메뉴 건너뛰기




Volumn 29, Issue 4, 1997, Pages 478-491

SHBG region of the anticoagulant cofactor protein S: Secondary structure prediction, circular dichroism spectroscopy, and analysis of naturally occurring mutations

Author keywords

Blood coagulation; Secondary structure prediction; Vitamin k dependent

Indexed keywords

GROWTH ARREST FACTOR 6; LAMININ; PROTEIN S; SEX HORMONE BINDING GLOBULIN; UNCLASSIFIED DRUG; VITAMIN K GROUP;

EID: 0030719434     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-0134(199712)29:4<478::AID-PROT8>3.0.CO;2-4     Document Type: Article
Times cited : (35)

References (126)
  • 1
    • 0001976355 scopus 로고
    • The protein C anticoagulant system
    • Stamatoyannopoulos, G., Nienhuis, A.W., Majerus, P.W., Varmus, H. (eds.). Philadelphia: W.B. Saunders
    • Dahlbäck, B., Stenflo, J. The protein C anticoagulant system. In: "The Molecular Basis of Blood Diseases." Stamatoyannopoulos, G., Nienhuis, A.W., Majerus, P.W., Varmus, H. (eds.). Philadelphia: W.B. Saunders, 1994:599-627.
    • (1994) The Molecular Basis of Blood Diseases , pp. 599-627
    • Dahlbäck, B.1    Stenflo, J.2
  • 2
    • 0017337301 scopus 로고
    • A comparison of human prothrombin, factor IX, factor X, and protein S
    • DiScipio, R.G., Hermodson, M.A., Yates, S.G., Davie, E.W. A comparison of human prothrombin, factor IX, factor X, and protein S. Biochemistry 16:698-706, 1977.
    • (1977) Biochemistry , vol.16 , pp. 698-706
    • DiScipio, R.G.1    Hermodson, M.A.2    Yates, S.G.3    Davie, E.W.4
  • 3
    • 0022624812 scopus 로고
    • Biosynthesis and secretion of factor VII, protein C, protein S and the protein C inhibitor from a human hepatoma cell line
    • Fair, D.S., Marlar, R.A. Biosynthesis and secretion of factor VII, protein C, protein S and the protein C inhibitor from a human hepatoma cell line. Blood 67:64-70, 1986.
    • (1986) Blood , vol.67 , pp. 64-70
    • Fair, D.S.1    Marlar, R.A.2
  • 4
    • 0019849380 scopus 로고
    • Regulation of activated protein C by protein S, the role of phospholipid in factor Va inactivation
    • Walker, F.J. Regulation of activated protein C by protein S, the role of phospholipid in factor Va inactivation. J. Biol. Chem. 256:11128-11131, 1981.
    • (1981) J. Biol. Chem. , vol.256 , pp. 11128-11131
    • Walker, F.J.1
  • 5
    • 0025833619 scopus 로고
    • Protein S and C4b-binding protein: Components involved in the regulation of the protein C anticoagulant system
    • Dahlbäck, B. Protein S and C4b-binding protein: Components involved in the regulation of the protein C anticoagulant system. Thromb. Haemost. 66:49-61, 1991.
    • (1991) Thromb. Haemost. , vol.66 , pp. 49-61
    • Dahlbäck, B.1
  • 6
    • 0027404562 scopus 로고
    • Binding of protein S to factor Va associated with inhibition of prothrombinase that is independent of activated protein C
    • Heeb, M.J., Mesters, R.M., Tans, G., Rosing, J., Griffin, J.H. Binding of protein S to factor Va associated with inhibition of prothrombinase that is independent of activated protein C. J. Biol. Chem. 268:2872-2877, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2872-2877
    • Heeb, M.J.1    Mesters, R.M.2    Tans, G.3    Rosing, J.4    Griffin, J.H.5
  • 7
    • 0029118512 scopus 로고
    • Inhibition of the intrinsic factor X activation by protein S: Evidence for a specific binding of protein S to factor VIII
    • Koppelman, S.J., van't Veer, C., Sixma, J.J., Bouma, B.N. Inhibition of the intrinsic factor X activation by protein S: Evidence for a specific binding of protein S to factor VIII. Blood 86:2653-2660, 1995.
    • (1995) Blood , vol.86 , pp. 2653-2660
    • Koppelman, S.J.1    Van't Veer, C.2    Sixma, J.J.3    Bouma, B.N.4
  • 8
    • 0021741550 scopus 로고
    • Familial protein S deficiency is associated with recurrent thrombosis
    • Comp, P.C., Nixon, R.R., Cooper, M.R., Esmon, C.T. Familial protein S deficiency is associated with recurrent thrombosis. J. Clin. Invest. 74:2082-2088, 1984.
    • (1984) J. Clin. Invest. , vol.74 , pp. 2082-2088
    • Comp, P.C.1    Nixon, R.R.2    Cooper, M.R.3    Esmon, C.T.4
  • 10
    • 0024605404 scopus 로고
    • Severe arterial cerebral thrombosis in a patient with protein S deficiency (moderately reduced total and markedly reduced free protein S): A family study
    • Girolami, A., Simioni, P., Lazzaro, A.R., Cordiano, I. Severe arterial cerebral thrombosis in a patient with protein S deficiency (moderately reduced total and markedly reduced free protein S): A family study. Thromb. Haemost. 61:144-147, 1989.
    • (1989) Thromb. Haemost. , vol.61 , pp. 144-147
    • Girolami, A.1    Simioni, P.2    Lazzaro, A.R.3    Cordiano, I.4
  • 12
    • 0029016883 scopus 로고
    • Resistance to activated protein C as an additional genetic risk factor in hereditary deficiency of protein S
    • Zöller, B., Berntsdotter, A., García de Frutos, P., Dahlbäck, B. Resistance to activated protein C as an additional genetic risk factor in hereditary deficiency of protein S. Blood 85:3518-3523, 1995.
    • (1995) Blood , vol.85 , pp. 3518-3523
    • Zöller, B.1    Berntsdotter, A.2    García De Frutos, P.3    Dahlbäck, B.4
  • 13
    • 0027182792 scopus 로고
    • The protein encoded by a growth arrest-specific gene (gas6) is a new member of the vitamin K-dependent proteins related to protein S, a negative coregulator in the blood coagulation cascade
    • Manfioletti, G., Brancolini, C., Avanzi, G., Schneider, C. The protein encoded by a growth arrest-specific gene (gas6) is a new member of the vitamin K-dependent proteins related to protein S, a negative coregulator in the blood coagulation cascade. Mol. Cell. Biol. 13:4976-4985, 1993.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4976-4985
    • Manfioletti, G.1    Brancolini, C.2    Avanzi, G.3    Schneider, C.4
  • 17
    • 0023146815 scopus 로고
    • Vitamin K-dependent protein S is similar to rat androgen-binding protein
    • Baker, M.E., French, F.S., Joseph, D.R. Vitamin K-dependent protein S is similar to rat androgen-binding protein. Biochem. J. 243:293-296, 1987.
