[1] Bioregulatory functions of thrombin. Eds D. A. Walz et al. New York : Acad. Sci., 1986. 450 p.

[2] Markwardt F. Pharmacology of hirudin: one hundred years after the first report of the anticoagulant agent in medicinal leeches. Biomed Biochim Acta. 1985;44(7-8):1007-13.

[3] Krstenansky JL, Owen TJ, Yates MT, Mao SJ. Anticoagulant peptides: nature of the interaction of the C-terminal region of hirudin with a noncatalytic binding site on thrombin. J Med Chem. 1987;30(9):1688-91.

[4] Markwardt F. Die Isolierung und chemische Charakterisierung des Hirudins. oppe Seylers Z Physiol Chem. 1957;308:147–56.

[5] Fenton JW 2nd. Thrombin specificity. Ann N Y Acad Sci. 1981;370:468-95.

[6] Serebryany SB. Thrombin: its structure and features of catalysis. Biokhimiya zhivotnykh i cheloveka. 1982; 6:14-26.

[7] Strukova SM. Structural and functional peculiarities of thrombin. Biokhimiya zhivotnykh i cheloveka. 1982; 6:26-38.

[8] Fenton JW II, Sonder SA. Thrombin active-site regions and functions. Ann NY Acad Sci. 1984;435:412–4.

[9] Schechter I, Berger A. On the size of the active site in proteases. I. Papain. Biochem Biophys Res Commun. 1967;27(2):157-62.

[10] Bode W, Mayr I, Baumann U, Huber R, Stone SR, Hofsteenge J. The refined 1.9 A crystal structure of human alpha-thrombin: interaction with D-Phe-Pro-Arg chloromethylketone and significance of the Tyr-Pro-Pro-Trp insertion segment. EMBO J. 1989;8(11):3467-75.

[11] Skrzypczak-Jankun E, Rydel TJ, Tulinsky A, Fenton JW 2nd, Mann KG. Human D-Phe-Pro-Arg-CH2-alpha-thrombin crystallization and diffraction data. J Mol Biol. 1989;206(4):755-7.

[12] Lewis SD, Lorand L, Fenton JW 2nd, Shafer JA. Catalytic competence of human alpha- and gamma-thrombin in the activation of fibrinogen and factor XIII. Biochemistry. 1987;26(24):7597-603.

[13] Dodt J, Müller H-P, Seemüller U, Chang J-Y. The complete amino acid sequence of hirudin, a thrombin specific inhibitor. FEBS Lett. 1984;165(2):180–4.

[14] Mao SJ, Yates MT, Blankenship DT, Cardin AD, Krstenansky JL, Lovenberg W, Jackson RL. Rapid purification and revised amino-terminal sequence of hirudin: a specific thrombin inhibitor of the bloodsucking leech. Anal Biochem. 1987;161(2):514-8.

[15] Harvey RP, Degryse E, Stefani L, Schamber F, Cazenave JP, Courtney M, Tolstoshev P, Lecocq JP. Cloning and expression of a cDNA coding for the anticoagulant hirudin from the bloodsucking leech, Hirudo medicinalis. Proc Natl Acad Sci U S A. 1986;83(4):1084-8.

[16] Dodt J, Machleidt W, Seemüller U, Maschler R, Fritz H. Isolation and characterization of hirudin isoinhibitors and sequence analysis of hirudin PA. Biol Chem Hoppe Seyler. 1986;367(8):803-11.

[17] Chang JY. The functional domain of hirudin, a thrombin-specific inhibitor. FEBS Lett. 1983;164(2):307-13.

[18] Degryse E, Acker M, Defreyn G, Bernat A, Maffrand JP, Roitsch C, Courtney M. Point mutations modifying the thrombin inhibition kinetics and antithrombotic activity in vivo of recombinant hirudin. Protein Eng. 1989;2(6):459-65.

[19] Clore GM, Sukumaran DK, Nilges M, Zarbock J, Gronenborn AM. The conformations of hirudin in solution: a study using nuclear magnetic resonance, distance geometry and restrained molecular dynamics. EMBO J. 1987;6(2):529-37.

