal of Biological Chemistry”. 285 (14), s. 10862–9, April 2010. DOI: 10.1074/jbc.M109.073171. PMID: 20123984. PMCID: PMC2856292.
Zou Z, Anisowicz A, Hendrix MJ, Thor A, Neveu M, Sheng S, Rafidi K, Seftor E, Sager R. Maspin, a serpin with tumor-suppressing activity in human mammary epithelial cells. „Science”. 263 (5146), s. 526–9, 1994. DOI: 10.1126/science.8290962. PMID: 8290962.
Teoh SS, Vieusseux J, Prakash M, Berkowicz S, Luu J, Bird CH, Law RH, Rosado C, Price JT, Whisstock JC, Bird PI. Maspin is not required for embryonic development or tumour suppression. „Nature Communications”. 5, s. 3164, 2014. DOI: 10.1038/ncomms4164. PMID: 24445777. PMCID: PMC3905777.
Gao F, Shi HY, Daughty C, Cella N, Zhang M. Maspin plays an essential role in early embryonic development. „Development”. 131 (7), s. 1479–89, 2004. DOI: 10.1242/dev.01048. PMID: 14985257.
Scott FL, Hirst CE, Sun J, Bird CH, Bottomley SP, Bird PI. The intracellular serpin proteinase inhibitor 6 is expressed in monocytes and granulocytes and is a potent inhibitor of the azurophilic granule protease, cathepsin G. „Blood”. 93 (6), s. 2089–97, 1999. PMID: 10068683.
Tan J, Prakash MD, Kaiserman D, Bird PI. Absence of SERPINB6A causes sensorineural hearing loss with multiple histopathologies in the mouse inner ear. „The American Journal of Pathology”. 183 (1), s. 49–59, July 2013. DOI: 10.1016/j.ajpath.2013.03.009. PMID: 23669344.
Scarff KL, Ung KS, Nandurkar H, Crack PJ, Bird CH, Bird PI. Targeted disruption of SPI3/Serpinb6 does not result in developmental or growth defects, leukocyte dysfunction, or susceptibility to stroke. „Molecular and Cellular Biology”. 24 (9), s. 4075–82, May 2004. DOI: 10.1128/MCB.24.9.4075-4082.2004. PMID: 15082799. PMCID: PMC387772.
Miyata T, Inagi R, Nangaku M, Imasawa T, Sato M, Izuhara Y, Suzuki D, Yoshino A, Onogi H, Kimura M, Sugiyama S, Kurokawa K. Overexpression of the serpin megsin induces progressive mesangial cell proliferation and expansion. „The Journal of Clinical Investigation”. 109 (5), s. 585–93, March 2002. DOI: 10.1172/JCI14336. PMID: 11877466. PMCID: PMC150894.
Miyata T, Li M, Yu X, Hirayama N. Megsin gene: its genomic analysis, pathobiological functions, and therapeutic perspectives. „Current Genomics”. 8 (3), s. 203–8, 2007. DOI: 10.2174/138920207780833856. PMID: 18645605. PMCID: PMC2435355.
Kubo A. Nagashima-type palmoplantar keratosis: a common Asian type caused by SERPINB7 protease inhibitor deficiency. „The Journal of Investigative Dermatology”. 134 (8), s. 2076–9, 2014. DOI: 10.1038/jid.2014.156. PMID: 25029323.
Dahlen JR, Jean F, Thomas G, Foster DC, Kisiel W. Inhibition of soluble recombinant furin by human proteinase inhibitor 8. „The Journal of Biological Chemistry”. 273 (4), s. 1851–4, 1998. DOI: 10.1074/jbc.273.4.1851. PMID: 9442015.
Sun J, Bird CH, Sutton V, McDonald L, Coughlin PB, De Jong TA, Trapani JA, Bird PI. A cytosolic granzyme B inhibitor related to the viral apoptotic regulator cytokine response modifier A is present in cytotoxic lymphocytes. „The Journal of Biological Chemistry”. 271 (44), s. 27802–9, 1996. DOI: 10.1074/jbc.271.44.27802. PMID: 8910377.
