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Volumn 43, Issue 21, 2004, Pages 6519-6534

Disulfide bonding arrangements in active forms of the somatomedin B domain of human vitronectin

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL BONDS; ENZYMES; HYDROPHOBICITY; MOLECULAR STRUCTURE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; SOLUTIONS;

EID: 2542633672     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi049647c     Document Type: Article
Times cited : (35)

References (75)
  • 2
    • 0031746579 scopus 로고    scopus 로고
    • Role of vitronectin and its receptors in haemostasis and vascular remodeling
    • Preissner, K. T., and Seiffert, D. (1998) Role of vitronectin and its receptors in haemostasis and vascular remodeling, Thromb. Res. 89, 1-21.
    • (1998) Thromb. Res. , vol.89 , pp. 1-21
    • Preissner, K.T.1    Seiffert, D.2
  • 3
    • 0028362876 scopus 로고
    • Requirement of vascular integrin alpha v beta 3 for angiogenesis
    • Brooks, P. C., Clark, R. A., and Cheresh, D. A. (1994) Requirement of vascular integrin alpha v beta 3 for angiogenesis, Science 264, 569-571.
    • (1994) Science , vol.264 , pp. 569-571
    • Brooks, P.C.1    Clark, R.A.2    Cheresh, D.A.3
  • 4
    • 0030960367 scopus 로고    scopus 로고
    • The cell adhesion domain in plasma vitronectin is cryptic
    • Seiffert, D., and Smith, J. W. (1997) The cell adhesion domain in plasma vitronectin is cryptic, J. Biol. Chem. 272, 13705-13710.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13705-13710
    • Seiffert, D.1    Smith, J.W.2
  • 5
    • 0025340173 scopus 로고
    • Purification and functional characterization of integrin alpha v beta 5. An adhesion receptor for vitronectin
    • Smith, J. W., Vestal, D. J., Irwin, S. V., Burke, T. A., and Cheresh, D. A. (1990) Purification and functional characterization of integrin alpha v beta 5. An adhesion receptor for vitronectin, J. Biol. Chem. 265, 11008-11013.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11008-11013
    • Smith, J.W.1    Vestal, D.J.2    Irwin, S.V.3    Burke, T.A.4    Cheresh, D.A.5
  • 6
    • 0028334672 scopus 로고
    • Reversible cellular adhesion to vitronectin linked to urokinase receptor occupancy
    • Waltz, D. A., and Chapman, H. A. (1994) Reversible cellular adhesion to vitronectin linked to urokinase receptor occupancy, J. Biol. Chem. 269, 14746-14750.
    • (1994) J. Biol. Chem. , vol.269 , pp. 14746-14750
    • Waltz, D.A.1    Chapman, H.A.2
  • 7
    • 0028569183 scopus 로고
    • Identification of the urokinase receptor as an adhesion receptor for vitronectin
    • Wei, Y., Waltz, D. A., Rao, N., Drummond, R. J., Rosenberg, S., and Chapman, H. A. (1994) Identification of the urokinase receptor as an adhesion receptor for vitronectin, J. Biol. Chem. 269, 32380-32388.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32380-32388
    • Wei, Y.1    Waltz, D.A.2    Rao, N.3    Drummond, R.J.4    Rosenberg, S.5    Chapman, H.A.6
  • 8
    • 0029816265 scopus 로고    scopus 로고
    • Is plasminogen activator inhibitor-1 the molecular switch that governs urokinase receptor-mediated cell adhesion and release?
    • Deng, G., Curriden, S. A., Wang, S., Rosenberg, S., and Loskutoff, D. J. (1996) Is plasminogen activator inhibitor-1 the molecular switch that governs urokinase receptor-mediated cell adhesion and release? J. Cell Biol. 134, 1563-1571.
