-
1
-
-
16844381981
-
Three-dimensional EM structure of the ectodomain of integrin αVβ3 in a complex with fibronectin
-
Adair, B.D., J.P. Xiong, C. Maddock, S.L. Goodman, M.A. Arnaout, and M. Yeager. 2005. Three-dimensional EM structure of the ectodomain of integrin αVβ3 in a complex with fibronectin. J. Cell Biol. 168:1109-1118. http://dx.doi.org/10.1083/jcb.200410068
-
(2005)
J. Cell Biol.
, vol.168
, pp. 1109-1118
-
-
Adair, B.D.1
Xiong, J.P.2
Maddock, C.3
Goodman, S.L.4
Arnaout, M.A.5
Yeager, M.6
-
2
-
-
76449098262
-
PHENIX: a comprehensive Python-based system for macromolecular structure solution
-
Adams, P.D., P.V. Afonine, G. Bunkóczi, V.B. Chen, I.W. Davis, N. Echols, J.J. Headd, L.W. Hung, G.J. Kapral, R.W. Grosse-Kunstleve, et al. 2010. PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr. D Biol. Crystallogr. 66:213-221. http://dx.doi.org/10.1107/S0907444909052925
-
(2010)
Acta Crystallogr. D Biol. Crystallogr.
, vol.66
, pp. 213-221
-
-
Adams, P.D.1
Afonine, P.V.2
Bunkóczi, G.3
Chen, V.B.4
Davis, I.W.5
Echols, N.6
Headd, J.J.7
Hung, L.W.8
Kapral, G.J.9
Grosse-Kunstleve, R.W.10
-
3
-
-
2342443223
-
UR- 3216: a new generation oral platelet GPIIb/IIIa antagonist
-
Aga, Y., K. Baba, S. Tam, T. Nakanishi, K. Yoneda, J. Kita, and H. Ueno. 2004. UR- 3216: a new generation oral platelet GPIIb/IIIa antagonist. Curr. Pharm. Des. 10:1597-1601. http://dx.doi.org/10.2174/1381612043384592
-
(2004)
Curr. Pharm. Des.
, vol.10
, pp. 1597-1601
-
-
Aga, Y.1
Baba, K.2
Tam, S.3
Nakanishi, T.4
Yoneda, K.5
Kita, J.6
Ueno, H.7
-
4
-
-
2942722352
-
Novel activating and inactivating mutations in the integrin β1 subunit A domain
-
Barton, S.J., M.A. Travis, J.A. Askari, P.A. Buckley, S.E. Craig, M.J. Humphries, and A.P. Mould. 2004. Novel activating and inactivating mutations in the integrin β1 subunit A domain. Biochem. J. 380:401-407. http://dx.doi.org/10.1042/BJ20031973
-
(2004)
Biochem. J.
, vol.380
, pp. 401-407
-
-
Barton, S.J.1
Travis, M.A.2
Askari, J.A.3
Buckley, P.A.4
Craig, S.E.5
Humphries, M.J.6
Mould, A.P.7
-
5
-
-
11244258886
-
The relative influence of metal ion binding sites in the I-like domain and the interface with the hybrid domain on rolling and firm adhesion by integrin α4β7
-
Chen, J.F., J. Takagi, C. Xie, T. Xiao, B.-H. Luo, and T.A. Springer. 2004. The relative influence of metal ion binding sites in the I-like domain and the interface with the hybrid domain on rolling and firm adhesion by integrin α4β7. J. Biol. Chem. 279:55556-55561. http://dx.doi.org/10.1074/jbc.M407773200
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 55556-55561
-
-
Chen, J.F.1
Takagi, J.2
Xie, C.3
Xiao, T.4
Luo, B.-H.5
Springer, T.A.6
-
6
-
-
77957034686
-
Requirement of open headpiece conformation for activation of leukocyte integrin αXβ2
-
Chen, X., C. Xie, N. Nishida, Z. Li, T. Walz, and T.A. Springer. 2010. Requirement of open headpiece conformation for activation of leukocyte integrin αXβ2. Proc. Natl. Acad. Sci. USA. 107:14727-14732. http://dx.doi.org/10.1073/pnas.1008663107
-
(2010)
Proc. Natl. Acad. Sci. USA.