Zhang M, Park SM, Wang Y, Shah R, Liu N, Murmann AE, Wang CR, Peter ME, Ashton-Rickardt PG. Serine protease inhibitor 6 protects cytotoxic T cells from self-inflicted injury by ensuring the integrity of cytotoxic granules. „Immunity”. 24 (4), s. 451–61, April 2006. DOI: 10.1016/j.immuni.2006.02.002. PMID: 16618603.
Rizzitelli A, Meuter S, Vega Ramos J, Bird CH, Mintern JD, Mangan MS, Villadangos J, Bird PI. Serpinb9 (Spi6)-deficient mice are impaired in dendritic cell-mediated antigen cross-presentation. „Immunology and Cell Biology”. 90 (9), s. 841–51, 2012. DOI: 10.1038/icb.2012.29. PMID: 22801574.
Askew DJ, Cataltepe S, Kumar V, Edwards C, Pace SM, Howarth RN, Pak SC, Askew YS, Brömme D, Luke CJ, Whisstock JC, Silverman GA. SERPINB11 is a new noninhibitory intracellular serpin. Common single nucleotide polymorphisms in the scaffold impair conformational change. „The Journal of Biological Chemistry”. 282 (34), s. 24948–60, August 2007. DOI: 10.1074/jbc.M703182200. PMID: 17562709.
Finno CJ, Stevens C, Young A, Affolter V, Joshi NA, Ramsay S, Bannasch DL. SERPINB11 frameshift variant associated with novel hoof specific phenotype in Connemara ponies. „PLoS Genetics”. 11 (4), s. e1005122, 2015. DOI: 10.1371/journal.pgen.1005122. PMID: 25875171.
Askew YS, Pak SC, Luke CJ, Askew DJ, Cataltepe S, Mills DR, Kato H, Lehoczky J, Dewar K, Birren B, Silverman GA. SERPINB12 is a novel member of the human ov-serpin family that is widely expressed and inhibits trypsin-like serine proteinases. „The Journal of Biological Chemistry”. 276 (52), s. 49320–30, December 2001. DOI: 10.1074/jbc.M108879200. PMID: 11604408.
Welss T, Sun J, Irving JA, Blum R, Smith AI, Whisstock JC, Pike RN, von Mikecz A, Ruzicka T, Bird PI, Abts HF. Hurpin is a selective inhibitor of lysosomal cathepsin L and protects keratinocytes from ultraviolet-induced apoptosis. „Biochemistry”. 42 (24), s. 7381–9, 2003. DOI: 10.1021/bi027307q. PMID: 12809493.
Ishiguro K, Kojima T, Kadomatsu K, Nakayama Y, Takagi A, Suzuki M, Takeda N, Ito M, Yamamoto K, Matsushita T, Kusugami K, Muramatsu T, Saito H. Complete antithrombin deficiency in mice results in embryonic lethality. „The Journal of Clinical Investigation”. 106 (7), s. 873–8, October 2000. DOI: 10.1172/JCI10489. PMID: 11018075. PMCID: PMC517819.
Vicente CP, He L, Pavão MS, Tollefsen DM. Antithrombotic activity of dermatan sulfate in heparin cofactor II-deficient mice. „Blood”. 104 (13), s. 3965–70, December 2004. DOI: 10.1182/blood-2004-02-0598. PMID: 15315969.
Aihara K, Azuma H, Akaike M, Ikeda Y, Sata M, Takamori N, Yagi S, Iwase T, Sumitomo Y, Kawano H, Yamada T, Fukuda T, Matsumoto T, Sekine K, Sato T, Nakamichi Y, Yamamoto Y, Yoshimura K, Watanabe T, Nakamura T, Oomizu A, Tsukada M, Hayashi H, Sudo T, Kato S, Matsumoto T. Strain-dependent embryonic lethality and exaggerated vascular remodeling in heparin cofactor II-deficient mice. „The Journal of Clinical Investigation”. 117 (6), s. 1514–26, June 2007. DOI: 10.1172/JCI27095. PMID: 17549254. PMCID: PMC1878511.
Cale JM, Lawrence DA. Structure-function relationships of plasminogen activator inhibitor-1 and its potential as a therapeutic agent. „Current Drug Targets”. 8 (9), s. 971–81, September 2007. DOI: 10.2174/138945007781662337. PMID: 17896949.