    • (1996) J. Cell Biol. , vol.134 , pp. 1563-1571
    • Deng, G.1    Curriden, S.A.2    Wang, S.3    Rosenberg, S.4    Loskutoff, D.J.5
  • 9
    • 0034678053 scopus 로고    scopus 로고
    • Domain 1 of the urokinase receptor (uPAR) is required for uPAR-mediated cell binding to vitronectin
    • Sidenius, N., and Blasi, F. (2000) Domain 1 of the urokinase receptor (uPAR) is required for uPAR-mediated cell binding to vitronectin, FEBS Lett. 470, 40-46.
    • (2000) FEBS Lett. , vol.470 , pp. 40-46
    • Sidenius, N.1    Blasi, F.2
  • 10
    • 0023685082 scopus 로고
    • Purification and characterization of a plasminogen activator inhibitor 1 binding protein from human plasma. Identification as a multimeric form of S protein (vitronectin)
    • Declerck, P. J., De Mol, M., Alessi, M. C., Baudner, S., Paques, E. P., Preissner, K. T., Muller-Berghaus, G., and Collen, D. (1988) Purification and characterization of a plasminogen activator inhibitor 1 binding protein from human plasma. Identification as a multimeric form of S protein (vitronectin), J. Biol. Chem. 263, 15454-15461.
    • (1988) J. Biol. Chem. , vol.263 , pp. 15454-15461
    • Declerck, P.J.1    De Mol, M.2    Alessi, M.C.3    Baudner, S.4    Paques, E.P.5    Preissner, K.T.6    Muller-Berghaus, G.7    Collen, D.8
  • 11
    • 0024213555 scopus 로고
    • Plasminogen activator inhibitor 1 (PAI) is bound to vitronectin in plasma
    • Wiman, B., Almquist, A., Sigurdardottir, O., and Lindahl, T. (1988) Plasminogen activator inhibitor 1 (PAI) is bound to vitronectin in plasma, FEBS Lett. 242, 125-128.
    • (1988) FEBS Lett. , vol.242 , pp. 125-128
    • Wiman, B.1    Almquist, A.2    Sigurdardottir, O.3    Lindahl, T.4
  • 12
    • 0024532550 scopus 로고
    • Purification of a protein from bovine plasma that binds to type 1 plasminogen activator inhibitor and prevents its interaction with extracellular matrix. Evidence that the protein is vitronectin
    • Mimuro, J., and Loskutoff, D. J. (1989) Purification of a protein from bovine plasma that binds to type 1 plasminogen activator inhibitor and prevents its interaction with extracellular matrix. Evidence that the protein is vitronectin, J. Biol. Chem. 264, 936-939.
    • (1989) J. Biol. Chem. , vol.264 , pp. 936-939
    • Mimuro, J.1    Loskutoff, D.J.2
  • 14
    • 0031054183 scopus 로고    scopus 로고
    • The use of fluorescent probes to characterize conformational changes in the interaction between vitronectin and plasminogen activator inhibitor-1
    • Gibson, A., Baburaj, K., Day, D. E., Verhamme, I., Shore, J. D., and Peterson, C. B. (1997) The use of fluorescent probes to characterize conformational changes in the interaction between vitronectin and plasminogen activator inhibitor-1, J. Biol. Chem. 272, 5112-5121.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5112-5121
    • Gibson, A.1    Baburaj, K.2    Day, D.E.3    Verhamme, I.4    Shore, J.D.5    Peterson, C.B.6
  • 15
    • 0028339118 scopus 로고
    • Localization of vitronectin binding domain in plasminogen activator inhibitor-1
    • Lawrence, D. A., Berkenpas, M. B., Palaniappan, S., and Ginsburg, D. (1994) Localization of vitronectin binding domain in plasminogen activator inhibitor-1, J. Biol. Chem. 269, 15223-15228.
    • (1994) J. Biol. Chem. , vol.269 , pp. 15223-15228
    • Lawrence, D.A.1    Berkenpas, M.B.2    Palaniappan, S.3    Ginsburg, D.4
  • 16
    • 0023930639 scopus 로고
    • Evidence for a discrete binding protein of plasminogen activator inhibitor in plasma
    • Wiman, B., Lindahl, T., and Almqvist, A. (1988) Evidence for a discrete binding protein of plasminogen activator inhibitor in plasma, Thromb. Haemostasis 59, 392-395.
