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Volumn 14, Issue 10, 2012, Pages 1046-1056

Stimulus-dependent phosphorylation of profilin-1 in angiogenesis

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN BINDING PROTEIN; PROFILIN I; PROTEIN TYROSINE KINASE; TYROSINE; UNCLASSIFIED DRUG; VASCULOTROPIN A; VASCULOTROPIN RECEPTOR 2;

EID: 84867072337     PISSN: 14657392     EISSN: 14764679     Source Type: Journal    
DOI: 10.1038/ncb2580     Document Type: Article
Times cited : (61)

References (65)
  • 1
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard, T. D. & Borisy, G. G. Cellular motility driven by assembly and disassembly of actin filaments. Cell 112, 453-465 (2003).
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 2
    • 0037378124 scopus 로고    scopus 로고
    • Actin binding proteins: Regulation of cytoskeletal microfilaments
    • Dos Remedios, C. G. et al. Actin binding proteins: regulation of cytoskeletal microfilaments. Physiol. Rev. 83, 433-473 (2003).
    • (2003) Physiol. Rev. , vol.83 , pp. 433-473
    • Dos Remedios, C.G.1
  • 3
    • 52649143876 scopus 로고    scopus 로고
    • Eukaryotic chemotaxis at a glance
    • Bagorda, A. & Parent, C. A. Eukaryotic chemotaxis at a glance. J. Cell Sci. 121, 2621-2624 (2008).
    • (2008) J. Cell Sci. , vol.121 , pp. 2621-2624
    • Bagorda, A.1    Parent, C.A.2
  • 4
    • 85013312416 scopus 로고
    • Tumor angiogenesis: Therapeutic implications
    • Folkman, J. Tumor angiogenesis: therapeutic implications. N. Engl. J. Med. 285, 1182-1186 (1971).
    • (1971) N. Engl. J. Med. , vol.285 , pp. 1182-1186
    • Folkman, J.1
  • 5
    • 27944473690 scopus 로고    scopus 로고
    • VEGF as a key mediator of angiogenesis in cancer
    • Carmeliet, P. VEGF as a key mediator of angiogenesis in cancer. Oncology 69 S3, 4-10 (2005).
    • (2005) Oncology , vol.69 , Issue.S3 , pp. 4-10
    • Carmeliet, P.1
  • 6
    • 34147171490 scopus 로고    scopus 로고
    • Endothelial cell migration during angiogenesis
    • Lamalice, L., Le Boeuf, F. & Huot, J. Endothelial cell migration during angiogenesis. Circ. Res. 100, 782-794 (2007).
    • (2007) Circ. Res. , vol.100 , pp. 782-794
    • Lamalice, L.1    Le Boeuf, F.2    Huot, J.3
  • 7
    • 16944362446 scopus 로고    scopus 로고
    • Angiogenesis in ischemic heart disease
    • Ware, J. A. & Simons, M. Angiogenesis in ischemic heart disease. Nat. Med. 3, 158-164 (1997).
    • (1997) Nat. Med. , vol.3 , pp. 158-164
    • Ware, J.A.1    Simons, M.2
  • 8
    • 34249689753 scopus 로고    scopus 로고
    • Molecular regulation of angiogenesis and lymphangiogen-esis
    • Adams, R. H. & Alitalo, K. Molecular regulation of angiogenesis and lymphangiogen-esis. Nat. Rev. Mol. Cell Biol. 8, 464-478 (2007).
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 464-478
    • Adams, R.H.1    Alitalo, K.2
  • 9
    • 0037815292 scopus 로고    scopus 로고
    • VEGF guides angiogenic sprouting utilizing endothelial tip cell filopodia
    • Gerhardt, H. et al. VEGF guides angiogenic sprouting utilizing endothelial tip cell filopodia. J. Cell Biol. 161, 1163-1177 (2003).