    • (1987) Biochem. J. , vol.243 , pp. 293-296
    • Baker, M.E.1    French, F.S.2    Joseph, D.R.3
  • 18
    • 0020638677 scopus 로고
    • Purification of human vitamin K-dependent protein S and its limited proteolysis by thrombin
    • Dahlbäck, B. Purification of human vitamin K-dependent protein S and its limited proteolysis by thrombin. Biochem. J. 209:837-846, 1983.
    • (1983) Biochem. J. , vol.209 , pp. 837-846
    • Dahlbäck, B.1
  • 20
    • 0024829563 scopus 로고
    • Protein S binding in relation to the subunit composition of human C4b-binding protein
    • Hillarp, A., Hessing, M., Dahlbäck, B. Protein S binding in relation to the subunit composition of human C4b-binding protein. FEBS Lett. 259:53-56, 1989.
    • (1989) FEBS Lett. , vol.259 , pp. 53-56
    • Hillarp, A.1    Hessing, M.2    Dahlbäck, B.3
  • 21
    • 0028103281 scopus 로고
    • Differential regulation of α and β chains of C4b-binding protein during acute phase response resulting in stable plasma levels of free anticoagulant protein S
    • García de Frutos, P., Alim, R.I.M., Härdig, Y., Zöller, B., Dahlbäck, B. Differential regulation of α and β chains of C4b-binding protein during acute phase response resulting in stable plasma levels of free anticoagulant protein S. Blood 84:815-822, 1994.
    • (1994) Blood , vol.84 , pp. 815-822
    • García De Frutos, P.1    Alim, R.I.M.2    Härdig, Y.3    Zöller, B.4    Dahlbäck, B.5
  • 22
    • 0024245613 scopus 로고
    • Novel subunit in C4b-binding protein required for protein S binding
    • Hillarp, A., Dahlbäck, B. Novel subunit in C4b-binding protein required for protein S binding. J. Biol. Chem. 263:12759-12764, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 12759-12764
    • Hillarp, A.1    Dahlbäck, B.2
  • 23
    • 0028030727 scopus 로고
    • A protein S binding site on C4b-binding protein involves beta chain residues 31-45
    • Fernández, J.A., Griffin, J.H. A protein S binding site on C4b-binding protein involves beta chain residues 31-45. J. Biol. Chem. 269:2535-2540, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2535-2540
    • Fernández, J.A.1    Griffin, J.H.2
  • 24
    • 0029053440 scopus 로고
    • Expression and characterization of a recombinant C4b-binding protein lacking the β-chain
    • Härdig, Y. García de Frutos, P., Dahlbäck, B. Expression and characterization of a recombinant C4b-binding protein lacking the β-chain. Biochem. J. 308:795-800, 1995.
    • (1995) Biochem. J. , vol.308 , pp. 795-800
    • Härdig, Y.1    García De Frutos, P.2    Dahlbäck, B.3
  • 25
    • 0029808210 scopus 로고    scopus 로고
    • The amino-terminal module of the C4b-binding protein β-chain contains the protein S-binding site
    • Härdig, Y. Dahlbäck, B. The amino-terminal module of the C4b-binding protein β-chain contains the protein S-binding site. J. Biol. Chem. 271:20861-20867, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 20861-20867
    • Härdig, Y.1    Dahlbäck, B.2
  • 26
    • 0025051272 scopus 로고    scopus 로고
    • High affinity interaction between C4b-binding protein and vitamin k-dependent protein S in the presence of calcium
    • Dahlbäck, B., Frohm, B., Nelsestuen, G. High affinity interaction between C4b-binding protein and vitamin k-dependent protein S in the presence of calcium. J. Biol. Chem. 265:16082-16087.
    • J. Biol. Chem. , vol.265 , pp. 16082-16087
    • Dahlbäck, B.1    Frohm, B.2    Nelsestuen, G.3
  • 27
    • 0024459550 scopus 로고
    • Characterization of a synthetic peptide that inhibits the interaction between protein S and C4b-binding protein
    • Walker, F.J. Characterization of a synthetic peptide that inhibits the interaction between protein S and C4b-binding protein. J. Biol. Chem. 264:17645-17648, 1989.
    • (1989) J. Biol. Chem. , vol.264 , pp. 17645-17648
    • Walker, F.J.1
  • 28
    • 0026781935 scopus 로고
    • Binding of protein S to C4b-binding protein
    • Nelson, R.M., Long, G.L. Binding of protein S to C4b-binding protein. J. Biol. Chem. 267:8140-8145, 1992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 8140-8145
    • Nelson, R.M.1    Long, G.L.2
  • 29
    • 0028202549 scopus 로고
    • Studies of the interaction between human protein S and human C4b-binding protein using deletion variants of recombinant human protein S
    • Chang, G.T.G., Maas, B.H.A., Ploos van Amstel, H.K., Reitsma, P.H., Bertina, R.M., Bouma, B.N. Studies of the interaction between human protein S and human C4b-binding protein using deletion variants of recombinant human protein S. Thromb. Haemost. 71:461-467, 1994.
    • (1994) Thromb. Haemost. , vol.71 , pp. 461-467
    • Chang, G.T.G.1    Maas, B.H.A.2    Ploos Van Amstel, H.K.3    Reitsma, P.H.4    Bertina, R.M.5    Bouma, B.N.6
  • 30
    • 0027203801 scopus 로고
    • Identification of residues 413-433 of plasma protein S as essential for binding to C4b-binding protein
    • Fernández, J.A., Heeb, M.J., Griffin, J.H. Identification of residues 413-433 of plasma protein S as essential for binding to C4b-binding protein. J. Biol. Chem. 268:16788-16794, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16788-16794
    • Fernández, J.A.1    Heeb, M.J.2    Griffin, J.H.3
  • 31
    • 0030951464 scopus 로고    scopus 로고
    • Binding site for C4b-binding protein in vitamin K-dependent protein S fully contained in the carboxy-terminal laminin-G-type repeats. A study using recombinant factor IX-protein S chimeras and surface plasmon resonance
    • He, X., Shen, L., Malmborg, A., Smith, K.J., Dahlbäck, B., Linse, S. Binding site for C4b-binding protein in vitamin K-dependent protein S fully contained in the carboxy-terminal laminin-G-type repeats. A study using recombinant factor IX-protein S chimeras and surface plasmon resonance. Biochemistry 36:3745-3754, 1997.
    • (1997) Biochemistry , vol.36 , pp. 3745-3754
    • He, X.1    Shen, L.2    Malmborg, A.3    Smith, K.J.4    Dahlbäck, B.5    Linse, S.6
  • 32
    • 0025217659 scopus 로고
    • Laboratory evaluation of protein S status
    • Comp, P.C. Laboratory evaluation of protein S status. Semin. Thromb. Haemost. 16:177-181, 1990.