, vol.107
, pp. 14727-14732
-
-
Chen, X.1
Xie, C.2
Nishida, N.3
Li, Z.4
Walz, T.5
Springer, T.A.6
-
7
-
-
7944225864
-
Structural insights into how the MIDAS ion stabilizes integrin binding to an RGD peptide under force
-
Craig, D., M. Gao, K. Schulten, and V. Vogel. 2004. Structural insights into how the MIDAS ion stabilizes integrin binding to an RGD peptide under force. Structure. 12:2049-2058. http://dx.doi.org/10.1016/j.str.2004.09.009
-
(2004)
Structure.
, vol.12
, pp. 2049-2058
-
-
Craig, D.1
Gao, M.2
Schulten, K.3
Vogel, V.4
-
8
-
-
34547592557
-
MolProbity: all-atom contacts and structure validation for proteins and nucleic acids
-
Davis, I.W., A. Leaver-Fay, V.B. Chen, J.N. Block, G.J. Kapral, X. Wang, L.W. Murray, W.B. Arendall III, J. Snoeyink, J.S. Richardson, and D.C. Richardson. 2007. MolProbity: all-atom contacts and structure validation for proteins and nucleic acids. Nucleic Acids Res. 35(Suppl. 2):W375- W383. http://dx.doi.org/10.1093/nar/gkm216
-
(2007)
Nucleic Acids Res.
, vol.35
, Issue.SUPPL. 2
-
-
Davis, I.W.1
Leaver-Fay, A.2
Chen, V.B.3
Block, J.N.4
Kapral, G.J.5
Wang, X.6
Murray, L.W.7
Arendall III, W.B.8
Snoeyink, J.9
Richardson, J.S.10
Richardson, D.C.11
-
10
-
-
13244281317
-
Coot: model-building tools for molecular graphics
-
Emsley, P., and K. Cowtan. 2004. Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60:2126-2132. http://dx.doi.org/10.1107/S0907444904019158
-
(2004)
Acta Crystallogr. D Biol. Crystallogr.
, vol.60
, pp. 2126-2132
-
-
Emsley, P.1
Cowtan, K.2
-
11
-
-
80053434774
-
3 integrin is extended after activation as measured by solution X-ray scattering and electron microscopy
-
3 integrin is extended after activation as measured by solution X-ray scattering and electron microscopy. J. Biol. Chem. 286:35218-35226. http://dx.doi.org/10.1074/jbc.M111.275107
-
(2011)
J. Biol. Chem.
, vol.286
, pp. 35218-35226
-
-
Eng, E.T.1
Smagghe, B.J.2
Walz, T.3
Springer, T.A.4
-
12
-
-
33644875355
-
Scaling and assessment of data quality
-
Evans, P. 2006. Scaling and assessment of data quality. Acta Crystallogr. D Biol. Crystallogr. 62:72-82. http://dx.doi.org/10.1107/S0907444905036693
-
(2006)
Acta Crystallogr. D Biol. Crystallogr.
, vol.62
, pp. 72-82
-
-
Evans, P.1
-
13
-
-
0024208260
-
Occupancy of an adhesive glycoprotein receptor modulates expression of an antigenic site involved in cell adhesion
-
Frelinger, A.L., III, S.C.T. Lam, E.F. Plow, M.A. Smith, J.C. Loftus, and M.H. Ginsberg. 1988. Occupancy of an adhesive glycoprotein receptor modulates expression of an antigenic site involved in cell adhesion. J. Biol. Chem. 263:12397-12402.