    • (2003) J. Cell Biol. , vol.161 , pp. 1163-1177
    • Gerhardt, H.1
  • 10
    • 0037699954 scopus 로고    scopus 로고
    • The biology of VEGF and its receptors
    • Ferrara, N., Gerber, H. P. & LeCouter, J. The biology of VEGF and its receptors. Nat. Med. 9, 669-676 (2003).
    • (2003) Nat. Med. , vol.9 , pp. 669-676
    • Ferrara, N.1    Gerber, H.P.2    Lecouter, J.3
  • 11
    • 0041743159 scopus 로고    scopus 로고
    • VEGF-induced neuroprotection, neurogenesis, and angiogenesis after focal cerebral ischemia
    • Sun, Y. et al. VEGF-induced neuroprotection, neurogenesis, and angiogenesis after focal cerebral ischemia. J. Clin. Invest. 111, 1843-1851 (2003).
    • (2003) J. Clin. Invest. , vol.111 , pp. 1843-1851
    • Sun, Y.1
  • 12
    • 0035957436 scopus 로고    scopus 로고
    • Profilin i is essential for cell survival and cell division in early mouse development
    • Witke, W., Sutherland, J. D., Sharpe, A., Arai, M. & Kwiatkowski, D. J. Profilin I is essential for cell survival and cell division in early mouse development. Proc. Natl Acad. Sci. USA 98, 3832-3836 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 3832-3836
    • Witke, W.1    Sutherland, J.D.2    Sharpe, A.3    Arai, M.4    Kwiatkowski, D.J.5
  • 13
    • 0021334627 scopus 로고
    • Physical, immunochemical, and functional properties of Acanthamoeba profilin
    • Tseng, P. C., Runge, M. S., Cooper, J. A., Williams, R. C. Jr & Pollard, T. D. Physical, immunochemical, and functional properties of Acanthamoeba profilin. J. Cell Biol. 98, 214-221 (1984).
    • (1984) J. Cell Biol. , vol.98 , pp. 214-221
    • Tseng, P.C.1    Runge, M.S.2    Cooper, J.A.3    Williams, Jr.R.C.4    Pollard, T.D.5
  • 15
    • 4143120075 scopus 로고    scopus 로고
    • The role of profilin complexes in cell motility and other cellular processes
    • Witke, W. The role of profilin complexes in cell motility and other cellular processes. Trends Cell Biol. 14, 461-469 (2004).
    • (2004) Trends Cell Biol. , vol.14 , pp. 461-469
    • Witke, W.1
  • 16
    • 0028004565 scopus 로고
    • Dictyostelium amoebae that lack G-actin-sequestering profilins show defects in F-actin content, cytokinesis, and development
    • Haugwitz, M., Noegel, A. A., Karakesisoglou, J. & Schleicher, M. Dictyostelium amoebae that lack G-actin-sequestering profilins show defects in F-actin content, cytokinesis, and development. Cell 79, 303-314 (1994).
    • (1994) Cell , vol.79 , pp. 303-314
    • Haugwitz, M.1    Noegel, A.A.2    Karakesisoglou, J.3    Schleicher, M.4
  • 17
    • 0028212157 scopus 로고
    • Profilin mutations disrupt multiple actin-dependent processes during Drosophila development
    • Verheyen, E. M. & Cooley, L. Profilin mutations disrupt multiple actin-dependent processes during Drosophila development. Development 120, 717-728 (1994).
    • (1994) Development , vol.120 , pp. 717-728
    • Verheyen, E.M.1    Cooley, L.2
  • 18
    • 33750443578 scopus 로고    scopus 로고
    • Silencing profilin-1 inhibits endothelial cell proliferation, migration and cord morphogenesis
    • Ding, Z., Lambrechts, A., Parepally, M. & Roy, P. Silencing profilin-1 inhibits endothelial cell proliferation, migration and cord morphogenesis. J. Cell Sci. 119, 4127-4137 (2006).
