메뉴 건너뛰기




Volumn 288, Issue 45, 2013, Pages 32289-32301

The N-terminal flanking region of the A1 domain regulates the force-dependent binding of von willebrand factor to platelet glycoprotein Ibα

Author keywords

[No Author keywords available]

Indexed keywords

FLANKING REGIONS; FLANKING SEQUENCE; HEMODYNAMIC FORCES; PLATELET ADHESION; ROLLING VELOCITY; STRUCTURAL DETERMINANTS; TRANSITION POINT; VON WILLEBRAND FACTOR;

EID: 84887430287     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.504001     Document Type: Article
Times cited : (91)

References (53)
  • 1
    • 0141498240 scopus 로고    scopus 로고
    • Von Willebrand factor, platelets and endothelial cell interactions
    • Ruggeri, Z. M. (2003) Von Willebrand factor, platelets and endothelial cell interactions. J. Thromb. Haemost. 1, 1335-1342
    • (2003) J. Thromb. Haemost , vol.1 , pp. 1335-1342
    • Ruggeri, Z.M.1
  • 2
    • 7044233073 scopus 로고    scopus 로고
    • Platelet physiology and thrombosis
    • Andrews, R. K., and Berndt, M. C. (2004) Platelet physiology and thrombosis. Thrombosis Research 114, 447-453
    • (2004) Thrombosis Research , vol.114 , pp. 447-453
    • Andrews, R.K.1    Berndt, M.C.2
  • 3
    • 34250818668 scopus 로고    scopus 로고
    • Adhesion mechanisms in platelet function
    • Ruggeri, Z. M., and Mendolicchio, G. L. (2007) Adhesion mechanisms in platelet function. Circ. Res. 100, 1673-1685
    • (2007) Circ. Res , vol.100 , pp. 1673-1685
    • Ruggeri, Z.M.1    Mendolicchio, G.L.2
  • 4
    • 77956628683 scopus 로고    scopus 로고
    • Regulation of von Willebrand factor-platelet interactions
    • Lenting, P. J., Pegon, J. N., Groot, E., and de Groot, P. G. (2010) Regulation of von Willebrand factor-platelet interactions. Thromb. Haemost. 104, 449-455
    • (2010) Thromb. Haemost , vol.104 , pp. 449-455
    • Lenting, P.J.1    Pegon, J.N.2    Groot, E.3    De Groot, P.G.4
  • 8
    • 0038446690 scopus 로고    scopus 로고
    • Aspects of hydrodynamic shear regulating shear-induced platelet activation and selfassociation of von Willebrand factor in suspension
    • Shankaran, H., Alexandridis, P., and Neelamegham, S. (2003) Aspects of hydrodynamic shear regulating shear-induced platelet activation and selfassociation of von Willebrand factor in suspension. Blood 101, 2637-2645
    • (2003) Blood , vol.101 , pp. 2637-2645
    • Shankaran, H.1    Alexandridis, P.2    Neelamegham, S.3
  • 9
    • 34250692515 scopus 로고    scopus 로고
    • Purified A2 domain of von Willebrand factor binds to the active conformation of von Willebrand factor and blocks the interaction with platelet glycoprotein Ibα
    • Martin, C., Morales, L. D., and Cruz, M. A. (2007) Purified A2 domain of von Willebrand factor binds to the active conformation of von Willebrand factor and blocks the interaction with platelet glycoprotein Ibα. J. Thromb. Haemost. 5, 1363-1370
    • (2007) J. Thromb. Haemost , vol.5 , pp. 1363-1370
    • Martin, C.1    Morales, L.D.2    Cruz, M.A.3
  • 10
    • 77954921247 scopus 로고    scopus 로고
    • Destabilization of the A1 domain in von Willebrand factor dissociates the A1A2A3 tri-domain and provokes spontaneous binding to glycoprotein Ibα and platelet activation under shear stress