-
(1988)
J. Biol. Chem.
, vol.263
, pp. 12397-12402
-
-
Frelinger, A.L.1
Lam, S.C.T.2
Plow, E.F.3
Smith, M.A.4
Loftus, J.C.5
Ginsberg, M.H.6
-
14
-
-
0025241904
-
Selective inhibition of integrin function by antibodies specific for ligand-occupied receptor conformers
-
Frelinger, A.L., III, I. Cohen, E.F. Plow, M.A. Smith, J. Roberts, S.C.T. Lam, and M.H. Ginsberg. 1990. Selective inhibition of integrin function by antibodies specific for ligand-occupied receptor conformers. J. Biol. Chem. 265:6346-6352.
-
(1990)
J. Biol. Chem.
, vol.265
, pp. 6346-6352
-
-
Frelinger, A.L.1
Cohen, I.2
Plow, E.F.3
Smith, M.A.4
Roberts, J.5
Lam, S.C.T.6
Ginsberg, M.H.7
-
15
-
-
34147153422
-
The beta-tail domain (betaTD) regulates physiologic ligand binding to integrin CD11b/CD18
-
Gupta, V., A. Gylling, J.L. Alonso, T. Sugimori, P. Ianakiev, J.P. Xiong, and M.A. Arnaout. 2007. The beta-tail domain (betaTD) regulates physiologic ligand binding to integrin CD11b/CD18. Blood. 109:3513-3520. http://dx.doi.org/10.1182/blood-2005-11-056689
-
(2007)
Blood.
, vol.109
, pp. 3513-3520
-
-
Gupta, V.1
Gylling, A.2
Alonso, J.L.3
Sugimori, T.4
Ianakiev, P.5
Xiong, J.P.6
Arnaout, M.A.7
-
16
-
-
37249032102
-
Dynamic personalities of proteins
-
Henzler-Wildman, K., and D. Kern. 2007. Dynamic personalities of proteins. Nature. 450:964-972. http://dx.doi.org/10.1038/nature06522
-
(2007)
Nature.
, vol.450
, pp. 964-972
-
-
Henzler-Wildman, K.1
Kern, D.2
-
18
-
-
0038786304
-
Chapter 25.2.9: XDS
-
Kluwer Academic Publishers, Dordrecht, Netherlands
-
Kabsch, W. 2001. Chapter 25.2.9: XDS. In International Tables for Crystallography, Volume F: Crystallography of Biological Macromolecules. M.G. Rossmann and E.V. Arnold, editors. Kluwer Academic Publishers, Dordrecht, Netherlands. 730-734.
-
(2001)
International Tables for Crystallography, Volume F: Crystallography of Biological Macromolecules. M.G. Rossmann and E.V. Arnold, editors
, pp. 730-734
-
-
Kabsch, W.1
-
19
-
-
78649680298
-
3 integrin
-
3 integrin. J. Biol. Chem. 285:38428-38437. http://dx.doi.org/10.1074/jbc.M110.139667
-
(2010)
J. Biol. Chem.
, vol.285
, pp. 38428-38437
-
-
Kamata, T.1
Handa, M.2
Ito, S.3
Sato, Y.4
Ohtani, T.5
Kawai, Y.6
Ikeda, Y.7
Aiso, S.8
-
20
-
-
0042681786
-
Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins
-
Kim, M., C.V. Carman, and T.A. Springer. 2003. Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins. Science. 301:1720-1725. http://dx.doi.org/10.1126/science.1084174
-
(2003)
Science.
, vol.301
, pp. 1720-1725
-
-
Kim, M.1
Carman, C.V.2
Springer, T.A.3
-
21
-
-
71649092785
-
Processing Diffraction Data With MOSFLM
-
R.J. Read and J.L. Sussman, editors. Springer
-
Leslie, A.G.W., and H.R. Powell. 2007. Processing Diffraction Data With MOSFLM. In Evolving Methods for Macromolecular Crystallography. Vol. 245. R.J. Read and J.L. Sussman, editors. Springer. 41-51.
