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Volumn 10, Issue , 2010, Pages

Structural investigation of zymogenic and activated forms of human blood coagulation factor VIII: A computational molecular dynamics study

Author keywords

[No Author keywords available]

Indexed keywords

ALANINE; ARGININE; ASPARTIC ACID; BINDING PROTEIN; BLOOD CLOTTING FACTOR 10A; BLOOD CLOTTING FACTOR 8; BLOOD CLOTTING FACTOR 8A; BLOOD CLOTTING FACTOR 9A; CALCIUM ION; COPPER ION; ENZYME PRECURSOR; PEPTIDE; SERINE; SOLVENT; THROMBIN; TYROSINE; METAL;

EID: 77949498628     PISSN: None     EISSN: 14726807     Source Type: Journal    
DOI: 10.1186/1472-6807-10-7     Document Type: Article
Times cited : (17)

References (74)
  • 2
    • 0036207024 scopus 로고    scopus 로고
    • Haemophilia A: Effects of inhibitory antibodies on factor VIII functional interactions and approaches to prevent their action
    • 10.1046/j.1365-2516.2002.00579.x. 11886458
    • Haemophilia A: effects of inhibitory antibodies on factor VIII functional interactions and approaches to prevent their action. EL Saenko NM Ananyeva DV Kouiavskaia AV Khrenov JA Anderson M Shima, et al. Haemophilia 2002 8 1 11 10.1046/j.1365-2516.2002.00579.x 11886458
    • (2002) Haemophilia , vol.8 , pp. 1-11
    • Saenko, E.L.1    Ananyeva, N.M.2    Kouiavskaia, D.V.3    Khrenov, A.V.4    Anderson, J.A.5    Shima, M.6
  • 3
    • 0025311157 scopus 로고
    • Surface-dependent reactions of the vitamin K-dependent enzyme complexes
    • 2194585
    • Surface-dependent reactions of the vitamin K-dependent enzyme complexes. KG Mann ME Nesheim WR Church P Haley S Krishnaswamy, Blood 1990 76 1 16 2194585
    • (1990) Blood , vol.76 , pp. 1-16
    • Mann, K.G.1    Nesheim, M.E.2    Church, W.R.3    Haley, P.4    Krishnaswamy, S.5
  • 4
    • 0019831499 scopus 로고
    • The role of phospholipid and factor VIIIa in the activation of bovine factor X
    • 6782101
    • The role of phospholipid and factor VIIIa in the activation of bovine factor X. G van Dieijen G Tans J Rosing HC Hemker, J Biol Chem 1981 256 3433 3442 6782101
    • (1981) J Biol Chem , vol.256 , pp. 3433-3442
    • Van Dieijen, G.1    Tans, G.2    Rosing, J.3    Hemker, H.C.4
  • 5
    • 0025923490 scopus 로고
    • Human factor VIIIa subunit structure. Reconstruction of factor VIIIa from the isolated A1/A3-C1-C2 dimer and A2 subunit
    • 1902833
    • Human factor VIIIa subunit structure. Reconstruction of factor VIIIa from the isolated A1/A3-C1-C2 dimer and A2 subunit. PJ Fay PJ Haidaris TM Smudzin, J Biol Chem 1991 266 8957 8962 1902833
    • (1991) J Biol Chem , vol.266 , pp. 8957-8962
    • Fay, P.J.1    Haidaris, P.J.2    Smudzin, T.M.3
  • 6
    • 45549088263 scopus 로고    scopus 로고
    • Identification of residues contributing to A2 domain-dependent structural stability in factor VIII and factor VIIIa
    • 10.1074/jbc.M710252200. 18299331
    • Identification of residues contributing to A2 domain-dependent structural stability in factor VIII and factor VIIIa. H Wakabayashi PJ Fay, J Biol Chem 2008 283 11645 11651 10.1074/jbc.M710252200 18299331
    • (2008) J Biol Chem , vol.283 , pp. 11645-11651
    • Wakabayashi, H.1    Fay, P.J.2
  • 7
    • 0032983331 scopus 로고    scopus 로고
    • The A1 and A2 subunits of factor VIIIa synergistically stimulate factor IXa catalytic activity
    • 10.1074/jbc.274.22.15401. 10336428
    • The A1 and A2 subunits of factor VIIIa synergistically stimulate factor IXa catalytic activity. PJ Fay K Koshibu M Mastri, J Biol Chem 1999 274 15401 15406 10.1074/jbc.274.22.15401 10336428
    • (1999) J Biol Chem , vol.274 , pp. 15401-15406
    • Fay, P.J.1    Koshibu, K.2    Mastri, M.3
  • 8
    • 0032563086 scopus 로고    scopus 로고
    • The A2 subunit of factor VIIIa modulates the active site of factor IXa
    • 10.1074/jbc.273.30.19049. 9668086
    • The A2 subunit of factor VIIIa modulates the active site of factor IXa. PJ Fay K Koshibu, J Biol Chem 1998 273 19049 19054 10.1074/jbc.273.30.19049 9668086
    • (1998) J Biol Chem , vol.273 , pp. 19049-19054
    • Fay, P.J.1    Koshibu, K.2
  • 9
    • 34247857684 scopus 로고    scopus 로고
    • A3 domain residue Glu1829 contributes to A2 subunit retention in factor VIIIa
    • 10.1111/j.1538-7836.2007.02458.x. 17371488
    • A3 domain residue Glu1829 contributes to A2 subunit retention in factor VIIIa. H Wakabayashi Q Zhou F Varfaj PJ Fay, J Thromb Haemost 2007 5 996 1001 10.1111/j.1538-7836.2007.02458.x 17371488
    • (2007) J Thromb Haemost , vol.5 , pp. 996-1001