    • (1988) Thromb. Haemostasis , vol.59 , pp. 392-395
    • Wiman, B.1    Lindahl, T.2    Almqvist, A.3
  • 18
    • 0029153839 scopus 로고
    • Plasminogen activator inhibitor 1 (PAI-1) in plasma: Its role in thrombotic disease
    • Wiman, B. (1995) Plasminogen activator inhibitor 1 (PAI-1) in plasma: its role in thrombotic disease, Thromb. Haemostasis 74, 71-76.
    • (1995) Thromb. Haemostasis , vol.74 , pp. 71-76
    • Wiman, B.1
  • 19
    • 0033981473 scopus 로고    scopus 로고
    • The plasminogen activation system in tumor growth, invasion, and metastasis
    • Andreasen, P. A., Egelund, R., and Petersen, H. H. (2000) The plasminogen activation system in tumor growth, invasion, and metastasis, Cell Mol. Life Sci. 57, 25-40.
    • (2000) Cell Mol. Life Sci. , vol.57 , pp. 25-40
    • Andreasen, P.A.1    Egelund, R.2    Petersen, H.H.3
  • 21
    • 0034830757 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor-1 regulates cell adhesion by binding to the somatomedin B domain of vitronectin
    • Deng, G., Curriden, S. A., Hu, G., Czekay, R. P., and Loskutoff, D. J. (2001) Plasminogen activator inhibitor-1 regulates cell adhesion by binding to the somatomedin B domain of vitronectin, J. Cell Physiol. 189, 23-33.
    • (2001) J. Cell Physiol. , vol.189 , pp. 23-33
    • Deng, G.1    Curriden, S.A.2    Hu, G.3    Czekay, R.P.4    Loskutoff, D.J.5
  • 22
    • 0029745109 scopus 로고    scopus 로고
    • The serpin PAI-1 inhibits cell migration by blocking integrin alpha V beta 3 binding to vitronectin
    • Stefansson, S., and Lawrence, D. A. (1996) The serpin PAI-1 inhibits cell migration by blocking integrin alpha V beta 3 binding to vitronectin, Nature 383, 441-443.
    • (1996) Nature , vol.383 , pp. 441-443
    • Stefansson, S.1    Lawrence, D.A.2
  • 23
    • 0000124642 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor-1 represses integrin- and vitronectin-mediated cell migration independently of its function as an inhibitor of plasminogen activation
    • Kjoller, L., Kanse, S. M., Kirkegaard, T., Rodenburg, K. W., Ronne, E., Goodman, S. L., Preissner, K. T., Ossowski, L., and Andreasen, P. A. (1997) Plasminogen activator inhibitor-1 represses integrin- and vitronectin-mediated cell migration independently of its function as an inhibitor of plasminogen activation, Exp. Cell Res. 232, 420-429.
    • (1997) Exp. Cell Res. , vol.232 , pp. 420-429
    • Kjoller, L.1    Kanse, S.M.2    Kirkegaard, T.3    Rodenburg, K.W.4    Ronne, E.5    Goodman, S.L.6    Preissner, K.T.7    Ossowski, L.8    Andreasen, P.A.9
  • 24
    • 0037416209 scopus 로고    scopus 로고
    • Plasminogen activator inhibitor-1 detaches cells from extracellular matrices by inactivating integrins
    • Czekay, R. P., Aertgeerts, K., Curriden, S. A., and Loskutoff, D. J. (2003) Plasminogen activator inhibitor-1 detaches cells from extracellular matrices by inactivating integrins, J. Cell Biol. 160, 781-791.