[20] Sukumaran DK, Clore GM, Preuss A, Zarbock J, Gronenborn AM. Proton nuclear magnetic resonance study of hirudin: resonance assignment and secondary structure. Biochemistry. 1987;26(2):333–8.

[21] Folkers PJ, Clore GM, Driscoll PC, Dodt J, Köhler S, Gronenborn AM. Solution structure of recombinant hirudin and the Lys-47----Glu mutant: a nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing study. Biochemistry. 1989;28(6):2601-17.

[22] Haruyama H, Wüthrich K. Conformation of recombinant desulfatohirudin in aqueous solution determined by nuclear magnetic resonance. Biochemistry. 1989;28(10):4301-12.

[23] Tertrin C, De La Llosa P, Jutisz M. Effect of chemical modification of hirudin on its inhibition of the enzymatic activity of thrombin. Bull Soc Chim Biol (Paris). 1967;49(12):1837-43.

[24] Stone SR, Dennis S, Hofsteenge J. Quantitative evaluation of the contribution of ionic interactions to the formation of the thrombin-hirudin complex. Biochemistry. 1989;28(17):6857-63.

[25] Stone SR, Hofsteenge J. Kinetics of the inhibition of thrombin by hirudin. Biochemistry. 1986;25(16):4622-8.

[26] Dodt J, Köhler S, Baici A. Interaction of site specific hirudin variants with alpha-thrombin. FEBS Lett. 1988;229(1):87-90.

[27] Braun PJ, Dennis S, Hofsteenge J, Stone SR. Use of site-directed mutagenesis to investigate the basis for the specificity of hirudin. Biochemistry. 1988;27(17):6517-22.

[28] Wallace A, Dennis S, Hofsteenge J, Stone SR. Contribution of the N-terminal region of hirudin to its interaction with thrombin. Biochemistry. 1989;28(26):10079-84.

[29] Dodt J, Köhler S, Schmitz T, Wilhelm B. Distinct binding sites of Ala48-hirudin1-47 and Ala48-hirudin48-65 on alpha-thrombin. J Biol Chem. 1990;265(2):713-8.

[30] Dennis S, Wallace A, Hofsteenge J, Stone SR. Use of fragments of hirudin to investigate thrombin-hirudin interaction. Eur J Biochem. 1990;188(1):61-6.

[31] Winant RC, Lazar JB, Johnson PH. Chemical modifications and amino acid substitutions in recombinant hirudin that increase hirudin-thrombin affinity. Biochemistry. 1991;30(5):1271-7.

[32] Chang JY. The hirudin-binding site of human alpha-thrombin. Identification of lysyl residues which participate in the combining site of hirudin-thrombin complex. J Biol Chem. 1989;264(13):7141-6.

[33] Stone SR, Braun PJ, Hofsteenge J. Identification of regions of alpha-thrombin involved in its interaction with hirudin. Biochemistry. 1987;26(15):4617-24.

[34] Noé G, Hofsteenge J, Rovelli G, Stone SR. The use of sequence-specific antibodies to identify a secondary binding site in thrombin. J Biol Chem. 1988;263(24):11729-35.

[35] Schlaeppi JM, Vekemans S, Rink H, Chang JY. Preparation of monoclonal antibodies to hirudin and hirudin peptides. A method for studying the hirudin--thrombin interaction. Eur J Biochem. 1990;188(2):463-70.

[36] Krstenansky JL, Mao SJ. Antithrombin properties of C-terminus of hirudin using synthetic unsulfated N alpha-acetyl-hirudin45-65. FEBS Lett. 1987;211(1):10-6.

[37] Owen TJ, Krstenansky JL, Yates MT, Mao SJ. N-terminal requirements of small peptide anticoagulants based on hirudin54-65. J Med Chem. 1988;31(5):1009-11.

[38] Mao SJ, Yates MT, Owen TJ, Krstenansky JL. Interaction of hirudin with thrombin: identification of a minimal binding domain of hirudin that inhibits clotting activity. Biochemistry. 1988;27(21):8170-3.