    • Wakabayashi, H.1    Zhou, Q.2    Varfaj, F.3    Fay, P.J.4
  • 10
    • 49749148398 scopus 로고    scopus 로고
    • Acidic residues C-terminal to the A2 domain facilitate thrombin-catalyzed activation of factor VIII
    • 10.1021/bi8007824. 18642885
    • Acidic residues C-terminal to the A2 domain facilitate thrombin-catalyzed activation of factor VIII. JL Newell PJ Fay, Biochemistry 2008 47 8786 8795 10.1021/bi8007824 18642885
    • (2008) Biochemistry , vol.47 , pp. 8786-8795
    • Newell, J.L.1    Fay, P.J.2
  • 11
    • 0037449806 scopus 로고    scopus 로고
    • Altered interactions between the A1 and A2 subunits of factor VIIIa following cleavage of A1 subunit by factor Xa
    • 10.1074/jbc.M209811200. 12426309
    • Altered interactions between the A1 and A2 subunits of factor VIIIa following cleavage of A1 subunit by factor Xa. K Nogami H Wakabayashi K Schmidt PJ Fay, J Biol Chem 2003 278 1634 1641 10.1074/jbc.M209811200 12426309
    • (2003) J Biol Chem , vol.278 , pp. 1634-1641
    • Nogami, K.1    Wakabayashi, H.2    Schmidt, K.3    Fay, P.J.4
  • 12
    • 2142835518 scopus 로고    scopus 로고
    • Clustered basic residues within segment 484-510 of the factor VIIIa A2 subunit contribute to the catalytic efficiency for factor Xa generation
    • 10.1111/j.1538-7933.2004.00625.x. 15009463
    • Clustered basic residues within segment 484-510 of the factor VIIIa A2 subunit contribute to the catalytic efficiency for factor Xa generation. PV Jenkins JL Dill Q Zhou PJ Fay, J Thromb Haemost 2004 2 452 458 10.1111/j.1538-7933.2004.00625.x 15009463
    • (2004) J Thromb Haemost , vol.2 , pp. 452-458
    • Jenkins, P.V.1    Dill, J.L.2    Zhou, Q.3    Fay, P.J.4
  • 13
    • 38949168866 scopus 로고    scopus 로고
    • The tertiary structure and domain organization of coagulation factor VIII
    • 10.1182/blood-2007-08-109918. 17965321
    • The tertiary structure and domain organization of coagulation factor VIII. BW Shen PC Spiegel CH Chang JW Huh JS Lee J Kim, et al. Blood 2008 111 1240 1247 10.1182/blood-2007-08-109918 17965321
    • (2008) Blood , vol.111 , pp. 1240-1247
    • Shen, B.W.1    Spiegel, P.C.2    Chang, C.H.3    Huh, J.W.4    Lee, J.S.5    Kim, J.6
  • 14
    • 41449117525 scopus 로고    scopus 로고
    • Crystal structure of human factor VIII: Implications for the formation of the factor IXa-factor VIIIa complex
    • 10.1016/j.str.2008.03.001. 18400180
    • Crystal structure of human factor VIII: implications for the formation of the factor IXa-factor VIIIa complex. JC Ngo M Huang DA Roth BC Furie B Furie, Structure 2008 16 597 606 10.1016/j.str.2008.03.001 18400180
    • (2008) Structure , vol.16 , pp. 597-606
    • Ngo, J.C.1    Huang, M.2    Roth, D.A.3    Furie, B.C.4    Furie, B.5
  • 15
    • 34547566446 scopus 로고    scopus 로고
    • ProSA-web: Interactive web service for the recognition of errors in three-dimensional structures of proteins
    • 10.1093/nar/gkm290. 17517781
    • ProSA-web: interactive web service for the recognition of errors in three-dimensional structures of proteins. M Wiederstein MJ Sippl, Nucleic Acids Res 2007 35 407 W410 10.1093/nar/gkm290 17517781
    • (2007) Nucleic Acids Res , vol.35
    • Wiederstein, M.1    Sippl, M.J.2
  • 16
    • 0035964179 scopus 로고    scopus 로고
    • Metal ion-independent association of factor VIII subunits and the roles of calcium and copper ions for cofactor activity and inter-subunit affinity
    • 10.1021/bi010353q. 11513607
    • Metal ion-independent association of factor VIII subunits and the roles of calcium and copper ions for cofactor activity and inter-subunit affinity. H Wakabayashi ME Koszelak M Mastri PJ Fay, Biochemistry 2001 40 10293 10300 10.1021/bi010353q 11513607
    • (2001) Biochemistry , vol.40 , pp. 10293-10300
    • Wakabayashi, H.1    Koszelak, M.E.2    Mastri, M.3    Fay, P.J.4
  • 17
    • 0037007964 scopus 로고    scopus 로고
    • Ca(2+) binding to both the heavy and light chains of factor VIII is required for cofactor activity
    • 10.1021/bi025589o. 12081499
    • Ca(2+) binding to both the heavy and light chains of factor VIII is required for cofactor activity. H Wakabayashi KM Schmidt PJ Fay, Biochemistry 2002 41 8485 8492 10.1021/bi025589o 12081499
    • (2002) Biochemistry , vol.41 , pp. 8485-8492
    • Wakabayashi, H.1    Schmidt, K.M.2    Fay, P.J.3
  • 18
    • 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
    • 10.1021/bi980084c. 9578574