    • (2003) J. Cell Biol. , vol.160 , pp. 781-791
    • Czekay, R.P.1    Aertgeerts, K.2    Curriden, S.A.3    Loskutoff, D.J.4
  • 26
    • 0017880606 scopus 로고
    • Primary structure of somatomedin B: A growth hormone-dependent serum factor with protease inhibiting activity
    • Fryklund, L., and Sievertsson, H. (1978) Primary structure of somatomedin B: a growth hormone-dependent serum factor with protease inhibiting activity, FEBS Lett. 87, 55-60.
    • (1978) FEBS Lett. , vol.87 , pp. 55-60
    • Fryklund, L.1    Sievertsson, H.2
  • 28
    • 0024025429 scopus 로고
    • Identification of the collagen-binding domain of vitronectin using monoclonal antibodies
    • Izumi, M., Shimo-Oka, T., Morishita, N., Ii, I., and Hayashi, M. (1988) Identification of the collagen-binding domain of vitronectin using monoclonal antibodies, Cell Struct. Funct. 13, 217-225.
    • (1988) Cell Struct. Funct. , vol.13 , pp. 217-225
    • Izumi, M.1    Shimo-Oka, T.2    Morishita, N.3    Ii, I.4    Hayashi, M.5
  • 30
    • 0025774971 scopus 로고
    • Evidence that type 1 plasminogen activator inhibitor binds to the somatomedin B domain of vitronectin
    • Seiffert, D., and Loskutoff, D. J. (1991) Evidence that type 1 plasminogen activator inhibitor binds to the somatomedin B domain of vitronectin, J. Biol. Chem. 266, 2824-2830.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2824-2830
    • Seiffert, D.1    Loskutoff, D.J.2
  • 31
    • 0028074531 scopus 로고
    • The somatomedin B domain of vitronectin. Structural requirements for the binding and stabilization of active type 1 plasminogen activator inhibitor
    • Seiffert, D., Ciambrone, G., Wagner, N. V., Binder, B. R., and Loskutoff, D. J. (1994) The somatomedin B domain of vitronectin. Structural requirements for the binding and stabilization of active type 1 plasminogen activator inhibitor, J. Biol. Chem. 269, 2659-2666.
    • (1994) J. Biol. Chem. , vol.269 , pp. 2659-2666
    • Seiffert, D.1    Ciambrone, G.2    Wagner, N.V.3    Binder, B.R.4    Loskutoff, D.J.5
  • 33
    • 0034128121 scopus 로고    scopus 로고
    • Characterization of a complex between active plasminogen activator inhibitor-1 and N-terminal fragments of vitronectin from human placenta
    • Philips, M., Johnsen, H., and Thorsen, S. (2000) Characterization of a complex between active plasminogen activator inhibitor-1 and N-terminal fragments of vitronectin from human placenta, Fibrinolysis Proteolysis 14, 22-34.
    • (2000) Fibrinolysis Proteolysis , vol.14 , pp. 22-34
    • Philips, M.1    Johnsen, H.2    Thorsen, S.3
  • 34
    • 0037178815 scopus 로고    scopus 로고
    • Identification of the disulfide bonds in the recombinant somatomedin B domain of human vitronectin
    • Kamikubo, Y., Okumura, Y., and Loskutoff, D. J. (2002) Identification of the disulfide bonds in the recombinant somatomedin B domain of human vitronectin, J. Biol. Chem. 277, 27109-27119.
    • (2002) J. Biol. Chem. , vol.277 , pp. 27109-27119
    • Kamikubo, Y.1    Okumura, Y.2    Loskutoff, D.J.3
  • 35
    • 0029931231 scopus 로고    scopus 로고
    • Structural and functional analysis of the plasminogen activator inhibitor-1 binding motif in the somatomedin B domain of vitronectin
    • Deng, G., Royle, G., Wang, S., Crain, K., and Loskutoff, D. J. (1996) Structural and functional analysis of the plasminogen activator inhibitor-1 binding motif in the somatomedin B domain of vitronectin, J. Biol. Chem. 271, 12716-12723.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12716-12723
    • Deng, G.1    Royle, G.2    Wang, S.3    Crain, K.4    Loskutoff, D.J.5
  • 37
  • 38
    • 0035884144 scopus 로고    scopus 로고
    • A method for defining binding sites involved in protein-protein interactions: Analysis of the binding of plasminogen activator inhibitor 1 to the somatomedin domain of vitronectin
    • Royle, G., Deng, G., Seiffert, D., and Loskutoff, D. J. (2001) A method for defining binding sites involved in protein-protein interactions: analysis of the binding of plasminogen activator inhibitor 1 to the somatomedin domain of vitronectin, Anal. Biochem. 296, 245-253.
