메뉴 건너뛰기




Volumn 26, Issue 1, 2008, Pages 114-119

Modifying murine von Willebrand factor A1 domain for in vivo assessment of human platelet therapies

Author keywords

[No Author keywords available]

Indexed keywords

DRUG THERAPY; MAMMALS; PHYSIOLOGICAL MODELS;

EID: 38049036483     PISSN: 10870156     EISSN: 15461696     Source Type: Journal    
DOI: 10.1038/nbt1373     Document Type: Article
Times cited : (25)

References (30)
  • 1
    • 0034705544 scopus 로고    scopus 로고
    • Mapping the glycoprotein Ib-binding site in the von Willebrand factor A1 domain
    • Cruz, M.A., Diacovo, T.G., Emsley, J., Liddington, R. & Handin, R.I. Mapping the glycoprotein Ib-binding site in the von Willebrand factor A1 domain. J. Biol. Chem. 275, 19098-19105 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 19098-19105
    • Cruz, M.A.1    Diacovo, T.G.2    Emsley, J.3    Liddington, R.4    Handin, R.I.5
  • 2
    • 0025880446 scopus 로고
    • Functional modulation of the isolated glycoprotein Ib binding domain of von Willebrand factor expressed in Escherichia coli
    • Sugimoto, M. et al. Functional modulation of the isolated glycoprotein Ib binding domain of von Willebrand factor expressed in Escherichia coli. Biochemistry 30, 5202-5209 (1991).
    • (1991) Biochemistry , vol.30 , pp. 5202-5209
    • Sugimoto, M.1
  • 3
    • 0024426748 scopus 로고
    • Production in Escherichia coli of a biologically active subfragment of von Willebrand factor corresponding to the platelet glycoprotein Ib, collagen and heparin binding domains
    • Pietu, G. et al. Production in Escherichia coli of a biologically active subfragment of von Willebrand factor corresponding to the platelet glycoprotein Ib, collagen and heparin binding domains. Biochem. Biophys. Res. Commun. 164, 1339-1347 (1989).
    • (1989) Biochem. Biophys. Res. Commun , vol.164 , pp. 1339-1347
    • Pietu, G.1
  • 4
    • 13344295095 scopus 로고    scopus 로고
    • Initiation of platelet adhesion by arrest onto fibrinogen or translocation on von Willebrand factor
    • Savage, B., Saldivar, E. & Ruggeri, Z.M. Initiation of platelet adhesion by arrest onto fibrinogen or translocation on von Willebrand factor. Cell 84, 289-297 (1996).
    • (1996) Cell , vol.84 , pp. 289-297
    • Savage, B.1    Saldivar, E.2    Ruggeri, Z.M.3
  • 5
    • 0036286198 scopus 로고    scopus 로고
    • Selectin-like kinetics and biomechanics promote rapid platelet adhesion in flow: The GPIb(alpha)-vWF tether bond
    • Doggett, T.A. et al. Selectin-like kinetics and biomechanics promote rapid platelet adhesion in flow: the GPIb(alpha)-vWF tether bond. Biophys. J. 83, 194-205 (2002).
    • (2002) Biophys. J , vol.83 , pp. 194-205
    • Doggett, T.A.1
  • 6
    • 0036796740 scopus 로고    scopus 로고
    • Distribution and evolution of von Willebrand/integrin A domains: Widely dispersed domains with roles in cell adhesion and elsewhere
    • Whittaker, C.A. & Hynes, R.O. Distribution and evolution of von Willebrand/integrin A domains: widely dispersed domains with roles in cell adhesion and elsewhere. Mol. Biol. Cell 13, 3369-3387 (2002).
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3369-3387
    • Whittaker, C.A.1    Hynes, R.O.2
  • 7
    • 0018770590 scopus 로고
    • Human blood platelet adhesion to artery subendothelium is mediated by factor VIII-Von Willebrand factor bound to the subendothelium
    • Sakariassen, K.S., Bolhuis, P.A. & Sixma, J.J. Human blood platelet adhesion to artery subendothelium is mediated by factor VIII-Von Willebrand factor bound to the subendothelium. Nature 279, 636-638 (1979).
    • (1979) Nature , vol.279 , pp. 636-638
    • Sakariassen, K.S.1    Bolhuis, P.A.2    Sixma, J.J.3
  • 8
    • 4644368365 scopus 로고    scopus 로고
    • Signalling through the platelet glycoprotein Ib-V-IX complex
    • Canobbio, I., Balduini, C. & Torti, M. Signalling through the platelet glycoprotein Ib-V-IX complex. Cell. Signal. 16, 1329-1344 (2004).
    • (2004) Cell. Signal , vol.16 , pp. 1329-1344
