메뉴 건너뛰기




Volumn 54, Issue 2, 2015, Pages 481-489

Cluster III of low-density lipoprotein receptor-related protein 1 binds activated blood coagulation factor VIII

Author keywords

[No Author keywords available]

Indexed keywords

ANTIBODIES; BLOOD; COAGULATION; LIPOPROTEINS; PROTEINS; SURFACE PLASMON RESONANCE;

EID: 84922417839     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi5011688     Document Type: Article
Times cited : (10)

References (61)
  • 1
    • 0141832797 scopus 로고    scopus 로고
    • Diverse role of LDL receptor-related protein in the clearance of proteases and in signaling
    • Strickland, D. K. and Ranganathan, S. (2003) Diverse role of LDL receptor-related protein in the clearance of proteases and in signaling J. Thromb. Haemostasis 1, 1663-1670
    • (2003) J. Thromb. Haemostasis , vol.1 , pp. 1663-1670
    • Strickland, D.K.1    Ranganathan, S.2
  • 2
    • 0030759357 scopus 로고    scopus 로고
    • Molecular basis of familial hypercholesterolaemia from structure of LDL receptor module
    • Fass, D., Blacklow, S., Kim, P. S., and Berger, J. M. (1997) Molecular basis of familial hypercholesterolaemia from structure of LDL receptor module Nature 388, 691-693
    • (1997) Nature , vol.388 , pp. 691-693
    • Fass, D.1    Blacklow, S.2    Kim, P.S.3    Berger, J.M.4
  • 3
    • 0034646442 scopus 로고    scopus 로고
    • Solution structure of the sixth LDL-A module of the LDL receptor
    • North, C. L. and Blacklow, S. C. (2000) Solution structure of the sixth LDL-A module of the LDL receptor Biochemistry 39, 2564-2571
    • (2000) Biochemistry , vol.39 , pp. 2564-2571
    • North, C.L.1    Blacklow, S.C.2
  • 4
    • 0029020912 scopus 로고
    • Three-dimensional structure of a cysteine-rich repeat from the low-density lipoprotein receptor
    • Daly, N. L., Scanlon, M. J., Djordjevic, J. T., Kroon, P. A., and Smith, R. (1995) Three-dimensional structure of a cysteine-rich repeat from the low-density lipoprotein receptor Proc. Natl. Acad. Sci. U.S.A. 92, 6334-6338
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 6334-6338
    • Daly, N.L.1    Scanlon, M.J.2    Djordjevic, J.T.3    Kroon, P.A.4    Smith, R.5
  • 5
    • 33646046808 scopus 로고    scopus 로고
    • Structure of an LDLR-RAP complex reveals a general mode for ligand recognition by lipoprotein receptors
    • Fisher, C., Beglova, N., and Blacklow, S. C. (2006) Structure of an LDLR-RAP complex reveals a general mode for ligand recognition by lipoprotein receptors Mol. Cell 22, 277-283
    • (2006) Mol. Cell , vol.22 , pp. 277-283
    • Fisher, C.1    Beglova, N.2    Blacklow, S.C.3
  • 7
    • 77649144078 scopus 로고    scopus 로고
    • Structural basis for specific recognition of reelin by its receptors
    • Yasui, N., Nogi, T., and Takagi, J. (2010) Structural basis for specific recognition of reelin by its receptors Structure 18, 320-331
    • (2010) Structure , vol.18 , pp. 320-331
    • Yasui, N.1    Nogi, T.2    Takagi, J.3
  • 9
    • 1942501580 scopus 로고    scopus 로고
    • The role of a conserved acidic residue in calcium-dependent protein folding for a low density lipoprotein (LDL)-A module: Implications in structure and function for the LDL receptor superfamily
    • Guo, Y., Yu, X., Rihani, K., Wang, Q. Y., and Rong, L. (2004) The role of a conserved acidic residue in calcium-dependent protein folding for a low density lipoprotein (LDL)-A module: Implications in structure and function for the LDL receptor superfamily J. Biol. Chem. 279, 16629-16637
    • (2004) J. Biol. Chem. , vol.279 , pp. 16629-16637
    • Guo, Y.1    Yu, X.2    Rihani, K.3    Wang, Q.Y.4    Rong, L.5
  • 11
    • 0034647901 scopus 로고    scopus 로고