Lino MM, Atanasoski S, Kvajo M, Fayard B, Moreno E, Brenner HR, Suter U, Monard D. Mice lacking protease nexin-1 show delayed structural and functional recovery after sciatic nerve crush. „The Journal of Neuroscience”. 27 (14), s. 3677–85, April 2007. DOI: 10.1523/JNEUROSCI.0277-07.2007. PMID: 17409231.
Murer V, Spetz JF, Hengst U, Altrogge LM, de Agostini A, Monard D. Male fertility defects in mice lacking the serine protease inhibitor protease nexin-1. „Proceedings of the National Academy of Sciences of the United States of America”. 98 (6), s. 3029–33, March 2001. DOI: 10.1073/pnas.051630698. PMID: 11248026. PMCID: PMC30601.
Lüthi A, Van der Putten H, Botteri FM, Mansuy IM, Meins M, Frey U, Sansig G, Portet C, Schmutz M, Schröder M, Nitsch C, Laurent JP, Monard D. Endogenous serine protease inhibitor modulates epileptic activity and hippocampal long-term potentiation. „The Journal of Neuroscience”. 17 (12), s. 4688–99, June 1997. PMID: 9169529.
Doll JA, Stellmach VM, Bouck NP, Bergh AR, Lee C, Abramson LP, Cornwell ML, Pins MR, Borensztajn J, Crawford SE. Pigment epithelium-derived factor regulates the vasculature and mass of the prostate and pancreas. „Nature Medicine”. 9 (6), s. 774–80, June 2003. DOI: 10.1038/nm870. PMID: 12740569.
Becerra SP, Perez-Mediavilla LA, Weldon JE, Locatelli-Hoops S, Senanayake P, Notari L, Notario V, Hollyfield JG. Pigment epithelium-derived factor binds to hyaluronan. Mapping of a hyaluronan binding site. „The Journal of Biological Chemistry”. 283 (48), s. 33310–20, November 2008. DOI: 10.1074/jbc.M801287200. PMID: 18805795. PMCID: PMC2586245.
Andreu-Agulló C, Morante-Redolat JM, Delgado AC, Fariñas I. Vascular niche factor PEDF modulates Notch-dependent stemness in the adult subependymal zone. „Nature Neuroscience”. 12 (12), s. 1514–23, December 2009. DOI: 10.1038/nn.2437. PMID: 19898467.
Wiman B, Collen D. On the mechanism of the reaction between human alpha 2-antiplasmin and plasmin. „The Journal of Biological Chemistry”. 254 (18), s. 9291–7, September 1979. PMID: 158022.
Lijnen HR, Okada K, Matsuo O, Collen D, Dewerchin M. Alpha2-antiplasmin gene deficiency in mice is associated with enhanced fibrinolytic potential without overt bleeding. „Blood”. 93 (7), s. 2274–81, April 1999. PMID: 10090937.
Carpenter SL, Mathew P. Alpha2-antiplasmin and its deficiency: fibrinolysis out of balance. „Haemophilia”. 14 (6), s. 1250–4, November 2008. DOI: 10.1111/j.1365-2516.2008.01766.x. PMID: 19141165.
Beinrohr L, Harmat V, Dobó J, Lörincz Z, Gál P, Závodszky P. C1 inhibitor serpin domain structure reveals the likely mechanism of heparin potentiation and conformational disease. „The Journal of Biological Chemistry”. 282 (29), s. 21100–9, July 2007. DOI: 10.1074/jbc.M700841200. PMID: 17488724.
Mollnes TE, Jokiranta TS, Truedsson L, Nilsson B, Rodriguez de Cordoba S, Kirschfink M. Complement analysis in the 21st century. „Molecular Immunology”. 44 (16), s. 3838–49, September 2007. DOI: 10.1016/j.molimm.2007.06.150. PMID: 17768101.
Triggianese P, Chimenti MS, Toubi E, Ballanti E, Guarino MD, Perricone C, Perricone R. The autoimmune side of hereditary angioedema: insights on the pathogenesis. „Autoimmunity Reviews”. 14 (8), s. 665–9, August 2015. DOI: 10.1016/j.autrev.2015.03.006. PMID: 25827463.
