• 1
    Spronk HM, Govers-Riemslag JW, ten Cate H. The blood coagulation system as a molecular machine. BioEssays 2003; 25: 12208.
  • 2
    Rau JC, Beaulieu LM, Huntington JA, Church FC. Serpins in thrombosis, hemostasis and fibrinolysis. J Thromb Haemost 2007; 5(Suppl. 1): 10215.
  • 3
    Bayston TA, Lane DA. Antithrombin: molecular basis of deficiency. Thromb Haemost 1997; 78: 33943.
  • 4
    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. J Clin Invest 2000; 106: 8738.
  • 5
    Gettins PG. Serpin structure, mechanism, and function. Chem Rev 2002; 102: 4751804.
  • 6
    Carrell RW, Huntington JA. How serpins change their fold for better and for worse. Biochem Soc Symp 2003; 70: 16378.
  • 7
    Hernandez-Espinosa D, Ordonez A, Vicente V, Corral J. Factors with conformational effects on haemostatic serpins: implications in thrombosis. Thromb Haemost 2007; 98: 55763.
  • 8
    Stein PE, Carrell RW. What do dysfunctional serpins tell us about molecular mobility and disease? Nat Struct Biol 1995; 2: 96113.
  • 9
    Lane DA, Bayston T, Olds RJ, Fitches AC, Cooper DN, Millar DS, Jochmans K, Perry DJ, Okajima K, Thein SL, Emmerich J. Antithrombin mutation database: 2nd (1997) update. For the Plasma Coagulation Inhibitors Subcommittee of the Scientific and Standardization Committee of the International Society on Thrombosis and Haemostasis. Thromb Haemost 1997; 77: 197211.
  • 10
    Raja SM, Chhablani N, Swanson R, Thompson E, Laffan M, Lane DA, Olson ST. Deletion of P1 arginine in a novel antithrombin variant (antithrombin London) abolishes inhibitory activity but enhances heparin affinity and is associated with early onset thrombosis. J Biol Chem 2003; 278: 1368895.
  • 11
    Corral J, Huntington JA, Gonzalez-Conejero R, Mushunje A, Navarro M, Marco P, Vicente V, Carrell RW. Mutations in the shutter region of antithrombin result in formation of disulfide-linked dimers and severe venous thrombosis. J Thromb Haemost 2004; 2: 9319.
  • 12
    Mushunje A, Evans G, Brennan SO, Carrell RW, Zhou A. Latent antithrombin and its detection, formation and turnover in the circulation. J Thromb Haemost 2004; 2: 21707.
  • 13
    Martinez-Martinez I, Ordonez A, Navarro-Fernandez J, Perez-Lara A, Gutierrez-Gallego R, Giraldo R, Martinez C, Llop E, Vicente V, Corral J. Antithrombin Murcia (K241E) causing antithrombin deficiency: a possible role for altered glycosylation. Haematologica 2010; 95: 135865.
  • 14
    McCoy AJ, Grosse-Kunstleve RW, Storoni LC, Read RJ. Likelihood-enhanced fast translation functions. Acta Crystallogr D Biol Crystallogr 2005; 61: 45864.
  • 15
    Murshudov GN, Vagin AA, Dodson EJ. Refinement of macromolecular structures by the maximum-likelihood method. Acta Crystallogr D Biol Crystallogr 1997; 53: 24055.
  • 16
    Emsley P, Cowtan K. Coot: model-building tools for molecular graphics. Acta Crystallogr D Biol Crystallogr 2004; 60: 212632.
  • 17
    McCoy AJ, Pei XY, Skinner R, Abrahams JP, Carrell RW. Structure of beta-antithrombin and the effect of glycosylation on antithrombin’s heparin affinity and activity. J Mol Biol 2003; 326: 82333.
  • 18
    Luxembourg B, Delev D, Geisen C, Spannagl M, Krause M, Miesbach W, Heller C, Bergmann F, Schmeink U, Grossmann R, Lindhoff-Last E, Seifried E, Oldenburg J, Pavlova A. Molecular basis of antithrombin deficiency. Thromb Haemost 2011; 105: 63546.