    • Identification of the minimal functional unit in the low density lipoprotein receptor-related protein for binding the receptor-associated protein (RAP). A conserved acidic residue in the complement-type repeats is important for recognition of RAP
    • Andersen, O. M., Christensen, L. L., Christensen, P. A., Sorensen, E. S., Jacobsen, C., Moestrup, S. K., Etzerodt, M., and Thogersen, H. C. (2000) Identification of the minimal functional unit in the low density lipoprotein receptor-related protein for binding the receptor-associated protein (RAP). A conserved acidic residue in the complement-type repeats is important for recognition of RAP J. Biol. Chem. 275, 21017-21024
    • (2000) J. Biol. Chem. , vol.275 , pp. 21017-21024
    • Andersen, O.M.1    Christensen, L.L.2    Christensen, P.A.3    Sorensen, E.S.4    Jacobsen, C.5    Moestrup, S.K.6    Etzerodt, M.7    Thogersen, H.C.8
  • 12
    • 2342648870 scopus 로고    scopus 로고
    • X-ray structure of a minor group human rhinovirus bound to a fragment of its cellular receptor protein
    • Verdaguer, N., Fita, I., Reithmayer, M., Moser, R., and Blaas, D. (2004) X-ray structure of a minor group human rhinovirus bound to a fragment of its cellular receptor protein Nat. Struct. Mol. Biol. 11, 429-434
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 429-434
    • Verdaguer, N.1    Fita, I.2    Reithmayer, M.3    Moser, R.4    Blaas, D.5
  • 13
    • 77649092080 scopus 로고    scopus 로고
    • Mode of interaction between β2GPI and lipoprotein receptors suggests mutually exclusive binding of β2GPI to the receptors and anionic phospholipids
    • Lee, C. J., De, B. A., and Beglova, N. (2010) Mode of interaction between β2GPI and lipoprotein receptors suggests mutually exclusive binding of β2GPI to the receptors and anionic phospholipids Structure 18, 366-376
    • (2010) Structure , vol.18 , pp. 366-376
    • Lee, C.J.1    De, B.A.2    Beglova, N.3
  • 15
    • 84873671045 scopus 로고    scopus 로고
    • Gentamicin binds to the megalin receptor as a competitive inhibitor using the common ligand binding motif of complement type repeats: Insight from the NMR structure of the 10th complement type repeat domain alone and in complex with gentamicin
    • Dagil, R., O'Shea, C., Nykjaer, A., Bonvin, A. M., and Kragelund, B. B. (2013) Gentamicin binds to the megalin receptor as a competitive inhibitor using the common ligand binding motif of complement type repeats: Insight from the NMR structure of the 10th complement type repeat domain alone and in complex with gentamicin J. Biol. Chem. 288, 4424-4435
    • (2013) J. Biol. Chem. , vol.288 , pp. 4424-4435
    • Dagil, R.1    O'Shea, C.2    Nykjaer, A.3    Bonvin, A.M.4    Kragelund, B.B.5
  • 17
    • 0942268917 scopus 로고    scopus 로고
    • A two-module region of the low-density lipoprotein receptor sufficient for formation of complexes with apolipoprotein e ligands
    • Fisher, C., Abdul-Aziz, D., and Blacklow, S. C. (2004) A two-module region of the low-density lipoprotein receptor sufficient for formation of complexes with apolipoprotein E ligands Biochemistry 43, 1037-1044
    • (2004) Biochemistry , vol.43 , pp. 1037-1044
    • Fisher, C.1    Abdul-Aziz, D.2    Blacklow, S.C.3
  • 18
    • 0035395799 scopus 로고    scopus 로고
    • Analysis of a two-domain binding site for the urokinase-type plasminogen activator-plasminogen activator inhibitor-1 complex in low-density-lipoprotein-receptor-related protein
    • Andersen, O. M., Petersen, H. H., Jacobsen, C., Moestrup, S. K., Etzerodt, M., Andreasen, P. A., and Thogersen, H. C. (2001) Analysis of a two-domain binding site for the urokinase-type plasminogen activator-plasminogen activator inhibitor-1 complex in low-density-lipoprotein-receptor-related protein Biochem. J. 357, 289-296