Nagai N, Hosokawa M, Itohara S, Adachi E, Matsushita T, Hosokawa N, Nagata K. Embryonic lethality of molecular chaperone hsp47 knockout mice is associated with defects in collagen biosynthesis. „The Journal of Cell Biology”. 150 (6), s. 1499–506, September 2000. DOI: 10.1083/jcb.150.6.1499. PMID: 10995453. PMCID: PMC2150697.
Marini JC, Reich A, Smith SM. Osteogenesis imperfecta due to mutations in non-collagenous genes: lessons in the biology of bone formation. „Current Opinion in Pediatrics”. 26 (4), s. 500–7, August 2014. DOI: 10.1097/MOP.0000000000000117. PMID: 25007323. PMCID: PMC4183132.
Osterwalder T, Cinelli P, Baici A, Pennella A, Krueger SR, Schrimpf SP, Meins M, Sonderegger P. The axonally secreted serine proteinase inhibitor, neuroserpin, inhibits plasminogen activators and plasmin but not thrombin. „The Journal of Biological Chemistry”. 273 (4), s. 2312–21, January 1998. DOI: 10.1074/jbc.273.4.2312. PMID: 9442076.
Crowther DC. Familial conformational diseases and dementias. „Human Mutation”. 20 (1), s. 1–14, July 2002. DOI: 10.1002/humu.10100. PMID: 12112652.
Belorgey D, Hägglöf P, Karlsson-Li S, Lomas DA. Protein misfolding and the serpinopathies. „Prion”. 1 (1), s. 15–20, 1 March 2007. PMID: 19164889. PMCID: PMC2633702.
Ozaki K, Nagata M, Suzuki M, Fujiwara T, Miyoshi Y, Ishikawa O, Ohigashi H, Imaoka S, Takahashi E, Nakamura Y. Isolation and characterization of a novel human pancreas-specific gene, pancpin, that is down-regulated in pancreatic cancer cells. „Genes, Chromosomes & Cancer”. 22 (3), s. 179–85, July 1998. DOI: 10.1002/(SICI)1098-2264(199807)22:3<179::AID-GCC3>3.0.CO;2-T. PMID: 9624529.
Loftus SK, Cannons JL, Incao A, Pak E, Chen A, Zerfas PM, Bryant MA, Biesecker LG, Schwartzberg PL, Pavan WJ. Acinar cell apoptosis in Serpini2-deficient mice models pancreatic insufficiency. „PLoS Genetics”. 1 (3), s. e38, September 2005. DOI: 10.1371/journal.pgen.0010038. PMID: 16184191. PMCID: PMC1231717.
Padua MB, Kowalski AA, Cañas MY, Hansen PJ. The molecular phylogeny of uterine serpins and its relationship to evolution of placentation. „FASEB Journal”. 24 (2), s. 526–37, February 2010. DOI: 10.1096/fj.09-138453. PMID: 19825977.
Padua MB, Hansen PJ. Evolution and function of the uterine serpins (SERPINA14). „American Journal of Reproductive Immunology”. 64 (4), s. 265–74, October 2010. DOI: 10.1111/j.1600-0897.2010.00901.x. PMID: 20678169.
Reichhart JM. Tip of another iceberg: Drosophila serpins. „Trends in Cell Biology”. 15 (12), s. 659–65, December 2005. DOI: 10.1016/j.tcb.2005.10.001. PMID: 16260136.
Tang H, Kambris Z, Lemaitre B, Hashimoto C. A serpin that regulates immune melanization in the respiratory system of Drosophila. „Developmental Cell”. 15 (4), s. 617–26, October 2008. DOI: 10.1016/j.devcel.2008.08.017. PMID: 18854145. PMCID: PMC2671232.
Scherfer C, Tang H, Kambris Z, Lhocine N, Hashimoto C, Lemaitre B. Drosophila Serpin-28D regulates hemolymph phenoloxidase activity and adult pigmentation. „Developmental Biology”. 323 (2), s. 189–96, November 2008. DOI: 10.1016/j.ydbio.2008.08.030. PMID: 18801354.
Rushlow C. Dorsoventral patterning: a serpin pinned down at last. „Current Biology”. 14 (1), s. R16-8, January 2004. DOI: 10.1016/j.cub.2003.12.015. PMID: 14711428.