-
(2007)
Evolving Methods for Macromolecular Crystallography
, vol.245
, pp. 41-51
-
-
Leslie, A.G.W.1
Powell, H.R.2
-
22
-
-
0037418254
-
Stabilizing the open conformation of the integrin headpiece with a glycan wedge increases affinity for ligand
-
Luo, B.-H., T.A. Springer, and J. Takagi. 2003. Stabilizing the open conformation of the integrin headpiece with a glycan wedge increases affinity for ligand. Proc. Natl. Acad. Sci. USA. 100:2403-2408. http://dx.doi.org/10.1073/pnas.0438060100
-
(2003)
Proc. Natl. Acad. Sci. USA.
, vol.100
, pp. 2403-2408
-
-
Luo, B.-H.1
Springer, T.A.2
Takagi, J.3
-
23
-
-
16644396938
-
A specific interface between integrin transmembrane helices and affinity for ligand
-
Luo, B.-H., T.A. Springer, and J. Takagi. 2004a. A specific interface between integrin transmembrane helices and affinity for ligand. PLoS Biol. 2:e153. http://dx.doi.org/10.1371/journal.pbio.0020153
-
(2004)
PLoS Biol.
, vol.2
-
-
Luo, B.-H.1
Springer, T.A.2
Takagi, J.3
-
24
-
-
3042602113
-
Allosteric β1 integrin antibodies that stabilize the low affinity state by preventing the swing-out of the hybrid domain
-
Luo, B.-H., K. Strokovich, T. Walz, T.A. Springer, and J. Takagi. 2004b. Allostericβ1 integrin antibodies that stabilize the low affinity state by preventing the swing-out of the hybrid domain. J. Biol. Chem. 279:27466-27471. http://dx.doi.org/10.1074/jbc.M404354200
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 27466-27471
-
-
Luo, B.-H.1
Strokovich, K.2
Walz, T.3
Springer, T.A.4
Takagi, J.5
-
25
-
-
1642305349
-
3 integrin I-like domain into high and low affinity conformations with disulfides
-
3 integrin I-like domain into high and low affinity conformations with disulfides. J. Biol. Chem. 279:10215-10221. http://dx.doi.org/10.1074/jbc.M312732200
-
(2004)
J. Biol. Chem.
, vol.279
, pp. 10215-10221
-
-
Luo, B.-H.1
Takagi, J.2
Springer, T.A.3
-
26
-
-
34247891506
-
Structural basis of integrin regulation and signaling
-
Luo, B.-H., C.V. Carman, and T.A. Springer. 2007. Structural basis of integrin regulation and signaling. Annu. Rev. Immunol. 25:619-647. http://dx.doi.org/10.1146/annurev.immunol.25.022106.141618
-
(2007)
Annu. Rev. Immunol.
, vol.25
, pp. 619-647
-
-
Luo, B.-H.1
Carman, C.V.2
Springer, T.A.3
-
28
-
-
34447508216
-
Phaser crystallographic software
-
McCoy, A.J., R.W. Grosse-Kunstleve, P.D. Adams, M.D. Winn, L.C. Storoni, and R.J. Read. 2007. Phaser crystallographic software. J. Appl. Cryst. 40:658-674. http://dx.doi.org/10.1107/S0021889807021206
-
(2007)
