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Volumn 349, Issue 1, 2011, Pages 1-19

Diverse functions for the semaphorin receptor PlexinD1 in development and disease

Author keywords

Angiogenesis; Axon guidance; Blood vessel; Cancer; Immune; Nervous system; Plexin; PlexinD1; Plxn; PlxnD1; Review; Sema; Semaphorin; Signaling; Tumor

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR 2; GAP JUNCTION PROTEIN; MESSENGER RNA; NEUROPILIN; PLEXIN; PLEXIN D1; PROTEIN TYROSINE KINASE; RAS PROTEIN; SEMAPHORIN; SEMAPHORIN 3; UNCLASSIFIED DRUG; VASCULOTROPIN RECEPTOR;

EID: 78649449674     PISSN: 00121606     EISSN: 1095564X     Source Type: Journal    
DOI: 10.1016/j.ydbio.2010.09.008     Document Type: Review
Times cited : (55)

References (213)
  • 1
    • 0030722135 scopus 로고    scopus 로고
    • The chemorepulsive activity of secreted semaphorins is regulated by furin-dependent proteolytic processing
    • Adams R.H., Lohrum M., Klostermann A., Betz H., Püschel A.W. The chemorepulsive activity of secreted semaphorins is regulated by furin-dependent proteolytic processing. EMBO J. 1997, 16:6077-6086.
    • (1997) EMBO J. , vol.16 , pp. 6077-6086
    • Adams, R.H.1    Lohrum, M.2    Klostermann, A.3    Betz, H.4    Püschel, A.W.5
  • 5
    • 77951224719 scopus 로고    scopus 로고
    • Morphogenesis of epithelial tubes: insights into tube formation, elongation, and elaboration
    • Andrew D.J., Ewald A.J. Morphogenesis of epithelial tubes: insights into tube formation, elongation, and elaboration. Dev. Biol. 2009, 341(1):34-55.
    • (2009) Dev. Biol. , vol.341 , Issue.1 , pp. 34-55
    • Andrew, D.J.1    Ewald, A.J.2
  • 7
    • 0042922829 scopus 로고    scopus 로고
    • Semaphorin 3F antagonizes neurotrophin-induced phosphatidylinositol 3-kinase and mitogen-activated protein kinase kinase signaling: a mechanism for growth cone collapse
    • Atwal J.K., Singh K.K., Tessier-Lavigne M., Miller F.D., Kaplan D.R. Semaphorin 3F antagonizes neurotrophin-induced phosphatidylinositol 3-kinase and mitogen-activated protein kinase kinase signaling: a mechanism for growth cone collapse. J. Neurosci. 2003, 23:7602-7609.
    • (2003) J. Neurosci. , vol.23 , pp. 7602-7609
    • Atwal, J.K.1    Singh, K.K.2    Tessier-Lavigne, M.3    Miller, F.D.4    Kaplan, D.R.5
  • 8
    • 0037126064 scopus 로고    scopus 로고
    • The semaphorin receptor plexin-B1 signals through a direct interaction with the Rho-specific nucleotide exchange factor, LARG
    • Aurandt J., Vikis H.G., Gutkind J.S., Ahn N., Guan K.-L. The semaphorin receptor plexin-B1 signals through a direct interaction with the Rho-specific nucleotide exchange factor, LARG. Proc. Natl. Acad. Sci. U. S. A. 2002, 99:12085-12090.
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 12085-12090
    • Aurandt, J.1    Vikis, H.G.2    Gutkind, J.S.3    Ahn, N.4    Guan, K.-L.5
  • 9
    • 33845642955 scopus 로고    scopus 로고
    • Semaphorin 3C regulates endothelial cell function by increasing integrin activity
    • Banu N., Teichman J., Dunlap-Brown M., Villegas G., Tufro A. Semaphorin 3C regulates endothelial cell function by increasing integrin activity. FASEB J. 2006, 20:2150-2152.
    • (2006) FASEB J. , vol.20 , pp. 2150-2152
    • Banu, N.1    Teichman, J.2    Dunlap-Brown, M.3    Villegas, G.4    Tufro, A.5
  • 11
    • 33745176581 scopus 로고    scopus 로고
    • Semaphorin 4D provides a link between axon guidance processes and tumor-induced angiogenesis
    • Basile J.R., Castilho R.M., Williams V.P., Gutkind J.S. Semaphorin 4D provides a link between axon guidance processes and tumor-induced angiogenesis. Proc. Natl. Acad. Sci. U. S. A. 2006, 103:9017-9022.
