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Volumn 1800, Issue 3, 2010, Pages 398-404

Residual Factor VIII-like cofactor activity of thioredoxin and related oxidoreductases

Author keywords

Blood coagulation; Cofactor; Oxidoreductase; Peptide mimetic; Protein folding; Redox catalyst; Tenase complex

Indexed keywords

BLOOD CLOTTING FACTOR 10; BLOOD CLOTTING FACTOR 8; BLOOD CLOTTING FACTOR 9A; CYSTEINE; DISULFIDE; OXIDOREDUCTASE; PEPTIDE; PROTEIN DISULFIDE ISOMERASE; RIBONUCLEASE A; THIOL; THIOREDOXIN;

EID: 76749169784     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2009.12.006     Document Type: Article
Times cited : (5)

References (59)
  • 1
    • 0024424227 scopus 로고
    • Factor VIII and haemophilia A
    • The Molecular Biology of Coagulation. Tuddenham E.G.D. (Ed)
    • Tuddenham E.G.D. Factor VIII and haemophilia A. In: Tuddenham E.G.D. (Ed). The Molecular Biology of Coagulation. Baillière's Clinical Haematology vol 2/number 4 (1989) 849-877
    • (1989) Baillière's Clinical Haematology , vol.2 -number 4 , pp. 849-877
    • Tuddenham, E.G.D.1
  • 2
    • 0024292694 scopus 로고
    • The molecular basis of blood coagulation
    • Furie B., and Furie B.C. The molecular basis of blood coagulation. Cell 53 (1988) 505-518
    • (1988) Cell , vol.53 , pp. 505-518
    • Furie, B.1    Furie, B.C.2
  • 3
    • 0022454539 scopus 로고
    • Proteolytic processing of human factor. VIII: Correlation of specific cleavages by thrombin, factor Xa, and activated protein C with activation and inactivation of factor VIII coagulant activity
    • Eaton D., Rodriguez H., and Vehar G.A. Proteolytic processing of human factor. VIII: Correlation of specific cleavages by thrombin, factor Xa, and activated protein C with activation and inactivation of factor VIII coagulant activity. Biochemistry 25 (1986) 505-512
    • (1986) Biochemistry , vol.25 , pp. 505-512
    • Eaton, D.1    Rodriguez, H.2    Vehar, G.A.3
  • 4
    • 0028833176 scopus 로고
    • Molecular etiology of factor VIII deficiency in hemophilia A
    • Antonarakis S.E., Kazazian H.H., and Tuddenham E.G. Molecular etiology of factor VIII deficiency in hemophilia A. Hum. Mutat. 5 (1995) 1-22
    • (1995) Hum. Mutat. , vol.5 , pp. 1-22
    • Antonarakis, S.E.1    Kazazian, H.H.2    Tuddenham, E.G.3
  • 5
    • 0025118967 scopus 로고
    • Molecular and cellular aspects of thiol-disulfide exchange
    • Gilbert H.F. Molecular and cellular aspects of thiol-disulfide exchange. Adv. Enzymol. 63 (1990) 69-172
    • (1990) Adv. Enzymol. , vol.63 , pp. 69-172
    • Gilbert, H.F.1
  • 6
    • 0037005934 scopus 로고    scopus 로고
    • Simple shifts in thiol/redox balance that perturb blood coagulation
    • Bayele H.K., Murdock P.J., Perry D.J., and Pasi K.J. Simple shifts in thiol/redox balance that perturb blood coagulation. FEBS Letts. 510 (2002) 67-70
    • (2002) FEBS Letts. , vol.510 , pp. 67-70
    • Bayele, H.K.1    Murdock, P.J.2    Perry, D.J.3    Pasi, K.J.4
  • 7
    • 0028947997 scopus 로고
    • Expression of thioredoxin random peptide libraries on the Escherichia coli cell surface as functional fusions to flagellin: a system designed for exploring protein-protein interactions
    • Lu Z., Murray K.S., Van Cleave V., LaVallie E.R., Stahl M.L., and McCoy J.M. Expression of thioredoxin random peptide libraries on the Escherichia coli cell surface as functional fusions to flagellin: a system designed for exploring protein-protein interactions. Nat. Biotech. 13 (1995) 366-372