J. Appl. Cryst.
, vol.40
, pp. 658-674
-
-
McCoy, A.J.1
Grosse-Kunstleve, R.W.2
Adams, P.D.3
Winn, M.D.4
Storoni, L.C.5
Read, R.J.6
-
29
-
-
0013307787
-
Conformational changes in the integrin β A domain provide a mechanism for signal transduction via hybrid domain movement
-
Mould, A.P., S.J. Barton, J.A. Askari, P.A. McEwan, P.A. Buckley, S.E. Craig, and M.J. Humphries. 2003a. Conformational changes in the integrin β A domain provide a mechanism for signal transduction via hybrid domain movement. J. Biol. Chem. 278:17028-17035. http://dx.doi.org/10.1074/jbc.M213139200
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 17028-17035
-
-
Mould, A.P.1
Barton, S.J.2
Askari, J.A.3
McEwan, P.A.4
Buckley, P.A.5
Craig, S.E.6
Humphries, M.J.7
-
30
-
-
0141960077
-
Structure of an integrin-ligand complex deduced from solution x-ray scattering and site-directed mutagenesis
-
Mould, A.P., E.J. Symonds, P.A. Buckley, J.G. Grossmann, P.A. McEwan, S.J. Barton, J.A. Askari, S.E. Craig, J. Bella, and M.J. Humphries. 2003b. Structure of an integrin-ligand complex deduced from solution x-ray scattering and site-directed mutagenesis. J. Biol. Chem. 278:39993-39999. http://dx.doi.org/10.1074/jbc.M304627200
-
(2003)
J. Biol. Chem.
, vol.278
, pp. 39993-39999
-
-
Mould, A.P.1
Symonds, E.J.2
Buckley, P.A.3
Grossmann, J.G.4
McEwan, P.A.5
Barton, S.J.6
Askari, J.A.7
Craig, S.E.8
Bella, J.9
Humphries, M.J.10
-
31
-
-
84860273145
-
Crystal structure of α5β1 integrin ectodomain: Atomic details of the fibronectin receptor
-
Nagae, M., S. Re, E. Mihara, T. Nogi, Y. Sugita, and J. Takagi. 2012. Crystal structure of α5β1 integrin ectodomain: Atomic details of the fibronectin receptor. J. Cell Biol. 197:131-140. http://dx.doi.org/10.1083/jcb.201111077
-
(2012)
J. Cell Biol.
, vol.197
, pp. 131-140
-
-
Nagae, M.1
Re, S.2
Mihara, E.3
Nogi, T.4
Sugita, Y.5
Takagi, J.6
-
32
-
-
0023233184
-
Synthetic peptides derived from fibrinogen and fibronectin change the conformation of purified platelet glycoprotein IIb-IIIa
-
Parise, L.V., S.L. Helgerson, B. Steiner, L. Nannizzi, and D.R. Phillips. 1987. Synthetic peptides derived from fibrinogen and fibronectin change the conformation of purified platelet glycoprotein IIb-IIIa. J. Biol. Chem. 262:12597-12602.
-
(1987)
J. Biol. Chem.
, vol.262
, pp. 12597-12602
-
-
Parise, L.V.1
Helgerson, S.L.2
Steiner, B.3
Nannizzi, L.4
Phillips, D.R.5
-
33
-
-
0345518379
-
The effect of Arg-Gly-Asp-containing peptides on fibrinogen and von Willebrand factor binding to platelets
-
Plow, E.F., M.D. Pierschbacher, E. Ruoslahti, G.A. Marguerie, and M.H. Ginsberg. 1985. The effect of Arg-Gly-Asp-containing peptides on fibrinogen and von Willebrand factor binding to platelets. Proc. Natl. Acad. Sci. USA. 82:8057-8061. http://dx.doi.org/10.1073/pnas.82.23.8057
-
(1985)
Proc. Natl. Acad. Sci. USA.