    • (2006) Proc. Natl. Acad. Sci. U. S. A. , vol.103 , pp. 9017-9022
    • Basile, J.R.1    Castilho, R.M.2    Williams, V.P.3    Gutkind, J.S.4
  • 14
    • 77952386743 scopus 로고    scopus 로고
    • VEGFR2 (KDR/Flk1) signaling mediates axon growth in response to semaphorin 3E in the developing brain
    • Bellon A., Luchino J., Haigh K., Rougon G., Haigh J., Chauvet S., Mann F. VEGFR2 (KDR/Flk1) signaling mediates axon growth in response to semaphorin 3E in the developing brain. Neuron 2010, 66:205-219.
    • (2010) Neuron , vol.66 , pp. 205-219
    • Bellon, A.1    Luchino, J.2    Haigh, K.3    Rougon, G.4    Haigh, J.5    Chauvet, S.6    Mann, F.7
  • 15
    • 0030588594 scopus 로고    scopus 로고
    • Cloning and characterization of mouse ACF7, a novel member of the dystonin subfamily of actin binding proteins
    • Bernier G., Mathieu M., De Repentigny Y., Vidal S.M., Kothary R. Cloning and characterization of mouse ACF7, a novel member of the dystonin subfamily of actin binding proteins. Genomics 1996, 38:19-29.
    • (1996) Genomics , vol.38 , pp. 19-29
    • Bernier, G.1    Mathieu, M.2    De Repentigny, Y.3    Vidal, S.M.4    Kothary, R.5
  • 16
    • 0033778790 scopus 로고    scopus 로고
    • Acf7 (MACF) is an actin and microtubule linker protein whose expression predominates in neural, muscle, and lung development
    • Bernier G., Pool M., Kilcup M., Alfoldi J., De Repentigny Y., Kothary R. Acf7 (MACF) is an actin and microtubule linker protein whose expression predominates in neural, muscle, and lung development. Dev. Dyn. 2000, 219:216-225.
    • (2000) Dev. Dyn. , vol.219 , pp. 216-225
    • Bernier, G.1    Pool, M.2    Kilcup, M.3    Alfoldi, J.4    De Repentigny, Y.5    Kothary, R.6
  • 17
    • 0001290687 scopus 로고    scopus 로고
    • Domains in plexins: links to integrins and transcription factors
    • Bork P., Doerks T., Springer T.A., Snel B. Domains in plexins: links to integrins and transcription factors. Trends Biochem. Sci. 1999, 24:261-263.
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 261-263
    • Bork, P.1    Doerks, T.2    Springer, T.A.3    Snel, B.4
  • 18
    • 0029084950 scopus 로고
    • Novel actin crosslinker superfamily member identified by a two step degenerate PCR procedure
    • Byers T.J., Beggs A.H., McNally E.M., Kunkel L.M. Novel actin crosslinker superfamily member identified by a two step degenerate PCR procedure. FEBS Lett. 1995, 368:500-504.
    • (1995) FEBS Lett. , vol.368 , pp. 500-504
    • Byers, T.J.1    Beggs, A.H.2    McNally, E.M.3    Kunkel, L.M.4
  • 19
    • 0033179591 scopus 로고    scopus 로고
    • Cloning and characterization of neuropilin-1-interacting protein: a PSD-95/Dlg/ZO-1 domain-containing protein that interacts with the cytoplasmic domain of neuropilin-1
    • Cai H., Reed R.R. Cloning and characterization of neuropilin-1-interacting protein: a PSD-95/Dlg/ZO-1 domain-containing protein that interacts with the cytoplasmic domain of neuropilin-1. J. Neurosci. 1999, 19:6519-6527.
    • (1999) J. Neurosci. , vol.19 , pp. 6519-6527
    • Cai, H.1    Reed, R.R.2
  • 20
    • 85029415775 scopus 로고    scopus 로고
    • The identification of cooperating mutations in TAL1-mediated leukemia in the mouse: a dissertation.
    • Calvo, J.A., 2005. The identification of cooperating mutations in TAL1-mediated leukemia in the mouse: a dissertation. 1-177.