    • (1995) Nat. Biotech. , vol.13 , pp. 366-372
    • Lu, Z.1    Murray, K.S.2    Van Cleave, V.3    LaVallie, E.R.4    Stahl, M.L.5    McCoy, J.M.6
  • 9
    • 0022387362 scopus 로고
    • Sequence of protein disulfide isomerase; implications of its relationship to thioredoxin
    • Edman J.C., Ellis L., Blacher R.W., Roth R.A., and Rutter W.J. Sequence of protein disulfide isomerase; implications of its relationship to thioredoxin. Nature 317 (1985) 267-270
    • (1985) Nature , vol.317 , pp. 267-270
    • Edman, J.C.1    Ellis, L.2    Blacher, R.W.3    Roth, R.A.4    Rutter, W.J.5
  • 10
    • 0024337857 scopus 로고
    • Protein disulfide isomerase: multiple roles in the modification of nascent secretory proteins
    • Freedman R.B. Protein disulfide isomerase: multiple roles in the modification of nascent secretory proteins. Cell 57 (1989) 1069-1072
    • (1989) Cell , vol.57 , pp. 1069-1072
    • Freedman, R.B.1
  • 11
    • 0026091179 scopus 로고
    • Identification of a protein required for disulfide bond formation in vivo
    • Bardwell J.C.A., McGovern K., and Beckwith J. Identification of a protein required for disulfide bond formation in vivo. Cell 67 (1991) 581-589
    • (1991) Cell , vol.67 , pp. 581-589
    • Bardwell, J.C.A.1    McGovern, K.2    Beckwith, J.3
  • 12
    • 0025331418 scopus 로고
    • Protein disulfide-isomerase is a substrate for thioredoxin reductase and has thioredoxin-like activity
    • Lundstrom J., and Holmgren A. Protein disulfide-isomerase is a substrate for thioredoxin reductase and has thioredoxin-like activity. J. Biol. Chem. 265 (1990) 9114-9120
    • (1990) J. Biol. Chem. , vol.265 , pp. 9114-9120
    • Lundstrom, J.1    Holmgren, A.2
  • 13
    • 0025972887 scopus 로고
    • Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: pre-steady-state kinetics and the utilization of the oxidizing equivalents of the isomerase
    • Lyles M.M., and Gilbert H.F. Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: pre-steady-state kinetics and the utilization of the oxidizing equivalents of the isomerase. Biochemistry 30 (1991) 619-625
    • (1991) Biochemistry , vol.30 , pp. 619-625
    • Lyles, M.M.1    Gilbert, H.F.2
  • 14
    • 0026793715 scopus 로고
    • A Pro to His mutation in the active site of thioredoxin increases its disulfide-isomerase activity 10-fold. New refolding systems for reduced or randomly oxidized ribonuclease
    • Lundström J., Krause G., and Holmgren A. A Pro to His mutation in the active site of thioredoxin increases its disulfide-isomerase activity 10-fold. New refolding systems for reduced or randomly oxidized ribonuclease. J. Biol. Chem. 267 (1992) 9047-9052
    • (1992) J. Biol. Chem. , vol.267 , pp. 9047-9052
    • Lundström, J.1    Krause, G.2    Holmgren, A.3
  • 15
    • 0031551018 scopus 로고    scopus 로고
    • A protein disulfide-thiol interchange activity of HeLa plasma membranes inhibited by the antitumor sulfonylurea N-(4-methylphenylsulfonyl)-N′-(4-chlorophenyl) urea (LY181984)
    • Morré D.J., Jacobs E., Sweeting M., de Cabo R., and Morré D.M. A protein disulfide-thiol interchange activity of HeLa plasma membranes inhibited by the antitumor sulfonylurea N-(4-methylphenylsulfonyl)-N′-(4-chlorophenyl) urea (LY181984). Biochem. Biophys. Acta 1325 (1997) 117-125
    • (1997) Biochem. Biophys. Acta , vol.1325 , pp. 117-125
    • Morré, D.J.1    Jacobs, E.2    Sweeting, M.3    de Cabo, R.4    Morré, D.M.5