, vol.82
, pp. 8057-8061
-
-
Plow, E.F.1
Pierschbacher, M.D.2
Ruoslahti, E.3
Marguerie, G.A.4
Ginsberg, M.H.5
-
34
-
-
73649108263
-
Integrin activation dynamics between the RGD-binding site and the headpiece hinge
-
Puklin-Faucher, E., and V. Vogel. 2009. Integrin activation dynamics between the RGD-binding site and the headpiece hinge. J. Biol. Chem. 284:36557-36568. http://dx.doi.org/10.1074/jbc.M109.041194
-
(2009)
J. Biol. Chem.
, vol.284
, pp. 36557-36568
-
-
Puklin-Faucher, E.1
Vogel, V.2
-
35
-
-
33750337536
-
How the headpiece hinge angle is opened: New insights into the dynamics of integrin activation
-
Puklin-Faucher, E., M. Gao, K. Schulten, and V. Vogel. 2006. How the headpiece hinge angle is opened: New insights into the dynamics of integrin activation. J. Cell Biol. 175:349-360. http://dx.doi.org/10.1083/jcb.200602071
-
(2006)
J. Cell Biol.
, vol.175
, pp. 349-360
-
-
Puklin-Faucher, E.1
Gao, M.2
Schulten, K.3
Vogel, V.4
-
36
-
-
82455189778
-
Regulation of integrin affinity on cell surfaces
-
Schürpf, T., and T.A. Springer. 2011. Regulation of integrin affinity on cell surfaces. EMBO J. 30:4712-4727. http://dx.doi.org/10.1038/emboj.2011.333
-
(2011)
EMBO J.
, vol.30
, pp. 4712-4727
-
-
Schürpf, T.1
Springer, T.A.2
-
37
-
-
79959250326
-
Latent TGF-β structure and activation
-
Shi, M., J. Zhu, R. Wang, X. Chen, L. Mi, T. Walz, and T.A. Springer. 2011. Latent TGF-β structure and activation. Nature. 474:343-349. http://dx.doi.org/10.1038/nature10152
-
(2011)
Nature.
, vol.474
, pp. 343-349
-
-
Shi, M.1
Zhu, J.2
Wang, R.3
Chen, X.4
Mi, L.5
Walz, T.6
Springer, T.A.7
-
38
-
-
77958477970
-
Modulation of integrin activation by an entropic spring in the β-knee
-
Smagghe, B.J., P.S. Huang, Y.-E. Ban, D. Baker, and T.A. Springer. 2010. Modulation of integrin activation by an entropic spring in the β-knee. J. Biol. Chem. 285:32954-32966. http://dx.doi.org/10.1074/jbc.M110.145177
-
(2010)
J. Biol. Chem.
, vol.285
, pp. 32954-32966
-
-
Smagghe, B.J.1
Huang, P.S.2
Ban, Y.-E.3
Baker, D.4
Springer, T.A.5
-
39
-
-
84857688656
-
Integrin inside-out signaling and the immunological synapse
-
Springer, T.A., and M.L. Dustin. 2012. Integrin inside-out signaling and the immunological synapse. Curr. Opin. Cell Biol. 24:107-115. http://dx.doi.org/10.1016/j.ceb.2011.10.004
-
(2012)
Curr. Opin. Cell Biol.
, vol.24
, pp. 107-115
-
-
Springer, T.A.1
Dustin, M.L.2
-
41
-
-
0037031906
-
Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling
-
Takagi, J., B.M. Petre, T. Walz, and T.A. Springer. 2002. Global conformational rearrangements in integrin extracellular domains in outside-in and inside-out signaling. Cell. 110:599-11. http://dx.doi.org/10.1016/S0092-8674(02)00935-2
-
(2002)
Cell.
, vol.110
, pp. 599-511
-
-
Takagi, J.1
Petre, B.M.2
Walz, T.3
Springer, T.A.4
-
42
-
-
0141625303
-
Structure of integrin α5β1 in complex with fibronectin
-
Takagi, J., K. Strokovich, T.A. Springer, and T. Walz. 2003. Structure of integrin α5β1 in complex with fibronectin. EMBO J. 22:4607-4615. http://dx.doi.org/10.1093/emboj/cdg445
-
(2003)
EMBO J.