    • (1990) Semin. Thromb. Haemost. , vol.16 , pp. 177-181
    • Comp, P.C.1
  • 34
    • 0029017118 scopus 로고
    • Evaluation of the relationship between protein S and C4b-binding protein isoforms in hereditary protein S deficiency demonstrating type I and type III deficiencies to be phenotypic variants of the same genetic disease
    • Zöller, B., García de Frutos, P., Dahlbäck, B. Evaluation of the relationship between protein S and C4b-binding protein isoforms in hereditary protein S deficiency demonstrating type I and type III deficiencies to be phenotypic variants of the same genetic disease. Blood 85:3524-3531, 1995.
    • (1995) Blood , vol.85 , pp. 3524-3531
    • Zöller, B.1    García De Frutos, P.2    Dahlbäck, B.3
  • 35
    • 0028871033 scopus 로고
    • Identification of 15 different candidate causal point mutations and three polymorphisms in 19 patients with protein S deficiency using a scanning method for the analysis of the protein S active gene
    • Gandrille, S., Borgel, D., Eschwege-Gufflet, V., Aillaud, M., Dreyfus, M., Matheron, C., Gaussem, P., Abgrall, J.F., Jude, B., Sie, P., Touion, P., Aiach, M. Identification of 15 different candidate causal point mutations and three polymorphisms in 19 patients with protein S deficiency using a scanning method for the analysis of the protein S active gene. Blood 85:130-138, 1995.
    • (1995) Blood , vol.85 , pp. 130-138
    • Gandrille, S.1    Borgel, D.2    Eschwege-Gufflet, V.3    Aillaud, M.4    Dreyfus, M.5    Matheron, C.6    Gaussem, P.7    Abgrall, J.F.8    Jude, B.9    Sie, P.10    Touion, P.11    Aiach, M.12
  • 36
    • 0029060076 scopus 로고
    • Identification of eight point mutations in protein S deficiency Type I - Analysis of 15 pedigrees. Thromb
    • Gómez, E., Poort, S.R., Bertina, R.M., Reitsma, P.H. Identification of eight point mutations in protein S deficiency Type I - analysis of 15 pedigrees. Thromb. Haemost. 73:750-755, 1995.
    • (1995) Haemost. , vol.73 , pp. 750-755
    • Gómez, E.1    Poort, S.R.2    Bertina, R.M.3    Reitsma, P.H.4
  • 37
    • 0028818519 scopus 로고
    • Protein S deficiency type I: Identification of points mutations in 9 of 10 families
    • Mustafa, S., Pabinger, I., Mannhalter, C. Protein S deficiency type I: Identification of points mutations in 9 of 10 families. Blood 86:3444-3451, 1995.
    • (1995) Blood , vol.86 , pp. 3444-3451
    • Mustafa, S.1    Pabinger, I.2    Mannhalter, C.3
  • 38
    • 0029792264 scopus 로고    scopus 로고
    • Molecular basis of protein S deficiency in three families also showing independent inheritance of factor V Leiden
    • Beauchamp, N.J., Daly, M.E., Cooper, P.C., Makris, M., Preston, E., Peake, I.R. Molecular basis of protein S deficiency in three families also showing independent inheritance of factor V Leiden. Blood 88:1700-1707, 1996.
    • (1996) Blood , vol.88 , pp. 1700-1707
    • Beauchamp, N.J.1    Daly, M.E.2    Cooper, P.C.3    Makris, M.4    Preston, E.5    Peake, I.R.6
  • 39
    • 0029981830 scopus 로고    scopus 로고
    • Severe perinatal thrombosis in double and triple heterozygous offspring of a family segregating two independent protein S mutations and a protein C mutation
    • Formstone, C.J., Hallam, P.J., Tuddenham, E.G.D., Voke, J., Layton, M., Nicolaides, K., Hann, I.M., Cooper, D.N. Severe perinatal thrombosis in double and triple heterozygous offspring of a family segregating two independent protein S mutations and a protein C mutation. Blood 87:3731-3737, 1996.
    • (1996) Blood , vol.87 , pp. 3731-3737
    • Formstone, C.J.1    Hallam, P.J.2    Tuddenham, E.G.D.3    Voke, J.4    Layton, M.5    Nicolaides, K.6    Hann, I.M.7    Cooper, D.N.8
  • 42
    • 10544236115 scopus 로고    scopus 로고
    • Identification of 19 protein S gene mutations in patients with phenotypic protein S deficiency and thrombosis
    • Simmonds, R.E., Ireland, H., Kunz, G., Lane, D.A., and the Protein S Study Group. Identification of 19 protein S gene mutations in patients with phenotypic protein S deficiency and thrombosis. Blood 88:4195-4204, 1996.
    • (1996) Blood , vol.88 , pp. 4195-4204
    • Simmonds, R.E.1    Ireland, H.2    Kunz, G.3    Lane, D.A.4
  • 43
    • 0030205254 scopus 로고    scopus 로고
    • Molecular basis for protein S hereditary deficiency: Genetic defects observed in 118 patients with type I and type IIa deficiencies
    • Borgel, D., Duchemin, J., Alhenc-Gelas, M., Matheron, C., Aiach, M., Gandrille, S., and the French Network on Molecular Abnormalities Responsible for Protein C and Protein S Deficiencies. Molecular basis for protein S hereditary deficiency: Genetic defects observed in 118 patients with type I and type IIa deficiencies. J. Lab. Clin. Med. 128:218-227, 1996.
    • (1996) J. Lab. Clin. Med. , vol.128 , pp. 218-227
    • Borgel, D.1    Duchemin, J.2    Alhenc-Gelas, M.3    Matheron, C.4    Aiach, M.5    Gandrille, S.6
  • 44
    • 0029910496 scopus 로고    scopus 로고
    • The Ser460Pro substitution of the protein S (PS) gene is rare in Italian patients with type IIa deficiency
    • Castaman, G., Ruggeri, M., Tosetto, A., Bernardi, F., Rodeghiero, F. The Ser460Pro substitution of the protein S (PS) gene is rare in Italian patients with type IIa deficiency. Blood 88:3666-3667, 1996.
    • (1996) Blood , vol.88 , pp. 3666-3667
    • Castaman, G.1    Ruggeri, M.2    Tosetto, A.3    Bernardi, F.4    Rodeghiero, F.5
  • 45
    • 1842287995 scopus 로고    scopus 로고
    • Genetic and phenotypic analysis of a large (122 member) protein S deficient kindred provides an explanation for the familial coexistence of type I and III plasma phenotypes
    • Simmonds, R.E., Zöller, B., Ireland, H., Thompson, E., García de Frutos, P., Dahlbäck, B., Lane, D.A. Genetic and phenotypic analysis of a large (122 member) protein S deficient kindred provides an explanation for the familial coexistence of type I and III plasma phenotypes. Blood 89:4364-4370, 1997.