    • (2001) Anal. Biochem. , vol.296 , pp. 245-253
    • Royle, G.1    Deng, G.2    Seiffert, D.3    Loskutoff, D.J.4
  • 39
    • 0024059120 scopus 로고
    • Novel purification of vitronectin from human plasma by heparin affinity chromatography
    • Yatohgo, T., Izumi, M., Kashiwagi, H., and Hayashi, M. (1988) Novel purification of vitronectin from human plasma by heparin affinity chromatography, Cell Struct. Funct. 13, 281-292.
    • (1988) Cell Struct. Funct. , vol.13 , pp. 281-292
    • Yatohgo, T.1    Izumi, M.2    Kashiwagi, H.3    Hayashi, M.4
  • 40
    • 0028832866 scopus 로고
    • The acid stabilization of plasminogen activator inhibitor-1 depends on protonation of a single group that affects loop insertion into beta-sheet A
    • Kvassman, J. O., Lawrence, D. A., and Shore, J. D. (1995) The acid stabilization of plasminogen activator inhibitor-1 depends on protonation of a single group that affects loop insertion into beta-sheet A, J. Biol. Chem. 270, 27942-27947.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27942-27947
    • Kvassman, J.O.1    Lawrence, D.A.2    Shore, J.D.3
  • 41
    • 0026486811 scopus 로고
    • In situ neutralization in Boc-chemistry solid-phase peptide synthesis. Rapid, high yield assembly of difficult sequences
    • Schnölzer, M., Alewood, P., Jones, A., Alewood, D., and Kent, S. B. H. (1992) In situ neutralization in Boc-chemistry solid-phase peptide synthesis. Rapid, high yield assembly of difficult sequences, Int. J. Pept. Protein Res. 40, 180-193.
    • (1992) Int. J. Pept. Protein Res. , vol.40 , pp. 180-193
    • Schnölzer, M.1    Alewood, P.2    Jones, A.3    Alewood, D.4    Kent, S.B.H.5
  • 42
    • 0022289172 scopus 로고
    • Molecular cloning of S-protein, a link between complement, coagulation and cell-substrate adhesion
    • Jenne, D., and Stanley, K. K. (1985) Molecular cloning of S-protein, a link between complement, coagulation and cell-substrate adhesion, EMBO J. 4, 3153-3157.
    • (1985) EMBO J. , vol.4 , pp. 3153-3157
    • Jenne, D.1    Stanley, K.K.2
  • 43
    • 0030581701 scopus 로고    scopus 로고
    • Analysis of the disulfide linkage pattern in circulin A and B, HIV-inhibitory macrocyclic peptides
    • Derua, R., Gustafson, K. R., and Pannell, L. K. (1996) Analysis of the disulfide linkage pattern in circulin A and B, HIV-inhibitory macrocyclic peptides, Biochem. Biophys. Res. Commun. 228, 632-638.
    • (1996) Biochem. Biophys. Res. Commun. , vol.228 , pp. 632-638
    • Derua, R.1    Gustafson, K.R.2    Pannell, L.K.3
  • 44
  • 45
    • 34249765651 scopus 로고
    • NMRView: A computer program for the visualization and analysis of NMR data
    • Johnson, B. A., and Blevins, R. A. (1994) NMRView: A computer program for the visualization and analysis of NMR data, J. Biomol. NMR 4, 604-613.
