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Volumn 48, Issue 30, 2009, Pages 7110-7122

Biophysical investigation of GpIbα binding to thrombin anion binding exosite II

Author keywords

[No Author keywords available]

Indexed keywords

ANALYTICAL ULTRACENTRIFUGATION; ANION BINDING; COFACTORS; CONFORMATIONAL EFFECT; D LINES; EXOSITES; HYDROGEN-DEUTERIUM EXCHANGE; MALDI TOF MS; MEMBRANE-BOUND RECEPTORS; NMR STUDIES; SERINE PROTEASE; STRUCTURAL FEATURE;

EID: 68049110271     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900745b     Document Type: Article
Times cited : (17)

References (93)
  • 2
    • 28044444092 scopus 로고    scopus 로고
    • The structure of thrombin, a chameleon-like proteinase
    • Bode, W. (2005) The structure of thrombin, a chameleon-like proteinase. J. Thromb. Haemostasis 3, 2379-2388.
    • (2005) J. Thromb. Haemostasis , vol.3 , pp. 2379-2388
    • Bode, W.1
  • 3
    • 27144505651 scopus 로고    scopus 로고
    • Molecular recognition mechanisms of thrombin
    • Huntington, J. A. (2005) Molecular recognition mechanisms of thrombin. J. Thromb. Haemostasis 3, 1861-1872.
    • (2005) J. Thromb. Haemostasis , vol.3 , pp. 1861-1872
    • Huntington, J.A.1
  • 4
    • 17444392120 scopus 로고    scopus 로고
    • Fibrinogen and fibrin
    • Weisel, J. W. (2005) Fibrinogen and fibrin. Adv. Protein Chem. 70, 247-299.
    • (2005) Adv. Protein Chem. , vol.70 , pp. 247-299
    • Weisel, J.W.1
  • 5
    • 0034921205 scopus 로고    scopus 로고
    • Protease-activated receptors in vascular biology
    • Coughlin, S. R. (2001) Protease-activated receptors in vascular biology. Thromb. Haemostasis 86, 298-307.
    • (2001) Thromb. Haemostasis , vol.86 , pp. 298-307
    • Coughlin, S.R.1
  • 6
    • 0141819138 scopus 로고    scopus 로고
    • The protein C pathway
    • Esmon, C. T. (2003) The protein C pathway. Chest 124, 26S-32S.
    • (2003) Chest , vol.124
    • Esmon, C.T.1
  • 7
    • 33646477150 scopus 로고    scopus 로고
    • The structure of thrombin: A janus-headed proteinase
    • Bode, W. (2006) The structure of thrombin: A janus-headed proteinase. Semin. Thromb. Hemostasis 32 (Suppl. 1), 16-31.
    • (2006) Semin. Thromb. Hemostasis , vol.32 , Issue.SUPPL. 1 , pp. 16-31
    • Bode, W.1
  • 8
    • 0027050807 scopus 로고
    • The refined 1.9-Å X-ray crystal structure of D-Phe-Pro-Arg chloromethylketone-inhibited human α-thrombin: Structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships
    • Bode, W., Turk, D., and Karshikov, A. (1992) The refined 1.9-Å X-ray crystal structure of D-Phe-Pro-Arg chloromethylketone-inhibited human α-thrombin: Structure analysis, overall structure, electrostatic properties, detailed active-site geometry, and structure-function relationships. Protein Sci. 1, 426-471.
    • (1992) Protein Sci. , vol.1 , pp. 426-471
    • Bode, W.1    Turk, D.2    Karshikov, A.3
  • 10
    • 34447529128 scopus 로고    scopus 로고
    • A short history of platelet glycoprotein Ib complex
    • Clemetson, K. J. (2007) A short history of platelet glycoprotein Ib complex. Thromb. Haemostasis 98, 63-68.
    • (2007) Thromb. Haemostasis , vol.98 , pp. 63-68
    • Clemetson, K.J.1
  • 14
    • 0035818425 scopus 로고    scopus 로고
    • Structural and functional mapping of the thrombin domain involved in the binding to the platelet glycoprotein Ib
    • DOI 10.1021/bi010491f
    • De Cristofaro, R., De Candia, E., Landolfi, R., Rutella, S., and Hall, S. W. (2001) Structural and functional mapping of the thrombin domain involved in the binding to the platelet glycoprotein Ib. Biochemistry 40, 13268-13273. (Pubitemid 33043542)
    • (2001) Biochemistry , vol.40 , Issue.44 , pp. 13268-13273
    • De Cristofaro, R.1    De Candia, E.2    Landolfi, R.3    Rutella, S.4    Hall, S.W.5
  • 15
    • 0035794133 scopus 로고    scopus 로고
    • Platelet glycoprotein Ib α binds to thrombin anion-binding exosite II inducing allosteric changes in the activity of thrombin
    • Li, C. Q., Vindigni, A., Sadler, J. E., and Wardell, M. R. (2001) Platelet glycoprotein Ib α binds to thrombin anion-binding exosite II inducing allosteric changes in the activity of thrombin. J. Biol. Chem. 276, 6161-6168.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6161-6168
    • Li, C.Q.1    Vindigni, A.2    Sadler, J.E.3    Wardell, M.R.4
  • 16
    • 0346850827 scopus 로고    scopus 로고
    • Thrombin activation of factor XI on activated platelets requires the interaction of factor XI and platelet glycoprotein Ib α with thrombin anion-binding exosites I and II, respectively
    • Yun, T. H., Baglia, F. A., Myles, T., Navaneetham, D., Lopez, J. A., Walsh, P. N., and Leung, L. L. (2003) Thrombin activation of factor XI on activated platelets requires the interaction of factor XI and platelet glycoprotein Ib α with thrombin anion-binding exosites I and II, respectively. J. Biol. Chem. 278, 48112-48119.