  • 16
    • 1842383220 scopus 로고
    • Thioredoxin-catalyzed refolding of disulfide-containing proteins
    • Pigiet V.P., and Schuster B.J. Thioredoxin-catalyzed refolding of disulfide-containing proteins. Proc. Natl. Acad. Sci. U. S. A. 83 (1986) 7643-7647
    • (1986) Proc. Natl. Acad. Sci. U. S. A. , vol.83 , pp. 7643-7647
    • Pigiet, V.P.1    Schuster, B.J.2
  • 17
    • 0028292985 scopus 로고
    • Protein folding activities of Escherichia coli protein disulfide isomerase
    • Joly J.C., and Swartz J.R. Protein folding activities of Escherichia coli protein disulfide isomerase. Biochemistry 33 (1994) 4231-4236
    • (1994) Biochemistry , vol.33 , pp. 4231-4236
    • Joly, J.C.1    Swartz, J.R.2
  • 18
    • 0025904916 scopus 로고
    • Comparison of the activities of protein disulphide-isomerase and thioredoxin in catalysing disulphide isomerization in a protein substrate
    • Hawkins H.C., Blackburn E.C., and Freedman R.B. Comparison of the activities of protein disulphide-isomerase and thioredoxin in catalysing disulphide isomerization in a protein substrate. Biochem. J. 275 (1991) 349-353
    • (1991) Biochem. J. , vol.275 , pp. 349-353
    • Hawkins, H.C.1    Blackburn, E.C.2    Freedman, R.B.3
  • 19
    • 0027270735 scopus 로고
    • Efficient catalysis of disulfide bond rearrangements by protein disulfide-isomerase
    • Weissman J.S., and Kim P.S. Efficient catalysis of disulfide bond rearrangements by protein disulfide-isomerase. Nature 365 (1993) 185-188
    • (1993) Nature , vol.365 , pp. 185-188
    • Weissman, J.S.1    Kim, P.S.2
  • 20
    • 0029377507 scopus 로고
    • Proposed structure of the A domains of factor VIII by homology modelling
    • Pan Y., DeFay T., Gitschier J., and Cohen F.E. Proposed structure of the A domains of factor VIII by homology modelling. Nat. Struct. Biol. 2 (1995) 740-744
    • (1995) Nat. Struct. Biol. , vol.2 , pp. 740-744
    • Pan, Y.1    DeFay, T.2    Gitschier, J.3    Cohen, F.E.4
  • 21
    • 0032510718 scopus 로고    scopus 로고
    • Effects of copper on the structure and function of Factor VIII subunits: evidence for an auxiliary role for copper ions in cofactor activity
    • Sudhakar K., and Fay P.J. Effects of copper on the structure and function of Factor VIII subunits: evidence for an auxiliary role for copper ions in cofactor activity. Biochemistry 37 (1998) 6874-6882
    • (1998) Biochemistry , vol.37 , pp. 6874-6882
    • Sudhakar, K.1    Fay, P.J.2
  • 22
    • 0025819371 scopus 로고
    • Redox properties and cross-linking of the dithiol/disulphide active sites of mammalian protein disulphide-isomerase
    • Hawkins H.C., de Nardi M., and Freedman R.B. Redox properties and cross-linking of the dithiol/disulphide active sites of mammalian protein disulphide-isomerase. Biochem. J. 275 (1991) 341-348
    • (1991) Biochem. J. , vol.275 , pp. 341-348
    • Hawkins, H.C.1    de Nardi, M.2    Freedman, R.B.3
  • 23
    • 0028953741 scopus 로고
    • Catalytic mechanism of DsbA and its comparison with that of protein disulfide isomerase
    • Darby N.J., and Creighton T.E. Catalytic mechanism of DsbA and its comparison with that of protein disulfide isomerase. Biochemistry 34 (1995) 3576-3587
    • (1995) Biochemistry , vol.34 , pp. 3576-3587
    • Darby, N.J.1    Creighton, T.E.2
  • 24
    • 0026705344 scopus 로고
    • Expression and site-directed mutagenesis of human protein disulfide isomerase in Escherichia coli. This multifunctional polypeptide has two independently acting catalytic sites for the isomerase activity