    • Canobbio, I.1    Balduini, C.2    Torti, M.3
  • 9
    • 33845606632 scopus 로고    scopus 로고
    • Activation of platelet function through G protein-coupled receptors
    • Offermanns, S. Activation of platelet function through G protein-coupled receptors. Circ. Res. 99, 1293-1304 (2006).
    • (2006) Circ. Res , vol.99 , pp. 1293-1304
    • Offermanns, S.1
  • 10
    • 0038494921 scopus 로고    scopus 로고
    • Platelet-collagen interaction: Is GPVI the central receptor?
    • Nieswandt, B. & Watson, S.P. Platelet-collagen interaction: is GPVI the central receptor? Blood 102, 449-461 (2003).
    • (2003) Blood , vol.102 , pp. 449-461
    • Nieswandt, B.1    Watson, S.P.2
  • 11
    • 4444264392 scopus 로고    scopus 로고
    • Integrins: Dynamic scaffolds for adhesion and signaling in platelets
    • Shattil, S.J. & Newman, P.J. Integrins: dynamic scaffolds for adhesion and signaling in platelets. Blood 104, 1606-1615 (2004).
    • (2004) Blood , vol.104 , pp. 1606-1615
    • Shattil, S.J.1    Newman, P.J.2
  • 12
    • 0032590042 scopus 로고    scopus 로고
    • Beta3-integrin-deficient mice are a model for Glanzmann thrombasthenia showing placental defects and reduced survival
    • Hodivala-Dilke, K.M. et al. Beta3-integrin-deficient mice are a model for Glanzmann thrombasthenia showing placental defects and reduced survival. J. Clin. Invest. 103, 229-238 (1999).
    • (1999) J. Clin. Invest , vol.103 , pp. 229-238
    • Hodivala-Dilke, K.M.1
  • 13
    • 33646799069 scopus 로고    scopus 로고
    • Global and regional burden of disease and risk factors, 2001: Systematic analysis of population health data
    • Lopez, A.D., Mathers, C.D., Ezzati, M., Jamison, D.T. & Murray, C.J. Global and regional burden of disease and risk factors, 2001: systematic analysis of population health data. Lancet 367, 1747-1757 (2006).
    • (2006) Lancet , vol.367 , pp. 1747-1757
    • Lopez, A.D.1    Mathers, C.D.2    Ezzati, M.3    Jamison, D.T.4    Murray, C.J.5
  • 15
    • 0035120357 scopus 로고    scopus 로고
    • Novel platelet inhibitors
    • Bennett, J.S. Novel platelet inhibitors. Annu. Rev. Med. 52, 161-184 (2001).
    • (2001) Annu. Rev. Med , vol.52 , pp. 161-184
    • Bennett, J.S.1
  • 16
    • 0034648757 scopus 로고    scopus 로고
    • Thrombin signalling and protease-activated receptors
    • Coughlin, S.R. Thrombin signalling and protease-activated receptors. Nature 407, 258-264 (2000).
    • (2000) Nature , vol.407 , pp. 258-264
    • Coughlin, S.R.1
  • 17
    • 33748704252 scopus 로고    scopus 로고
    • Activation-independent platelet adhesion and aggregation under elevated shear stress
    • Ruggeri, Z.M., Orje, J.N., Habermann, R., Federici, A.B. & Reininger, A.J. Activation-independent platelet adhesion and aggregation under elevated shear stress. Blood 108, 1903-1910 (2006).
    • (2006) Blood , vol.108 , pp. 1903-1910
    • Ruggeri, Z.M.1    Orje, J.N.2    Habermann, R.3    Federici, A.B.4    Reininger, A.J.5
  • 18
    • 15544366749 scopus 로고    scopus 로고
    • The snake venom protein botrocetin acts as a biological brace to promote dysfunctional platelet aggregation
    • Fukuda, K., Doggett, T., Laurenzi, I.J., Liddington, R.C. & Diacovo, T.G. The snake venom protein botrocetin acts as a biological brace to promote dysfunctional platelet aggregation. Nat. Struct. Mol. Biol. 12, 152-159 (2005).
    • (2005) Nat. Struct. Mol. Biol , vol.12 , pp. 152-159
    • Fukuda, K.1    Doggett, T.2    Laurenzi, I.J.3    Liddington, R.C.4    Diacovo, T.G.5
  • 19
    • 2542480051 scopus 로고    scopus 로고
    • Crystal structure of the wild-type von Willebrand factor A1-glycoprotein Ibalpha complex reveals conformation differences with a complex bearing von Willebrand disease mutations
    • Dumas, J.J. et al. Crystal structure of the wild-type von Willebrand factor A1-glycoprotein Ibalpha complex reveals conformation differences with a complex bearing von Willebrand disease mutations. J. Biol. Chem. 279, 23327-23334 (2004).