    • (2003) J. Biol. Chem. , vol.278 , pp. 48112-48119
    • Yun, T.H.1    Baglia, F.A.2    Myles, T.3    Navaneetham, D.4    Lopez, J.A.5    Walsh, P.N.6    Leung, L.L.7
  • 17
    • 0031825436 scopus 로고    scopus 로고
    • Characteristics of the interaction between thrombin exosite 1 and the sequence 269-297 of platelet glycoprotein Ibα
    • Bouton, M. C., Thurieau, C., Guillin, M. C., and Jandrot-Perrus, M. (1998) Characteristics of the interaction between thrombin exosite 1 and the sequence 269-287 [correction of 269-297] of platelet glycoprotein Ibα. Thromb. Haemostasis 80, 310-315. (Pubitemid 28393629)
    • (1998) Thrombosis and Haemostasis , vol.80 , Issue.2 , pp. 310-315
    • Bouton, M.-C.1    Thurieau, C.2    Guillin, M.-C.3    Jandrot-Perrus, M.4
  • 19
    • 0025859659 scopus 로고
    • Effect of the hirudin carboxy-terminal peptide 54-65 on the interaction of thrombin with platelets
    • Jandrot-Perrus, M., Huisse, M. G., Krstenansky, J. L., Bezeaud, A., and Guillin, M. C. (1991) Effect of the hirudin carboxy-terminal peptide 54-65 on the interaction of thrombin with platelets. Thromb. Haemostasis 66, 300-305.
    • (1991) Thromb. Haemostasis , vol.66 , pp. 300-305
    • Jandrot-Perrus, M.1    Huisse, M.G.2    Krstenansky, J.L.3    Bezeaud, A.4    Guillin, M.C.5
  • 20
    • 0027053116 scopus 로고
    • Electrostatic interactions in the association of proteins: An analysis of the thrombin-hirudin complex
    • Karshikov, A., Bode, W., Tulinsky, A., and Stone, S. R. (1992) Electrostatic interactions in the association of proteins: An analysis of the thrombin-hirudin complex. Protein Sci. 1, 727-735. (Pubitemid 23007312)
    • (1992) Protein Science , vol.1 , Issue.6 , pp. 727-735
    • Karshikov, A.1    Bode, W.2    Tulinsky, A.3    Stone, S.R.4
  • 21
    • 0028181751 scopus 로고
    • Localization and characterization of an α-thrombin-binding site on platelet glycoprotein Ib α
    • De Marco, L., Mazzucato, M., Masotti, A., and Ruggeri, Z. M. (1994) Localization and characterization of an α-thrombin-binding site on platelet glycoprotein Ib α. J. Biol. Chem. 269, 6478-6484.
    • (1994) J. Biol. Chem. , vol.269 , pp. 6478-6484
    • De Marco, L.1    Mazzucato, M.2    Masotti, A.3    Ruggeri, Z.M.4
  • 22
    • 0026458485 scopus 로고
    • Thrombin interaction with platelet glycoprotein Ib: Effect of glycocalicin on thrombin specificity
    • Jandrot-Perrus, M., Clemetson, K. J., Huisse, M. G., and Guillin, M. C. (1992) Thrombin interaction with platelet glycoprotein Ib: Effect of glycocalicin on thrombin specificity. Blood 80, 2781-2786.
    • (1992) Blood , vol.80 , pp. 2781-2786
    • Jandrot-Perrus, M.1    Clemetson, K.J.2    Huisse, M.G.3    Guillin, M.C.4
  • 23
    • 0035895962 scopus 로고    scopus 로고
    • Binding of thrombin to glycoprotein Ib accelerates the hydrolysis of Par-1 on intact platelets
    • De Candia, E., Hall, S. W., Rutella, S., Landolfi, R., Andrews, R. K., and De Cristofaro, R. (2001) Binding of thrombin to glycoprotein Ib accelerates the hydrolysis of Par-1 on intact platelets. J. Biol. Chem. 276, 4692-4698.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4692-4698
    • De Candia, E.1    Hall, S.W.2    Rutella, S.3    Landolfi, R.4    Andrews, R.K.5    De Cristofaro, R.6
  • 24
    • 0041344493 scopus 로고    scopus 로고
    • Interaction of the 268-282 region of glycoprotein Ibα with the heparin-binding site of thrombin inhibits the enzyme activation of factor VIII
    • DOI 10.1042/BJ20030167
    • De Cristofaro, R., and De Filippis, V. (2003) Interaction of the 268-282 region of glycoprotein Ibα with the heparin-binding site of thrombin inhibits the enzyme activation of factor VIII. Biochem. J. 373, 593-601. (Pubitemid 36897861)
    • (2003) Biochemical Journal , vol.373 , Issue.2 , pp. 593-601
    • De Cristofaro, R.1    De Filippis, V.2
  • 25
    • 0037815126 scopus 로고    scopus 로고
    • Modulation of α-thrombin function by distinct interactions with platelet glycoprotein Ibα
    • DOI 10.1126/science.1084183
    • Celikel, R., McClintock, R. A., Roberts, J. R., Mendolicchio, G. L., Ware, J., Varughese, K. I., and Ruggeri, Z. M. (2003) Modulation of α-thrombin function by distinct interactions with platelet glycoprotein Ibα. Science 301, 218-221. (Pubitemid 36858476)
    • (2003) Science , vol.301 , Issue.5630 , pp. 218-221
    • Celikel, R.1    McClintock, R.A.2    Roberts, J.R.3    Mendolicchio, G.L.4    Ware, J.5    Varughese, K.I.6    Ruggeri, Z.M.7