    • (2006) J. Cell Sci. , vol.119 , pp. 4127-4137
    • Ding, Z.1    Lambrechts, A.2    Parepally, M.3    Roy, P.4
  • 19
    • 65549110635 scopus 로고    scopus 로고
    • Spatial coordination of actin polymerization and ILK-Akt2 activity during endothelial cell migration
    • Fan, Y., Gong, Y., Ghosh, P. K., Graham, L. M. & Fox, P. L. Spatial coordination of actin polymerization and ILK-Akt2 activity during endothelial cell migration. Dev. Cell 16, 661-674 (2009).
    • (2009) Dev. Cell , vol.16 , pp. 661-674
    • Fan, Y.1    Gong, Y.2    Ghosh, P.K.3    Graham, L.M.4    Fox, P.L.5
  • 20
    • 21144458164 scopus 로고    scopus 로고
    • Immunoaffinity profiling of tyrosine phosphorylation in cancer cells
    • Rush, J. et al. Immunoaffinity profiling of tyrosine phosphorylation in cancer cells. Nat. Biotechnol. 23, 94-101 (2005).
    • (2005) Nat. Biotechnol. , vol.23 , pp. 94-101
    • Rush, J.1
  • 21
    • 36849065315 scopus 로고    scopus 로고
    • Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer
    • Rikova, K. et al. Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer. Cell 131, 1190-1203 (2007).
    • (2007) Cell , vol.131 , pp. 1190-1203
    • Rikova, K.1
  • 22
    • 1642575214 scopus 로고    scopus 로고
    • Phosphorylation of profilin regulates its interaction with actin and poly (L-proline)
    • Sathish, K. et al. Phosphorylation of profilin regulates its interaction with actin and poly (L-proline). Cell Signal. 16, 589-596 (2004).
    • (2004) Cell Signal. , vol.16 , pp. 589-596
    • Sathish, K.1
  • 23
    • 0344653597 scopus 로고    scopus 로고
    • Effects of single amino acid substitutions in the actin-binding site on the biological activity of bovine profilin i
    • Schluter, K., Schleicher, M. & Jockusch, B. M. Effects of single amino acid substitutions in the actin-binding site on the biological activity of bovine profilin I. J. Cell Sci. 111, 3261-3273 (1998).
    • (1998) J. Cell Sci. , vol.111 , pp. 3261-3273
    • Schluter, K.1    Schleicher, M.2    Jockusch, B.M.3
  • 25
    • 0033601258 scopus 로고    scopus 로고
    • Profilin promotes barbed-end actin filament assembly without lowering the critical concentration
    • Kang, F., Purich, D. L. & Southwick, F. S. Profilin promotes barbed-end actin filament assembly without lowering the critical concentration. J. Biol. Chem. 274, 36963-36972 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 36963-36972
    • Kang, F.1    Purich, D.L.2    Southwick, F.S.3
  • 26
    • 0035185978 scopus 로고    scopus 로고
    • Cell motility: Proline-rich proteins promote protrusions
    • Holt, M. R. & Koffer, A. Cell motility: proline-rich proteins promote protrusions. Trends Cell Biol. 11, 38-46 (2001).
    • (2001) Trends Cell Biol. , vol.11 , pp. 38-46
    • Holt, M.R.1    Koffer, A.2
  • 27
    • 0027772556 scopus 로고
    • How profilin promotes actin filament assembly in the presence of thymosin β4
    • Pantaloni, D. & Carlier, M. F. How profilin promotes actin filament assembly in the presence of thymosin β4. Cell 75, 1007-1014 (1993).
    • (1993) Cell , vol.75 , pp. 1007-1014
    • Pantaloni, D.1    Carlier, M.F.2
  • 28
    • 70349459722 scopus 로고    scopus 로고
    • Both actin and polyproline interactions of profilin-1 are required for migration, invasion and capillary morphogenesis of vascular endothelial cells
    • Ding, Z., Gau, D., Deasy, B., Wells, A. & Roy, P. Both actin and polyproline interactions of profilin-1 are required for migration, invasion and capillary morphogenesis of vascular endothelial cells. Exp. Cell Res. 315, 2963-2973 (2009).