    • (2005) , pp. 1-177
    • Calvo, J.A.1
  • 21
    • 0037205048 scopus 로고    scopus 로고
    • The phosphoinositide 3-kinase pathway
    • Cantley L.C. The phosphoinositide 3-kinase pathway. Science 2002, 296:1655-1657.
    • (2002) Science , vol.296 , pp. 1655-1657
    • Cantley, L.C.1
  • 22
    • 30744479430 scopus 로고    scopus 로고
    • Angiogenesis in life, disease and medicine
    • Carmeliet P. Angiogenesis in life, disease and medicine. Nature 2005, 438:932-936.
    • (2005) Nature , vol.438 , pp. 932-936
    • Carmeliet, P.1
  • 23
    • 22444447946 scopus 로고    scopus 로고
    • Common mechanisms of nerve and blood vessel wiring
    • Carmeliet P., Tessier-Lavigne M. Common mechanisms of nerve and blood vessel wiring. Nature 2005, 436:193-200.
    • (2005) Nature , vol.436 , pp. 193-200
    • Carmeliet, P.1    Tessier-Lavigne, M.2
  • 24
    • 84934444702 scopus 로고    scopus 로고
    • Semaphorin signals in cell adhesion and cell migration: functional role and molecular mechanisms
    • Casazza A., Fazzari P., Tamagnone L. Semaphorin signals in cell adhesion and cell migration: functional role and molecular mechanisms. Adv. Exp. Med. Biol. 2007, 600:90-108.
    • (2007) Adv. Exp. Med. Biol. , vol.600 , pp. 90-108
    • Casazza, A.1    Fazzari, P.2    Tamagnone, L.3
  • 26
    • 60549094267 scopus 로고    scopus 로고
    • The plexin-A1 receptor activates vascular endothelial growth factor-receptor 2 and nuclear factor-kappaB to mediate survival and anchorage-independent growth of malignant mesothelioma cells
    • Catalano A., Lazzarini R., Di Nuzzo S., Orciari S., Procopio A. The plexin-A1 receptor activates vascular endothelial growth factor-receptor 2 and nuclear factor-kappaB to mediate survival and anchorage-independent growth of malignant mesothelioma cells. Cancer Res. 2009, 69:1485-1493.
    • (2009) Cancer Res. , vol.69 , pp. 1485-1493
    • Catalano, A.1    Lazzarini, R.2    Di Nuzzo, S.3    Orciari, S.4    Procopio, A.5
  • 29
    • 33746058994 scopus 로고    scopus 로고
    • The role of microtubule actin cross-linking factor 1 (MACF1) in the Wnt signaling pathway
    • Chen H.-J., Lin C.-M., Lin C.-S., Perez-Olle R., Leung C.L., Liem R.K.H. The role of microtubule actin cross-linking factor 1 (MACF1) in the Wnt signaling pathway. Genes Dev. 2006, 20:1933-1945.
    • (2006) Genes Dev. , vol.20 , pp. 1933-1945
    • Chen, H.-J.1    Lin, C.-M.2    Lin, C.-S.3    Perez-Olle, R.4    Leung, C.L.5    Liem, R.K.H.6
  • 30
    • 0035950227 scopus 로고    scopus 로고
    • Plexin-A3 mediates semaphorin signaling and regulates the development of hippocampal axonal projections
    • Cheng H.J., Bagri A., Yaron A., Stein E., Pleasure S.J., Tessier-Lavigne M. Plexin-A3 mediates semaphorin signaling and regulates the development of hippocampal axonal projections. Neuron 2001, 32:249-263.
    • (2001) Neuron , vol.32 , pp. 249-263
    • Cheng, H.J.1    Bagri, A.2    Yaron, A.3    Stein, E.4    Pleasure, S.J.5    Tessier-Lavigne, M.6
  • 35
    • 49049121661 scopus 로고    scopus 로고
    • Serial analysis of the vascular endothelial transcriptome under static and shear stress conditions
    • Chu T.J., Peters D.G. Serial analysis of the vascular endothelial transcriptome under static and shear stress conditions. Physiol. Genomics 2008, 34:185-192.
    • (2008) Physiol. Genomics , vol.34 , pp. 185-192
    • Chu, T.J.1    Peters, D.G.2
  • 36
    • 34548546568 scopus 로고    scopus 로고
    • Semaphorin signaling facilitates cleft formation in the developing salivary gland
    • Chung L., Yang T.-L., Huang H.-R., Hsu S.-M., Cheng H.-J., Huang P.-H. Semaphorin signaling facilitates cleft formation in the developing salivary gland. Development 2007, 134:2935-2945.