  • 26
    • 0038157329 scopus 로고    scopus 로고
    • Crystal structure of the Gplbα-thrombin complex essential for platelet aggregation
    • DOI 10.1126/science.1083917
    • Dumas, J. J., Kumar, R., Seehra, J., Somers, W. S., and Mosyak, L. (2003) Crystal structure of the GpIbα-thrombin complex essential for platelet aggregation. Science 301, 222-226. (Pubitemid 36868962)
    • (2003) Science , vol.301 , Issue.5630 , pp. 222-226
    • Dumas, J.J.1    Kumar, R.2    Seehra, J.3    Somers, W.S.4    Mosyak, L.5
  • 27
    • 0023918947 scopus 로고
    • Localization of the binding site on fibrin for the secondary binding site of thrombin
    • Vali, Z., and Scheraga, H. A. (1988) Localization of the binding site on fibrin for the secondary binding site of thrombin. Biochemistry 27, 1956-1963. (Pubitemid 18102033)
    • (1988) Biochemistry , vol.27 , Issue.6 , pp. 1956-1963
    • Vali, Z.1    Scheraga, H.A.2
  • 29
    • 0037821812 scopus 로고    scopus 로고
    • Evidence that both exosites on thrombin participate in its high affinity interaction with fibrin
    • Pospisil, C. H., Stafford, A. R., Fredenburgh, J. C., and Weitz, J. I. (2003) Evidence that both exosites on thrombin participate in its high affinity interaction with fibrin. J. Biol. Chem. 278, 21584-21591.
    • (2003) J. Biol. Chem. , vol.278 , pp. 21584-21591
    • Pospisil, C.H.1    Stafford, A.R.2    Fredenburgh, J.C.3    Weitz, J.I.4
  • 30
    • 0034964447 scopus 로고    scopus 로고
    • The structure and biological features of fibrinogen and fibrin
    • Mosesson, M. W., Siebenlist, K. R., and Meh, D. A. (2001) The structure and biological features of fibrinogen and fibrin. Ann. N.Y. Acad. Sci. 936, 11-30.
    • (2001) Ann. N.Y. Acad. Sci. , vol.936 , pp. 11-30
    • Mosesson, M.W.1    Siebenlist, K.R.2    Meh, D.A.3
  • 31
    • 0021184750 scopus 로고
    • γ and γ′ chains of human fibrinogen are produced by alternative mRNA processing
    • Chung, D. W., and Davie, E. W. (1984) γ and γ′ chains of human fibrinogen are produced by alternative mRNA processing. Biochemistry 23, 4232-4236.
    • (1984) Biochemistry , vol.23 , pp. 4232-4236
    • Chung, D.W.1    Davie, E.W.2
  • 32
    • 0021744551 scopus 로고
    • Structure of the human γ-fibrinogen gene. Alternate mRNA splicing near the 30 end of the gene produces γA and γB forms of γ-fibrinogen
    • Fornace, A. J.Jr., Cummings, D. E., Comeau, C. M., Kant, J. A., and Crabtree, G. R. (1984) Structure of the human γ-fibrinogen gene. Alternate mRNA splicing near the 30 end of the gene produces γA and γB forms of γ-fibrinogen. J. Biol. Chem. 259, 12826-12830.
    • (1984) J. Biol. Chem. , vol.259 , pp. 12826-12830
    • Fornace Jr., A.J.1    Cummings, D.E.2    Comeau, C.M.3    Kant, J.A.4    Crabtree, G.R.5
  • 34
    • 0001452932 scopus 로고
    • Biochemical and chromatographic studies of certain activities associated with human fibrinogen preparations
    • Mosesson, M. W., and Finlayson, J. S. (1963) Biochemical and chromatographic studies of certain activities associated with human fibrinogen preparations. J. Clin. Invest. 42, 747-755.
    • (1963) J. Clin. Invest. , vol.42 , pp. 747-755
    • Mosesson, M.W.1    Finlayson, J.S.2
  • 35
    • 34147133409 scopus 로고    scopus 로고
    • Elevated plasma fibrinogen γ′ concentration is associated with myocardial infarction: Effects of variation in fibrinogen genes and environmental factors
    • DOI 10.1111/j.1538-7836.2007.02406.x
    • Mannila, M. N., Lovely, R. S., Kazmierczak, S. C., Eriksson, P., Samnegard, A., Farrell, D. H., Hamsten, A., and Silveira, A. (2007) Elevated plasma fibrinogen γ′ concentration is associated with myocardial infarction: Effects of variation in fibrinogen genes and environmental factors. J. Thromb. Haemostasis 5, 766-773. (Pubitemid 46563576)
    • (2007) Journal of Thrombosis and Haemostasis , vol.5 , Issue.4 , pp. 766-773
    • Mannila, M.N.1    Lovely, R.S.2    Kazmierczak, S.C.3    Eriksson, P.4    Samnegard, A.5    Farrell, D.H.6    Hamsten, A.7    Silveira, A.8
  • 37
    • 28844473918 scopus 로고    scopus 로고
    • Genetic variation in the fibrinogen γ gene increases the risk for deep venous thrombosis by reducing plasma fibrinogen γ′ levels
    • Uitte de Willige, S., de Visser, M. C., Houwing-Duistermaat, J. J., Rosendaal, F.R., Vos,H.L., and Bertina, R.M. (2005)Genetic variation in the fibrinogen γ gene increases the risk for deep venous thrombosis by reducing plasma fibrinogen γ′ levels. Blood 106, 4176-4183.