[39] Maraganore JM, Chao B, Joseph ML, Jablonski J, Ramachandran KL. Anticoagulant activity of synthetic hirudin peptides. J Biol Chem. 1989;264(15):8692-8.

[40] Binnie CG, Erickson BW, Hermans J. Inhibition of thrombin by synthetic hirudin peptides. FEBS Lett. 1990;270(1-2):85-9.

[41] Bourdon P, Fenton JW 2nd, Maraganore JM. Affinity labeling of lysine-149 in the anion-binding exosite of human alpha-thrombin with an N alpha-(dinitrofluorobenzyl)hirudin C-terminal peptide. Biochemistry. 1990;29(27):6379-84.

[42] Konno S, Fenton JW 2nd, Villanueva GB. Analysis of the secondary structure of hirudin and the mechanism of its interaction with thrombin. Arch Biochem Biophys. 1988;267(1):158-66.

[43] Ni F, Konishi Y, Scheraga HA. Thrombin-bound conformation of the C-terminal fragments of hirudin determined by transferred nuclear Overhauser effects. Biochemistry. 1990;29(18):4479-89.

[44] Grütter MG, Priestle JP, Rahuel J, Grossenbacher H, Bode W, Hofsteenge J, Stone SR. Crystal structure of the thrombin-hirudin complex: a novel mode of serine protease inhibition. EMBO J. 1990;9(8):2361-5.

[45] Rydel TJ, Ravichandran KG, Tulinsky A, Bode W, Huber R, Roitsch C, Fenton JW 2nd. The structure of a complex of recombinant hirudin and human alpha-thrombin. Science. 1990;249(4966):277-80.

[46] Ishikawa A, Hafter R, Seemüller U, Gokel JM, Graeff H. The effect of hirudin on endotoxin induced disseminated intravascular coagulation (DIC). Thromb Res. 1980;19(3):351-8.

[47] Markwardt F, Hauptmann J, Nowak G, Klessen C, Walsmann P. Pharmacological studies on the antithrombotic action of hirudin in experimental animals. Thromb Haemost. 1982;47(3):226-9.

[48] Markwardt F, Nowak G, Stürzebecher J, Griessbach U, Walsmann P, Vogel G. Pharmacokinetics and anticoagulant effect of hirudin in man. Thromb Haemost. 1984;52(2):160-3.

[49] Markwardt F. Pharmacology of selective thrombin inhibitors. Nouv Rev Fr Hematol. 1988;30(3):161-5.

[50] Fortkamp E, Rieger M, Heisterberg-Moutses G, Schweitzer S, Sommer R. Cloning and expression in Escherichia coli of a synthetic DNA for hirudin, the blood coagulation inhibitor in the leech. DNA. 1986;5(6):511-7.

[51] Harvey RP, Degryse E, Stefani L, Schamber F, Cazenave JP, Courtney M, Tolstoshev P, Lecocq JP. Cloning and expression of a cDNA coding for the anticoagulant hirudin from the bloodsucking leech, Hirudo medicinalis. Proc Natl Acad Sci U S A. 1986;83(4):1084-8.

[52] Loison G, Findeli A, Bernard S, Nguyen-Juilleret M, Marquet M, Riehl-Bellon N, et al. Expression and Secretion in S. Cerevisiae of Biologically Active Leech Hirudin. Bio/Technology. 1988;6(1):72–7.

[53] Eric D. Determination of the specific activity of recombinant hirudin. Thromb Res. 1990;60(6):433-43.

[54] Hortin GL, Benutto BM. Inhibition of thrombin's clotting activity by synthetic peptide segments of its inhibitors and substrates. Biochem Biophys Res Commun. 1990;169(2):437-42.

[55] Pat. 299576 USA, IC1 A6IK37. 02, C07K 7. 10. G. L. Hortin (23.01.89). R.ZH «Fiziko-khimicheskaya biologiya i biotekhnologiya». 1990.N 10. Ref. 10A208P.

[56] Maraganore JM, Bourdon P, Jablonski J, Ramachandran KL, Fenton JW 2nd. Design and characterization of hirulogs: a novel class of bivalent peptide inhibitors of thrombin. Biochemistry. 1990;29(30):7095-101.