    • (1997) Blood , vol.89 , pp. 4364-4370
    • Simmonds, R.E.1    Zöller, B.2    Ireland, H.3    Thompson, E.4    García De Frutos, P.5    Dahlbäck, B.6    Lane, D.A.7
  • 47
    • 0030062954 scopus 로고    scopus 로고
    • GAS6, the ligand of Ax1 tyrosine kinase receptor, has mitogenic and survival activities for serum starved NIH3T3 fibroblasts
    • Goruppi, S., Ruaro, E., Schneider, C. GAS6, the ligand of Ax1 tyrosine kinase receptor, has mitogenic and survival activities for serum starved NIH3T3 fibroblasts. Oncogene 12:471-480, 1996.
    • (1996) Oncogene , vol.12 , pp. 471-480
    • Goruppi, S.1    Ruaro, E.2    Schneider, C.3
  • 48
  • 49
    • 0029994283 scopus 로고    scopus 로고
    • Prevention of growth arrest-induced cell death of vascular smooth muscle cells by a product of growth arrest-specific gene, gas6
    • Nakano, T., Kawamoto, K., Higashino, K., Arita, H. Prevention of growth arrest-induced cell death of vascular smooth muscle cells by a product of growth arrest-specific gene, gas6. FEBS Lett. 387:78-80, 1996.
    • (1996) FEBS Lett. , vol.387 , pp. 78-80
    • Nakano, T.1    Kawamoto, K.2    Higashino, K.3    Arita, H.4
  • 50
    • 0022654745 scopus 로고
    • Physicochemical characteristics of human sex hormone binding globulin: Evidence for two identical subunits
    • Hammond, G.L., Robinson, P.A., Sugino, H., Ward, D.N., Finne, J. Physicochemical characteristics of human sex hormone binding globulin: Evidence for two identical subunits. J. Steroid Biochem. 24:815-824, 1986.
    • (1986) J. Steroid Biochem. , vol.24 , pp. 815-824
    • Hammond, G.L.1    Robinson, P.A.2    Sugino, H.3    Ward, D.N.4    Finne, J.5
  • 51
    • 0025938767 scopus 로고
    • The plasma sex steroid binding protein (bBr-or SHBG). A critical review of recent developments on the structure, molecular biology and function
    • Petra, P.H. The plasma sex steroid binding protein (bBr-or SHBG). A critical review of recent developments on the structure, molecular biology and function. J. Steroid Biochem. Mol. Biol. 40:735-753, 1991.
    • (1991) J. Steroid Biochem. Mol. Biol. , vol.40 , pp. 735-753
    • Petra, P.H.1
  • 52
    • 0029135297 scopus 로고
    • Sex hormone-binding globulin/androgen-binding protein: Steroid-binding and dimerization
    • Hammond, G.L., Bocchinfuso, W.P. Sex hormone-binding globulin/androgen-binding protein: Steroid-binding and dimerization. J. Steroid Biochem. Mol. Biol. 53:543-552, 1995.
    • (1995) J. Steroid Biochem. Mol. Biol. , vol.53 , pp. 543-552
    • Hammond, G.L.1    Bocchinfuso, W.P.2
  • 53
    • 0025732502 scopus 로고
    • Sex steroid binding protein interacts with a specific receptor on human premenopausal endometrium membrane: Modulating effects of estradiol
    • Fortunati, N., Fissore, F., Fazzari, A., Berta, L., Giudici, M., Frairia, R. Sex steroid binding protein interacts with a specific receptor on human premenopausal endometrium membrane: Modulating effects of estradiol. Steroids 56:341-346, 1991.
    • (1991) Steroids , vol.56 , pp. 341-346
    • Fortunati, N.1    Fissore, F.2    Fazzari, A.3    Berta, L.4    Giudici, M.5    Frairia, R.6
  • 54
    • 0019220559 scopus 로고
    • Serum sex hormone-binding globulin capacity and the percentage of free estradiol in postmenopausal women with and without endometrial cancer
    • Nisker, J.A., Hammond, G.L., Davidson, B.J., Frumar, A.M., Takaki, N.K., Judd, H.L., Siiteri, P.K. Serum sex hormone-binding globulin capacity and the percentage of free estradiol in postmenopausal women with and without endometrial cancer. Am. J. Obstet. Gynecol. 138:637-641, 1980.
    • (1980) Am. J. Obstet. Gynecol. , vol.138 , pp. 637-641
    • Nisker, J.A.1    Hammond, G.L.2    Davidson, B.J.3    Frumar, A.M.4    Takaki, N.K.5    Judd, H.L.6    Siiteri, P.K.7
  • 55
    • 0025273750 scopus 로고
    • Molecular properties of corticosteroid binding globulin and the sex-steroid binding proteins
    • Hammond, G.L. Molecular properties of corticosteroid binding globulin and the sex-steroid binding proteins. Endocr. Rev. 11:65-79, 1990.
    • (1990) Endocr. Rev. , vol.11 , pp. 65-79
    • Hammond, G.L.1
  • 56
    • 0026589331 scopus 로고
    • Structure/function analyses of human sex hormone binding globulin by site directed mutagenesis
    • Bocchinfuso, W.P., Warmels-Rodenhiser, S., Hammond, G.L. Structure/function analyses of human sex hormone binding globulin by site directed mutagenesis. FEBS Lett. 301:227-230, 1992.
    • (1992) FEBS Lett. , vol.301 , pp. 227-230
    • Bocchinfuso, W.P.1    Warmels-Rodenhiser, S.2    Hammond, G.L.3
  • 57
    • 0028956670 scopus 로고
    • Resolution of the steroid binding and dimerization domains of human sex hormone binding globulin by expression in Escherichia coli
    • Hudebrand, C., Bocchinfuso, W.P., Dales, D., Hammond, G.L. Resolution of the steroid binding and dimerization domains of human sex hormone binding globulin by expression in Escherichia coli. Biochemistry 34:3231-3238, 1995.
    • (1995) Biochemistry , vol.34 , pp. 3231-3238
    • Hudebrand, C.1    Bocchinfuso, W.P.2    Dales, D.3    Hammond, G.L.4
  • 58
    • 0026649324 scopus 로고
    • Localization of the steroid binding site of the human sex steroid binding protein of plasma (SBP or SHBG) by site directed mutagenesis
    • Sui, L.M., Cheung, A.W.C., Namkung, P.C., Pétra, P.H. Localization of the steroid binding site of the human sex steroid binding protein of plasma (SBP or SHBG) by site directed mutagenesis. FEBS Lett. 310:115-118, 1992.