    • (2005) Blood , vol.106 , pp. 4176-4183
    • De Uitte Willige, S.1    De Visser, M.C.2    Houwing-Duistermaat, J.J.3    Rosendaal, F.R.4    Vos, H.L.5    Bertina, R.M.6
  • 38
    • 33745144292 scopus 로고    scopus 로고
    • Conformational analysis of γ′ peptide (410-427) interactions with thrombin anion binding exosite II
    • Sabo, T. M., Farrell, D. H., and Maurer, M. C. (2006) Conformational analysis of γ′ peptide (410-427) interactions with thrombin anion binding exosite II. Biochemistry 45, 7434-7445.
    • (2006) Biochemistry , vol.45 , pp. 7434-7445
    • Sabo, T.M.1    Farrell, D.H.2    Maurer, M.C.3
  • 40
    • 0022521744 scopus 로고
    • Kinetics of the inhibition of thrombin by hirudin
    • Stone, S. R., and Hofsteenge, J. (1986) Kinetics of the inhibition of thrombin by hirudin. Biochemistry 25, 4622-4628.
    • (1986) Biochemistry , vol.25 , pp. 4622-4628
    • Stone, S.R.1    Hofsteenge, J.2
  • 41
    • 0034617203 scopus 로고    scopus 로고
    • Examining thrombin hydrolysis of the factor XIII activation peptide segment leads to a proposal for explaining the cardioprotective effects observed with the factor XIII V34L mutation
    • Trumbo, T. A., and Maurer, M. C. (2000) Examining thrombin hydrolysis of the factor XIII activation peptide segment leads to a proposal for explaining the cardioprotective effects observed with the factor XIII V34L mutation. J. Biol. Chem. 275, 20627-20631.
    • (2000) J. Biol. Chem. , vol.275 , pp. 20627-20631
    • Trumbo, T.A.1    Maurer, M.C.2
  • 42
    • 2442419061 scopus 로고    scopus 로고
    • Allosteric Changes in Solvent Accessibility Observed in Thrombin upon Active Site Occupation
    • DOI 10.1021/bi0499718
    • Croy, C. H., Koeppe, J. R., Bergqvist, S., and Komives, E. A. (2004) Allosteric changes in solvent accessibility observed in thrombin upon active site occupation. Biochemistry 43, 5246-5255. (Pubitemid 38620916)
    • (2004) Biochemistry , vol.43 , Issue.18 , pp. 5246-5255
    • Croy, C.H.1    Koeppe, J.R.2    Bergqvist, S.3    Komives, E.A.4
  • 43
    • 0029151607 scopus 로고
    • Thrombin-Bound Structures of Designed Analogs of Human Fibrinopeptide-A Determined by Quantitative Transferred Noe Spectroscopy: A New Structural Basis for Thrombin Specificity
    • Ni, F., Zhu, Y., and Scheraga, H. A. (1995) Thrombin-Bound Structures of Designed Analogs of Human Fibrinopeptide-A Determined by Quantitative Transferred Noe Spectroscopy: A New Structural Basis for Thrombin Specificity. J. Mol. Biol. 252, 656-671.
    • (1995) J. Mol. Biol. , vol.252 , pp. 656-671
    • Ni, F.1    Zhu, Y.2    Scheraga, H.A.3
  • 44
    • 0024544276 scopus 로고
    • High-resolution NMR studies of fibrinogen-like peptides in solution: Structure of a thrombin-bound peptide corresponding to residues 716 of the Aα chain of human fibrinogen
    • DOI 10.1021/bi00433a053
    • Ni, F., Meinwald, Y. C., Vasquez, M., and Scheraga, H. A. (1989) High-resolution NMR studies of fibrinogen-like peptides in solution: Structure of a thrombin-bound peptide corresponding to residues 7-16 of the A α chain of human fibrinogen. Biochemistry 28, 3094-3105. (Pubitemid 19099493)
    • (1989) Biochemistry , vol.28 , Issue.7 , pp. 3094-3105
    • Ni, F.1    Meinwald, Y.C.2    Vasquez, M.3    Scheraga, H.A.4
  • 45
    • 0026459469 scopus 로고
    • Solution structure of a platelet receptor peptide bound to bovine α-thrombin
    • Ni, F., Ripoll, D. R., Martin, P. D., and Edwards, B. F. (1992) Solution structure of a platelet receptor peptide bound to bovine α-thrombin. Biochemistry 31, 11551-11557.