    • Vuori K., Myllylä R., Pihlajaniemi T., and Kivirikko K.I. Expression and site-directed mutagenesis of human protein disulfide isomerase in Escherichia coli. This multifunctional polypeptide has two independently acting catalytic sites for the isomerase activity. J. Biol. Chem. 267 (1992) 7211-7214
    • (1992) J. Biol. Chem. , vol.267 , pp. 7211-7214
    • Vuori, K.1    Myllylä, R.2    Pihlajaniemi, T.3    Kivirikko, K.I.4
  • 25
    • 0026738643 scopus 로고
    • The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase
    • Tachibana C., and Stevens T.H. The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase. Mol. Cell. Biol. 12 (1992) 4601-4611
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 4601-4611
    • Tachibana, C.1    Stevens, T.H.2
  • 26
    • 0028956318 scopus 로고
    • Efficient catalysis of disulfide formation during protein folding with a single active-site cysteine
    • Wunderlich M., Otto A., Maskos K., Mucke M., Seckler R., and Glockshuber R. Efficient catalysis of disulfide formation during protein folding with a single active-site cysteine. J. Mol. Biol. 247 (1995) 28-33
    • (1995) J. Mol. Biol. , vol.247 , pp. 28-33
    • Wunderlich, M.1    Otto, A.2    Maskos, K.3    Mucke, M.4    Seckler, R.5    Glockshuber, R.6
  • 27
    • 0030061006 scopus 로고    scopus 로고
    • Catalysis of oxidative protein folding by mutants of protein disulfide isomerase with a single active-site cysteine
    • Walker K.W., Lyles M.M., and Gilbert H.F. Catalysis of oxidative protein folding by mutants of protein disulfide isomerase with a single active-site cysteine. Biochemistry 35 (1996) 1972-1980
    • (1996) Biochemistry , vol.35 , pp. 1972-1980
    • Walker, K.W.1    Lyles, M.M.2    Gilbert, H.F.3
  • 28
    • 0028885790 scopus 로고
    • The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds
    • Laboissiere M.C., Sturley S.L., and Raines R.T. The essential function of protein-disulfide isomerase is to unscramble non-native disulfide bonds. J. Biol. Chem. 270 (1995) 28006-28009
    • (1995) J. Biol. Chem. , vol.270 , pp. 28006-28009
    • Laboissiere, M.C.1    Sturley, S.L.2    Raines, R.T.3
  • 29
    • 0029934516 scopus 로고
    • The CXXC motif: imperatives for the formation of native disulfide bonds in the cell
    • Chivers P.T., Laboissiere M.C., and Raines R.T. The CXXC motif: imperatives for the formation of native disulfide bonds in the cell. EMBO J. 15 (1995) 2659-2667
    • (1995) EMBO J. , vol.15 , pp. 2659-2667
    • Chivers, P.T.1    Laboissiere, M.C.2    Raines, R.T.3
  • 30
    • 0030783138 scopus 로고    scopus 로고
    • Identification and functional requirement of Cu(I) and its ligands within coagulation Factor VIII
    • Tagliavacca L., Moon N., Dunham W.R., and Kaufman R.J. Identification and functional requirement of Cu(I) and its ligands within coagulation Factor VIII. J. Biol. Chem. 272 (1997) 27428-27434
    • (1997) J. Biol. Chem. , vol.272 , pp. 27428-27434
    • Tagliavacca, L.1    Moon, N.2    Dunham, W.R.3    Kaufman, R.J.4
  • 31
    • 0027183546 scopus 로고
    • Transition metals in control of gene expression
    • O'Halloran T.V. Transition metals in control of gene expression. Science 261 (1993) 715-725
    • (1993) Science , vol.261 , pp. 715-725
    • O'Halloran, T.V.1
  • 32
    • 0035986705 scopus 로고    scopus 로고