    • Auton, M., Sowa, K. E., Smith, S. M., Sedlák, E., Vijayan, K. V., and Cruz, M. A. (2010) Destabilization of the A1 domain in von Willebrand factor dissociates the A1A2A3 tri-domain and provokes spontaneous binding to glycoprotein Ibα and platelet activation under shear stress. J. Biol. Chem. 285, 22831-22839
    • (2010) J. Biol. Chem , vol.285 , pp. 22831-22839
    • Auton, M.1    Sowa, K.E.2    Smith, S.M.3    Sedlák, E.4    Vijayan, K.V.5    Cruz, M.A.6
  • 11
    • 33646194222 scopus 로고    scopus 로고
    • Shielding of the A1 domain by the D'D3 domains of von Willebrand factor modulates its interaction with platelet glycoprotein Ib-IX-V
    • Ulrichts, H., Udvardy, M., Lenting, P. J., Pareyn, I., Vandeputte, N., Vanhoorelbeke, K., and Deckmyn, H. (2006) Shielding of the A1 domain by the D'D3 domains of von Willebrand factor modulates its interaction with platelet glycoprotein Ib-IX-V. J. Biol. Chem. 281, 4699-4707
    • (2006) J. Biol. Chem , vol.281 , pp. 4699-4707
    • Ulrichts, H.1    Udvardy, M.2    Lenting, P.J.3    Pareyn, I.4    Vandeputte, N.5    Vanhoorelbeke, K.6    Deckmyn, H.7
  • 12
    • 68949119686 scopus 로고    scopus 로고
    • Changes in thermodynamic stability of von Willebrand factor differentially affect the force-dependent binding to platelet GPIbα
    • Auton, M., Sedlák, E., Marek, J., Wu, T., Zhu, C., and Cruz, M. (2009) Changes in thermodynamic stability of von Willebrand factor differentially affect the force-dependent binding to platelet GPIbα. Biophys. J. 97, 618-627
    • (2009) Biophys. J , vol.97 , pp. 618-627
    • Auton, M.1    Sedlák, E.2    Marek, J.3    Wu, T.4    Zhu, C.5    Cruz, M.6
  • 13
    • 77958168869 scopus 로고    scopus 로고
    • The mechanism of VWFmediated platelet GPIbα binding
    • Auton, M., Zhu, C., and Cruz, M. A. (2010) The mechanism of VWFmediated platelet GPIbα binding. Biophys. J. 99, 1192-1201
    • (2010) Biophys. J , vol.99 , pp. 1192-1201
    • Auton, M.1    Zhu, C.2    Cruz, M.A.3
  • 14
    • 78751685657 scopus 로고    scopus 로고
    • GPIbα-vWF rolling under shear stress shows differences between type 2B and 2M von Willebrand disease
    • Coburn, L. A., Damaraju, V. S., Dozic, S., Eskin, S. G., Cruz, M. A., and McIntire, L. V. (2011) GPIbα-vWF rolling under shear stress shows differences between type 2B and 2M von Willebrand disease. Biophys. J. 100, 304-312
    • (2011) Biophys. J , vol.100 , pp. 304-312
    • Coburn, L.A.1    Damaraju, V.S.2    Dozic, S.3    Eskin, S.G.4    Cruz, M.A.5    McIntire, L.V.6
  • 15
    • 77955915209 scopus 로고    scopus 로고
    • Amechanically stabilized receptor-ligand flex-bond important in the vasculature
    • Kim, J., Zhang, C.-Z., Zhang, X., and Springer, T. A. (2010)Amechanically stabilized receptor-ligand flex-bond important in the vasculature. Nature 466, 992-995
    • (2010) Nature , vol.466 , pp. 992-995
    • Kim, J.1    Zhang, C.-Z.2    Zhang, X.3    Springer, T.A.4
  • 16
    • 0027427962 scopus 로고
    • The interaction of the von Willebrand factor-A1 domain with platelet glycoprotein Ib/IX
    • Cruz, M. A., and Handin, R. I. (1993) The interaction of the von Willebrand factor-A1 domain with platelet glycoprotein Ib/IX. J. Biol. Chem. 268, 21238-21245
    • (1993) J. Biol. Chem , vol.268 , pp. 21238-21245