    • (1992) FEBS Lett. , vol.310 , pp. 115-118
    • Sui, L.M.1    Cheung, A.W.C.2    Namkung, P.C.3    Pétra, P.H.4
  • 59
    • 0027314521 scopus 로고
    • Mutagenesis of essential functional residues of rat androgen binding protein/sex hormone binding globulin
    • Joseph, D.R., Lawrence, W. Mutagenesis of essential functional residues of rat androgen binding protein/sex hormone binding globulin. Mol. Endocrinol. 7:488-496, 1993.
    • (1993) Mol. Endocrinol. , vol.7 , pp. 488-496
    • Joseph, D.R.1    Lawrence, W.2
  • 61
    • 0030460333 scopus 로고
    • Direct evidence for the localization of the steroid-binding site of the plasma sex steroid-binding protein (SBP or SHBG) at the interface between the subunits
    • Sui, L.M., Hughes, W., Hoppe, A.J., Pétra, P.H. Direct evidence for the localization of the steroid-binding site of the plasma sex steroid-binding protein (SBP or SHBG) at the interface between the subunits. Protein Sci. 5:2514-2520, 1966.
    • (1966) Protein Sci. , vol.5 , pp. 2514-2520
    • Sui, L.M.1    Hughes, W.2    Hoppe, A.J.3    Pétra, P.H.4
  • 62
    • 0024580360 scopus 로고
    • 1 form of uteroglobin at 1.64 Å resolution
    • 1 form of uteroglobin at 1.64 Å resolution. J. Mol. Biol. 206:153-170, 1989.
    • (1989) J. Mol. Biol. , vol.206 , pp. 153-170
    • Bally, R.1    Selettre, J.2
  • 63
    • 0025793579 scopus 로고
    • Crystal structure of cholesterol oxidase from Brevibacterium sterolicum refined at 1.8 Å resolution
    • Vrielink, A., Lloyd, L.F., Blow, D.M. Crystal structure of cholesterol oxidase from Brevibacterium sterolicum refined at 1.8 Å resolution. J. Mol. Biol. 219:533-554, 1991.
    • (1991) J. Mol. Biol. , vol.219 , pp. 533-554
    • Vrielink, A.1    Lloyd, L.F.2    Blow, D.M.3
  • 64
    • 0025838697 scopus 로고
    • Three-dimensional structure of holo 3 alpha, 20 beta-hydroxysteroid dehydrogenase: A member of a short chain dehydrogenase family
    • Ghosh, D., Weeks, C.M., Grochulski, P., Duax, W.L., Erman, M., Rimsay, R.L., Orr, J.C. Three-dimensional structure of holo 3 alpha, 20 beta-hydroxysteroid dehydrogenase: A member of a short chain dehydrogenase family. Proc. Natl. Acad. Sci. U.S.A. 88:10064-10068, 1991.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 10064-10068
    • Ghosh, D.1    Weeks, C.M.2    Grochulski, P.3    Duax, W.L.4    Erman, M.5    Rimsay, R.L.6    Orr, J.C.7
  • 65
    • 0026634648 scopus 로고
    • Molecular modelling and site directed mutagenesis on a bovine anti-testosterone monoclonal antibody
    • Jackson, T., Morris, B.A., Martin, A.C.R., Lewis, D.F., Sanders, P.G. Molecular modelling and site directed mutagenesis on a bovine anti-testosterone monoclonal antibody. Protein Eng. 5:343-350, 1992.
    • (1992) Protein Eng. , vol.5 , pp. 343-350
    • Jackson, T.1    Morris, B.A.2    Martin, A.C.R.3    Lewis, D.F.4    Sanders, P.G.5
  • 66
    • 0027299695 scopus 로고
    • Three-dimensional structure of an anti-steroid Fab and progesterone-Fab' complex
    • Arevalo, J.H., Stura, E.A., Taussig, M.J., Wilson, I.A. Three-dimensional structure of an anti-steroid Fab and progesterone-Fab' complex. J. Mol. Biol. 231:103-118, 1993.
    • (1993) J. Mol. Biol. , vol.231 , pp. 103-118
    • Arevalo, J.H.1    Stura, E.A.2    Taussig, M.J.3    Wilson, I.A.4
  • 67
    • 0028944194 scopus 로고
    • Progesterone binding to uteroglobin: Two alternative orientations of the ligand
    • Dunkel, R., Vriend, G., Beato, M., Suske, G. Progesterone binding to uteroglobin: Two alternative orientations of the ligand. Protein Eng. 8:71-79, 1995.
    • (1995) Protein Eng. , vol.8 , pp. 71-79
    • Dunkel, R.1    Vriend, G.2    Beato, M.3    Suske, G.4
  • 68
    • 0029761692 scopus 로고    scopus 로고
    • Crystal structure of human estrogenic 17β-hydroxysteroid dehydrogenase complexed with 17β-estradiol
    • Azzi A., Rehse, P.H., Zhu, D.W., Campbell, R.L., Labrie, F., Lin, S.X. Crystal structure of human estrogenic 17β-hydroxysteroid dehydrogenase complexed with 17β-estradiol. Nat. Struct. Biol. 3:665-668, 1996.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 665-668
    • Azzi, A.1    Rehse, P.H.2    Zhu, D.W.3    Campbell, R.L.4    Labrie, F.5    Lin, S.X.6
  • 69
    • 0025165018 scopus 로고
    • Structure and function of laminin: Anatomy of a multidomain glycoprotein
    • Beck, K., Hunter, I., Engel, J. Structure and function of laminin: Anatomy of a multidomain glycoprotein. FASEB J. 4:148-160, 1990.
    • (1990) FASEB J. , vol.4 , pp. 148-160
    • Beck, K.1    Hunter, I.2    Engel, J.3
  • 70
    • 0026691698 scopus 로고
    • Sex hormone binding globulin, androgen binding protein and vitamin K dependent protein S are homologous to laminin A, merosin and drosophila crumbs protein
    • Joseph, D.R., Baker, M.E. Sex hormone binding globulin, androgen binding protein and vitamin K dependent protein S are homologous to laminin A, merosin and drosophila crumbs protein. FASEB J. 6:2477-2481, 1992.
    • (1992) FASEB J. , vol.6 , pp. 2477-2481
    • Joseph, D.R.1    Baker, M.E.2
  • 73
    • 0027416755 scopus 로고
    • Recombinant laminin G domain mediates myoblast adhesion and heparin binding
    • Yurchenco, P.D., Sung, U., Ward, M.D., Yamada, Y., O'Rear J. Recombinant laminin G domain mediates myoblast adhesion and heparin binding. J. Biol. Chem. 268:8356-8365, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 8356-8365
    • Yurchenco, P.D.1    Sung, U.2    Ward, M.D.3    Yamada, Y.4    O'Rear, J.5
  • 74
    • 0023503414 scopus 로고
    • Laminin and other basement membrane components
    • Martin, G.R., Timpl, R. Laminin and other basement membrane components. Annu. Rev. Cell Biol. 3:57-85, 1987.