    • Effects of copper on the structure and function of factor VIII subunits: evidence for an auxiliary role for copper ions in cofactor activity. K Sudhakar PJ Fay, Biochemistry 1998 37 6874 6882 10.1021/bi980084c 9578574
    • (1998) Biochemistry , vol.37 , pp. 6874-6882
    • Sudhakar, K.1    Fay, P.J.2
  • 19
    • 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
    • 10.1021/bi980084c. 9578574
    • Effects of copper on the structure and function of factor VIII subunits: evidence for an auxiliary role for copper ions in cofactor activity. K Sudhakar PJ Fay, Biochemistry 1998 37 6874 6882 10.1021/bi980084c 9578574
    • (1998) Biochemistry , vol.37 , pp. 6874-6882
    • Sudhakar, K.1    Fay, P.J.2
  • 20
    • 0037007964 scopus 로고    scopus 로고
    • Ca(2+) binding to both the heavy and light chains of factor VIII is required for cofactor activity
    • 10.1021/bi025589o. 12081499
    • Ca(2+) binding to both the heavy and light chains of factor VIII is required for cofactor activity. H Wakabayashi KM Schmidt PJ Fay, Biochemistry 2002 41 8485 8492 10.1021/bi025589o 12081499
    • (2002) Biochemistry , vol.41 , pp. 8485-8492
    • Wakabayashi, H.1    Schmidt, K.M.2    Fay, P.J.3
  • 21
    • 0037007964 scopus 로고    scopus 로고
    • Ca(2+) binding to both the heavy and light chains of factor VIII is required for cofactor activity
    • 10.1021/bi025589o. 12081499
    • Ca(2+) binding to both the heavy and light chains of factor VIII is required for cofactor activity. H Wakabayashi KM Schmidt PJ Fay, Biochemistry 2002 41 8485 8492 10.1021/bi025589o 12081499
    • (2002) Biochemistry , vol.41 , pp. 8485-8492
    • Wakabayashi, H.1    Schmidt, K.M.2    Fay, P.J.3
  • 22
    • 1842581996 scopus 로고    scopus 로고
    • Residues 110-126 in the A1 domain of factor VIII contain a Ca2+ binding site required for cofactor activity
    • 10.1074/jbc.M311042200. 14722121
    • Residues 110-126 in the A1 domain of factor VIII contain a Ca2+ binding site required for cofactor activity. H Wakabayashi J Freas Q Zhou PJ Fay, J Biol Chem 2004 279 12677 12684 10.1074/jbc.M311042200 14722121
    • (2004) J Biol Chem , vol.279 , pp. 12677-12684
    • Wakabayashi, H.1    Freas, J.2    Zhou, Q.3    Fay, P.J.4
  • 23
    • 0036192859 scopus 로고    scopus 로고
    • Structure and dynamics of zymogen human blood coagulation factor X
    • 10.1016/S0006-3495(02)75476-3. 11867437
    • Structure and dynamics of zymogen human blood coagulation factor X. D Venkateswarlu L Perera T Darden LG Pedersen, Biophys J 2002 82 1190 1206 10.1016/S0006-3495(02)75476-3 11867437
    • (2002) Biophys J , vol.82 , pp. 1190-1206
    • Venkateswarlu, D.1    Perera, L.2    Darden, T.3    Pedersen, L.G.4
  • 24
    • 1442285238 scopus 로고    scopus 로고
    • An all-atom solution-equilibrated model for human extrinsic blood coagulation complex (sTF-VIIa-Xa): A protein-protein docking and molecular dynamics refinement study
    • 10.1111/j.1538-7836.2003.00421.x. 14750502
    • An all-atom solution-equilibrated model for human extrinsic blood coagulation complex (sTF-VIIa-Xa): a protein-protein docking and molecular dynamics refinement study. D Venkateswarlu RE Duke L Perera TA Darden LG Pedersen, J Thromb Haemost 2003 1 2577 2588 10.1111/j.1538-7836.2003.00421.x 14750502
    • (2003) J Thromb Haemost , vol.1 , pp. 2577-2588
    • Venkateswarlu, D.1    Duke, R.E.2    Perera, L.3    Darden, T.A.4    Pedersen, L.G.5
  • 25
    • 23044498602 scopus 로고    scopus 로고
    • A Glu113Ala mutation within a factor VIII Ca2+-binding site enhances cofactor interactions in factor Xase
    • 10.1021/bi050638t. 16042406
    • A Glu113Ala mutation within a factor VIII Ca2+-binding site enhances cofactor interactions in factor Xase. H Wakabayashi YC Su SS Ahmad PN Walsh PJ Fay, Biochemistry 2005 44 10298 10304 10.1021/bi050638t 16042406
    • (2005) Biochemistry , vol.44 , pp. 10298-10304
    • Wakabayashi, H.1    Su, Y.C.2    Ahmad, S.S.3    Walsh, P.N.4    Fay, P.J.5
  • 26
    • 1842581996 scopus 로고    scopus 로고
    • Residues 110-126 in the A1 domain of factor VIII contain a Ca2+ binding site required for cofactor activity
    • 10.1074/jbc.M311042200. 14722121
    • Residues 110-126 in the A1 domain of factor VIII contain a Ca2+ binding site required for cofactor activity. H Wakabayashi J Freas Q Zhou PJ Fay, J Biol Chem 2004 279 12677 12684 10.1074/jbc.M311042200 14722121
    • (2004) J Biol Chem , vol.279 , pp. 12677-12684
    • Wakabayashi, H.1    Freas, J.2    Zhou, Q.3    Fay, P.J.4
  • 27
    • 33846678076 scopus 로고    scopus 로고