    • Cruz, M.A.1    Handin, R.I.2
  • 17
    • 0033525513 scopus 로고    scopus 로고
    • Distinct structural attributes regulating von Willebrand factor A1 domain interaction with platelet glycoprotein Ibα under flow
    • Miyata, S., and Ruggeri, Z. M. (1999) Distinct structural attributes regulating von Willebrand factor A1 domain interaction with platelet glycoprotein Ibα under flow. J. Biol. Chem. 274, 6586-6593
    • (1999) J. Biol. Chem , vol.274 , pp. 6586-6593
    • Miyata, S.1    Ruggeri, Z.M.2
  • 18
    • 0033793331 scopus 로고    scopus 로고
    • Von Willebrand factor conformation and adhesive function is modulated by an internalized water molecule
    • Celikel, R., Ruggeri, Z. M., and Varughese, K. I. (2000) von Willebrand factor conformation and adhesive function is modulated by an internalized water molecule. Nat. Struct. Biol. 7, 881-884
    • (2000) Nat. Struct. Biol , vol.7 , pp. 881-884
    • Celikel, R.1    Ruggeri, Z.M.2    Varughese, K.I.3
  • 19
    • 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., and Handin, R. I. (2000) Mapping the glycoprotein Ib-binding site in the von willebrand factor A1 domain. J. Biol. Chem. 275, 19098-19105
    • (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
  • 20
    • 0036286198 scopus 로고    scopus 로고
    • Selectin-like kinetics and biomechanics promote rapid platelet adhesion in flow. The GPIbα-vWF tether bond
    • Doggett, T. A., Girdhar, G., Lawshé, A., Schmidtke, D. W., Laurenzi, I. J., Diamond, S. L., and Diacovo, T. G. (2002) Selectin-like kinetics and biomechanics promote rapid platelet adhesion in flow. The GPIbα-vWF tether bond. Biophys. J. 83, 194-205
    • (2002) Biophys. J , vol.83 , pp. 194-205
    • Doggett, T.A.1    Girdhar, G.2    Lawshé, A.3    Schmidtke, D.W.4    Laurenzi, I.J.5    Diamond, S.L.6    Diacovo, T.G.7
  • 21
    • 0036624844 scopus 로고    scopus 로고
    • Ultralarge multimers of von Willebrand factor form spontaneous high-strength bonds with the platelet glycoprotein Ib-IX complex. Studies using optical tweezers
    • Arya, M., Anvari, B., Romo, G. M., Cruz, M. A., Dong, J.-F., McIntire, L. V., Moake, J. L., and López, J. A. (2002) Ultralarge multimers of von Willebrand factor form spontaneous high-strength bonds with the platelet glycoprotein Ib-IX complex. Studies using optical tweezers. Blood 99, 3971-3977
    • (2002) Blood , vol.99 , pp. 3971-3977
    • Arya, M.1    Anvari, B.2    Romo, G.M.3    Cruz, M.A.4    Dong, J.-F.5    McIntire, L.V.6    Moake, J.L.7    López, J.A.8
  • 22
    • 33645565906 scopus 로고    scopus 로고
    • The interaction of von Willebrand factor-A1 domain with collagen. Mutation G1324S (type 2M von Willebrand disease) impairs the conformational change in A1 domain induced by collagen
    • Morales, L. D., Martin, C., and Cruz, M. A. (2006) The interaction of von Willebrand factor-A1 domain with collagen. Mutation G1324S (type 2M von Willebrand disease) impairs the conformational change in A1 domain induced by collagen. J. Thromb. Haemost. 4, 417-425
    • (2006) J. Thromb. Haemost , vol.4 , pp. 417-425
    • Morales, L.D.1    Martin, C.2    Cruz, M.A.3
  • 23
    • 0032562698 scopus 로고    scopus 로고
    • Crystal structure of the von Willebrand factor A1 domain and implications for the binding of platelet glycoprotein Ib