    • (1987) Annu. Rev. Cell Biol. , vol.3 , pp. 57-85
    • Martin, G.R.1    Timpl, R.2
  • 75
    • 0024022763 scopus 로고
    • Structure and distribution of N-linked ohgosaccharide chains on various domains of mouse tumour laminin
    • Fujiwara, S., Shinkai, H., Deutzmann, R., Paulsson, M., Timpl, R. Structure and distribution of N-linked ohgosaccharide chains on various domains of mouse tumour laminin. Biochem. J. 252:453-461, 1988.
    • (1988) Biochem. J. , vol.252 , pp. 453-461
    • Fujiwara, S.1    Shinkai, H.2    Deutzmann, R.3    Paulsson, M.4    Timpl, R.5
  • 76
    • 0026340908 scopus 로고
    • Drosophila laminin A chain sequence, interspecies comparison and domain structure of a major carboxyl portion
    • Garrison, K., MacKrell, A.J., Fessier, J.H. Drosophila laminin A chain sequence, interspecies comparison and domain structure of a major carboxyl portion. J. Biol. Chem. 266:22899-22904, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 22899-22904
    • Garrison, K.1    MacKrell, A.J.2    Fessier, J.H.3
  • 77
    • 0014757386 scopus 로고
    • A general method to search for similarities in the amino acid sequence of two proteins
    • Needleman, S.B., Wunsch, C.D. A general method to search for similarities in the amino acid sequence of two proteins. J. Mol. Biol. 48:443-453, 1970.
    • (1970) J. Mol. Biol. , vol.48 , pp. 443-453
    • Needleman, S.B.1    Wunsch, C.D.2
  • 78
    • 0020649886 scopus 로고
    • Establishing homologies in protein sequences
    • Dayhoff, M.O., Barker, W.C., Hunt, L.T. Establishing homologies in protein sequences. Methods Enzymol. 91: 524-545, 1983.
    • (1983) Methods Enzymol. , vol.91 , pp. 524-545
    • Dayhoff, M.O.1    Barker, W.C.2    Hunt, L.T.3
  • 79
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice
    • Thompson, J.D., Higgins, D.G., Gibson, T.J. CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:4673-4680, 1994.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 80
    • 0029889988 scopus 로고    scopus 로고
    • PHD: Predicting one-dimensional protein structure by profile based neural networks
    • Rost, B. PHD: Predicting one-dimensional protein structure by profile based neural networks. Methods Enzymol. 266:525-539, 1996.
    • (1996) Methods Enzymol. , vol.266 , pp. 525-539
    • Rost, B.1
  • 81
    • 0027291015 scopus 로고
    • Prediction of protein secondary structure at better than 70% accuracy
    • Rost, B., Sander, C. Prediction of protein secondary structure at better than 70% accuracy. J. Mol. Biol. 232:584-599, 1993.
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 82
    • 0028109886 scopus 로고
    • Conservation and prediction of solvent accessibility in protein families
    • Rost, B., Sander, C. Conservation and prediction of solvent accessibility in protein families. Proteins 20:216-226, 1994.
    • (1994) Proteins , vol.20 , pp. 216-226
    • Rost, B.1    Sander, C.2
  • 83
    • 0027076848 scopus 로고
    • Binding of anticoagulant vitamin K-dependent protein S to platelet-derived microparticles
    • Dahlbäck, B., Wiedmer, T., Sims, P.J. Binding of anticoagulant vitamin K-dependent protein S to platelet-derived microparticles. Biochemistry 31:12769-12777, 1992.
    • (1992) Biochemistry , vol.31 , pp. 12769-12777
    • Dahlbäck, B.1    Wiedmer, T.2    Sims, P.J.3
  • 84
    • 0022503457 scopus 로고
    • Calculation of protein conformation from circular dichroism
    • Yang, J.T., Wu, C.-S.C., Martinez, H.M. Calculation of protein conformation from circular dichroism. Methods Enzymol. 130:208-225, 1986.
    • (1986) Methods Enzymol. , vol.130 , pp. 208-225
    • Yang, J.T.1    Wu, C.-S.C.2    Martinez, H.M.3
  • 85
    • 0027447099 scopus 로고
    • A self-consistent method for the analysis of protein secondary structure from circular dichroism
    • Sreerama, N., Woody, R.W. A self-consistent method for the analysis of protein secondary structure from circular dichroism. Anal. Biochem. 209:32-44, 1993.
    • (1993) Anal. Biochem. , vol.209 , pp. 32-44
    • Sreerama, N.1    Woody, R.W.2
  • 86
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structures: Pattern recognition of hydrogen-bonded and geometric features
    • Kabsch, W., Sanders, C. Dictionary of protein secondary structures: Pattern recognition of hydrogen-bonded and geometric features. Biopolymers 22:2577-2637, 1983.
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sanders, C.2
  • 87
    • 0019871893 scopus 로고
    • Information content in the circular dichroism of proteins
    • Hennessey, J.P., Johnson, W.C. Information content in the circular dichroism of proteins. Biochemistry 20:1085-1094, 1981.
    • (1981) Biochemistry , vol.20 , pp. 1085-1094
    • Hennessey, J.P.1    Johnson, W.C.2
  • 88
    • 0017701604 scopus 로고
    • Automatic identification of secondary structure in globular proteins
    • Levitt, M., Greer, J. Automatic identification of secondary structure in globular proteins. J. Mol. Biol. 114:181-239, 1977.
    • (1977) J. Mol. Biol. , vol.114 , pp. 181-239
    • Levitt, M.1    Greer, J.2
  • 89
    • 0026254055 scopus 로고
    • Parameters of helix-coil transition theory for alanine-based peptides of varying chain lengths in water
    • Scholtz, J.M., Qian, H., York, E.J., Stewart, J.M., Baldwin, R.L. Parameters of helix-coil transition theory for alanine-based peptides of varying chain lengths in water. Biopolymers 31:1463-1470, 1991.
    • (1991) Biopolymers , vol.31 , pp. 1463-1470
    • Scholtz, J.M.1    Qian, H.2    York, E.J.3    Stewart, J.M.4    Baldwin, R.L.5
  • 90
    • 0029888625 scopus 로고    scopus 로고
    • Converting sequence block alignments into structural insights
    • Poch, O., Delarue, M. Converting sequence block alignments into structural insights. Methods Enzymol. 266: 662-680, 1996.
    • (1996) Methods Enzymol. , vol.266 , pp. 662-680
    • Poch, O.1    Delarue, M.2
  • 91
    • 0028956959 scopus 로고
    • A new approach to the evaluation of protein secondary structure predictions at the level of the elements of secondary structure
    • Zhu, Z-Y. A new approach to the evaluation of protein secondary structure predictions at the level of the elements of secondary structure. Protein Eng. 8:103-108, 1995.