    • (1994) J. Biomol. NMR , vol.4 , pp. 604-613
    • Johnson, B.A.1    Blevins, R.A.2
  • 48
    • 0032454094 scopus 로고    scopus 로고
    • Protein chemical shift analysis: A practical guide
    • Wishart, D. S., and Nip, A. M. (1998) Protein chemical shift analysis: a practical guide, Biochem. Cell Biol. 76, 153-163.
    • (1998) Biochem. Cell Biol. , vol.76 , pp. 153-163
    • Wishart, D.S.1    Nip, A.M.2
  • 50
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Güntert, P., Mumenthaler, C., and Wüthrich, K. (1997) Torsion angle dynamics for NMR structure calculation with the new program DYANA, J. Mol. Biol. 273, 283-298.
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Güntert, P.1    Mumenthaler, C.2    Wüthrich, K.3
  • 52
    • 0032922174 scopus 로고    scopus 로고
    • A modified version of the Cornell et al. force field with improved sugar pucker phases and helical repeat
    • Cheatham, T. E., III, Cieplak, P., and Kollman, P. A. (1999) A modified version of the Cornell et al. force field with improved sugar pucker phases and helical repeat, J. Biomol. Struct. Dyn. 16, 845-862.
    • (1999) J. Biomol. Struct. Dyn. , vol.16 , pp. 845-862
    • Cheatham III, T.E.1    Cieplak, P.2    Kollman, P.A.3
  • 53
    • 85047691965 scopus 로고
    • Self-consistent field-theory of solvent effect representation by continuum models - Introduction of desolvation contribution
    • Constanciel, R., and Contreras, R. (1984) Self-consistent field-theory of solvent effect representation by continuum models - introduction of desolvation contribution, Theor. Chim. Acta 65, 1-11.
    • (1984) Theor. Chim. Acta , vol.65 , pp. 1-11
    • Constanciel, R.1    Contreras, R.2
  • 54
    • 0034701222 scopus 로고    scopus 로고
    • Molecular simulations of nucleic acids using a generalized Born solvation model
    • Tsui, V., and Case, D. A. (2000) Molecular simulations of nucleic acids using a generalized Born solvation model, J. Am. Chem. Soc. 122, 2489-2498.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 2489-2498
    • Tsui, V.1    Case, D.A.2
  • 55
    • 14244273182 scopus 로고    scopus 로고
    • Theory and applications of the generalized born solvation model in macromolecular simulations
    • Tsui, V., and Case, D. A. (2000) Theory and applications of the generalized born solvation model in macromolecular simulations, Biopolymers 56, 275-291.
    • (2000) Biopolymers , vol.56 , pp. 275-291
    • Tsui, V.1    Case, D.A.2
  • 56
    • 0036234027 scopus 로고    scopus 로고
    • Comparison of solution structures refined by molecular dynamics simulation in a vacuum, with a generalized Born model and with explicit water
    • Xia, B., Tsui, V., Case, D. A., Dyson, H. J., and Wright, P. E. (2002) Comparison of solution structures refined by molecular dynamics simulation in a vacuum, with a generalized Born model and with explicit water, J. Biomol. NMR 22, 317-331.
    • (2002) J. Biomol. NMR , vol.22 , pp. 317-331
    • Xia, B.1    Tsui, V.2    Case, D.A.3    Dyson, H.J.4    Wright, P.E.5
  • 57
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski, R. A., Rullmann, J. A. C., MacArthur, M. W., Kaptein, R., and Thornton, J. M. (1996) AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR, J. Biomol. NMR 8, 477-486.
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmann, J.A.C.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 58
    • 0030039296 scopus 로고    scopus 로고
    • PROMOTIF - A program to identify and analyze structural motifs in proteins
    • Hutchinson, E. G., and Thornton, J. M. (1996) PROMOTIF-A program to identify and analyze structural motifs in proteins, Protein Sci. 5, 212-220.