Ligoxygakis P, Roth S, Reichhart JM. A serpin regulates dorsal-ventral axis formation in the Drosophila embryo. „Current Biology”. 13 (23), s. 2097–102, December 2003. DOI: 10.1016/j.cub.2003.10.062. PMID: 14654000.
Jiang R, Zhang B, Kurokawa K, So YI, Kim EH, Hwang HO, Lee JH, Shiratsuchi A, Zhang J, Nakanishi Y, Lee HS, Lee BL. 93-kDa twin-domain serine protease inhibitor (Serpin) has a regulatory function on the beetle Toll proteolytic signaling cascade. „The Journal of Biological Chemistry”. 286 (40), s. 35087–95, October 2011. DOI: 10.1074/jbc.M111.277343. PMID: 21862574. PMCID: PMC3186399.
Pak SC, Kumar V, Tsu C, Luke CJ, Askew YS, Askew DJ, Mills DR, Brömme D, Silverman GA. SRP-2 is a cross-class inhibitor that participates in postembryonic development of the nematode Caenorhabditis elegans: initial characterization of the clade L serpins. „The Journal of Biological Chemistry”. 279 (15), s. 15448–59, April 2004. DOI: 10.1074/jbc.M400261200. PMID: 14739286.
Luke CJ, Pak SC, Askew YS, Naviglia TL, Askew DJ, Nobar SM, Vetica AC, Long OS, Watkins SC, Stolz DB, Barstead RJ, Moulder GL, Brömme D, Silverman GA. An intracellular serpin regulates necrosis by inhibiting the induction and sequelae of lysosomal injury. „Cell”. 130 (6), s. 1108–19, September 2007. DOI: 10.1016/j.cell.2007.07.013. PMID: 17889653. PMCID: PMC2128786.
Dahl SW, Rasmussen SK, Petersen LC, Hejgaard J. Inhibition of coagulation factors by recombinant barley serpin BSZx. „FEBS Letters”. 394 (2), s. 165–8, September 1996. DOI: 10.1016/0014-5793(96)00940-4. PMID: 8843156.
Hejgaard J. Inhibitory serpins from rye grain with glutamine as P1 and P2 residues in the reactive center. „FEBS Letters”. 488 (3), s. 149–53, January 2001. DOI: 10.1016/S0014-5793(00)02425-X. PMID: 11163762.
Ostergaard H, Rasmussen SK, Roberts TH, Hejgaard J. Inhibitory serpins from wheat grain with reactive centers resembling glutamine-rich repeats of prolamin storage proteins. Cloning and characterization of five major molecular forms. „The Journal of Biological Chemistry”. 275 (43), s. 33272–9, October 2000. DOI: 10.1074/jbc.M004633200. PMID: 10874043.
Yoo BC, Aoki K, Xiang Y, Campbell LR, Hull RJ, Xoconostle-Cázares B, Monzer J, Lee JY, Ullman DE, Lucas WJ. Characterization of cucurbita maxima phloem serpin-1 (CmPS-1). A developmentally regulated elastase inhibitor. „The Journal of Biological Chemistry”. 275 (45), s. 35122–8, November 2000. DOI: 10.1074/jbc.M006060200. PMID: 10960478.
la Cour Petersen M, Hejgaard J, Thompson GA, Schulz A. Cucurbit phloem serpins are graft-transmissible and appear to be resistant to turnover in the sieve element-companion cell complex. „Journal of Experimental Botany”. 56 (422), s. 3111–20, December 2005. DOI: 10.1093/jxb/eri308. PMID: 16246856.
Roberts TH, Hejgaard J. Serpins in plants and green algae. „Functional & Integrative Genomics”. 8 (1), s. 1–27, February 2008. DOI: 10.1007/s10142-007-0059-2. PMID: 18060440.
Lampl N, Alkan N, Davydov O, Fluhr R. Set-point control of RD21 protease activity by AtSerpin1 controls cell death in Arabidopsis. „The Plant Journal”. 74 (3), s. 498–510, May 2013. DOI: 10.1111/tpj.12141. PMID: 23398119.