    • (1995) Protein Eng. , vol.8 , pp. 103-108
    • Zhu, Z.-Y.1
  • 95
    • 0024369176 scopus 로고
    • Characterization of the human sex hormone binding globulin (SHBG) gene and demonstration of two transcripts in both liver and testis
    • Gershagen, S., Lundwall, Å., Fernlund, P. Characterization of the human sex hormone binding globulin (SHBG) gene and demonstration of two transcripts in both liver and testis. Nucleic Acids Res. 17:9245-9258, 1989.
    • (1989) Nucleic Acids Res. , vol.17 , pp. 9245-9258
    • Gershagen, S.1    Lundwall, Å.2    Fernlund, P.3
  • 96
    • 0026456703 scopus 로고
    • Laminin A chain: Expression during Drosophila development and genomic sequence
    • Kusche-Gullberg, M., Garrison, K., Mackrell, A.J., Fesslet, L.I., Fessler, J.H. Laminin A chain: Expression during Drosophila development and genomic sequence. EMBO J. 11:4519-4527, 1992.
    • (1992) EMBO J. , vol.11 , pp. 4519-4527
    • Kusche-Gullberg, M.1    Garrison, K.2    Mackrell, A.J.3    Fesslet, L.I.4    Fessler, J.H.5
  • 97
    • 0021440884 scopus 로고
    • Correlation of exons with structural domains in alcohol dehydrogenase
    • Branden, C.I., Eklund, H., Cambillau, C., Pryor, A.J. Correlation of exons with structural domains in alcohol dehydrogenase. EMBO J. 3:1307-1310, 1984.
    • (1984) EMBO J. , vol.3 , pp. 1307-1310
    • Branden, C.I.1    Eklund, H.2    Cambillau, C.3    Pryor, A.J.4
  • 99
    • 0027070912 scopus 로고
    • Complete enzymatic deglycosylation of native sex steroid binding protein (SBP or SHBG) of human and rabbit plasma: Effect on the steroid-binding activity
    • Petra, P.H., Griffin, P.R., Yates, J.R. III, Moore, K., Zhang, W. Complete enzymatic deglycosylation of native sex steroid binding protein (SBP or SHBG) of human and rabbit plasma: Effect on the steroid-binding activity. Protein Sci. 1:902-909, 1992.
    • (1992) Protein Sci. , vol.1 , pp. 902-909
    • Petra, P.H.1    Griffin, P.R.2    Yates III, J.R.3    Moore, K.4    Zhang, W.5
  • 100
    • 0029186289 scopus 로고
    • TOPITS: Threading one-dimensional predictions into three-dimensional structures
    • Rawlings, C., Clark, C., Altman, R., Hunter, L., Lengauer, T., Wodak, S. (eds.). Menlo Park, CA: AAAI Press
    • Rost, B. TOPITS: threading one-dimensional predictions into three-dimensional structures. In: "The Third International Conference on Intelligent Systems for Molecular Biology (ISMB)." Rawlings, C., Clark, C., Altman, R., Hunter, L., Lengauer, T., Wodak, S. (eds.). Menlo Park, CA: AAAI Press, 1995:314-321.
    • (1995) The Third International Conference on Intelligent Systems for Molecular Biology (ISMB) , pp. 314-321
    • Rost, B.1
  • 103
    • 0031137254 scopus 로고    scopus 로고
    • A theoretical model for the Gla-TSR-EGF-1 region of the anticoagulant cofactor protein S: From biostructural pathology to species specific cofactor activity
    • Villoutreix, B.O., Teleman, O., Dahlbäck, B. A theoretical model for the Gla-TSR-EGF-1 region of the anticoagulant cofactor protein S: From biostructural pathology to species specific cofactor activity. J. Comput. Aided Mol. Des. 11:293-304, 1997.
    • (1997) J. Comput. Aided Mol. Des. , vol.11 , pp. 293-304
    • Villoutreix, B.O.1    Teleman, O.2    Dahlbäck, B.3
  • 105
    • 0025047460 scopus 로고
    • Delineation and synthesis of the membrane receptor binding domain of sex hormone binding globulin
    • Kahn, M.S., Hryb, D.J., Hashim, G.A., Romas, N.A., Rosner, W. Delineation and synthesis of the membrane receptor binding domain of sex hormone binding globulin. J. Biol. Chem. 265:18362-18365, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 18362-18365
    • Kahn, M.S.1    Hryb, D.J.2    Hashim, G.A.3    Romas, N.A.4    Rosner, W.5
  • 106
    • 0030605024 scopus 로고    scopus 로고
    • Active peptides from the carboxyl-terminal globular domain of laminin a2 and drosophila a chains
    • Nomizu, M., Song, S.-Y., Kuratomi, Y., Tanaka, M., Kim, W.H., Kleinman, H.K., Yamada, Y. Active peptides from the carboxyl-terminal globular domain of laminin a2 and drosophila a chains. FEBS Lett. 396:37-42, 1996.
    • (1996) FEBS Lett. , vol.396 , pp. 37-42
    • Nomizu, M.1    Song, S.-Y.2    Kuratomi, Y.3    Tanaka, M.4    Kim, W.H.5    Kleinman, H.K.6    Yamada, Y.7
  • 107
    • 0030478027 scopus 로고    scopus 로고
    • Familial thrombophilia: Clinical and molecular analysis of Swedish families with inherited resistance to activated protein C and protein S deficiency
    • Zöller, B. Familial thrombophilia: Clinical and molecular analysis of Swedish families with inherited resistance to activated protein C and protein S deficiency. Scand. J. Clin. Lab. Invest. 56:19-46, 1996.
    • (1996) Scand. J. Clin. Lab. Invest. , vol.56 , pp. 19-46
    • Zöller, B.1
  • 108
    • 0027742936 scopus 로고
    • Resistance to activated protein C in nine thrombophilic families: Interference in a protein S functional assay
    • Faioni, E.M., Franchi, F., Asti, D., Sacchi, E., Bernardi, F., Mannucci, P.M. Resistance to activated protein C in nine thrombophilic families: Interference in a protein S functional assay. Thromb. Haemost. 70:1067-1071, 1993.
    • (1993) Thromb. Haemost. , vol.70 , pp. 1067-1071
    • Faioni, E.M.1    Franchi, F.2    Asti, D.3    Sacchi, E.4    Bernardi, F.5    Mannucci, P.M.6
  • 109
    • 0027446268 scopus 로고
    • Familial thrombophilia due to a previously unrecognised mechanism by poor anticoagulant response to activated protein C: Prediction of a cofactor to activated protein C
    • Dahlbäck, B., Carlsson, M., Svensson, P.J. Familial thrombophilia due to a previously unrecognised mechanism by poor anticoagulant response to activated protein C: Prediction of a cofactor to activated protein C. Proc. Natl. Acad. Sci. U.S.A. 90:1004-1008, 1993.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 1004-1008
    • Dahlbäck, B.1    Carlsson, M.2    Svensson, P.J.3
  • 111
    • 0029921211 scopus 로고    scopus 로고
    • Destabilizing effect of proline substitutions in two helical regions of T4 lysozyme: Leucine 66 to proline and leucine 91 to proline
    • Gray, T.M., Arnoys, E.J., Blankespoor, S., Born, T., Jagar, R., Everman, R., Plowman, D., Stair, A., Zhang, D. Destabilizing effect of proline substitutions in two helical regions of T4 lysozyme: Leucine 66 to proline and leucine 91 to proline. Protein Sci. 5:742-751, 1996.