    • (1992) Biochemistry , vol.31 , pp. 11551-11557
    • Ni, F.1    Ripoll, D.R.2    Martin, P.D.3    Edwards, B.F.4
  • 46
    • 0026657151 scopus 로고
    • The structure of residues 7-16 of the a α-chain of human fibrinogen bound to bovine thrombin at 2.3-Å resolution
    • Martin, P. D., Robertson, W., Turk, D., Huber, R., Bode, W., and Edwards, B. F. (1992) The structure of residues 7-16 of the A α-chain of human fibrinogen bound to bovine thrombin at 2.3-Å resolution. J. Biol. Chem. 267, 7911-7920.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7911-7920
    • Martin, P.D.1    Robertson, W.2    Turk, D.3    Huber, R.4    Bode, W.5    Edwards, B.F.6
  • 47
    • 0028209977 scopus 로고
    • Crystallographic structures of thrombin complexed with thrombin receptor peptides: Existence of expected and novel binding modes
    • Mathews, I. I., Padmanabhan, K. P., Ganesh, V., Tulinsky, A., Ishii, M., Chen, J., Turck, C. W., Coughlin, S. R., and Fenton, J. W.II (1994) Crystallographic structures of thrombin complexed with thrombin receptor peptides: Existence of expected and novel binding modes. Biochemistry 33, 3266-3279. (Pubitemid 24112639)
    • (1994) Biochemistry , vol.33 , Issue.11 , pp. 3266-3279
    • Mathews, I.I.1    Padmanabhan, K.P.2    Ganesh, V.3    Tulinsky, A.4
  • 48
    • 0345483182 scopus 로고
    • 2-Dimensional Transferred Nuclear-Overhauser-Effects with Incomplete Averaging of Free-Ligand and Bound-Ligand Resonances
    • Ni, F. (1995) 2-Dimensional Transferred Nuclear-Overhauser-Effects with Incomplete Averaging of Free-Ligand and Bound-Ligand Resonances. J. Magn. Reson., Ser. B 106, 147-155.
    • (1995) J. Magn. Reson., Ser. B , vol.106 , pp. 147-155
    • Ni, F.1
  • 49
    • 12044258461 scopus 로고
    • Use of the Transferred Nuclear Overhauser Effect to Determine the Conformations of Ligands Bound to Proteins
    • Ni, F., and Scheraga, H. A. (1994) Use of the Transferred Nuclear Overhauser Effect to Determine the Conformations of Ligands Bound to Proteins. Acc. Chem. Res. 27, 257-264.
    • (1994) Acc. Chem. Res. , vol.27 , pp. 257-264
    • Ni, F.1    Scheraga, H.A.2
  • 50
    • 33644866813 scopus 로고    scopus 로고
    • Structural basis for reduced staphylocoagulase-mediated bovine prothrombin activation
    • Friedrich, R., Panizzi, P., Kawabata, S., Bode, W., Bock, P. E., and Fuentes-Prior, P. (2006) Structural basis for reduced staphylocoagulase-mediated bovine prothrombin activation. J. Biol. Chem. 281, 1188-1195.
    • (2006) J. Biol. Chem. , vol.281 , pp. 1188-1195
    • Friedrich, R.1    Panizzi, P.2    Kawabata, S.3    Bode, W.4    Bock, P.E.5    Fuentes-Prior, P.6
  • 51
    • 34548475092 scopus 로고    scopus 로고
    • Perturbations in Factor XIII Resulting from Activation and Inhibition Examined by Solution Based Methods and Detected by MALDI-TOF MS
    • Sabo, T. M., Brasher, P. B., and Maurer, M. C. (2007) Perturbations in Factor XIII Resulting from Activation and Inhibition Examined by Solution Based Methods and Detected by MALDI-TOF MS. Biochemistry 46, 10089-10101.
    • (2007) Biochemistry , vol.46 , pp. 10089-10101
    • Sabo, T.M.1    Brasher, P.B.2    Maurer, M.C.3
  • 52
    • 0035061716 scopus 로고    scopus 로고
    • Amide hydrogen exchange shows that malate dehydrogenase is a folded monomer at pH 5
    • DOI 10.1110/ps.53201
    • Chen, J., and Smith, D. L. (2001) Amide hydrogen exchange shows that malate dehydrogenase is a folded monomer at pH 5. Protein Sci. 10, 1079-1083. (Pubitemid 32367499)
    • (2001) Protein Science , vol.10 , Issue.5 , pp. 1079-1083
    • Chen, J.1    Smith, D.L.2
  • 53
    • 0035019857 scopus 로고    scopus 로고
    • Detecting structural changes in viral capsids by hydrogen exchange and mass spectrometry
    • DOI 10.1110/ps.100101
    • Wang, L., Lane, L. C., and Smith, D. L. (2001) Detecting structural changes in viral capsids by hydrogen exchange and mass spectrometry. Protein Sci. 10, 1234-1243. (Pubitemid 32476484)
    • (2001) Protein Science , vol.10 , Issue.6 , pp. 1234-1243
    • Wang, L.1    Lane, L.C.2    Smith, D.L.3
  • 54
    • 0037172780 scopus 로고    scopus 로고
    • Evaluating the roles of thrombin and calcium in the activation of coagulation factor XIII using H/D exchange and MALDI-TOF MS
    • Turner, B. T.Jr., and Maurer, M. C. (2002) Evaluating the roles of thrombin and calcium in the activation of coagulation factor XIII using H/D exchange and MALDI-TOF MS. Biochemistry 41, 7947-7954.
    • (2002) Biochemistry , vol.41 , pp. 7947-7954
    • Turner Jr., B.T.1    Maurer, M.C.2
  • 55
    • 0036707991 scopus 로고    scopus 로고
    • Modern analytical ultracentrifugation in protein science: A tutorial review
    • DOI 10.1110/ps.0207702
    • Lebowitz, J., Lewis, M. S., and Schuck, P. (2002) Modern analytical ultracentrifugation in protein science: A tutorial review. Protein Sci. 11, 2067-2079. (Pubitemid 34919611)
    • (2002) Protein Science , vol.11 , Issue.9 , pp. 2067-2079
    • Lebowitz, J.1    Lewis, M.S.2    Schuck, P.3
  • 56
    • 0033474495 scopus 로고    scopus 로고
    • Modeling deuterium exchange behavior of ERK2 using pepsin mapping to probe secondary structure
    • Resing, K. A., Hoofnagle, A. N., and Ahn, N. G. (1999) Modeling deuterium exchange behavior of ERK2 using pepsin mapping to probe secondary structure. J. Am. Soc. Mass Spectrom. 10, 685-702.