    • (2007) Development , vol.134 , pp. 2935-2945
    • Chung, L.1    Yang, T.-L.2    Huang, H.-R.3    Hsu, S.-M.4    Cheng, H.-J.5    Huang, P.-H.6
  • 39
    • 2442520826 scopus 로고    scopus 로고
    • Interplay between scatter factor receptors and B plexins controls invasive growth
    • Conrotto P., Corso S., Gamberini S., Comoglio P.M., Giordano S. Interplay between scatter factor receptors and B plexins controls invasive growth. Oncogene 2004, 23:5131-5137.
    • (2004) Oncogene , vol.23 , pp. 5131-5137
    • Conrotto, P.1    Corso, S.2    Gamberini, S.3    Comoglio, P.M.4    Giordano, S.5
  • 43
    • 33846610475 scopus 로고    scopus 로고
    • Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry
    • Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R. Protein phosphorylation and expression profiling by Yin-yang multidimensional liquid chromatography (Yin-yang MDLC) mass spectrometry. J. Proteome Res. 2007, 6:250-262.
    • (2007) J. Proteome Res. , vol.6 , pp. 250-262
    • Dai, J.1    Jin, W.-H.2    Sheng, Q.-H.3    Shieh, C.-H.4    Wu, J.-R.5    Zeng, R.6
  • 44
    • 0032514630 scopus 로고    scopus 로고
    • GIPC, a PDZ domain containing protein, interacts specifically with the C terminus of RGS-GAIP
    • De Vries L., Lou X., Zhao G., Zheng B., Farquhar M.G. GIPC, a PDZ domain containing protein, interacts specifically with the C terminus of RGS-GAIP. Proc. Natl. Acad. Sci. U. S. A. 1998, 95:12340-12345.
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 12340-12345
    • De Vries, L.1    Lou, X.2    Zhao, G.3    Zheng, B.4    Farquhar, M.G.5
  • 45
    • 0035814887 scopus 로고    scopus 로고
    • Plexin-B semaphorin receptors interact directly with active Rac and regulate the actin cytoskeleton by activating Rho
    • Driessens M.H., Hu H., Nobes C.D., Self A., Jordens I., Goodman C.S., Hall A. Plexin-B semaphorin receptors interact directly with active Rac and regulate the actin cytoskeleton by activating Rho. Curr. Biol. 2001, 11:339-344.
    • (2001) Curr. Biol. , vol.11 , pp. 339-344
    • Driessens, M.H.1    Hu, H.2    Nobes, C.D.3    Self, A.4    Jordens, I.5    Goodman, C.S.6    Hall, A.7
  • 47
    • 31944442964 scopus 로고    scopus 로고
    • The Arf6 GEF GEP100/BRAG2 regulates cell adhesion by controlling endocytosis of beta1 integrins
    • Dunphy J.L., Moravec R., Ly K., Lasell T.K., Melancon P., Casanova J.E. The Arf6 GEF GEP100/BRAG2 regulates cell adhesion by controlling endocytosis of beta1 integrins. Curr. Biol. 2006, 16:315-320.
    • (2006) Curr. Biol. , vol.16 , pp. 315-320
    • Dunphy, J.L.1    Moravec, R.2    Ly, K.3    Lasell, T.K.4    Melancon, P.5    Casanova, J.E.6
  • 48
    • 52449120895 scopus 로고    scopus 로고
    • Functional diversity and mechanisms of action of the semaphorins
    • Eickholt B.J. Functional diversity and mechanisms of action of the semaphorins. Development 2008, 135:2689-2694.
    • (2008) Development , vol.135 , pp. 2689-2694
    • Eickholt, B.J.1
  • 49
    • 58149512060 scopus 로고    scopus 로고
    • Tubulin cofactor B regulates microtubule densities during microglia transition to the reactive states
    • Fanarraga M.L., Villegas J.C., Carranza G., Castaño R., Zabala J.C. Tubulin cofactor B regulates microtubule densities during microglia transition to the reactive states. Exp. Cell Res. 2009, 315:535-541.