    • (2009) Exp. Cell Res. , vol.315 , pp. 2963-2973
    • Ding, Z.1    Gau, D.2    Deasy, B.3    Wells, A.4    Roy, P.5
  • 29
    • 0034605099 scopus 로고    scopus 로고
    • Profilin enhances Cdc42-induced nucleation of actin polymerization
    • Yang, C. et al. Profilin enhances Cdc42-induced nucleation of actin polymerization. J. Cell Biol. 150, 1001-1012 (2000).
    • (2000) J. Cell Biol. , vol.150 , pp. 1001-1012
    • Yang, C.1
  • 30
    • 0029025248 scopus 로고
    • The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins
    • Reinhard, M. et al. The proline-rich focal adhesion and microfilament protein VASP is a ligand for profilins. EMBO J. 14, 1583-1589 (1995).
    • (1995) EMBO J. , vol.14 , pp. 1583-1589
    • Reinhard, M.1
  • 31
    • 35649021883 scopus 로고    scopus 로고
    • Structural basis for the recruitment of profilin-actin complexes during filament elongation by Ena/VASP
    • Ferron, F., Rebowski, G., Lee, S. H. & Dominguez, R. Structural basis for the recruitment of profilin-actin complexes during filament elongation by Ena/VASP. EMBO J. 26, 4597-4606 (2007).
    • (2007) EMBO J. , vol.26 , pp. 4597-4606
    • Ferron, F.1    Rebowski, G.2    Lee, S.H.3    Dominguez, R.4
  • 32
  • 33
    • 0034000699 scopus 로고    scopus 로고
    • VEGF receptor signaling in tumor angiogenesis
    • McMahon, G. VEGF receptor signaling in tumor angiogenesis. Oncologist 5 S1, 3-10 (2000).
    • (2000) Oncologist , vol.5 , Issue.S1 , pp. 3-10
    • McMahon, G.1
  • 35
    • 0031905861 scopus 로고    scopus 로고
    • Vascular endothelial growth factor D (VEGF-D) is a ligand for the tyrosine kinases VEGF receptor 2 (Flk1) and VEGF receptor 3 (Flt4)
    • Achen, M. G. et al. Vascular endothelial growth factor D (VEGF-D) is a ligand for the tyrosine kinases VEGF receptor 2 (Flk1) and VEGF receptor 3 (Flt4). Proc. Natl Acad. Sci. USA 95, 548-553 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 548-553
    • Achen, M.G.1
  • 36
    • 0030026897 scopus 로고    scopus 로고
    • A novel vascular endothelial growth factor, VEGF-C, is a ligand for the Flt4 (VEGFR-3) and KDR (VEGFR-2) receptor tyrosine kinases
    • Joukov, V. et al. A novel vascular endothelial growth factor, VEGF-C, is a ligand for the Flt4 (VEGFR-3) and KDR (VEGFR-2) receptor tyrosine kinases. EMBO J. 15, 290-298 (1996).
    • (1996) EMBO J. , vol.15 , pp. 290-298
    • Joukov, V.1
  • 37
    • 0036962410 scopus 로고    scopus 로고
    • Placental growth factor (PlGF) and its receptor Flt-1 (VEGFR-1): Novel therapeutic targets for angiogenic disorders
    • Luttun, A., Tjwa, M. & Carmeliet, P. Placental growth factor (PlGF) and its receptor Flt-1 (VEGFR-1): novel therapeutic targets for angiogenic disorders. Ann. N.Y. Acad. Sci. 979, 80-93 (2002).
    • (2002) Ann. N.Y. Acad. Sci. , vol.979 , pp. 80-93
    • Luttun, A.1    Tjwa, M.2    Carmeliet, P.3
  • 38
    • 22744447871 scopus 로고    scopus 로고
    • VEGF receptor-2 Y951 signaling and a role for the adapter molecule TSAd in tumor angiogenesis
    • Matsumoto, T. et al. VEGF receptor-2 Y951 signaling and a role for the adapter molecule TSAd in tumor angiogenesis. EMBO J. 24, 2342-2353 (2005).