    • Ceruloplasmin revisited: Structural and functional roles of various metal cation-binding sites
    • 10.1107/S090744490604947X. 17242517
    • Ceruloplasmin revisited: structural and functional roles of various metal cation-binding sites. I Bento C Peixoto VN Zaitsev PF Lindley, Acta Crystallogr D Biol Crystallogr 2007 63 240 248 10.1107/S090744490604947X 17242517
    • (2007) Acta Crystallogr D Biol Crystallogr , vol.63 , pp. 240-248
    • Bento, I.1    Peixoto, C.2    Zaitsev, V.N.3    Lindley, P.F.4
  • 28
    • 2942669901 scopus 로고    scopus 로고
    • The crystal structure of activated protein C-inactivated bovine factor Va: Implications for cofactor function
    • 10.1073/pnas.0403072101. 15184653
    • The crystal structure of activated protein C-inactivated bovine factor Va: Implications for cofactor function. TE Adams MF Hockin KG Mann SJ Everse, Proc Natl Acad Sci USA 2004 101 8918 8923 10.1073/pnas.0403072101 15184653
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 8918-8923
    • Adams, T.E.1    Hockin, M.F.2    Mann, K.G.3    Everse, S.J.4
  • 30
    • 0035964179 scopus 로고    scopus 로고
    • Metal ion-independent association of factor VIII subunits and the roles of calcium and copper ions for cofactor activity and inter-subunit affinity
    • 10.1021/bi010353q. 11513607
    • Metal ion-independent association of factor VIII subunits and the roles of calcium and copper ions for cofactor activity and inter-subunit affinity. H Wakabayashi ME Koszelak M Mastri PJ Fay, Biochemistry 2001 40 10293 10300 10.1021/bi010353q 11513607
    • (2001) Biochemistry , vol.40 , pp. 10293-10300
    • Wakabayashi, H.1    Koszelak, M.E.2    Mastri, M.3    Fay, P.J.4
  • 31
    • 0035964179 scopus 로고    scopus 로고
    • Metal ion-independent association of factor VIII subunits and the roles of calcium and copper ions for cofactor activity and inter-subunit affinity
    • 10.1021/bi010353q. 11513607
    • Metal ion-independent association of factor VIII subunits and the roles of calcium and copper ions for cofactor activity and inter-subunit affinity. H Wakabayashi ME Koszelak M Mastri PJ Fay, Biochemistry 2001 40 10293 10300 10.1021/bi010353q 11513607
    • (2001) Biochemistry , vol.40 , pp. 10293-10300
    • Wakabayashi, H.1    Koszelak, M.E.2    Mastri, M.3    Fay, P.J.4
  • 32
    • 0027381910 scopus 로고
    • Histidines 138 and 143 are copper binding ligands in Chromobacterium violaceum phenylalanine hydroxylase
    • 8304204
    • Histidines 138 and 143 are copper binding ligands in Chromobacterium violaceum phenylalanine hydroxylase. S Balasubramanian RT Carr CJ Bender J Peisach SJ Benkovic, Adv Exp Med Biol 1993 338 67 70 8304204
    • (1993) Adv Exp Med Biol , vol.338 , pp. 67-70
    • Balasubramanian, S.1    Carr, R.T.2    Bender, C.J.3    Peisach, J.4    Benkovic, S.J.5
  • 33
    • 35948936850 scopus 로고    scopus 로고
    • Three histidine residues of amyloid-beta peptide control the redox activity of copper and iron
    • 10.1021/bi701079z. 17929832
    • Three histidine residues of amyloid-beta peptide control the redox activity of copper and iron. M Nakamura N Shishido A Nunomura MA Smith G Perry Y Hayashi, et al. Biochemistry 2007 46 12737 12743 10.1021/bi701079z 17929832
    • (2007) Biochemistry , vol.46 , pp. 12737-12743
    • Nakamura, M.1    Shishido, N.2    Nunomura, A.3    Smith, M.A.4    Perry, G.5    Hayashi, Y.6
  • 34
    • 52349102890 scopus 로고    scopus 로고
    • CuII binding sites located at His-96 and His-111 of the human prion protein: Thermodynamic and spectroscopic studies on model peptides
    • 10.1039/b806192k. 18813375
    • CuII binding sites located at His-96 and His-111 of the human prion protein: thermodynamic and spectroscopic studies on model peptides. E Gralka D Valensin E Porciatti C Gajda E Gaggelli G Valensin, et al. Dalton Trans 2008 5207 5219 10.1039/b806192k 18813375
    • (2008) Dalton Trans , pp. 5207-5219
    • Gralka, E.1    Valensin, D.2    Porciatti, E.3    Gajda, C.4    Gaggelli, E.5    Valensin, G.6
  • 35
    • 0035159198 scopus 로고    scopus 로고
    • Structural and functional characteristics of the B-domain-deleted recombinant factor VIII protein, r-VIII SQ
    • 11204595
    • Structural and functional characteristics of the B-domain-deleted recombinant factor VIII protein, r-VIII SQ. H Sandberg A Almstedt J Brandt E Gray L Holmquist U Oswaldsson, et al. Thromb Haemost 2001 85 93 100 11204595
    • (2001) Thromb Haemost , vol.85 , pp. 93-100
