Structural stability of human α-thrombin studied by disulfide reduction and scrambling
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Fenton, 1988, Regulation of thrombin, generation and function, Semin. Thromb. Hemost., 14, 234, 10.1055/s-2007-1002783
Vergnolle, 2002, Characterization of thrombin-induced leukocyte rolling and adherence: a potential proinflammatory role for proteinase-activated receptor-4, J. Immunol., 169, 1467, 10.4049/jimmunol.169.3.1467
Sambrano, 2001, Role of thrombin signalling in platelets in haemostasis and thrombosis, Nature, 413, 74, 10.1038/35092573
Esmon, 1996, Involvement of thrombin anion-binding exosites 1 and 2 in the activation of factor V and factor VIII, J. Biol. Chem., 271, 13882, 10.1074/jbc.271.23.13882
Baglia, 2000, Thrombin-mediated feedback activation of factor XI on the activated platelet surface is preferred over contact activation by factor XIIa or factor Xia, J. Biol. Chem., 275, 20514, 10.1074/jbc.M000464200
Sadasivan, 2000, Interaction of the factor XIII activation peptide with α-thrombin. Crystal structure of its enzyme–substrate analog complex, J. Biol. Chem., 275, 36942, 10.1074/jbc.M006076200
Esmon, 2000, Hematology, 1714
Liem, 1974, Mechanism of action of thrombin or fibrinogen: IV. Further mapping on the active sites of thrombin and trypsin, Arch. Biochem. Biophys., 160, 333, 10.1016/S0003-9861(74)80041-X
Lottenberg, 1983, The action of thrombin on peptide p-nitroanilide substrates: substrate selectivity and examination of hydrolysis under different reaction conditions, Biochim. Biophys. Acta, 742, 539, 10.1016/0167-4838(83)90272-8
Butkowski, 1977, Primary structure of human prothrombin 2 and alpha-thrombin, J. Biol. Chem., 252, 4942, 10.1016/S0021-9258(17)40144-X
Degen, 1983, Characterization of the complementary deoxyribonucleic acid and gene coding for human prothrombin, Biochemistry, 22, 2087, 10.1021/bi00278a008
Fenton, 1977, Human thrombins. Production, evaluation, and properties of alpha-thrombin, J. Biol. Chem., 252, 3587, 10.1016/S0021-9258(17)40293-6
Fenton, 1977, 43
Berliner, 1977, 197
Chang, 2001, The structure of denatured α-lactalbumin elucidated by the technique of disulfide scrambling. Fractionation of conformational isomers of α-lactalbumin, J. Biol. Chem., 276, 9705, 10.1074/jbc.M010700200
Chang, 2002, The unfolding mechanism and the disulfide structures of denatured lysozyme, FEBS. Lett., 511, 73, 10.1016/S0014-5793(01)03284-7
Chang, 1999, Denatured states of tick anticoagulant peptide. Compositional analysis of unfolded scrambled isomers, J. Biol. Chem., 274, 123, 10.1074/jbc.274.1.123
Chang, 2000, The unfolding pathway and conformational stability of potato carboxypeptidase inhibitor, J. Biol. Chem., 275, 14205, 10.1074/jbc.275.19.14205
Chang, 2000, The structure of denatured bovine pancreatic trypsin inhibitor (BPTI), FEBS Lett., 473, 183, 10.1016/S0014-5793(00)01515-5
Labhardt, 1986, Folding intermediates studied by circular dichroism, Methods Enzymol., 131, 126, 10.1016/0076-6879(86)31038-3
Surewicz, 1993, Determination of protein secondary structure by Fourier transform infrared spectroscopy: a critical assessment, Biochemistry, 32, 389, 10.1021/bi00053a001
Triullier, 2000, Transient non-native secondary structures during the refolding of alpha-lactalbumin detected by infrared spectroscopy, Nat. Struct. Biol., 7, 78, 10.1038/71286
Kim, 1986, Amide proton exchange as a probe of protein folding pathways, Methods Enzymol., 131, 136, 10.1016/0076-6879(86)31039-5
Forge, 1999, Rapid collapse and slow structural reorganisation during the refolding of bovine alpha-lactalbumin, J. Mol. Biol., 288, 673, 10.1006/jmbi.1999.2687
Klefhaber, 1995, Direct NMR evidence for an intermediate preceding the rate-limiting step in the unfolding of ribonuclease A, Nature, 375, 513, 10.1038/375513a0
Kuwajima, 1990, Kinetics of disulfide bond reduction in alpha. α-lactalbumin by dithiothreitol and molecular basis of superreactivity of the Cys6_Cys120 disulfide bond, Biochemistry, 29, 8240, 10.1021/bi00488a007
Kress, 1967, The basic trypsin inhibitor of bovine pancreas: VII. Reduction with borohydride of disulfide bond linking half-cystine residues 14 and 38, J. Biol. Chem., 242, 4925, 10.1016/S0021-9258(18)99457-3
Liu, 1968, Preparation of 14,38-bis-[S-carbamidomethyl]–(basic trypsin inhibitor) possessing full biological activity, Biochem. Biophys. Res. Commun., 31, 467, 10.1016/0006-291X(68)90500-7
Hollecker, 1983, Evolutionary conservation and variation of protein folding pathways. Two protease inhibitor homologues from black mamba venom, J. Mol. Biol., 168, 409, 10.1016/S0022-2836(83)80026-6
Chang, 1997, A two-stage mechanism for the reductive unfolding of disulfide-containing proteins, J. Biol. Chem., 272, 69, 10.1074/jbc.272.1.69
Chang, 1999, Quantitative analysis of the composition of the native and scrambled ribonuclease A, Anal. Biochem., 268, 147, 10.1006/abio.1998.3047
Chang, 1993, Production of disulfide-linked hirudin dimer by in vitro folding, FEBS Lett., 336, 53, 10.1016/0014-5793(93)81607-2
Bode, 1992, The refined 1.9-A X-ray crystal structure of d-Phe-Pro-Arg chloromethylketone-inhibited human alpha-thrombin: structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure–function relationships, Protein Sci., 1, 426, 10.1002/pro.5560010402
Gruetter, 1990, Crystal structure of the thrombin–hirudin complex: a novel mode of serine protease inhibition, EMBO J., 9, 2361, 10.1002/j.1460-2075.1990.tb07410.x
Rydel, 1990, The structure of a complex of recombinant hirudin and human alpha-thrombin, Science, 249, 277, 10.1126/science.2374926
White, 1996, The fifth epidermal growth factor-like domain of thrombomodulin does not have an epidermal growth factor-like disulfide bonding pattern, Proc. Natl. Acad. Sci. U. S. A., 93, 10177, 10.1073/pnas.93.19.10177