    • (2005) EMBO J. , vol.24 , pp. 2342-2353
    • Matsumoto, T.1
  • 39
    • 0035947584 scopus 로고    scopus 로고
    • Identification of tyrosine residues in vascular endothelial growth factor receptor-2/FLK-1 involved in activation of phosphatidylinositol 3-kinase and cell proliferation
    • Dayanir, V., Meyer, R. D., Lashkari, K. & Rahimi, N. Identification of tyrosine residues in vascular endothelial growth factor receptor-2/FLK-1 involved in activation of phosphatidylinositol 3-kinase and cell proliferation. J. Biol. Chem. 276, 17686-17692 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 17686-17692
    • Dayanir, V.1    Meyer, R.D.2    Lashkari, K.3    Rahimi, N.4
  • 40
    • 0344305784 scopus 로고    scopus 로고
    • Cell migration: Integrating signals from front to back
    • Ridley, A. J. et al. Cell migration: integrating signals from front to back. Science 302, 1704-1709 (2003).
    • (2003) Science , vol.302 , pp. 1704-1709
    • Ridley, A.J.1
  • 41
    • 17344363565 scopus 로고    scopus 로고
    • Cell polarization mechanisms during directed cell migration
    • Huttenlocher, A. Cell polarization mechanisms during directed cell migration. Nat. Cell Biol. 7, 336-337 (2005).
    • (2005) Nat. Cell Biol. , vol.7 , pp. 336-337
    • Huttenlocher, A.1
  • 42
    • 25444522479 scopus 로고    scopus 로고
    • Role of angiogenesis in cardiovascular disease: A critical appraisal
    • Khurana, R., Simons, M., Martin, J. F. & Zachary, I. C. Role of angiogenesis in cardiovascular disease: a critical appraisal. Circulation 112, 1813-1824 (2005).
    • (2005) Circulation , vol.112 , pp. 1813-1824
    • Khurana, R.1    Simons, M.2    Martin, J.F.3    Zachary, I.C.4
  • 43
    • 0035865048 scopus 로고    scopus 로고
    • Tie2-Cre transgenic mice: A new model for endothelial cell-lineage analysis in vivo
    • Kisanuki, Y. Y. et al. Tie2-Cre transgenic mice: a new model for endothelial cell-lineage analysis in vivo. Dev. Biol. 230, 230-242 (2001).
    • (2001) Dev. Biol. , vol.230 , pp. 230-242
    • Kisanuki, Y.Y.1
  • 44
    • 10744231991 scopus 로고    scopus 로고
    • Endothelial cells require STAT3 for protection against endotoxin-induced inflammation
    • Kano, A. et al. Endothelial cells require STAT3 for protection against endotoxin-induced inflammation. J. Exp. Med. 198, 1517-1525 (2003).
    • (2003) J. Exp. Med. , vol.198 , pp. 1517-1525
    • Kano, A.1
  • 45
    • 77953029002 scopus 로고    scopus 로고
    • Ephrin-B2 controls VEGF-induced angiogenesis and lymphangiogen-esis
    • Wang, Y. et al. Ephrin-B2 controls VEGF-induced angiogenesis and lymphangiogen-esis. Nature 465, 483-486 (2010).
    • (2010) Nature , vol.465 , pp. 483-486
    • Wang, Y.1
  • 46
    • 84859453770 scopus 로고    scopus 로고
    • Notch-dependent VEGFR3 upregulation allows angiogenesis without VEGF-VEGFR2 signalling
    • Benedito, R. et al. Notch-dependent VEGFR3 upregulation allows angiogenesis without VEGF-VEGFR2 signalling. Nature 484, 110-114 (2012).