    • Emsley, J., Cruz, M., Handin, R., and Liddington, R. (1998) Crystal structure of the von Willebrand factor A1 domain and implications for the binding of platelet glycoprotein Ib. J. Biol. Chem. 273, 10396-10401
    • (1998) J. Biol. Chem , vol.273 , pp. 10396-10401
    • Emsley, J.1    Cruz, M.2    Handin, R.3    Liddington, R.4
  • 24
    • 0031941354 scopus 로고    scopus 로고
    • Crystal structure of the von Willebrand factor A1 domain in complex with the function blocking NMC-4 Fab
    • Celikel, R., Varughese, K. I., Madhusudan, Yoshioka, A., Ware, J., and Ruggeri, Z. M. (1998) Crystal structure of the von Willebrand factor A1 domain in complex with the function blocking NMC-4 Fab. Nat. Struct. Biol. 5, 189-194
    • (1998) Nat. Struct. Biol , vol.5 , pp. 189-194
    • Celikel, R.1    Varughese, K.I.2    Madhusudan3    Yoshioka, A.4    Ware, J.5    Ruggeri, Z.M.6
  • 25
    • 0034677986 scopus 로고    scopus 로고
    • Interaction of von Willebrand factor domain A1 with platelet glycoprotein Ibα-(1-289). Slow intrinsic binding kinetics mediate rapid platelet adhesion
    • Miura, S., Li, C. Q., Cao, Z., Wang, H., Wardell, M. R., and Sadler, J. E. (2000) Interaction of von Willebrand factor domain A1 with platelet glycoprotein Ibα-(1-289). Slow intrinsic binding kinetics mediate rapid platelet adhesion. J. Biol. Chem. 275, 7539-7546
    • (2000) J. Biol. Chem , vol.275 , pp. 7539-7546
    • Miura, S.1    Li, C.Q.2    Cao, Z.3    Wang, H.4    Wardell, M.R.5    Sadler, J.E.6
  • 26
    • 0037144544 scopus 로고    scopus 로고
    • Crystal structure of the platelet glycoprotein Ibα N-terminal domain reveals an unmasking mechanism for receptor activation
    • Uff, S., Clemetson, J. M., Harrison, T., Clemetson, K. J., and Emsley, J. (2002) Crystal structure of the platelet glycoprotein Ibα N-terminal domain reveals an unmasking mechanism for receptor activation. J. Biol. Chem. 277, 35657-35663
    • (2002) J. Biol. Chem , vol.277 , pp. 35657-35663
    • Uff, S.1    Clemetson, J.M.2    Harrison, T.3    Clemetson, K.J.4    Emsley, J.5
  • 28
    • 2542480051 scopus 로고    scopus 로고
    • Crystal structure of the wild-type von Willebrand factor A1-glycoprotein Ibα complex reveals conformation differences with a complex bearing von Willebrand disease mutations
    • Dumas, J. J., Kumar, R., McDonagh, T., Sullivan, F., Stahl, M. L., Somers, W. S., and Mosyak, L. (2004) Crystal structure of the wild-type von Willebrand factor A1-glycoprotein Ibα complex reveals conformation differences with a complex bearing von Willebrand disease mutations. J. Biol. Chem. 279, 23327-23334
    • (2004) J. Biol. Chem , vol.279 , pp. 23327-23334
    • Dumas, J.J.1    Kumar, R.2    McDonagh, T.3    Sullivan, F.4    Stahl, M.L.5    Somers, W.S.6    Mosyak, L.7
  • 29
    • 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., and Diacovo, T. G. (2005) The snake venom protein botrocetin acts as a biological brace to promote dysfunctional platelet aggregation. Nat. Struct. Mol. Biol. 12, 152-159
    • (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
  • 31
    • 84860376548 scopus 로고    scopus 로고
    • N-terminal flanking region of A1 domain in von Willebrand factor stabilizes structure of A1A2A3 complex and modulates platelet activation under shear stress