    • (2001) Biochem. J. , vol.357 , pp. 289-296
    • Andersen, O.M.1    Petersen, H.H.2    Jacobsen, C.3    Moestrup, S.K.4    Etzerodt, M.5    Andreasen, P.A.6    Thogersen, H.C.7
  • 19
    • 0033615548 scopus 로고    scopus 로고
    • The second and fourth cluster of class A cysteine-rich repeats of the low density lipoprotein receptor-related protein share ligand-binding properties
    • Neels, J. G., van Den Berg, B. M., Lookene, A., Olivecrona, G., Pannekoek, H., and van Zonneveld, A. J. (1999) The second and fourth cluster of class A cysteine-rich repeats of the low density lipoprotein receptor-related protein share ligand-binding properties J. Biol. Chem. 274, 31305-31311
    • (1999) J. Biol. Chem. , vol.274 , pp. 31305-31311
    • Neels, J.G.1    Van Den Berg, B.M.2    Lookene, A.3    Olivecrona, G.4    Pannekoek, H.5    Van Zonneveld, A.J.6
  • 20
    • 0242424094 scopus 로고    scopus 로고
    • All three LDL receptor homology regions of the LDL receptor-related protein bind multiple ligands
    • Croy, J. E., Shin, W. D., Knauer, M. F., Knauer, D. J., and Komives, E. A. (2003) All three LDL receptor homology regions of the LDL receptor-related protein bind multiple ligands Biochemistry 42, 13049-13057
    • (2003) Biochemistry , vol.42 , pp. 13049-13057
    • Croy, J.E.1    Shin, W.D.2    Knauer, M.F.3    Knauer, D.J.4    Komives, E.A.5
  • 21
    • 0030973626 scopus 로고    scopus 로고
    • Differential functions of triplicated repeats suggest two independent roles for the receptor-associated protein as a molecular chaperone
    • Obermoeller, L. M., Warshawsky, I., Wardell, M. R., and Bu, G. (1997) Differential functions of triplicated repeats suggest two independent roles for the receptor-associated protein as a molecular chaperone J. Biol. Chem. 272, 10761-10768
    • (1997) J. Biol. Chem. , vol.272 , pp. 10761-10768
    • Obermoeller, L.M.1    Warshawsky, I.2    Wardell, M.R.3    Bu, G.4
  • 22
    • 0028800945 scopus 로고
    • 2-macroglobulin receptor/low density lipoprotein receptor-related protein. Evidence that lipoprotein lipase and the carboxyl-terminal domain of the receptor-associated protein bind to the same site
    • 2-macroglobulin receptor/low density lipoprotein receptor-related protein. Evidence that lipoprotein lipase and the carboxyl-terminal domain of the receptor-associated protein bind to the same site J. Biol. Chem. 270, 23713-23719
    • (1995) J. Biol. Chem. , vol.270 , pp. 23713-23719
    • Nielsen, M.S.1    Nykjaer, A.2    Warshawsky, I.3    Schwartz, A.L.4    Gliemann, J.5
  • 24
    • 0033621486 scopus 로고    scopus 로고
    • Role of the low density lipoprotein-related protein receptor in mediation of factor VIII catabolism
    • Saenko, E. L., Yakhyaev, A. V., Mikhailenko, I., Strickland, D. K., and Sarafanov, A. G. (1999) Role of the low density lipoprotein-related protein receptor in mediation of factor VIII catabolism J. Biol. Chem. 274, 37685-37692
    • (1999) J. Biol. Chem. , vol.274 , pp. 37685-37692
    • Saenko, E.L.1    Yakhyaev, A.V.2    Mikhailenko, I.3    Strickland, D.K.4    Sarafanov, A.G.5
  • 25
    • 23044478501 scopus 로고    scopus 로고
    • LDL receptor cooperates with LDL receptor-related protein in regulating plasma levels of coagulation factor VIII in vivo
    • Bovenschen, N., Mertens, K., Hu, L., Havekes, L. M., and van Vlijmen, B. J. (2005) LDL receptor cooperates with LDL receptor-related protein in regulating plasma levels of coagulation factor VIII in vivo Blood 106, 906-912
    • (2005) Blood , vol.106 , pp. 906-912
    • Bovenschen, N.1    Mertens, K.2    Hu, L.3    Havekes, L.M.4    Van Vlijmen, B.J.5
  • 26
    • 0035853843 scopus 로고    scopus 로고