    • (2012) Nature , vol.484 , pp. 110-114
    • Benedito, R.1
  • 47
    • 0034635513 scopus 로고    scopus 로고
    • Polarization of chemoattractant receptor signaling during neutrophil chemotaxis
    • Servant, G. et al. Polarization of chemoattractant receptor signaling during neutrophil chemotaxis. Science 287, 1037-1040 (2000).
    • (2000) Science , vol.287 , pp. 1037-1040
    • Servant, G.1
  • 49
    • 0037205265 scopus 로고    scopus 로고
    • Spatial and temporal regulation of 3-phosphoinositides by PI 3-kinase and PTEN mediates chemotaxis
    • Funamoto, S., Meili, R., Lee, S., Parry, L. & Firtel, R. A. Spatial and temporal regulation of 3-phosphoinositides by PI 3-kinase and PTEN mediates chemotaxis. Cell 109, 611-623 (2002).
    • (2002) Cell , vol.109 , pp. 611-623
    • Funamoto, S.1    Meili, R.2    Lee, S.3    Parry, L.4    Firtel, R.A.5
  • 50
    • 33750948427 scopus 로고    scopus 로고
    • Spatial and temporal control of cofilin activity is required for directional sensing during chemotaxis
    • Mouneimne, G. et al. Spatial and temporal control of cofilin activity is required for directional sensing during chemotaxis. Curr. Biol. 16, 2193-2205 (2006).
    • (2006) Curr. Biol. , vol.16 , pp. 2193-2205
    • Mouneimne, G.1
  • 51
    • 44349119736 scopus 로고    scopus 로고
    • Angiogenesis selectively requires the p110α isoform of PI3K to control endothelial cell migration
    • Graupera, M. et al. Angiogenesis selectively requires the p110α isoform of PI3K to control endothelial cell migration. Nature 453, 662-666 (2008).
    • (2008) Nature , vol.453 , pp. 662-666
    • Graupera, M.1
  • 52
    • 13944267041 scopus 로고    scopus 로고
    • Inhibition of endothelial cell migration by thrombospondin-1 type-1 repeats is mediated by β1 integrins
    • Short, S. M. et al. Inhibition of endothelial cell migration by thrombospondin-1 type-1 repeats is mediated by β1 integrins. J. Cell Biol. 168, 643-653 (2005).
    • (2005) J. Cell Biol. , vol.168 , pp. 643-653
    • Short, S.M.1
  • 53
    • 0033602091 scopus 로고    scopus 로고
    • Autophosphorylation of KDR in the kinase domain is required for maximal VEGF-stimulated kinase activity and receptor internalization
    • Dougher, M. & Terman, B. I. Autophosphorylation of KDR in the kinase domain is required for maximal VEGF-stimulated kinase activity and receptor internalization. Oncogene 18, 1619-1627 (1999).
    • (1999) Oncogene , vol.18 , pp. 1619-1627
    • Dougher, M.1    Terman, B.I.2
  • 54
    • 24344446438 scopus 로고    scopus 로고
    • The PTEN/PI3K pathway governs normal vascular development and tumor angiogenesis
    • Hamada, K. et al. The PTEN/PI3K pathway governs normal vascular development and tumor angiogenesis. Genes Dev. 19, 2054-2065 (2005).
    • (2005) Genes Dev. , vol.19 , pp. 2054-2065
    • Hamada, K.1
  • 55
    • 0037188941 scopus 로고    scopus 로고
    • Role of Akt signaling in vascular homeostasis and angiogenesis
    • Shiojima, I. & Walsh, K. Role of Akt signaling in vascular homeostasis and angiogenesis. Circ. Res. 90, 1243-1250 (2002).
    • (2002) Circ. Res. , vol.90 , pp. 1243-1250
    • Shiojima, I.1    Walsh, K.2
  • 56
    • 0037205048 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase pathway
    • Cantley, L. C. The phosphoinositide 3-kinase pathway. Science 296, 1655-1657 (2002).