    • (1999) J. Am. Soc. Mass Spectrom. , vol.10 , pp. 685-702
    • Resing, K.A.1    Hoofnagle, A.N.2    Ahn, N.G.3
  • 57
    • 0034733386 scopus 로고    scopus 로고
    • Correlated motions in native proteins from MS analysis of NH exchange: Evidence for a manifold of unfolding reactions in ovomucoid third domain
    • Arrington, C. B., and Robertson, A. D. (2000) Correlated motions in native proteins from MS analysis of NH exchange: Evidence for a manifold of unfolding reactions in ovomucoid third domain. J. Mol. Biol. 300, 221-232.
    • (2000) J. Mol. Biol. , vol.300 , pp. 221-232
    • Arrington, C.B.1    Robertson, A.D.2
  • 58
  • 59
    • 0030047378 scopus 로고    scopus 로고
    • Temperature and pH dependences of hydrogen exchange and global stability for ovomucoid third domain
    • DOI 10.1021/bi9517603
    • Swint-Kruse, L., and Robertson, A. D. (1996) Temperature and pH dependences of hydrogen exchange and global stability for ovomucoid third domain. Biochemistry 35, 171-180. (Pubitemid 26036420)
    • (1996) Biochemistry , vol.35 , Issue.1 , pp. 171-180
    • Swint-Kruse, L.1    Robertson, A.D.2
  • 61
    • 0032428378 scopus 로고    scopus 로고
    • Identification of protein-protein interfaces by decreased amide proton solvent accessibility
    • Mandell, J. G., Falick, A. M., and Komives, E. A. (1998) Identification of protein-protein interfaces by decreased amide proton solvent accessibility. Proc. Natl. Acad. Sci. U.S.A. 95, 14705-14710.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 14705-14710
    • Mandell, J.G.1    Falick, A.M.2    Komives, E.A.3
  • 62
    • 0032186122 scopus 로고    scopus 로고
    • Measurement of amide hydrogen exchange by MALDI-TOF mass spectrometry
    • Mandell, J. G., Falick, A. M., and Komives, E. A. (1998) Measurement of amide hydrogen exchange by MALDI-TOF mass spectrometry. Anal. Chem. 70, 3987-3995.
    • (1998) Anal. Chem. , vol.70 , pp. 3987-3995
    • Mandell, J.G.1    Falick, A.M.2    Komives, E.A.3
  • 64
    • 0034635224 scopus 로고    scopus 로고
    • The Asp(272)-Glu(282) region of platelet glycoprotein Ibα interacts with the heparin-binding site of α-thrombin and protects the enzyme from the heparin-catalyzed inhibition by antithrombin III
    • De Cristofaro, R., De Candia, E., Rutella, S., and Weitz, J. I. (2000) The Asp(272)-Glu(282) region of platelet glycoprotein Ibα interacts with the heparin-binding site of α-thrombin and protects the enzyme from the heparin-catalyzed inhibition by antithrombin III. J. Biol. Chem. 275, 3887-3895.
    • (2000) J. Biol. Chem. , vol.275 , pp. 3887-3895
    • De Cristofaro, R.1    De Candia, E.2    Rutella, S.3    Weitz, J.I.4
  • 65
    • 34447499926 scopus 로고    scopus 로고
    • Expression of allosteric linkage between the sodium ion binding site and exosite I of thrombin during prothrombin activation
    • Kroh, H. K., Tans, G., Nicolaes, G. A., Rosing, J., and Bock, P. E. (2007) Expression of allosteric linkage between the sodium ion binding site and exosite I of thrombin during prothrombin activation. J. Biol. Chem. 282, 16095-16104.
    • (2007) J. Biol. Chem. , vol.282 , pp. 16095-16104
    • Kroh, H.K.1    Tans, G.2    Nicolaes, G.A.3    Rosing, J.4    Bock, P.E.5
  • 66
    • 0028940892 scopus 로고
    • Identification of three tyrosine residues of glycoprotein Ibα with distinct roles in von Willebrand factor and α-thrombin binding
    • Marchese, P., Murata, M., Mazzucato, M., Pradella, P., De Marco, L., Ware, J., and Ruggeri, Z. M. (1995) Identification of three tyrosine residues of glycoprotein Ibα with distinct roles in von Willebrand factor and α-thrombin binding. J. Biol. Chem. 270, 9571-9578.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9571-9578
    • Marchese, P.1    Murata, M.2    Mazzucato, M.3    Pradella, P.4    De Marco, L.5    Ware, J.6    Ruggeri, Z.M.7
  • 67
    • 0026610497 scopus 로고
    • 2+ dependence of the interactions between protein C, thrombin, and the elastase fragment of thrombomodulin. Analysis by ultracentrifugation
    • 2+ dependence of the interactions between protein C, thrombin, and the elastase fragment of thrombomodulin. Analysis by ultracentrifugation. Biochemistry 31, 746-754.