    • Redox-active cyclic bis(cysteinyl)peptides as catalysts for in vitro oxidative protein folding
    • Cabrele C., Fiori S., Pegoraro S., and Moroder L. Redox-active cyclic bis(cysteinyl)peptides as catalysts for in vitro oxidative protein folding. Chem. Biol. 9 (2002) 731-740
    • (2002) Chem. Biol. , vol.9 , pp. 731-740
    • Cabrele, C.1    Fiori, S.2    Pegoraro, S.3    Moroder, L.4
  • 33
    • 0027529952 scopus 로고
    • Evolution of protein complexity: the blue copper-containing oxidases and related proteins
    • Rydén L.G., and Hunt L.T. Evolution of protein complexity: the blue copper-containing oxidases and related proteins. J. Mol. Evol. 36 (1993) 41-46
    • (1993) J. Mol. Evol. , vol.36 , pp. 41-46
    • Rydén, L.G.1    Hunt, L.T.2
  • 34
    • 0034711439 scopus 로고    scopus 로고
    • Biochemical basis of oxidative protein folding in the endoplasmic reticulum
    • Tu B.P., Ho-Schleyer S.C., Travers K.J., and Weissman J.S. Biochemical basis of oxidative protein folding in the endoplasmic reticulum. Science 290 (2000) 1571-1574
    • (2000) Science , vol.290 , pp. 1571-1574
    • Tu, B.P.1    Ho-Schleyer, S.C.2    Travers, K.J.3    Weissman, J.S.4
  • 35
    • 0031609760 scopus 로고    scopus 로고
    • The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum
    • Frand A.R., and Kaiser C.A. The ERO1 gene of yeast is required for oxidation of protein dithiols in the endoplasmic reticulum. Mol. Cell 1 (1998) 161-170
    • (1998) Mol. Cell , vol.1 , pp. 161-170
    • Frand, A.R.1    Kaiser, C.A.2
  • 36
    • 0033163758 scopus 로고    scopus 로고
    • Competition between glutathione and protein thiols for disulphide-bond formation
    • Cuozzo J.W., and Kaiser C.A. Competition between glutathione and protein thiols for disulphide-bond formation. Nat. Cell. Biol. 1 (1999) 130-135
    • (1999) Nat. Cell. Biol. , vol.1 , pp. 130-135
    • Cuozzo, J.W.1    Kaiser, C.A.2
  • 37
    • 0026731788 scopus 로고
    • Protein disulfide isomerase. A multifunctional protein resident in the lumen of the endoplasmic reticulum
    • Noiva R., and Lennarz W.J. Protein disulfide isomerase. A multifunctional protein resident in the lumen of the endoplasmic reticulum. J. Biol. Chem. 267 (1992) 3553-3556
    • (1992) J. Biol. Chem. , vol.267 , pp. 3553-3556
    • Noiva, R.1    Lennarz, W.J.2
  • 38
    • 0025077481 scopus 로고
    • Redox regulation of Fos and Jun DNA-binding activity in vitro
    • Abate C., Patel L., Rauscher III F.J., and Curran T. Redox regulation of Fos and Jun DNA-binding activity in vitro. Science 249 (1990) 1157-1161
    • (1990) Science , vol.249 , pp. 1157-1161
    • Abate, C.1    Patel, L.2    Rauscher III, F.J.3    Curran, T.4
  • 39
    • 0025214474 scopus 로고
    • Transcriptional regulator of oxidative stress-inducible genes: direct activation by oxidation
    • Storz G., Tartaglia L.A., and Ames B.N. Transcriptional regulator of oxidative stress-inducible genes: direct activation by oxidation. Science 248 (1990) 189-194
    • (1990) Science , vol.248 , pp. 189-194
    • Storz, G.1    Tartaglia, L.A.2    Ames, B.N.3
  • 40
    • 0029984062 scopus 로고    scopus 로고
    • Antioxidant and redox regulation of gene transcription
    • Sen C.K., and Packer L. Antioxidant and redox regulation of gene transcription. FASEB J. 10 (1996) 709-720
    • (1996) FASEB J. , vol.10 , pp. 709-720
    • Sen, C.K.1    Packer, L.2
  • 41
    • 0032584166 scopus 로고    scopus 로고
    • Thiolate ligands in metallothionein confer redox activity on zinc clusters