Ahn JW, Atwell BJ, Roberts TH. Serpin genes AtSRP2 and AtSRP3 are required for normal growth sensitivity to a DNA alkylating agent in Arabidopsis. „BMC Plant Biology”. 9, s. 52, 2009. DOI: 10.1186/1471-2229-9-52. PMID: 19426562. PMCID: PMC2689219.
Kang S, Barak Y, Lamed R, Bayer EA, Morrison M. The functional repertoire of prokaryote cellulosomes includes the serpin superfamily of serine proteinase inhibitors. „Molecular Microbiology”. 60 (6), s. 1344–54, June 2006. DOI: 10.1111/j.1365-2958.2006.05182.x. PMID: 16796673.
Irving JA, Cabrita LD, Rossjohn J, Pike RN, Bottomley SP, Whisstock JC. The 1.5 A crystal structure of a prokaryote serpin: controlling conformational change in a heated environment. „Structure”. 11 (4), s. 387–97, April 2003. DOI: 10.1016/S0969-2126(03)00057-1. PMID: 12679017.
Fulton KF, Buckle AM, Cabrita LD, Irving JA, Butcher RE, Smith I, Reeve S, Lesk AM, Bottomley SP, Rossjohn J, Whisstock JC. The high resolution crystal structure of a native thermostable serpin reveals the complex mechanism underpinning the stressed to relaxed transition. „The Journal of Biological Chemistry”. 280 (9), s. 8435–42, March 2005. DOI: 10.1074/jbc.M410206200. PMID: 15590653.
Turner PC, Moyer RW. Poxvirus immune modulators: functional insights from animal models. „Virus Research”. 88 (1-2), s. 35–53, September 2002. DOI: 10.1016/S0168-1702(02)00119-3. PMID: 12297326.
Richardson J, Viswanathan K, Lucas A. Serpins, the vasculature, and viral therapeutics. „Frontiers in Bioscience”. 11, s. 1042–56, 2006. DOI: 10.2741/1862. PMID: 16146796.
Jiang J, Arp J, Kubelik D, Zassoko R, Liu W, Wise Y, Macaulay C, Garcia B, McFadden G, Lucas AR, Wang H. Induction of indefinite cardiac allograft survival correlates with toll-like receptor 2 and 4 downregulation after serine protease inhibitor-1 (Serp-1) treatment. „Transplantation”. 84 (9), s. 1158–67, November 2007. DOI: 10.1097/01.tp.0000286099.50532.b0. PMID: 17998872.
Dai E, Guan H, Liu L, Little S, McFadden G, Vaziri S, Cao H, Ivanova IA, Bocksch L, Lucas A. Serp-1, a viral anti-inflammatory serpin, regulates cellular serine proteinase and serpin responses to vascular injury. „The Journal of Biological Chemistry”. 278 (20), s. 18563–72, May 2003. DOI: 10.1074/jbc.M209683200. PMID: 12637546.
Turner PC, Sancho MC, Thoennes SR, Caputo A, Bleackley RC, Moyer RW. Myxoma virus Serp2 is a weak inhibitor of granzyme B and interleukin-1beta-converting enzyme in vitro and unlike CrmA cannot block apoptosis in cowpox virus-infected cells. „Journal of Virology”. 73 (8), s. 6394–404, August 1999. PMID: 10400732. PMCID: PMC112719.
Munuswamy-Ramanujam G, Khan KA, Lucas AR. Viral anti-inflammatory reagents: the potential for treatment of arthritic and vasculitic disorders. „Endocrine, Metabolic & Immune Disorders Drug Targets”. 6 (4), s. 331–43, December 2006. DOI: 10.2174/187153006779025720. PMID: 17214579.
Renatus M, Zhou Q, Stennicke HR, Snipas SJ, Turk D, Bankston LA, Liddington RC, Salvesen GS. Crystal structure of the apoptotic suppressor CrmA in its cleaved form. „Structure”. 8 (7), s. 789–97, 2000. DOI: 10.1016/S0969-2126(00)00165-9. PMID: 10903953.
worldcat.org
R. Favier, N. Aoki, P. De Moerloose. Congenital α2-plasmin inhibitor deficiencies: a review. „British Journal of Haematology”. 114 (1), s. 4–10, 1 July 2001. DOI: 10.1046/j.1365-2141.2001.02845.x. ISSN1365-2141.