    • Cell surface heparan sulfate proteoglycans participate in factor VIII catabolism mediated by low density lipoprotein receptor-related protein
    • Sarafanov, A. G., Ananyeva, N. M., Shima, M., and Saenko, E. L. (2001) Cell surface heparan sulfate proteoglycans participate in factor VIII catabolism mediated by low density lipoprotein receptor-related protein J. Biol. Chem. 276, 11970-11979
    • (2001) J. Biol. Chem. , vol.276 , pp. 11970-11979
    • Sarafanov, A.G.1    Ananyeva, N.M.2    Shima, M.3    Saenko, E.L.4
  • 27
    • 33646839132 scopus 로고    scopus 로고
    • Factor VIII structure and function
    • Fay, P. J. (2006) Factor VIII structure and function Int. J. Hematol. 83, 103-108
    • (2006) Int. J. Hematol. , vol.83 , pp. 103-108
    • Fay, P.J.1
  • 28
    • 84900839290 scopus 로고    scopus 로고
    • Factor VIII therapy for hemophilia A: Current and future issues
    • Aledort, L., Ljung, R., Mann, K., and Pipe, S. (2014) Factor VIII therapy for hemophilia A: Current and future issues Expert Rev. Hematol. 7, 373-385
    • (2014) Expert Rev. Hematol. , vol.7 , pp. 373-385
    • Aledort, L.1    Ljung, R.2    Mann, K.3    Pipe, S.4
  • 29
    • 0037646492 scopus 로고    scopus 로고
    • Low density lipoprotein receptor-related protein and factor IXa share structural requirements for binding to the A3 domain of coagulation factor VIII
    • Bovenschen, N., Boertjes, R. C., van Stempvoort, G., Voorberg, J., Lenting, P. J., Meijer, A. B., and Mertens, K. (2003) Low density lipoprotein receptor-related protein and factor IXa share structural requirements for binding to the A3 domain of coagulation factor VIII J. Biol. Chem. 278, 9370-9377
    • (2003) J. Biol. Chem. , vol.278 , pp. 9370-9377
    • Bovenschen, N.1    Boertjes, R.C.2    Van Stempvoort, G.3    Voorberg, J.4    Lenting, P.J.5    Meijer, A.B.6    Mertens, K.7
  • 30
    • 33745281224 scopus 로고    scopus 로고
    • Proteolytic cleavage of factor VIII heavy chain is required to expose the binding-site for low-density lipoprotein receptor-related protein within the A2 domain
    • Bovenschen, N., van, S. G., Voorberg, J., Mertens, K., and Meijer, A. B. (2006) Proteolytic cleavage of factor VIII heavy chain is required to expose the binding-site for low-density lipoprotein receptor-related protein within the A2 domain J. Thromb. Haemostasis 4, 1487-1493
    • (2006) J. Thromb. Haemostasis , vol.4 , pp. 1487-1493
    • Bovenschen, N.1    Van, S.G.2    Voorberg, J.3    Mertens, K.4    Meijer, A.B.5
  • 31
  • 32
    • 84881238277 scopus 로고    scopus 로고
    • Low Density Lipoprotein Receptor-Related Protein (LRP) Cluster II Interact with the Factor VIII Light Chain via an Extended Surface Comprising Multiple Lysine Residues
    • van den Biggelaar, M., van der Zwaan, C., Mertens, K., and Meijer, A. (2011) Low Density Lipoprotein Receptor-Related Protein (LRP) Cluster II Interact with the Factor VIII Light Chain via an Extended Surface Comprising Multiple Lysine Residues J. Thromb. Haemostasis 9, 821
    • (2011) J. Thromb. Haemostasis , vol.9 , pp. 821
    • Van Den Biggelaar, M.1    Van Der Zwaan, C.2    Mertens, K.3    Meijer, A.4
  • 33
    • 84881244787 scopus 로고    scopus 로고
    • Mapping the Binding Region on the Low Density Lipoprotein Receptor for Blood Coagulation Factor VIII
    • Kurasawa, J. H., Shestopal, S. A., Karnaukhova, E., Struble, E. B., Lee, T. K., and Sarafanov, A. G. (2013) Mapping the Binding Region on the Low Density Lipoprotein Receptor for Blood Coagulation Factor VIII J. Biol. Chem. 288, 22033-22041
    • (2013) J. Biol. Chem. , vol.288 , pp. 22033-22041
    • Kurasawa, J.H.1    Shestopal, S.A.2    Karnaukhova, E.3    Struble, E.B.4    Lee, T.K.5    Sarafanov, A.G.6
  • 34