    • Auton, M., Sowa, K. E., Behymer, M., and Cruz, M. A. (2012) N-terminal flanking region of A1 domain in von Willebrand factor stabilizes structure of A1A2A3 complex and modulates platelet activation under shear stress. J. Biol. Chem. 287, 14579-14585
    • (2012) J. Biol. Chem , vol.287 , pp. 14579-14585
    • Auton, M.1    Sowa, K.E.2    Behymer, M.3    Cruz, M.A.4
  • 32
    • 38349065134 scopus 로고    scopus 로고
    • Monitoring receptor-ligand interactions between surfaces by thermal fluctuations
    • Chen, W., Evans, E. A., McEver, R. P., and Zhu, C. (2008) Monitoring receptor-ligand interactions between surfaces by thermal fluctuations. Biophys. J. 94, 694-701
    • (2008) Biophys. J , vol.94 , pp. 694-701
    • Chen, W.1    Evans, E.A.2    McEver, R.P.3    Zhu, C.4
  • 33
    • 0034623054 scopus 로고    scopus 로고
    • Novel gain-of-function mutations of platelet glycoprotein Ibα by valine mutagenesis in the Cys209-Cys248 disulfide loop. Functional analysis under statis and dynamic conditions
    • Dong, J., Schade, A. J., Romo, G. M., Andrews, R. K., Gao, S., McIntire, L. V., and López, J. A. (2000) Novel gain-of-function mutations of platelet glycoprotein Ibα by valine mutagenesis in the Cys209-Cys248 disulfide loop. Functional analysis under statis and dynamic conditions. J. Biol. Chem. 275, 27663-27670
    • (2000) J. Biol. Chem , vol.275 , pp. 27663-27670
    • Dong, J.1    Schade, A.J.2    Romo, G.M.3    Andrews, R.K.4    Gao, S.5    McIntire, L.V.6    López, J.A.7
  • 34
    • 84869127061 scopus 로고    scopus 로고
    • Observing force-regulated conformational changes and ligand dissociation from a single integrin on cells
    • Chen, W., Lou, J., Evans, E. A., and Zhu, C. (2012) Observing force-regulated conformational changes and ligand dissociation from a single integrin on cells. J. Cell Biol. 199, 497-512
    • (2012) J. Cell Biol , vol.199 , pp. 497-512
    • Chen, W.1    Lou, J.2    Evans, E.A.3    Zhu, C.4
  • 35
    • 78149245953 scopus 로고    scopus 로고
    • Forcing switch from short- to intermediate- and long-lived states of the A domain generates LFA-1/ICAM-1 catch bonds
    • Chen, W., Lou, J., and Zhu, C. (2010) Forcing switch from short- to intermediate- and long-lived states of the A domain generates LFA-1/ICAM-1 catch bonds. J. Biol. Chem. 285, 35967-35978
    • (2010) J. Biol. Chem , vol.285 , pp. 35967-35978
    • Chen, W.1    Lou, J.2    Zhu, C.3
  • 36
    • 77950809538 scopus 로고    scopus 로고
    • The kinetics of two-dimensional TCR and pMHC interactions determine T-cell responsiveness
    • Huang, J., Zarnitsyna, V. I., Liu, B., Edwards, L. J., Jiang, N., Evavold, B. D., and Zhu, C. (2010) The kinetics of two-dimensional TCR and pMHC interactions determine T-cell responsiveness. Nature 464, 932-936
    • (2010) Nature , vol.464 , pp. 932-936
    • Huang, J.1    Zarnitsyna, V.I.2    Liu, B.3    Edwards, L.J.4    Jiang, N.5    Evavold, B.D.6    Zhu, C.7
  • 37
    • 0031682733 scopus 로고    scopus 로고
    • Measuring two-dimensional receptor-ligand binding kinetics by micropipette
    • Chesla, S. E., Selvaraj, P., and Zhu, C. (1998) Measuring two-dimensional receptor-ligand binding kinetics by micropipette. Biophys. J. 75, 1553-1572