    • (1996) Protein Sci. , vol.5 , pp. 212-220
    • Hutchinson, E.G.1    Thornton, J.M.2
  • 59
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi, R., Billeter, M., and Wüthrich, K. (1996) MOLMOL: A program for display and analysis of macromolecular structures, J. Mol. Graphics 14, 51-55.
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 60
    • 0026319199 scopus 로고
    • Protein folding and association: Insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls, A., Sharp, K. A., and Honig, B. (1991) Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons, Proteins 11, 281-296.
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 61
    • 0037133165 scopus 로고    scopus 로고
    • A method for optimizing potential-energy functions by a hierarchical design of the potential-energy landscape: Application to the UNRES force field
    • Liwo, A., Arlukowicz, P., Czaplewski, C., Oldziej, S., Pillardy, J., and Scheraga, H. A. (2002) A method for optimizing potential-energy functions by a hierarchical design of the potential-energy landscape: application to the UNRES force field, Proc. Natl. Acad. Sci. U.S.A. 99, 1937-1942.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 1937-1942
    • Liwo, A.1    Arlukowicz, P.2    Czaplewski, C.3    Oldziej, S.4    Pillardy, J.5    Scheraga, H.A.6
  • 62
    • 0001176785 scopus 로고    scopus 로고
    • New optimization method for conformational energy calculations on polypeptides: Conformational space annealing
    • Lee, J., Scheraga, H. A., and Rackovsky, S. (1997) New optimization method for conformational energy calculations on polypeptides: Conformational space annealing, J. Comput. Chem. 18, 1222-1232.
    • (1997) J. Comput. Chem. , vol.18 , pp. 1222-1232
    • Lee, J.1    Scheraga, H.A.2    Rackovsky, S.3
  • 64
    • 0037438462 scopus 로고    scopus 로고
    • Addition of side chains to a known backbone with defined side-chain centroids
    • Kazmierkiewicz, R., Liwo, A., and Scheraga, H. A. (2003) Addition of side chains to a known backbone with defined side-chain centroids, Biophys. Chem. 100, 261-280.
    • (2003) Biophys. Chem. , vol.100 , pp. 261-280
    • Kazmierkiewicz, R.1    Liwo, A.2    Scheraga, H.A.3
  • 66
    • 0022336792 scopus 로고
    • Calculation of protein conformations by proton-proton distance constraints. A new efficient algorithm
    • Braun, W., and Go, N. (1985) Calculation of protein conformations by proton-proton distance constraints. A new efficient algorithm, J. Mol. Biol. 186, 611-626.
    • (1985) J. Mol. Biol. , vol.186 , pp. 611-626
    • Braun, W.1    Go, N.2
  • 67
    • 0000408363 scopus 로고    scopus 로고
    • Approximate atomic surfaces from linear combinations of pairwise overlaps (LCPO)
    • Weiser, J., Shenkin, P. S., and Still, W. C. (1999) Approximate atomic surfaces from linear combinations of pairwise overlaps (LCPO), J. Comput. Chem. 20, 217-230.
    • (1999) J. Comput. Chem. , vol.20 , pp. 217-230
    • Weiser, J.1    Shenkin, P.S.2    Still, W.C.3
  • 68
    • 0034671463 scopus 로고    scopus 로고
    • Structure of the PHD zinc finger from human Williams-Beuren syndrome transcription factor
    • Pascual, J., Martinez-Yamout, M., Dyson, H. J., and Wright, P. E. (2000) Structure of the PHD zinc finger from human Williams-Beuren syndrome transcription factor, J. Mol. Biol. 304, 723-729.
    • (2000) J. Mol. Biol. , vol.304 , pp. 723-729
    • Pascual, J.1    Martinez-Yamout, M.2    Dyson, H.J.3    Wright, P.E.4
  • 69
    • 0035029325 scopus 로고    scopus 로고
    • SANE (Structure assisted NOE evaluation): An automated model-based approach for NOE assignment
    • Duggan, B. M., Legge, G. B., Dyson, H. J., and Wright, P. E. (2001) SANE (Structure assisted NOE evaluation): an automated model-based approach for NOE assignment, J. Biomol. NMR 19, 321-329.