    • 32344444865 scopus 로고    scopus 로고
    • Identification of Coagulation Factor VIII A2 Domain Residues Forming the Binding Epitope for Low-Density Lipoprotein Receptor-Related Protein
    • Sarafanov, A. G., Makogonenko, E. M., Pechik, I. V., Radtke, K. P., Khrenov, A. V., Ananyeva, N. M., Strickland, D. K., and Saenko, E. L. (2006) Identification of Coagulation Factor VIII A2 Domain Residues Forming the Binding Epitope for Low-Density Lipoprotein Receptor-Related Protein Biochemistry 45, 1829-1840
    • (2006) Biochemistry , vol.45 , pp. 1829-1840
    • Sarafanov, A.G.1    Makogonenko, E.M.2    Pechik, I.V.3    Radtke, K.P.4    Khrenov, A.V.5    Ananyeva, N.M.6    Strickland, D.K.7    Saenko, E.L.8
  • 35
    • 0029919613 scopus 로고    scopus 로고
    • Model for the factor VIIIa-dependent decay of the intrinsic factor Xase. Role of subunit dissociation and factor IXa-catalyzed proteolysis
    • Fay, P. J., Beattie, T. L., Regan, L. M., O'Brien, L. M., and Kaufman, R. J. (1996) Model for the factor VIIIa-dependent decay of the intrinsic factor Xase. Role of subunit dissociation and factor IXa-catalyzed proteolysis J. Biol. Chem. 271, 6027-6032
    • (1996) J. Biol. Chem. , vol.271 , pp. 6027-6032
    • Fay, P.J.1    Beattie, T.L.2    Regan, L.M.3    O'Brien, L.M.4    Kaufman, R.J.5
  • 37
    • 84873624702 scopus 로고    scopus 로고
    • Insect cell-based expression and characterization of a single-chain variable antibody fragment directed against blood coagulation factor VIII
    • Kurasawa, J. H., Shestopal, S. A., Jha, N. K., Ovanesov, M. V., Lee, T. K., and Sarafanov, A. G. (2013) Insect cell-based expression and characterization of a single-chain variable antibody fragment directed against blood coagulation factor VIII Protein Expression Purif. 88, 201-206
    • (2013) Protein Expression Purif. , vol.88 , pp. 201-206
    • Kurasawa, J.H.1    Shestopal, S.A.2    Jha, N.K.3    Ovanesov, M.V.4    Lee, T.K.5    Sarafanov, A.G.6
  • 38
    • 1842786993 scopus 로고    scopus 로고
    • High-throughput optimization of protein expression in the baculovirus system based on determination of relative expression efficiency of viral stocks
    • Sarafanov, A. and Saenko, E. (2004) High-throughput optimization of protein expression in the baculovirus system based on determination of relative expression efficiency of viral stocks Anal. Biochem. 328, 98-100
    • (2004) Anal. Biochem. , vol.328 , pp. 98-100
    • Sarafanov, A.1    Saenko, E.2
  • 40
    • 67650917714 scopus 로고    scopus 로고
    • Receptor-associated protein (RAP) has two high-affinity binding sites for the low-density lipoprotein receptor-related protein (LRP): Consequences for the chaperone functions of RAP
    • Jensen, J. K., Dolmer, K., Schar, C., and Gettins, P. G. (2009) Receptor-associated protein (RAP) has two high-affinity binding sites for the low-density lipoprotein receptor-related protein (LRP): Consequences for the chaperone functions of RAP Biochem. J. 421, 273-282
    • (2009) Biochem. J. , vol.421 , pp. 273-282
    • Jensen, J.K.1    Dolmer, K.2    Schar, C.3    Gettins, P.G.4
  • 43
    • 0033565673 scopus 로고    scopus 로고
    • 39-kDa receptor-associated protein (RAP) facilitates secretion and ligand binding of extracellular region of very-low-density-lipoprotein receptor: Implications for a distinct pathway from low-density-lipoprotein receptor
    • Sato, A., Shimada, Y., Herz, J., Yamamoto, T., and Jingami, H. (1999) 39-kDa receptor-associated protein (RAP) facilitates secretion and ligand binding of extracellular region of very-low-density-lipoprotein receptor: Implications for a distinct pathway from low-density-lipoprotein receptor Biochem. J. 341, 377-383
    • (1999) Biochem. J. , vol.341 , pp. 377-383