    • Sandberg, H.1    Almstedt, A.2    Brandt, J.3    Gray, E.4    Holmquist, L.5    Oswaldsson, U.6
  • 36
    • 0026511729 scopus 로고
    • Identification and functional importance of tyrosine sulfate residues within recombinant factor VIII
    • 10.1021/bi00128a003. 1554716
    • Identification and functional importance of tyrosine sulfate residues within recombinant factor VIII. DD Pittman JH Wang RJ Kaufman, Biochemistry 1992 31 3315 3325 10.1021/bi00128a003 1554716
    • (1992) Biochemistry , vol.31 , pp. 3315-3325
    • Pittman, D.D.1    Wang, J.H.2    Kaufman, R.J.3
  • 37
    • 0032992904 scopus 로고    scopus 로고
    • Characterization of tyrosine sulfate residues in antihemophilic recombinant factor VIII by liquid chromatography electrospray ionization tandem mass spectrometry and amino acid analysis
    • 10.1002/(SICI)1097-0231(19990615)13:11<1016::AID-RCM5993.0.CO;2-5. 10368977
    • Characterization of tyrosine sulfate residues in antihemophilic recombinant factor VIII by liquid chromatography electrospray ionization tandem mass spectrometry and amino acid analysis. JC Severs M Carnine H Eguizabal KK Mock, Rapid Commun Mass Spectrom 1999 13 1016 1023 10.1002/(SICI)1097- 0231(19990615)13:11<1016::AID-RCM5993.0.CO;2-5 10368977
    • (1999) Rapid Commun Mass Spectrom , vol.13 , pp. 1016-1023
    • Severs, J.C.1    Carnine, M.2    Eguizabal, H.3    Mock, K.K.4
  • 38
    • 0028058606 scopus 로고
    • Identification of individual tyrosine sulfation sites within factor VIII required for optimal activity and efficient thrombin cleavage
    • 8051097
    • Identification of individual tyrosine sulfation sites within factor VIII required for optimal activity and efficient thrombin cleavage. DA Michnick DD Pittman RJ Wise RJ Kaufman, J Biol Chem 1994 269 20095 20102 8051097
    • (1994) J Biol Chem , vol.269 , pp. 20095-20102
    • Michnick, D.A.1    Pittman, D.D.2    Wise, R.J.3    Kaufman, R.J.4
  • 39
    • 0035982216 scopus 로고    scopus 로고
    • A Tyr346 - Cys substitution in the interdomain acidic region a1 of factor VIII in an individual with factor VIII:C assay discrepancy
    • 10.1046/j.1365-2141.2002.03617.x. 12139751
    • A Tyr346 - Cys substitution in the interdomain acidic region a1 of factor VIII in an individual with factor VIII:C assay discrepancy. AD Mumford M Laffan J O'Donnell JH McVey DJ Johnson RA Manning, et al. Br J Haematol 2002 118 589 594 10.1046/j.1365-2141.2002.03617.x 12139751
    • (2002) Br J Haematol , vol.118 , pp. 589-594
    • Mumford, A.D.1    Laffan, M.2    O'Donnell, J.3    McVey, J.H.4    Johnson, D.J.5    Manning, R.A.6
  • 40
    • 66449121335 scopus 로고    scopus 로고
    • Cleavage at Arg-1689 influences heavy chain cleavages during thrombin-catalyzed activation of factor VIII
    • 10.1074/jbc.M900234200. 19240027
    • Cleavage at Arg-1689 influences heavy chain cleavages during thrombin-catalyzed activation of factor VIII. JL Newell PJ Fay, J Biol Chem 2009 284 11080 11089 10.1074/jbc.M900234200 19240027
    • (2009) J Biol Chem , vol.284 , pp. 11080-11089
    • Newell, J.L.1    Fay, P.J.2
  • 41
    • 0035853784 scopus 로고    scopus 로고
    • Cleavage of factor VIII heavy chain is required for the functional interaction of a2 subunit with factor IXA
    • 10.1074/jbc.M009539200. 11278520
    • Cleavage of factor VIII heavy chain is required for the functional interaction of a2 subunit with factor IXA. PJ Fay M Mastri ME Koszelak H Wakabayashi, J Biol Chem 2001 276 12434 12439 10.1074/jbc.M009539200 11278520
    • (2001) J Biol Chem , vol.276 , pp. 12434-12439
    • Fay, P.J.1    Mastri, M.2    Koszelak, M.E.3    Wakabayashi, H.4
  • 42
    • 0025923490 scopus 로고
    • Human factor VIIIa subunit structure. Reconstruction of factor VIIIa from the isolated A1/A3-C1-C2 dimer and A2 subunit
    • 1902833
    • Human factor VIIIa subunit structure. Reconstruction of factor VIIIa from the isolated A1/A3-C1-C2 dimer and A2 subunit. PJ Fay PJ Haidaris TM Smudzin, J Biol Chem 1991 266 8957 8962 1902833
    • (1991) J Biol Chem , vol.266 , pp. 8957-8962
    • Fay, P.J.1    Haidaris, P.J.2    Smudzin, T.M.3
  • 43
    • 0025866980 scopus 로고
    • Structural basis for the decreased procoagulant activity of human factor VIII compared to the porcine homolog
    • 1905722
    • Structural basis for the decreased procoagulant activity of human factor VIII compared to the porcine homolog. P Lollar ET Parker, J Biol Chem 1991 266 12481 12486 1905722
    • (1991) J Biol Chem , vol.266 , pp. 12481-12486