    • (2001) J. Biomol. NMR , vol.19 , pp. 321-329
    • Duggan, B.M.1    Legge, G.B.2    Dyson, H.J.3    Wright, P.E.4
  • 70
    • 0028912190 scopus 로고
    • A fluorescent probe study of plasminogen activator inhibitor-1. Evidence for reactive center loop insertion and its role in the inhibitory mechanism
    • Shore, J. D., Day, D. E., Francis-Chmura, A. M., Verhamme, I., Kvassman, J., Lawrence, D. A., and Ginsburg, D. (1995) A fluorescent probe study of plasminogen activator inhibitor-1. Evidence for reactive center loop insertion and its role in the inhibitory mechanism, J. Biol. Chem. 270, 5395-5398.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5395-5398
    • Shore, J.D.1    Day, D.E.2    Francis-Chmura, A.M.3    Verhamme, I.4    Kvassman, J.5    Lawrence, D.A.6    Ginsburg, D.7
  • 71
    • 0036005954 scopus 로고    scopus 로고
    • The molecular basis for anti-proteolytic and non-proteolytic functions of plasminogen activator inhibitor type-1: Roles of the reactive centre loop, the shutter region, the flexible joint region and the small serpin fragment
    • Wind, T., Hansen, M., Jensen, J. K., and Andreasen, P. A. (2002) The molecular basis for anti-proteolytic and non-proteolytic functions of plasminogen activator inhibitor type-1: roles of the reactive centre loop, the shutter region, the flexible joint region and the small serpin fragment, Biol. Chem. 383, 21-36.
    • (2002) Biol. Chem. , vol.383 , pp. 21-36
    • Wind, T.1    Hansen, M.2    Jensen, J.K.3    Andreasen, P.A.4
  • 72
    • 0033081498 scopus 로고    scopus 로고
    • The active conformation of plasminogen activator inhibitor 1, a target for drugs to control fibrinolysis and cell adhesion
    • Sharp, A. M., Stein, P. E., Pannu, N. S., Carrell, R. W., Berkenpas, M. B., Ginsburg, D., Lawrence, D. A., and Read, R. J. (1999) The active conformation of plasminogen activator inhibitor 1, a target for drugs to control fibrinolysis and cell adhesion, Structure 7, 111-118.
    • (1999) Structure , vol.7 , pp. 111-118
    • Sharp, A.M.1    Stein, P.E.2    Pannu, N.S.3    Carrell, R.W.4    Berkenpas, M.B.5    Ginsburg, D.6    Lawrence, D.A.7    Read, R.J.8
  • 73
    • 0032522374 scopus 로고    scopus 로고
    • Functional effects of single amino acid substitutions in the region of Phe113 to Asp138 in the plasminogen activator inhibitor 1 molecule
    • Sui, G. C., and Wiman, B. (1998) Functional effects of single amino acid substitutions in the region of Phe113 to Asp138 in the plasminogen activator inhibitor 1 molecule, Biochem. J. 331 (Pt 2), 409-415.
    • (1998) Biochem. J. , vol.331 , Issue.PART 2 , pp. 409-415
    • Sui, G.C.1    Wiman, B.2
  • 74
    • 0037134909 scopus 로고    scopus 로고
    • The vitronectin binding area of plasminogen activator inhibitor-1, mapped by mutagenesis and protection against an inactivating organochemical ligand
    • Jensen, J. K., Wind, T., and Andreasen, P. A. (2002) The vitronectin binding area of plasminogen activator inhibitor-1, mapped by mutagenesis and protection against an inactivating organochemical ligand, FEBS Lett. 521, 91-94.
    • (2002) FEBS Lett. , vol.521 , pp. 91-94
    • Jensen, J.K.1    Wind, T.2    Andreasen, P.A.3


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