, vol.22
, pp. 4607-4615
-
-
Takagi, J.1
Strokovich, K.2
Springer, T.A.3
Walz, T.4
-
43
-
-
84863371008
-
GARP regulates the bioavailability and activation of TGFβ
-
Wang, R., J. Zhu, X. Dong, M. Shi, C. Lu, and T.A. Springer. 2012. GARP regulates the bioavailability and activation of TGFβ. Mol. Biol. Cell. 23:1129-1139. http://dx.doi.org/10.1091/mbc.E11-12-1018
-
(2012)
Mol. Biol. Cell.
, vol.23
, pp. 1129-1139
-
-
Wang, R.1
Zhu, J.2
Dong, X.3
Shi, M.4
Lu, C.5
Springer, T.A.6
-
44
-
-
8544259562
-
Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeutics
-
Xiao, T., J. Takagi, B.S. Coller, J.H. Wang, and T.A. Springer. 2004. Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeutics. Nature. 432:59-67. http://dx.doi.org/10.1038/nature02976
-
(2004)
Nature.
, vol.432
, pp. 59-67
-
-
Xiao, T.1
Takagi, J.2
Coller, B.S.3
Wang, J.H.4
Springer, T.A.5
-
45
-
-
76349099822
-
Structure of an integrin with an αI domain, complement receptor type 4
-
Xie, C., J. Zhu, X. Chen, L. Mi, N. Nishida, and T.A. Springer. 2010. Structure of an integrin with an αI domain, complement receptor type 4. EMBO J. 29:666-679. http://dx.doi.org/10.1038/emboj.2009.367
-
(2010)
EMBO J.
, vol.29
, pp. 666-679
-
-
Xie, C.1
Zhu, J.2
Chen, X.3
Mi, L.4
Nishida, N.5
Springer, T.A.6
-
46
-
-
0035850669
-
Crystal structure of the extracellular segment of integrin αVβ3
-
Xiong, J.-P., T. Stehle, B. Diefenbach, R. Zhang, R. Dunker, D.L. Scott, A. Joachimiak, S.L. Goodman, and M.A. Arnaout. 2001. Crystal structure of the extracellular segment of integrin αVβ3. Science. 294:339-345. http://dx.doi.org/10.1126/science.1064535
-
(2001)
Science.
, vol.294
, pp. 339-345
-
-
Xiong, J.-P.1
Stehle, T.2
Diefenbach, B.3
Zhang, R.4
Dunker, R.5
Scott, D.L.6
Joachimiak, A.7
Goodman, S.L.8
Arnaout, M.A.9
-
47
-
-
0037023363
-
Crystal structure of the extracellular segment of integrin αVβ3 in complex with an Arg-Gly-Asp ligand
-
Xiong, J.-P., T. Stehle, R. Zhang, A. Joachimiak, M. Frech, S.L. Goodman, and M.A. Arnaout. 2002. Crystal structure of the extracellular segment of integrin αVβ3 in complex with an Arg-Gly-Asp ligand. Science. 296:151-155. http://dx.doi.org/10.1126/science.1069040
-
(2002)
Science.
, vol.296
, pp. 151-155
-
-
Xiong, J.-P.1
Stehle, T.2
Zhang, R.3
Joachimiak, A.4
Frech, M.5
Goodman, S.L.6
Arnaout, M.A.7
-
48
-
-
69449084406
-
Crystal structure of the complete integrin αVβ3 ectodomain plus an α/β transmembrane fragment
-
Xiong, J.-P., B. Mahalingham, J.L. Alonso, L.A. Borrelli, X. Rui, S. Anand, B.T. Hyman, T. Rysiok, D. Müller-Pompalla, S.L. Goodman, and M.A. Arnaout. 2009. Crystal structure of the complete integrin αVβ3 ectodomain plus an α/β transmembrane fragment. J. Cell Biol. 186:589-600. http://dx.doi.org/10.1083/jcb.200905085
-
(2009)