    • Lollar, P.1    Parker, E.T.2
  • 45
    • 53449102315 scopus 로고    scopus 로고
    • Generation of enhanced stability factor VIII variants by replacement of charged residues at the A2 domain interface
    • 10.1182/blood-2008-02-142158. 18650448
    • Generation of enhanced stability factor VIII variants by replacement of charged residues at the A2 domain interface. H Wakabayashi F Varfaj J Deangelis PJ Fay, Blood 2008 112 2761 2769 10.1182/blood-2008-02-142158 18650448
    • (2008) Blood , vol.112 , pp. 2761-2769
    • Wakabayashi, H.1    Varfaj, F.2    Deangelis, J.3    Fay, P.J.4
  • 46
    • 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
    • 10.1021/bi00350a035. 3082357
    • 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. D Eaton H Rodriguez GA Vehar, Biochemistry 1986 25 505 512 10.1021/bi00350a035 3082357
    • (1986) Biochemistry , vol.25 , pp. 505-512
    • Eaton, D.1    Rodriguez, H.2    Vehar, G.A.3
  • 47
    • 0030849972 scopus 로고    scopus 로고
    • Subunit structure and function of porcine factor Xa-activated factor VIII
    • 10.1021/bi970599o. 9235979
    • Subunit structure and function of porcine factor Xa-activated factor VIII. ET Parker J Pohl MN Blackburn P Lollar, Biochemistry 1997 36 9365 9373 10.1021/bi970599o 9235979
    • (1997) Biochemistry , vol.36 , pp. 9365-9373
    • Parker, E.T.1    Pohl, J.2    Blackburn, M.N.3    Lollar, P.4
  • 48
    • 34548486693 scopus 로고    scopus 로고
    • Proteolysis at Arg740 facilitates subsequent bond cleavages during thrombin-catalyzed activation of factor VIII
    • 10.1074/jbc.M703433200. 17595160
    • Proteolysis at Arg740 facilitates subsequent bond cleavages during thrombin-catalyzed activation of factor VIII. JL Newell PJ Fay, J Biol Chem 2007 282 25367 25375 10.1074/jbc.M703433200 17595160
    • (2007) J Biol Chem , vol.282 , pp. 25367-25375
    • Newell, J.L.1    Fay, P.J.2
  • 49
    • 0035853784 scopus 로고    scopus 로고
    • Cleavage of factor VIII heavy chain is required for the functional interaction of a2 subunit with factor IXA
    • 10.1074/jbc.M009539200. 11278520
    • Cleavage of factor VIII heavy chain is required for the functional interaction of a2 subunit with factor IXA. PJ Fay M Mastri ME Koszelak H Wakabayashi, J Biol Chem 2001 276 12434 12439 10.1074/jbc.M009539200 11278520
    • (2001) J Biol Chem , vol.276 , pp. 12434-12439
    • Fay, P.J.1    Mastri, M.2    Koszelak, M.E.3    Wakabayashi, H.4
  • 50
    • 0027938728 scopus 로고
    • Factor VIIIa A2 subunit residues 558-565 represent a factor IXa interactive site
    • 8051150
    • Factor VIIIa A2 subunit residues 558-565 represent a factor IXa interactive site. PJ Fay T Beattie CF Huggins LM Regan, J Biol Chem 1994 269 20522 20527 8051150
    • (1994) J Biol Chem , vol.269 , pp. 20522-20527
    • Fay, P.J.1    Beattie, T.2    Huggins, C.F.3    Regan, L.M.4
  • 51
    • 0035844226 scopus 로고    scopus 로고
    • Factor IXa:factor VIIIa interaction. helix 330-338 of factor ixa interacts with residues 558-565 and spatially adjacent regions of the a2 subunit of factor VIIIa
    • 10.1074/jbc.M011680200. 11278963
    • Factor IXa:factor VIIIa interaction. helix 330-338 of factor ixa interacts with residues 558-565 and spatially adjacent regions of the a2 subunit of factor VIIIa. SP Bajaj AE Schmidt A Mathur K Padmanabhan D Zhong M Mastri, et al. J Biol Chem 2001 276 16302 16309 10.1074/jbc.M011680200 11278963
    • (2001) J Biol Chem , vol.276 , pp. 16302-16309
    • Bajaj, S.P.1    Schmidt, A.E.2    Mathur, A.3    Padmanabhan, K.4    Zhong, D.5    Mastri, M.6
  • 52
    • 0020043657 scopus 로고
    • Monoclonal antibodies to porcine factor VIII coagulant and their use in the isolation of active coagulant protein
    • 6800419
    • Monoclonal antibodies to porcine factor VIII coagulant and their use in the isolation of active coagulant protein. DN Fass GJ Knutson JA Katzmann, Blood 1982 59 594 600 6800419
    • (1982) Blood , vol.59 , pp. 594-600
    • Fass, D.N.1    Knutson, G.J.2    Katzmann, J.A.3
  • 53
    • 0028939696 scopus 로고
    • Locations of disulfide bonds and free cysteines in the heavy and light chains of recombinant human factor VIII (antihemophilic factor A)
    • 7613471
    • Locations of disulfide bonds and free cysteines in the heavy and light chains of recombinant human factor VIII (antihemophilic factor A). BA McMullen K Fujikawa EW Davie U Hedner M Ezban, Protein Sci 1995 4 740 746 7613471
    • (1995) Protein Sci , vol.4 , pp. 740-746