    • (2002) Science , vol.296 , pp. 1655-1657
    • Cantley, L.C.1
  • 57
    • 51849084360 scopus 로고    scopus 로고
    • The PTEN-PI3K pathway: Of feedbacks and cross-talks
    • Carracedo, A. & Pandolfi, P. P. The PTEN-PI3K pathway: of feedbacks and cross-talks. Oncogene 27, 5527-5541 (2008).
    • (2008) Oncogene , vol.27 , pp. 5527-5541
    • Carracedo, A.1    Pandolfi, P.P.2
  • 58
    • 1642617693 scopus 로고    scopus 로고
    • PI3K/Akt signalling pathway and cancer
    • Fresno Vara, J. A. et al. PI3K/Akt signalling pathway and cancer. Cancer Treat. Rev. 30, 193-204 (2004).
    • (2004) Cancer Treat. Rev. , vol.30 , pp. 193-204
    • Fresno Vara, J.A.1
  • 59
    • 67651095905 scopus 로고    scopus 로고
    • Two-site phosphorylation of EPRS coordinates multimodal regulation of noncanonical translational control activity
    • Arif, A. et al. Two-site phosphorylation of EPRS coordinates multimodal regulation of noncanonical translational control activity. Mol. Cell 35, 164-180 (2009).
    • (2009) Mol. Cell , vol.35 , pp. 164-180
    • Arif, A.1
  • 60
    • 0032581001 scopus 로고    scopus 로고
    • The role of profilin in actin polymerization and nucleotide exchange
    • Korenbaum, E. et al. The role of profilin in actin polymerization and nucleotide exchange. Biochemistry 37, 9274-9283 (1998).
    • (1998) Biochemistry , vol.37 , pp. 9274-9283
    • Korenbaum, E.1
  • 61
    • 65449131260 scopus 로고    scopus 로고
    • Lipid binding to the tail domain of vinculin: Specificity and the role of the N and C termini
    • Palmer, S. M., Playford, M. P., Craig, S. W., Schaller, M. D. & Campbell, S. L. Lipid binding to the tail domain of vinculin: specificity and the role of the N and C termini. J. Biol. Chem. 284, 7223-7231 (2009).
    • (2009) J. Biol. Chem. , vol.284 , pp. 7223-7231
    • Palmer, S.M.1    Playford, M.P.2    Craig, S.W.3    Schaller, M.D.4    Campbell, S.L.5
  • 62
    • 0037014662 scopus 로고    scopus 로고
    • Evidence for two interaction regions for phosphatidylinositol(4, 5)-bisphosphate on mammalian profilin i
    • Skare, P. & Karlsson, R. Evidence for two interaction regions for phosphatidylinositol(4, 5)-bisphosphate on mammalian profilin I. FEBS Lett. 522, 119-124 (2002).
    • (2002) FEBS Lett , vol.522 , pp. 119-124
    • Skare, P.1    Karlsson, R.2
  • 63
    • 54249117883 scopus 로고    scopus 로고
    • Elucidation of a TRPC6-TRPC5 channel cascade that restricts endothelial cell movement
    • Chaudhuri, P. et al. Elucidation of a TRPC6-TRPC5 channel cascade that restricts endothelial cell movement. Mol. Biol. Cell 19, 3203-3211 (2008).
    • (2008) Mol. Biol. Cell , vol.19 , pp. 3203-3211
    • Chaudhuri, P.1
  • 64
    • 85006265331 scopus 로고    scopus 로고
    • Membrane microviscosity regulates endothelial cell motility
    • Ghosh, P. K. et al. Membrane microviscosity regulates endothelial cell motility. Nat. Cell Biol. 4, 894-900 (2002).
    • (2002) Nat. Cell Biol. , vol.4 , pp. 894-900
    • Ghosh, P.K.1
  • 65
    • 33751186112 scopus 로고    scopus 로고
    • Cutaneous wound healing is impaired in hemophilia B
    • Hoffman, M. et al. Cutaneous wound healing is impaired in hemophilia B. Blood 108, 3053-3060 (2006).
    • (2006) Blood , vol.108 , pp. 3053-3060
    • Hoffman, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.