    • (1992) Biochemistry , vol.31 , pp. 746-754
    • Olsen, P.H.1    Esmon, N.L.2    Esmon, C.T.3    Laue, T.M.4
  • 68
    • 0242670005 scopus 로고    scopus 로고
    • Thermodynamic non-ideality as an alternative source of the effect of sucrose on the thrombin-catalyzed hydrolysis of peptide p-nitroanilide substrates
    • Lonhienne, T. G., Jackson, C. M., and Winzor, D. J. (2003) Thermodynamic non-ideality as an alternative source of the effect of sucrose on the thrombin-catalyzed hydrolysis of peptide p-nitroanilide substrates. Biophys. Chem. 103, 259-269.
    • (2003) Biophys. Chem. , vol.103 , pp. 259-269
    • Lonhienne, T.G.1    Jackson, C.M.2    Winzor, D.J.3
  • 69
    • 0025309452 scopus 로고
    • Crystal structure of the thrombin-hirudin complex: A novel mode of serine protease inhibition
    • Grutter, M. G., Priestle, J. P., Rahuel, J., Grossenbacher, H., Bode, W., Hofsteenge, J., and Stone, S. R. (1990) Crystal structure of the thrombin-hirudin complex: A novel mode of serine protease inhibition. EMBO J. 9, 2361-2365. (Pubitemid 20218329)
    • (1990) EMBO Journal , vol.9 , Issue.8 , pp. 2361-2365
    • Grutter, M.G.1    Priestle, J.2    Rahuel, J.3    Grossenbacher, H.4    Bode, W.5    Hofsteenge, J.6    Stone, S.R.7
  • 71
    • 0025866812 scopus 로고
    • Refined structure of the hirudin-thrombin complex
    • Rydel, T. J., Tulinsky, A., Bode, W., and Huber, R. (1991) Refined structure of the hirudin-thrombin complex. J. Mol. Biol. 221, 583-601.
    • (1991) J. Mol. Biol. , vol.221 , pp. 583-601
    • Rydel, T.J.1    Tulinsky, A.2    Bode, W.3    Huber, R.4
  • 73
    • 0025338124 scopus 로고
    • Thrombin-bound conformation of the C-terminal fragments of hirudin determined by transferred nuclear Overhauser effects
    • DOI 10.1021/bi00470a030
    • Ni, F., Konishi, Y., and Scheraga, H. A. (1990) Thrombin-bound conformation of the C-terminal fragments of hirudin determined by transferred nuclear Overhauser effects. Biochemistry 29, 4479-4489. (Pubitemid 20153652)
    • (1990) Biochemistry , vol.29 , Issue.18 , pp. 4479-4489
    • Ni, F.1    Konishi, Y.2    Scheraga, H.A.3
  • 74
    • 0026511433 scopus 로고
    • Conformational stability of a thrombin-binding peptide derived from the hirudin C-terminus
    • Ni, F., Ripoll, D. R., and Purisima, E. O. (1992) Conformational stability of a thrombin-binding peptide derived from the hirudin C-terminus. Biochemistry 31, 2545-2554.
    • (1992) Biochemistry , vol.31 , pp. 2545-2554
    • Ni, F.1    Ripoll, D.R.2    Purisima, E.O.3
  • 75
    • 0035942306 scopus 로고    scopus 로고
    • Electrostatic steering and ionic tethering in the formation of thrombin-hirudin complexes: The role of the thrombin anion-binding exosite-I
    • DOI 10.1021/bi0023549
    • Myles, T., Le Bonniec, B. F., Betz, A., and Stone, S. R. (2001) Electrostatic steering and ionic tethering in the formation of thrombin-hirudin complexes: The role of the thrombin anion-binding exosite-I. Biochemistry 40, 4972-4979. (Pubitemid 32332543)
    • (2001) Biochemistry , vol.40 , Issue.16 , pp. 4972-4979
    • Myles, T.1    Le Bonniec, B.F.2    Betz, A.3    Stone, S.R.4
  • 77
    • 57649183329 scopus 로고    scopus 로고
    • Fibrinogen-elongated γ chain inhibits thrombin-induced platelet response, hindering the interaction with different receptors
    • Lancellotti, S., Rutella, S., De Filippis, V., Pozzi, N., Rocca, B., and De Cristofaro, R. (2008) Fibrinogen-elongated γ chain inhibits thrombin-induced platelet response, hindering the interaction with different receptors. J. Biol. Chem. 283, 30193-30204.
    • (2008) J. Biol. Chem. , vol.283 , pp. 30193-30204
    • Lancellotti, S.1    Rutella, S.2    De Filippis, V.3    Pozzi, N.4    Rocca, B.5    De Cristofaro, R.6
  • 78
    • 33646582680 scopus 로고    scopus 로고
    • Glycoprotein Ibα-mediated platelet adhesion and aggregation to immobilized thrombin under conditions of flow
    • Weeterings, C., Adelmeijer, J., Myles, T., de Groot, P. G., and Lisman, T. (2006) Glycoprotein Ibα-mediated platelet adhesion and aggregation to immobilized thrombin under conditions of flow. Arterioscler. Thromb. Vasc. Biol. 26, 670-675.
    • (2006) Arterioscler. Thromb. Vasc. Biol. , vol.26 , pp. 670-675
    • Weeterings, C.1    Adelmeijer, J.2    Myles, T.3    De Groot, P.G.4    Lisman, T.5
  • 79
    • 0036510533 scopus 로고    scopus 로고
    • Binding of exosite ligands to human thrombin. Re-evaluation of allosteric linkage between thrombin exosites I and II
    • Verhamme, I. M., Olson, S. T., Tollefsen, D. M., and Bock, P. E. (2002) Binding of exosite ligands to human thrombin. Re-evaluation of allosteric linkage between thrombin exosites I and II. J. Biol. Chem. 277, 6788-6798.