    • (1998) Biophys. J , vol.75 , pp. 1553-1572
    • Chesla, S.E.1    Selvaraj, P.2    Zhu, C.3
  • 38
    • 14944369328 scopus 로고    scopus 로고
    • The platelet glycoprotein Ib-von Willebrand factor interaction activates the collagen receptor α2β1 to bind collagen. Activation-dependent conformational change of the α2-I domain
    • Cruz, M. A., Chen, J., Whitelock, J. L., Morales, L. D., and López, J. A. (2005) The platelet glycoprotein Ib-von Willebrand factor interaction activates the collagen receptor α2β1 to bind collagen. Activation-dependent conformational change of the α2-I domain. Blood 105, 1986-1991
    • (2005) Blood , vol.105 , pp. 1986-1991
    • Cruz, M.A.1    Chen, J.2    Whitelock, J.L.3    Morales, L.D.4    López, J.A.5
  • 39
    • 4544238275 scopus 로고    scopus 로고
    • Catch bonds govern adhesion through L-selectin at threshold shear
    • Yago, T., Wu, J., Wey, C. D., Klopocki, A. G., Zhu, C., and McEver, R. P. (2004) Catch bonds govern adhesion through L-selectin at threshold shear. J. Cell Biol. 166, 913-923
    • (2004) J. Cell Biol , vol.166 , pp. 913-923
    • Yago, T.1    Wu, J.2    Wey, C.D.3    Klopocki, A.G.4    Zhu, C.5    McEver, R.P.6
  • 41
    • 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., and Reininger, A. J. (2006) Activation-independent platelet adhesion and aggregation under elevated shear stress. Blood 108, 1903-1910
    • (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
  • 42
    • 0033529317 scopus 로고    scopus 로고
    • Adhesive properties of the isolated amino-terminal domain of platelet glycoprotein Ibα in a flow field
    • Marchese, P., Saldívar, E., Ware, J., and Ruggeri, Z. (1999) Adhesive properties of the isolated amino-terminal domain of platelet glycoprotein Ibα in a flow field. Proc. Natl. Acad. Sci. U.S.A. 96, 7837-7842
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 7837-7842
    • Marchese, P.1    Saldívar, E.2    Ware, J.3    Ruggeri, Z.4
  • 43
    • 0038644632 scopus 로고    scopus 로고
    • Alterations in the intrinsic properties of the GPIb- VWF tether bond define the kinetics of the platelet-type von Willebrand disease mutation, Gly233Val
    • Doggett, T. A. (2003) Alterations in the intrinsic properties of the GPIb- VWF tether bond define the kinetics of the platelet-type von Willebrand disease mutation, Gly233Val. Blood 102, 152-160
    • (2003) Blood , vol.102 , pp. 152-160
    • Doggett, T.A.1
  • 44
    • 0345412698 scopus 로고    scopus 로고
    • Kinetics of GPIbα-vWF-A1 tether bond under flow. Effect of GPIbα mutations on the association and dissociation rates
    • Kumar, R. A., Dong, J.-F., Thaggard, J. A., Cruz, M. A., López, J. A., and McIntire, L. V. (2003) Kinetics of GPIbα-vWF-A1 tether bond under flow. Effect of GPIbα mutations on the association and dissociation rates. Biophys. J. 85, 4099-4109
    • (2003) Biophys. J , vol.85 , pp. 4099-4109
    • Kumar, R.A.1    Dong, J.-F.2    Thaggard, J.A.3    Cruz, M.A.4    López, J.A.5    McIntire, L.V.6
  • 45
    • 67649598285 scopus 로고    scopus 로고
    • Demonstration of catch bonds between an integrin and its ligand
    • Kong, F., García, A. J., Mould, A. P., Humphries, M. J., and Zhu, C. (2009) Demonstration of catch bonds between an integrin and its ligand. J. Cell Biol. 185, 1275-1284