    • Sato, A.1    Shimada, Y.2    Herz, J.3    Yamamoto, T.4    Jingami, H.5
  • 44
    • 39149108978 scopus 로고    scopus 로고
    • An Antibody Fragment Against Factor VIII That Inhibits Factor VIII Assembly with von Willebrand Factor and LDL Receptor Family Members
    • Limburg, V., van der Zwaan, C., Boertjes, R. C., Bovenschen, N., Mertens, K., and Meijer, A. (2005) An Antibody Fragment Against Factor VIII That Inhibits Factor VIII Assembly with von Willebrand Factor and LDL Receptor Family Members J. Thromb. Haemostasis 3, OR162
    • (2005) J. Thromb. Haemostasis , vol.3 , pp. 162
    • Limburg, V.1    Van Der Zwaan, C.2    Boertjes, R.C.3    Bovenschen, N.4    Mertens, K.5    Meijer, A.6
  • 45
    • 79958759710 scopus 로고    scopus 로고
    • The Factor VIII C1 Domain Contributes to Efficient LRP/LDL Receptor Binding
    • Meijer, A., Limburg, V., van der Zwaan, C., and Mertens, K. (2007) The Factor VIII C1 Domain Contributes to Efficient LRP/LDL Receptor Binding J. Thromb. Haemostasis 5, P-M-040
    • (2007) J. Thromb. Haemostasis , vol.5 , pp. 040
    • Meijer, A.1    Limburg, V.2    Van Der Zwaan, C.3    Mertens, K.4
  • 46
    • 70449709337 scopus 로고    scopus 로고
    • Factor VIII C1 domain residues Lys 2092 and Phe 2093 contribute to membrane binding and cofactor activity
    • Meems, H., Meijer, A. B., Cullinan, D. B., Mertens, K., and Gilbert, G. E. (2009) Factor VIII C1 domain residues Lys 2092 and Phe 2093 contribute to membrane binding and cofactor activity Blood 114, 3938-3946
    • (2009) Blood , vol.114 , pp. 3938-3946
    • Meems, H.1    Meijer, A.B.2    Cullinan, D.B.3    Mertens, K.4    Gilbert, G.E.5
  • 47
    • 76749135871 scopus 로고    scopus 로고
    • Decoding of lipoprotein-receptor interactions: Properties of ligand binding modules governing interactions with apolipoprotein e
    • Guttman, M., Prieto, J. H., Croy, J. E., and Komives, E. A. (2010) Decoding of lipoprotein-receptor interactions: Properties of ligand binding modules governing interactions with apolipoprotein E Biochemistry 49, 1207-1216
    • (2010) Biochemistry , vol.49 , pp. 1207-1216
    • Guttman, M.1    Prieto, J.H.2    Croy, J.E.3    Komives, E.A.4
  • 48
    • 33845931332 scopus 로고    scopus 로고
    • 2-macroglobulin binding site in the second ligand binding cluster of the low density lipoprotein receptor-related protein
    • 2-macroglobulin binding site in the second ligand binding cluster of the low density lipoprotein receptor-related protein J. Biol. Chem. 281, 34189-34196
    • (2006) J. Biol. Chem. , vol.281 , pp. 34189-34196
    • Dolmer, K.1    Gettins, P.G.2
  • 49
    • 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., van Mourik, J. A., and Mertens, K. (1994) Identification of a binding site for blood coagulation factor IXa on the light chain of human factor VIII J. Biol. Chem. 269, 7150-7155
    • (1994) J. Biol. Chem. , vol.269 , pp. 7150-7155
    • Lenting, P.J.1    Donath, M.J.2    Van Mourik, J.A.3    Mertens, K.4
  • 50
    • 84858321170 scopus 로고    scopus 로고
    • A proximal pair of positive charges provides the dominant ligand-binding contribution to complement-like domains from the LRP (low-density lipoprotein receptor-related protein)
    • Gettins, P. G. and Dolmer, K. (2012) A proximal pair of positive charges provides the dominant ligand-binding contribution to complement-like domains from the LRP (low-density lipoprotein receptor-related protein) Biochem. J. 443, 65-73
    • (2012) Biochem. J. , vol.443 , pp. 65-73
    • Gettins, P.G.1    Dolmer, K.2
  • 51
    • 0029786288 scopus 로고    scopus 로고
    • Receptor-associated protein is a folding chaperone for low density lipoprotein receptor-related protein