    • (1996) Protein Sci. , vol.5 , pp. 742-751
    • Gray, T.M.1    Arnoys, E.J.2    Blankespoor, S.3    Born, T.4    Jagar, R.5    Everman, R.6    Plowman, D.7    Stair, A.8    Zhang, D.9
  • 112
    • 0023430560 scopus 로고
    • Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding
    • Matthews, B.W., Nicholson, H., Becktel, W.J. Enhanced protein thermostability from site-directed mutations that decrease the entropy of unfolding. Proc. Natl. Acad. Sci. U.S.A. 84:6663-6667, 1987.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 6663-6667
    • Matthews, B.W.1    Nicholson, H.2    Becktel, W.J.3
  • 113
    • 0029549192 scopus 로고
    • Comparative modeling of the three SCR domains of the β chain of C4b-binding and evaluation of potential sites of interaction with protein S
    • Villoutreix, B.O., Fernández. J.A., Teleman, O., Griffin, J.H. Comparative modeling of the three SCR domains of the β chain of C4b-binding and evaluation of potential sites of interaction with protein S. Protein Eng. 8:1253-1258, 1995.
    • (1995) Protein Eng. , vol.8 , pp. 1253-1258
    • Villoutreix, B.O.1    Fernández, J.A.2    Teleman, O.3    Griffin, J.H.4
  • 114
    • 0030055023 scopus 로고    scopus 로고
    • Hydrophobic patches on the surfaces of protein structures
    • Lijnzaad, P., Berendsen, H.J.C., Argos, P. Hydrophobic patches on the surfaces of protein structures. Proteins 25:389-397, 1996.
    • (1996) Proteins , vol.25 , pp. 389-397
    • Lijnzaad, P.1    Berendsen, H.J.C.2    Argos, P.3
  • 115
    • 0026508383 scopus 로고
    • Expression and characterization of recombinant human protein S in heterologous cells-studies of the interaction of amino acid residues Leu 608 to Glu 612 with human C4b-binding protein
    • Chang G.T.G., Ploos van Amstel, H.K., Hessing, M., Reitsma, PH., Bertina, R.M., Bouma, B.N. Expression and characterization of recombinant human protein S in heterologous cells-studies of the interaction of amino acid residues Leu 608 to Glu 612 with human C4b-binding protein. Thromb. Haemost. 67:526-532, 1992.
    • (1992) Thromb. Haemost. , vol.67 , pp. 526-532
    • Chang, G.T.G.1    Ploos Van Amstel, H.K.2    Hessing, M.3    Reitsma, P.H.4    Bertina, R.M.5    Bouma, B.N.6
  • 116
    • 0030947233 scopus 로고    scopus 로고
    • Aregion of vitamin K-dependent protein S that binds to C4b binding protein (C4BP) identified using bacteriophage peptide display libraries
    • Linse, S., Härdig, Y., Schultz, D.A., Dahlbäck, B. Aregion of vitamin K-dependent protein S that binds to C4b binding protein (C4BP) identified using bacteriophage peptide display libraries. J. Biol. Chem. 272:14658-14665, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 14658-14665
    • Linse, S.1    Härdig, Y.2    Schultz, D.A.3    Dahlbäck, B.4
  • 117
    • 0028813821 scopus 로고
    • Identification of candidate residues for interaction of protein S with C4b binding protein and activated protein C
    • Greengard, J.S., Fernández, J.A., Radtke, K.-P., Griffin, J.H. Identification of candidate residues for interaction of protein S with C4b binding protein and activated protein C. Biochem J. 305:397-403, 1995.
    • (1995) Biochem J. , vol.305 , pp. 397-403
    • Greengard, J.S.1    Fernández, J.A.2    Radtke, K.-P.3    Griffin, J.H.4
  • 118
    • 0027431508 scopus 로고
    • Molecular cloning, expression and functional characterization of rabbit anticoagulant vitamin-K dependent protein S
    • He, X., Dahlbäck, B. Molecular cloning, expression and functional characterization of rabbit anticoagulant vitamin-K dependent protein S. Eur. J. Biochem. 217:857-865, 1993.
    • (1993) Eur. J. Biochem. , vol.217 , pp. 857-865
    • He, X.1    Dahlbäck, B.2
  • 120
    • 0028323598 scopus 로고
    • Cloning and sequencing of a cDNa encoding the murine vitamin K-dependent protein S
    • Chu, M.D., Sun, J., Bird, P. Cloning and sequencing of a cDNA encoding the murine vitamin K-dependent protein S. Biochim. Biophys. Acta 1217:325-328, 1994.
    • (1994) Biochim. Biophys. Acta , vol.1217 , pp. 325-328
    • Chu, M.D.1    Sun, J.2    Bird, P.3
  • 121
    • 0028949435 scopus 로고
    • Molecular cloning and functional characterization of rat plasma protein S
    • Tokyo
    • Yasuda, F., Hayashi, T., Tanitame, K., Nishioka, J., Suzuki, K. Molecular cloning and functional characterization of rat plasma protein S. J. Biochem. (Tokyo) 117:374-383, 1995.
    • (1995) J. Biochem. , vol.117 , pp. 374-383
    • Yasuda, F.1    Hayashi, T.2    Tanitame, K.3    Nishioka, J.4    Suzuki, K.5
  • 122
    • 0023273737 scopus 로고
    • A cDNA coding for human sex hormone binding globulin. Homology to vitamin K-dependent protein S
    • Gershagen, S., Fernlund, P., Lundwall, Å. A cDNA coding for human sex hormone binding globulin. Homology to vitamin K-dependent protein S. FEBS Lett. 220:129-135, 1987.
    • (1987) FEBS Lett. , vol.220 , pp. 129-135
    • Gershagen, S.1    Fernlund, P.2    Lundwall, Å.3
  • 124
    • 0023109338 scopus 로고
    • Rat androgen-binding protein: Evidence for identical subunits and amino acid sequence homology with human sex hormone-binding globulin
    • Joseph, D.R., Hall, S.H., French, F.S. Rat androgen-binding protein: Evidence for identical subunits and amino acid sequence homology with human sex hormone-binding globulin. Proc. Natl. Acad. Sci. U.S.A. 84:339-343, 1987.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 339-343
    • Joseph, D.R.1    Hall, S.H.2    French, F.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.