  • 19
    Picard V, Nowak-Göttl U, Biron-Andreani C, Fouassier M, Frere C, Goualt-Heilman M, de Maistre E, Regina S, Rugeri L, Ternisien C, Trichet C, Vergnes C, Aiach M, Alhenc-Gelas M. Molecular bases of antithrombin deficiency: twenty-two novel mutations in the antithrombin gene. Hum Mutat 2006; 27: 600.
  • 20
    Corral J, Vicente V, Carrell RW. Thrombosis as a conformational disease. Haematologica 2005; 90: 23846.
  • 21
    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 1998; 92: 2696706.
  • 22
    Lomas DA, Belorgey D, Mallya M, Onda M, Kinghorn KJ, Sharp LK, Phillips RL, Page R, Crowther DC, Miranda E. Polymerisation underlies alpha1-antitrypsin deficiency, dementia and other serpinopathies. Front Biosci 2004; 9: 287391.
  • 23
    Corral J, Aznar J, Gonzalez-Conejero R, Villa P, Miñano A, Vayá A, Carrell RW, Huntington JA, Vicente V. Homozygous deficiency of heparin cofactor II: relevance of P17 glutamate residue in serpins, relationship with conformational diseases, and role in thrombosis. Circulation 2004; 110: 13037.
  • 24
    Tanaka Y, Ueda K, Ozawa T, Sakuragawa N, Yokota S, Sato R, Okamura S, Morita M, Imanaka T. Intracellular accumulation of antithrombin Morioka (C95R), a novel mutation causing type I antithrombin deficiency. J Biol Chem 2002; 277: 5105867.
  • 25
    Picard V, Dautzenberg MD, Villoutreix BO, Orliaguet G, Alhenc-Gelas M, Aiach M. Antithrombin Phe229Leu: a new homozygous variant leading to spontaneous antithrombin polymerization in vivo associated with severe childhood thrombosis. Blood 2003; 102: 91925.
  • 26
    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 Rep 2011; 12: 10117.
  • 27
    Wang F, Song W, Brancati G, Segatori L. Inhibition of Endoplasmic Reticulum-associated Degradation Rescues Native Folding in Loss of Function Protein Misfolding Diseases. J Biol Chem 2011; 286: 4345464.
  • 28
    Sun XJ, Chang JY. Re-formation of disulphide bonds in reduced antithrombin III. Biochem J 1990; 269: 6659.
  • 29
    Fitton HL, Skinner R, Dafforn TR, Jin L, Pike RN. The N-terminal segment of antithrombin acts as a steric gate for the binding of heparin. Protein Sci 1998; 7: 7828.
  • 30
    Dupont DM, Madsen JB, Kristensen T, Bodker JS, Blouse GE, Wind T, Andreasen PA. Biochemical properties of plasminogen activator inhibitor-1. Front Biosci 2009; 14: 133761.
  • 31
    Xue Y, Björquist P, Inghardt T, Linschoten M, Musil D, Sjölin L, Deinum J. Interfering with the inhibitory mechanism of serpins: crystal structure of a complex formed between cleaved plasminogen activator inhibitor type 1 and a reactive-centre loop peptide. Structure 1998; 6: 62736.
  • 32
    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. Proc Natl Acad Sci USA 2000; 97: 6772.
  • 33
    Pearce MC, Powers GA, Feil SC, Hansen G, Parker MW, Bottomley SP. Identification and characterization of a misfolded monomeric serpin formed at physiological temperature. J Mol Biol 2010; 403: 45967.
  • 34
    Olson ST, Richard B, Izaguirre G, Schedin-Weiss S, Gettins PG. Molecular mechanisms of antithrombin-heparin regulation of blood clotting proteinases. A paradigm for understanding proteinase regulation by serpin family protein proteinase inhibitors. Biochimie 2010; 92: 158796.
  • 35
    Davis IW, Leaver-Fay A, Chen VB, Block JN, Kapral GJ, Wang X, Murray LW, Arendall WB 3rd, Snoeyink J, Richardson JS, Richardson DC. MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res 2007; 35: 37583.