    • Bu, G. and Rennke, S. (1996) Receptor-associated protein is a folding chaperone for low density lipoprotein receptor-related protein J. Biol. Chem. 271, 22218-22224
    • (1996) J. Biol. Chem. , vol.271 , pp. 22218-22224
    • Bu, G.1    Rennke, S.2
  • 52
    • 0037147191 scopus 로고    scopus 로고
    • Coordinated nonvectorial folding in a newly synthesized multidomain protein
    • Jansens, A., van, D. E., and Braakman, I. (2002) Coordinated nonvectorial folding in a newly synthesized multidomain protein Science 298, 2401-2403
    • (2002) Science , vol.298 , pp. 2401-2403
    • Jansens, A.1    Van, D.E.2    Braakman, I.3
  • 53
    • 0033032451 scopus 로고    scopus 로고
    • A new animal model of thrombophilia confirms that high plasma factor VIII levels are thrombogenic
    • Kawasaki, T., Kaida, T., Arnout, J., Vermylen, J., and Hoylaerts, M. F. (1999) A new animal model of thrombophilia confirms that high plasma factor VIII levels are thrombogenic Thromb. Haemostasis 81, 306-311
    • (1999) Thromb. Haemostasis , vol.81 , pp. 306-311
    • Kawasaki, T.1    Kaida, T.2    Arnout, J.3    Vermylen, J.4    Hoylaerts, M.F.5
  • 54
    • 0029035099 scopus 로고
    • The affinity and stoichiometry of binding of human factor VIII to von Willebrand factor
    • Vlot, A. J., Koppelman, S. J., van den Berg, M. H., Bouma, B. N., and Sixma, J. J. (1995) The affinity and stoichiometry of binding of human factor VIII to von Willebrand factor Blood 85, 3150-3157
    • (1995) Blood , vol.85 , pp. 3150-3157
    • Vlot, A.J.1    Koppelman, S.J.2    Van Den Berg, M.H.3    Bouma, B.N.4    Sixma, J.J.5
  • 55
    • 58149106235 scopus 로고    scopus 로고
    • Interaction of coagulation factor VIII with members of the low-density lipoprotein receptor family follows common mechanism and involves consensus residues within the A2 binding site 484-509
    • Ananyeva, N. M., Makogonenko, Y. M., Sarafanov, A. G., Pechik, I. V., Gorlatova, N., Radtke, K. P., Shima, M., and Saenko, E. L. (2008) Interaction of coagulation factor VIII with members of the low-density lipoprotein receptor family follows common mechanism and involves consensus residues within the A2 binding site 484-509 Blood Coagulation Fibrinolysis 19, 543-555
    • (2008) Blood Coagulation Fibrinolysis , vol.19 , pp. 543-555
    • Ananyeva, N.M.1    Makogonenko, Y.M.2    Sarafanov, A.G.3    Pechik, I.V.4    Gorlatova, N.5    Radtke, K.P.6    Shima, M.7    Saenko, E.L.8
  • 57
    • 4544310501 scopus 로고    scopus 로고
    • Clearance of coagulation factor VIII in very low-density lipoprotein receptor knockout mice
    • Bovenschen, N., van Dijk, K. W., Havekes, L. M., Mertens, K., and van Vlijmen, B. J. (2004) Clearance of coagulation factor VIII in very low-density lipoprotein receptor knockout mice Br. J. Haematol. 126, 722-725
    • (2004) Br. J. Haematol. , vol.126 , pp. 722-725
    • Bovenschen, N.1    Van Dijk, K.W.2    Havekes, L.M.3    Mertens, K.4    Van Vlijmen, B.J.5
  • 59
    • 34250767667 scopus 로고    scopus 로고
    • Clearance mechanisms of von Willebrand factor and factor VIII
    • Lenting, P. J., van Schooten, C. J., and Denis, C. V. (2007) Clearance mechanisms of von Willebrand factor and factor VIII J. Thromb. Haemostasis 5, 1353-1360
    • (2007) J. Thromb. Haemostasis , vol.5 , pp. 1353-1360
    • Lenting, P.J.1    Van Schooten, C.J.2    Denis, C.V.3
  • 61
    • 84899567922 scopus 로고    scopus 로고
    • Novel products for haemostasis: Current status
    • Oldenburg, J. and Albert, T. (2014) Novel products for haemostasis: Current status Haemophilia 20 (Suppl. 4) 23-28
    • (2014) Haemophilia , vol.20 , pp. 23-28
    • Oldenburg, J.1    Albert, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.