    • McMullen, B.A.1    Fujikawa, K.2    Davie, E.W.3    Hedner, U.4    Ezban, M.5
  • 54
    • 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
    • 10.1021/bi980084c. 9578574
    • Effects of copper on the structure and function of factor VIII subunits: evidence for an auxiliary role for copper ions in cofactor activity. K Sudhakar PJ Fay, Biochemistry 1998 37 6874 6882 10.1021/bi980084c 9578574
    • (1998) Biochemistry , vol.37 , pp. 6874-6882
    • Sudhakar, K.1    Fay, P.J.2
  • 55
    • 33745196647 scopus 로고    scopus 로고
    • PH-dependent association of factor VIII chains: Enhancement of affinity at physiological pH by Cu2 +
    • 16731058
    • pH-dependent association of factor VIII chains: enhancement of affinity at physiological pH by Cu2 +. H Wakabayashi Q Zhou K Nogami C Ansong F Varfaj S Miles, et al. Biochim Biophys Acta 2006 1764 1094 1101 16731058
    • (2006) Biochim Biophys Acta , vol.1764 , pp. 1094-1101
    • Wakabayashi, H.1    Zhou, Q.2    Nogami, K.3    Ansong, C.4    Varfaj, F.5    Miles, S.6
  • 56
    • 0037007964 scopus 로고    scopus 로고
    • Ca(2+) binding to both the heavy and light chains of factor VIII is required for cofactor activity
    • 10.1021/bi025589o. 12081499
    • Ca(2+) binding to both the heavy and light chains of factor VIII is required for cofactor activity. H Wakabayashi KM Schmidt PJ Fay, Biochemistry 2002 41 8485 8492 10.1021/bi025589o 12081499
    • (2002) Biochemistry , vol.41 , pp. 8485-8492
    • Wakabayashi, H.1    Schmidt, K.M.2    Fay, P.J.3
  • 57
    • 0035964179 scopus 로고    scopus 로고
    • Metal ion-independent association of factor VIII subunits and the roles of calcium and copper ions for cofactor activity and inter-subunit affinity
    • 10.1021/bi010353q. 11513607
    • Metal ion-independent association of factor VIII subunits and the roles of calcium and copper ions for cofactor activity and inter-subunit affinity. H Wakabayashi ME Koszelak M Mastri PJ Fay, Biochemistry 2001 40 10293 10300 10.1021/bi010353q 11513607
    • (2001) Biochemistry , vol.40 , pp. 10293-10300
    • Wakabayashi, H.1    Koszelak, M.E.2    Mastri, M.3    Fay, P.J.4
  • 58
    • 0037007964 scopus 로고    scopus 로고
    • Ca(2+) binding to both the heavy and light chains of factor VIII is required for cofactor activity
    • 10.1021/bi025589o. 12081499
    • Ca(2+) binding to both the heavy and light chains of factor VIII is required for cofactor activity. H Wakabayashi KM Schmidt PJ Fay, Biochemistry 2002 41 8485 8492 10.1021/bi025589o 12081499
    • (2002) Biochemistry , vol.41 , pp. 8485-8492
    • Wakabayashi, H.1    Schmidt, K.M.2    Fay, P.J.3
  • 59
    • 0035964179 scopus 로고    scopus 로고
    • Metal ion-independent association of factor VIII subunits and the roles of calcium and copper ions for cofactor activity and inter-subunit affinity
    • 10.1021/bi010353q. 11513607
    • Metal ion-independent association of factor VIII subunits and the roles of calcium and copper ions for cofactor activity and inter-subunit affinity. H Wakabayashi ME Koszelak M Mastri PJ Fay, Biochemistry 2001 40 10293 10300 10.1021/bi010353q 11513607
    • (2001) Biochemistry , vol.40 , pp. 10293-10300
    • Wakabayashi, H.1    Koszelak, M.E.2    Mastri, M.3    Fay, P.J.4
  • 60
    • 33646839132 scopus 로고    scopus 로고
    • Factor VIII structure and function
    • 10.1532/IJH97.05113. 16513527
    • Factor VIII structure and function. PJ Fay, Int J Hematol 2006 83 103 108 10.1532/IJH97.05113 16513527
    • (2006) Int J Hematol , vol.83 , pp. 103-108
    • Fay, P.J.1
  • 61
    • 0028818856 scopus 로고
    • Characterization of des-(741-1668)-factor VIII, a single-chain factor VIII variant with a fusion site susceptible to proteolysis by thrombin and factor Xa
    • 7492334
    • Characterization of des-(741-1668)-factor VIII, a single-chain factor VIII variant with a fusion site susceptible to proteolysis by thrombin and factor Xa. MJ Donath RT de Laaf PT Biessels PJ Lenting JW van de Loo JA van Mourik, et al. Biochem J 1995 312 Pt 1 49 55 7492334
    • (1995) Biochem J , vol.312 , Issue.PT 1 , pp. 49-55
    • Donath, M.J.1    De Laaf, R.T.2    Biessels, P.T.3    Lenting, P.J.4    De Van, W.L.J.5    Van Mourik, J.A.6
  • 62
    • 0347383758 scopus 로고    scopus 로고
    • Modeller: Generation and refinement of homology-based protein structure models
    • full-text. 14696385
    • Modeller: generation and refinement of homology-based protein structure models. A Fiser A Sali, Methods Enzymol 2003 374 461 491 full-text 14696385