    • (2004) J. Biol. Chem , vol.279 , pp. 23327-23334
    • Dumas, J.J.1
  • 20
    • 0037119003 scopus 로고    scopus 로고
    • Structures of glycoprotein Ibalpha and its complex with von Willebrand factor A1 domain
    • Huizinga, E.G. et al. Structures of glycoprotein Ibalpha and its complex with von Willebrand factor A1 domain. Science 297, 1176-1179 (2002).
    • (2002) Science , vol.297 , pp. 1176-1179
    • Huizinga, E.G.1
  • 21
    • 0032479179 scopus 로고    scopus 로고
    • Anatomy of hot spots in protein interfaces
    • Bogan, A.A. & Thorn, K.S. Anatomy of hot spots in protein interfaces. J. Mol. Biol. 280, 1-9 (1998).
    • (1998) J. Mol. Biol , vol.280 , pp. 1-9
    • Bogan, A.A.1    Thorn, K.S.2
  • 22
    • 12944317287 scopus 로고    scopus 로고
    • Requirement of leucine-rich repeats of glycoprotein (GP) Ibalpha for shear-dependent and static binding of von Willebrand factor to the platelet membrane GP Ib-IX-V complex
    • Shen, Y. et al. Requirement of leucine-rich repeats of glycoprotein (GP) Ibalpha for shear-dependent and static binding of von Willebrand factor to the platelet membrane GP Ib-IX-V complex. Blood 95, 903-910 (2000).
    • (2000) Blood , vol.95 , pp. 903-910
    • Shen, Y.1
  • 23
    • 0032533592 scopus 로고    scopus 로고
    • Shear-dependent rolling on von Willebrand factor of mammalian cells expressing the platelet glycoprotein Ib-IX-V complex
    • Fredrickson, B.J., Dong, J.F., McIntire, L.V. & Lopez, J.A. Shear-dependent rolling on von Willebrand factor of mammalian cells expressing the platelet glycoprotein Ib-IX-V complex. Blood 92, 3684-3693 (1998).
    • (1998) Blood , vol.92 , pp. 3684-3693
    • Fredrickson, B.J.1    Dong, J.F.2    McIntire, L.V.3    Lopez, J.A.4
  • 24
    • 31044445108 scopus 로고    scopus 로고
    • Thrombus formation in vivo
    • Furie, B. & Furie, B.C. Thrombus formation in vivo. J. Clin. Invest. 115, 3355-3362 (2005).
    • (2005) J. Clin. Invest , vol.115 , pp. 3355-3362
    • Furie, B.1    Furie, B.C.2
  • 25
    • 0034646267 scopus 로고    scopus 로고
    • Generation and rescue of a murine model of platelet dysfunction: The Bernard-Soulier syndrome
    • Ware, J., Russell, S. & Ruggeri, Z.M. Generation and rescue of a murine model of platelet dysfunction: the Bernard-Soulier syndrome. Proc. Natl. Acad. Sci. USA 97, 2803-2808 (2000).
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2803-2808
    • Ware, J.1    Russell, S.2    Ruggeri, Z.M.3
  • 26
    • 33750941414 scopus 로고    scopus 로고
    • The role of platelet adhesion receptor GPIbalpha far exceeds that of its main ligand, von Willebrand factor, in arterial thrombosis
    • Bergmeier, W. et al. The role of platelet adhesion receptor GPIbalpha far exceeds that of its main ligand, von Willebrand factor, in arterial thrombosis. Proc. Natl. Acad. Sci. USA 103, 16900-16905 (2006).
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 16900-16905
    • Bergmeier, W.1
  • 27
    • 0032483024 scopus 로고    scopus 로고
    • A mouse model of severe von Willebrand disease: Defects in hemostasis and thrombosis
    • Denis, C. et al. A mouse model of severe von Willebrand disease: defects in hemostasis and thrombosis. Proc. Natl. Acad. Sci. USA 95, 9524-9529 (1998).
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 9524-9529
    • Denis, C.1
  • 29
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project
    • Collaborative Computational Project. No. 4 The CCP4 suite: programs for protein crystallography. Acta Crystallogr.D 50, 760-763 (1994).
    • (1994) Acta Crystallogr.D , vol.50 , pp. 760-763
  • 30
    • 0030729838 scopus 로고    scopus 로고
    • An extensively modified version of Molscript that includes greatly enhanced coloring capabilities
    • Esnouf, R.M. An extensively modified version of Molscript that includes greatly enhanced coloring capabilities. J. Mol. Graph. Model. 15, 132-136 (1997).
    • (1997) J. Mol. Graph. Model , vol.15 , pp. 132-136
    • Esnouf, R.M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.