    • Maret W., and Vallee B.L. Thiolate ligands in metallothionein confer redox activity on zinc clusters. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 3478-3482
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 3478-3482
    • Maret, W.1    Vallee, B.L.2
  • 42
    • 0031452439 scopus 로고    scopus 로고
    • Protein disulfide isomerase as a regulator of chloroplast translational activation
    • Kim J., and Mayfield S.P. Protein disulfide isomerase as a regulator of chloroplast translational activation. Science 278 (1997) 1954-1957
    • (1997) Science , vol.278 , pp. 1954-1957
    • Kim, J.1    Mayfield, S.P.2
  • 43
    • 0029144477 scopus 로고
    • Localization of protein disulfide isomerase to the external surface of the platelet plasma membrane
    • Essex D.W., Chen K., and Swiatkowska M. Localization of protein disulfide isomerase to the external surface of the platelet plasma membrane. Blood 86 (1995) 2168-2173
    • (1995) Blood , vol.86 , pp. 2168-2173
    • Essex, D.W.1    Chen, K.2    Swiatkowska, M.3
  • 44
    • 0035918587 scopus 로고    scopus 로고
    • Protein disulfide isomerase and sulfhydryl-dependent pathways in platelet activation
    • Essex D.W., Li M., Miller A., and Feinman R.D. Protein disulfide isomerase and sulfhydryl-dependent pathways in platelet activation. Biochemistry 40 (2001) 6070-6075
    • (2001) Biochemistry , vol.40 , pp. 6070-6075
    • Essex, D.W.1    Li, M.2    Miller, A.3    Feinman, R.D.4
  • 45
    • 0029025521 scopus 로고
    • Characterization of protein disulphide isomerase released from activated platelets
    • Chen K., Detwiler T.C., and Essex D.W. Characterization of protein disulphide isomerase released from activated platelets. Brit. J. Haematol. 90 (1995) 425-431
    • (1995) Brit. J. Haematol. , vol.90 , pp. 425-431
    • Chen, K.1    Detwiler, T.C.2    Essex, D.W.3
  • 46
    • 0032078806 scopus 로고    scopus 로고
    • Measurements of plasma glutaredoxin and thioredoxin in healthy volunteers and during open-heart surgery
    • Nakamura H., Vaage J., Valen G., Padilla C.A., Bjornstedt M., and Holmgren A. Measurements of plasma glutaredoxin and thioredoxin in healthy volunteers and during open-heart surgery. Free Radic. Biol. Med. 24 (1998) 1176-1186
    • (1998) Free Radic. Biol. Med. , vol.24 , pp. 1176-1186
    • Nakamura, H.1    Vaage, J.2    Valen, G.3    Padilla, C.A.4    Bjornstedt, M.5    Holmgren, A.6
  • 47
    • 0029013943 scopus 로고
    • Platelet-derived microvesicles and activated platelets express Factor Xa activity
    • Holme P.A., Brosstad F., and Solum N.O. Platelet-derived microvesicles and activated platelets express Factor Xa activity. Blood Coagul. Fibrinolysis 6 (1995) 302-310
    • (1995) Blood Coagul. Fibrinolysis , vol.6 , pp. 302-310
    • Holme, P.A.1    Brosstad, F.2    Solum, N.O.3
  • 48
    • 0032985071 scopus 로고    scopus 로고
    • Protein disulphide isomerase mediates platelet aggregation and secretion
    • Essex D.W., and Li M. Protein disulphide isomerase mediates platelet aggregation and secretion. Brit. J. Haematol. 104 (1998) 448-454
    • (1998) Brit. J. Haematol. , vol.104 , pp. 448-454
    • Essex, D.W.1    Li, M.2
  • 50
    • 40549084318 scopus 로고    scopus 로고
    • A critical role for extracellular protein disulfide isomerase during thrombus formation in mice
    • Cho J., Furie B.C., Coughlin S.R., and Furie B. A critical role for extracellular protein disulfide isomerase during thrombus formation in mice. J. Clin. Invest. 118 (2008) 1123-1131