    • (2002) J. Biol. Chem. , vol.277 , pp. 6788-6798
    • Verhamme, I.M.1    Olson, S.T.2    Tollefsen, D.M.3    Bock, P.E.4
  • 80
    • 27144433871 scopus 로고    scopus 로고
    • Studies on the basis for the properties of fibrin produced from fibrinogen-containing γ′ chains
    • DOI 10.1182/blood-2005-01-0240
    • Siebenlist, K. R., Mosesson, M. W., Hernandez, I., Bush, L. A., Di Cera, E., Shainoff, J. R., Di Orio, J. P., and Stojanovic, L. (2005) Studies on the basis for the properties of fibrin produced from fibrinogen-containing γ′ chains. Blood 106, 2730-2736. (Pubitemid 41510747)
    • (2005) Blood , vol.106 , Issue.8 , pp. 2730-2736
    • Siebenlist, K.R.1    Mosesson, M.W.2    Hernandez, I.3    Bush, L.A.4    Di Cera, E.5    Shainoff, J.R.6    Di Orio, J.P.7    Stojanovic, L.8
  • 82
    • 0030830185 scopus 로고    scopus 로고
    • Evidence for allosteric linkage between exosites 1 and 2 of thrombin
    • Fredenburgh, J. C., Stafford, A. R., and Weitz, J. I. (1997) Evidence for allosteric linkage between exosites 1 and 2 of thrombin. J. Biol. Chem. 272, 25493-25499.
    • (1997) J. Biol. Chem. , vol.272 , pp. 25493-25499
    • Fredenburgh, J.C.1    Stafford, A.R.2    Weitz, J.I.3
  • 83
    • 0029995667 scopus 로고    scopus 로고
    • Binding of fibrin monomer and heparin to thrombin in a ternary complex alters the environment of the thrombin catalytic site, reduces affinity for hirudin, and inhibits cleavage of fibrinogen
    • Hogg, P. J., Jackson, C. M., Labanowski, J. K., and Bock, P. E. (1996) Binding of fibrin monomer and heparin to thrombin in a ternary complex alters the environment of the thrombin catalytic site, reduces affinity for hirudin, and inhibits cleavage of fibrinogen. J. Biol. Chem. 271, 26088-26095.
    • (1996) J. Biol. Chem. , vol.271 , pp. 26088-26095
    • Hogg, P.J.1    Jackson, C.M.2    Labanowski, J.K.3    Bock, P.E.4
  • 84
    • 27744530963 scopus 로고    scopus 로고
    • Thrombomodulin tightens the thrombin active site loops to promote protein C activation
    • DOI 10.1021/bi0510577
    • Koeppe, J. R., Seitova, A., Mather, T., and Komives, E. A. (2005) Thrombomodulin tightens the thrombin active site loops to promote protein C activation. Biochemistry 44, 14784-14791. (Pubitemid 41612258)
    • (2005) Biochemistry , vol.44 , Issue.45 , pp. 14784-14791
    • Koeppe, J.R.1    Seitova, A.2    Mather, T.3    Komives, E.A.4
  • 87
    • 0001470976 scopus 로고
    • Studies of Chemically Reacting Systems on Sephadex. II. Molecular Weights of Monomers in Rapid Association Equilibrium
    • Winzor, D. J., and Scheraga, H. A. (1964) Studies of Chemically Reacting Systems on Sephadex. II. Molecular Weights of Monomers in Rapid Association Equilibrium. J. Phys. Chem. 68, 338-343.
    • (1964) J. Phys. Chem. , vol.68 , pp. 338-343
    • Winzor, D.J.1    Scheraga, H.A.2
  • 89
    • 0026317444 scopus 로고
    • Function of glycoprotein Ib α in platelet activation induced by α-thrombin
    • De Marco, L., Mazzucato, M., Masotti, A., Fenton, J. W.II, and Ruggeri, Z. M. (1991) Function of glycoprotein Ib α in platelet activation induced by α-thrombin. J. Biol. Chem. 266, 23776-23783.
    • (1991) J. Biol. Chem. , vol.266 , pp. 23776-23783
    • De Marco, L.1    Mazzucato, M.2    Masotti, A.3    Fenton II, J.W.4    Ruggeri, Z.M.5
  • 91
    • 0032535778 scopus 로고    scopus 로고
    • A dimeric form of prothrombin on membrane surfaces
    • Anderson, P. J. (1998) A dimeric form of prothrombin on membrane surfaces. Biochem. J. 336 (Part 3), 631-638.
    • (1998) Biochem. J. , vol.336 , Issue.PART 3 , pp. 631-638
    • Anderson, P.J.1
  • 92
    • 0344440802 scopus 로고    scopus 로고
    • Thrombin interaction with platelet membrane glycoprotein Ib R
    • Adam, F., Bouton, M. C., Huisse, M. G., and Jandrot-Perrus, M. (2003) Thrombin interaction with platelet membrane glycoprotein Ib R. Trends Mol. Med. 9, 461-464.
    • (2003) Trends Mol. Med. , vol.9 , pp. 461-464
    • Adam, F.1    Bouton, M.C.2    Huisse, M.G.3    Jandrot-Perrus, M.4


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