J. Cell Biol.
, vol.186
, pp. 589-600
-
-
Xiong, J.-P.1
Mahalingham, B.2
Alonso, J.L.3
Borrelli, L.A.4
Rui, X.5
Anand, S.6
Hyman, B.T.7
Rysiok, T.8
Müller-Pompalla, D.9
Goodman, S.L.10
Arnaout, M.A.11
-
49
-
-
1442306162
-
Activation of integrin β-subunit I-like domains by one-turn C-terminal α-helix deletions
-
Yang, W., M. Shimaoka, J.F. Chen, and T.A. Springer. 2004. Activation of integrin β-subunit I-like domains by one-turn C-terminal α-helix deletions. Proc. Natl. Acad. Sci. USA. 101:2333-2338. http://dx.doi.org/10.1073/pnas.0307291101
-
(2004)
Proc. Natl. Acad. Sci. USA.
, vol.101
, pp. 2333-2338
-
-
Yang, W.1
Shimaoka, M.2
Chen, J.F.3
Springer, T.A.4
-
50
-
-
84863012638
-
7, an integrin that mediates rolling adhesion
-
7, an integrin that mediates rolling adhesion. J. Cell Biol. 196:131-146. http://dx.doi.org/10.1083/jcb.201110023
-
(2012)
J. Cell Biol.
, vol.196
, pp. 131-146
-
-
Yu, Y.1
Zhu, J.2
Mi, L.Z.3
Walz, T.4
Sun, H.5
Chen, J.-F.6
Springer, T.A.7
-
51
-
-
34249685565
-
Tests of the extension and deadbolt models of integrin activation
-
Zhu, J., B. Boylan, B.-H. Luo, P.J. Newman, and T.A. Springer. 2007a. Tests of the extension and deadbolt models of integrin activation. J. Biol. Chem. 282:11914-11920. http://dx.doi.org/10.1074/jbc.M700249200
-
(2007)
J. Biol. Chem.
, vol.282
, pp. 11914-11920
-
-
Zhu, J.1
Boylan, B.2
Luo, B.-H.3
Newman, P.J.4
Springer, T.A.5
-
52
-
-
34948882323
-
Requirement of α and β subunit transmembrane helix separation for integrin outside-in signaling
-
Zhu, J., C.V. Carman, M. Kim, M. Shimaoka, T.A. Springer, and B.-H. Luo. 2007b. Requirement of α and β subunit transmembrane helix separation for integrin outside-in signaling. Blood. 110:2475-2483. http://dx.doi.org/10.1182/blood-2007-03-080077
-
(2007)
Blood.
, vol.110
, pp. 2475-2483
-
-
Zhu, J.1
Carman, C.V.2
Kim, M.3
Shimaoka, M.4
Springer, T.A.5
Luo, B.-H.6
-
53
-
-
57749116060
-
Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces
-
Zhu, J., B.H. Luo, T. Xiao, C. Zhang, N. Nishida, and T.A. Springer. 2008. Structure of a complete integrin ectodomain in a physiologic resting state and activation and deactivation by applied forces. Mol. Cell. 32:849-861. http://dx.doi.org/10.1016/j.molcel.2008.11.018
-
(2008)
Mol. Cell.
, vol.32
, pp. 849-861
-
-
Zhu, J.1
Luo, B.H.2
Xiao, T.3
Zhang, C.4
Nishida, N.5
Springer, T.A.6
-
55
-
-
84863375270
-
2+ binding to the MIDAS
-
125ra32
-
2+ binding to the MIDAS. Sci. Transl. Med. 4:125ra32. http://dx.doi.org/10.1126/scitranslmed.3003576
-
(2012)
Sci. Transl. Med.
, vol.4
-
-
Zhu, J.1
Choi, W.-S.2
McCoy, J.G.3
Negri, A.4
Zhu, J.5
Naini, S.6
Li, J.7
Shen, M.8
Huang, W.9
Bougie, D.10
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