    • (2008) J. Clin. Invest. , vol.118 , pp. 1123-1131
    • Cho, J.1    Furie, B.C.2    Coughlin, S.R.3    Furie, B.4
  • 51
    • 48449100433 scopus 로고    scopus 로고
    • Protein disulfide isomerase as a trigger for tissue factor-dependent fibrin generation
    • Manukyan D., von Bruehl M.L., Massberg S., and Engelmann B. Protein disulfide isomerase as a trigger for tissue factor-dependent fibrin generation. Thromb. Res. 122 Suppl 1 (2008) S19-S22
    • (2008) Thromb. Res. , vol.122 , Issue.SUPPL. 1
    • Manukyan, D.1    von Bruehl, M.L.2    Massberg, S.3    Engelmann, B.4
  • 54
    • 0015954388 scopus 로고
    • Enzymatic reduction of disulfide bonds in fibrinogen by the thioredoxin system. I. Identification of reduced bonds and studies on reoxidation process
    • Blombäck B., Blombäck M., Finkbeiner W., Holmgren A., Kowalska-Loth B., and Olovson G. Enzymatic reduction of disulfide bonds in fibrinogen by the thioredoxin system. I. Identification of reduced bonds and studies on reoxidation process. Thromb. Res. 4 (1974) 55-75
    • (1974) Thromb. Res. , vol.4 , pp. 55-75
    • Blombäck, B.1    Blombäck, M.2    Finkbeiner, W.3    Holmgren, A.4    Kowalska-Loth, B.5    Olovson, G.6
  • 55
    • 0025109879 scopus 로고
    • Free thiols of platelet thrombospondin. Evidence for disulfide isomerization
    • Speziale M.V., and Detwiler T.C. Free thiols of platelet thrombospondin. Evidence for disulfide isomerization. J. Biol. Chem. 265 (1990) 17859-17867
    • (1990) J. Biol. Chem. , vol.265 , pp. 17859-17867
    • Speziale, M.V.1    Detwiler, T.C.2
  • 56
    • 0028239173 scopus 로고
    • Identification of a binding site for blood coagulation Factor IXa on the light chain of human factor VIII
    • Lenting P.J., Donath M.-J.S.H., van Mourik J.A., and Mertens K. Identification of a binding site for blood coagulation Factor IXa on the light chain of human factor VIII. J Biol Chem. 269 (1994) 7150-7155
    • (1994) J Biol Chem. , vol.269 , pp. 7150-7155
    • Lenting, P.J.1    Donath, M.-J.S.H.2    van Mourik, J.A.3    Mertens, K.4
  • 57
    • 0031027575 scopus 로고    scopus 로고
    • Localization of a Factor X interactive site in the A1 subunit of Factor VIIIa
    • Lapan K.A., and Fay P.J. Localization of a Factor X interactive site in the A1 subunit of Factor VIIIa. J. Biol. Chem. 272 (1997) 2082-2088
    • (1997) J. Biol. Chem. , vol.272 , pp. 2082-2088
    • Lapan, K.A.1    Fay, P.J.2
  • 58
    • 0030903424 scopus 로고    scopus 로고
    • A molecular model for the triplicated A domains of human Factor VIII based on the crystal structure of human ceruloplasmin
    • Pemberton S., Lindley P., Zaitsev V., Card G., Tuddenham E.G.D., and Kemball-Cook G. A molecular model for the triplicated A domains of human Factor VIII based on the crystal structure of human ceruloplasmin. Blood 89 (1997) 2413-2421
    • (1997) Blood , vol.89 , pp. 2413-2421
    • Pemberton, S.1    Lindley, P.2    Zaitsev, V.3    Card, G.4    Tuddenham, E.G.D.5    Kemball-Cook, G.6
  • 59
    • 0031876273 scopus 로고    scopus 로고
    • Can we improve on nature? "Super molecules" of factor VIII
    • Kaufman R.J., and Pipe S.W. Can we improve on nature? "Super molecules" of factor VIII. Haemophilia 4 (1998) 370-379
    • (1998) Haemophilia , vol.4 , pp. 370-379
    • Kaufman, R.J.1    Pipe, S.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.