    • (2009) J. Cell Biol , vol.185 , pp. 1275-1284
    • Kong, F.1    García, A.J.2    Mould, A.P.3    Humphries, M.J.4    Zhu, C.5
  • 47
    • 0037653696 scopus 로고    scopus 로고
    • Direct observation of catch bonds involving cell-adhesion molecules
    • Marshall, B. T., Long, M., Piper, J. W., Yago, T., McEver, R. P., and Zhu, C. (2003) Direct observation of catch bonds involving cell-adhesion molecules. Nature 423, 190-193
    • (2003) Nature , vol.423 , pp. 190-193
    • Marshall, B.T.1    Long, M.2    Piper, J.W.3    Yago, T.4    McEver, R.P.5    Zhu, C.6
  • 49
    • 77958158403 scopus 로고    scopus 로고
    • Triphasic force dependence of E-selectin/ligand dissociation governs cell rolling under flow
    • Wayman, A. M., Chen, W., McEver, R. P., and Zhu, C. (2010) Triphasic force dependence of E-selectin/ligand dissociation governs cell rolling under flow. Biophys. J. 99, 1166-1174
    • (2010) Biophys. J , vol.99 , pp. 1166-1174
    • Wayman, A.M.1    Chen, W.2    McEver, R.P.3    Zhu, C.4
  • 50
    • 0029042992 scopus 로고
    • Identification of amino acid residues essential for von Willebrand factor binding to platelet glycoprotein Ib. Charged-to-alanine scanning mutagenesis of the A1 domain of human von Willebrand factor
    • Matsushita, T., and Sadler, J. E. (1995) Identification of amino acid residues essential for von Willebrand factor binding to platelet glycoprotein Ib. Charged-to-alanine scanning mutagenesis of the A1 domain of human von Willebrand factor. J. Biol. Chem. 270, 13406-13414
    • (1995) J. Biol. Chem , vol.270 , pp. 13406-13414
    • Matsushita, T.1    Sadler, J.E.2
  • 51
    • 4444278190 scopus 로고    scopus 로고
    • Type IIB von Willebrand disease.Aparadox explains how von Willebrand factor works
    • Ruggeri, Z. M. (2004) Type IIB von Willebrand disease.Aparadox explains how von Willebrand factor works. J. Thromb. Haemost. 2, 2-6
    • (2004) J. Thromb. Haemost , vol.2 , pp. 2-6
    • Ruggeri, Z.M.1
  • 52
    • 0026756331 scopus 로고
    • Von Willebrand disease type B. A missense mutation selectively abolishes ristocetin-induced von Willebrand factor binding to platelet glycoprotein Ib
    • Rabinowitz, I., Tuley, E. A., Mancuso, D. J., Randi, A. M., Firkin, B. G., Howard, M. A., and Sadler, J. E. (1992) von Willebrand disease type B. A missense mutation selectively abolishes ristocetin-induced von Willebrand factor binding to platelet glycoprotein Ib. Proc. Natl. Acad. Sci. U.S.A. 89, 9846-9849
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 9846-9849
    • Rabinowitz, I.1    Tuley, E.A.2    Mancuso, D.J.3    Randi, A.M.4    Firkin, B.G.5    Howard, M.A.6    Sadler, J.E.7
  • 53
    • 84881283044 scopus 로고    scopus 로고
    • The linker between the D3 and A1 domains of vWF suppresses A1-GPIbα catch bonds by site-specific binding to the A1 domain
    • Tischer, A., Cruz, M. A., and Auton, M. (2013) The linker between the D3 and A1 domains of vWF suppresses A1-GPIbα catch bonds by site-specific binding to the A1 domain. Protein Sci. 22, 1049-1059
    • (2013) Protein Sci , vol.22 , pp. 1049-1059
    • Tischer, A.1    Cruz, M.A.2    Auton, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.