    • (2003) Methods Enzymol , vol.374 , pp. 461-491
    • Fiser, A.1    Sali, A.2
  • 63
    • 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
    • 10.1021/bi980084c. 9578574
    • Effects of copper on the structure and function of factor VIII subunits: evidence for an auxiliary role for copper ions in cofactor activity. K Sudhakar PJ Fay, Biochemistry 1998 37 6874 6882 10.1021/bi980084c 9578574
    • (1998) Biochemistry , vol.37 , pp. 6874-6882
    • Sudhakar, K.1    Fay, P.J.2
  • 64
    • 33745196647 scopus 로고    scopus 로고
    • PH-dependent association of factor VIII chains: Enhancement of affinity at physiological pH by Cu2 +
    • 16731058
    • pH-dependent association of factor VIII chains: enhancement of affinity at physiological pH by Cu2 +. H Wakabayashi Q Zhou K Nogami C Ansong F Varfaj S Miles, et al. Biochim Biophys Acta 2006 1764 1094 1101 16731058
    • (2006) Biochim Biophys Acta , vol.1764 , pp. 1094-1101
    • Wakabayashi, H.1    Zhou, Q.2    Nogami, K.3    Ansong, C.4    Varfaj, F.5    Miles, S.6
  • 65
    • 0037007964 scopus 로고    scopus 로고
    • Ca(2+) binding to both the heavy and light chains of factor VIII is required for cofactor activity
    • 10.1021/bi025589o. 12081499
    • Ca(2+) binding to both the heavy and light chains of factor VIII is required for cofactor activity. H Wakabayashi KM Schmidt PJ Fay, Biochemistry 2002 41 8485 8492 10.1021/bi025589o 12081499
    • (2002) Biochemistry , vol.41 , pp. 8485-8492
    • Wakabayashi, H.1    Schmidt, K.M.2    Fay, P.J.3
  • 66
    • 0035964179 scopus 로고    scopus 로고
    • Metal ion-independent association of factor VIII subunits and the roles of calcium and copper ions for cofactor activity and inter-subunit affinity
    • 10.1021/bi010353q. 11513607
    • Metal ion-independent association of factor VIII subunits and the roles of calcium and copper ions for cofactor activity and inter-subunit affinity. H Wakabayashi ME Koszelak M Mastri PJ Fay, Biochemistry 2001 40 10293 10300 10.1021/bi010353q 11513607
    • (2001) Biochemistry , vol.40 , pp. 10293-10300
    • Wakabayashi, H.1    Koszelak, M.E.2    Mastri, M.3    Fay, P.J.4
  • 67
    • 0021151729 scopus 로고
    • The effect of carbohydrate depletion on procoagulant activity and in vivo survival of highly purified human factor VIII
    • 6430352
    • The effect of carbohydrate depletion on procoagulant activity and in vivo survival of highly purified human factor VIII. PJ Fay SI Chavin JE Malone D Schroeder FE Young VJ Marder, Biochim Biophys Acta 1984 800 152 158 6430352
    • (1984) Biochim Biophys Acta , vol.800 , pp. 152-158
    • Fay, P.J.1    Chavin, S.I.2    Malone, J.E.3    Schroeder, D.4    Young, F.E.5    Marder, V.J.6
  • 68
    • 0032932325 scopus 로고    scopus 로고
    • Mild hemophilia A caused by increased rate of factor VIII A2 subunit dissociation: Evidence for nonproteolytic inactivation of factor VIIIa in vivo
    • 9864159
    • Mild hemophilia A caused by increased rate of factor VIII A2 subunit dissociation: evidence for nonproteolytic inactivation of factor VIIIa in vivo. SW Pipe AN Eickhorst SH McKinley EL Saenko RJ Kaufman, Blood 1999 93 176 183 9864159
    • (1999) Blood , vol.93 , pp. 176-183
    • Pipe, S.W.1    Eickhorst, A.N.2    McKinley, S.H.3    Saenko, E.L.4    Kaufman, R.J.5
  • 69
    • 0035254221 scopus 로고    scopus 로고
    • Hemophilia A mutations associated with 1-stage/2-stage activity discrepancy disrupt protein-protein interactions within the triplicated A domains of thrombin-activated factor VIIIa
    • 10.1182/blood.V97.3.685. 11157485
    • Hemophilia A mutations associated with 1-stage/2-stage activity discrepancy disrupt protein-protein interactions within the triplicated A domains of thrombin-activated factor VIIIa. SW Pipe EL Saenko AN Eickhorst G Kemball-Cook RJ Kaufman, Blood 2001 97 685 691 10.1182/blood.V97.3.685 11157485
    • (2001) Blood , vol.97 , pp. 685-691
    • Pipe, S.W.1    Saenko, E.L.2    Eickhorst, A.N.3    Kemball-Cook, G.4    Kaufman, R.J.5
  • 72
    • 0036558223 scopus 로고    scopus 로고
    • A new molecular mechanics force field for the oxidized form of blue copper proteins
    • 10.1002/jcc.10084. 11948587
    • A new molecular mechanics force field for the oxidized form of blue copper proteins. P Comba R Remenyi, J Comput Chem 2002 23 697 705 10.1002/jcc.10084 11948587
    • (2002) J Comput Chem , vol.23 , pp. 697-705
    • Comba, P.1    Remenyi, R.2


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