    • (2009) Exp. Cell Res. , vol.315 , pp. 535-541
    • Fanarraga, M.L.1    Villegas, J.C.2    Carranza, G.3    Castaño, R.4    Zabala, J.C.5
  • 51
    • 7944237936 scopus 로고    scopus 로고
    • The many faces of filamin: a versatile molecular scaffold for cell motility and signalling
    • Feng Y., Walsh C.A. The many faces of filamin: a versatile molecular scaffold for cell motility and signalling. Nat. Cell Biol. 2004, 6:1034-1038.
    • (2004) Nat. Cell Biol. , vol.6 , pp. 1034-1038
    • Feng, Y.1    Walsh, C.A.2
  • 52
    • 76749089224 scopus 로고    scopus 로고
    • Myeloid translocation gene 16b is a dual A-kinase anchoring protein that interacts selectively with plexins in a phospho-regulated manner
    • Fiedler S.E., Schillace R.V., Daniels C.J., Andrews S.F., Carr D.W. Myeloid translocation gene 16b is a dual A-kinase anchoring protein that interacts selectively with plexins in a phospho-regulated manner. FEBS Lett. 2010, 584:873-877.
    • (2010) FEBS Lett. , vol.584 , pp. 873-877
    • Fiedler, S.E.1    Schillace, R.V.2    Daniels, C.J.3    Andrews, S.F.4    Carr, D.W.5
  • 53
    • 64049095240 scopus 로고    scopus 로고
    • TREM and TREM-like receptors in inflammation and disease
    • Ford J.W., McVicar D.W. TREM and TREM-like receptors in inflammation and disease. Curr. Opin. Immunol. 2009, 21:38-46.
    • (2009) Curr. Opin. Immunol. , vol.21 , pp. 38-46
    • Ford, J.W.1    McVicar, D.W.2
  • 54
    • 0029894664 scopus 로고    scopus 로고
    • Identification of a novel human Rho protein with unusual properties: GTPase deficiency and in vivo farnesylation
    • Foster R., Hu K.Q., Lu Y., Nolan K.M., Thissen J., Settleman J. Identification of a novel human Rho protein with unusual properties: GTPase deficiency and in vivo farnesylation. Mol. Cell. Biol. 1996, 16:2689-2699.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2689-2699
    • Foster, R.1    Hu, K.Q.2    Lu, Y.3    Nolan, K.M.4    Thissen, J.5    Settleman, J.6
  • 55
    • 51049118334 scopus 로고    scopus 로고
    • Tyrosine phosphorylation in semaphorin signalling: shifting into overdrive
    • Franco M., Tamagnone L. Tyrosine phosphorylation in semaphorin signalling: shifting into overdrive. EMBO Rep. 2008, 9:865-871.
    • (2008) EMBO Rep. , vol.9 , pp. 865-871
    • Franco, M.1    Tamagnone, L.2
  • 56
    • 0037160026 scopus 로고    scopus 로고
    • Rapostlin is a novel effector of Rnd2 GTPase inducing neurite branching
    • Fujita H., Katoh H., Ishikawa Y., Mori K., Negishi M. Rapostlin is a novel effector of Rnd2 GTPase inducing neurite branching. J. Biol. Chem. 2002, 277:45428-45434.
    • (2002) J. Biol. Chem. , vol.277 , pp. 45428-45434
    • Fujita, H.1    Katoh, H.2    Ishikawa, Y.3    Mori, K.4    Negishi, M.5
  • 57
    • 54249151581 scopus 로고    scopus 로고
    • Diagnostic mRNA expression patterns of inflamed, benign, and malignant colorectal biopsy specimen and their correlation with peripheral blood results
    • Galamb O., Sipos F., Solymosi N., Spisak S., Krenacs T., Toth K., Tulassay Z., Molnar B. Diagnostic mRNA expression patterns of inflamed, benign, and malignant colorectal biopsy specimen and their correlation with peripheral blood results. Cancer Epidemiol. Biomark. Prev. 2008, 17:2835-2845.
    • (2008) Cancer Epidemiol. Biomark. Prev. , vol.17 , pp. 2835-2845
    • Galamb, O.1    Sipos, F.2    Solymosi, N.3    Spisak, S.4    Krenacs, T.5    Toth, K.6    Tulassay, Z.7    Molnar, B.8
  • 58
    • 44849097147 scopus 로고    scopus 로고
    • Semaphorin 3A inhibits ERM protein phosphorylation in growth cone filopodia through inactivation of PI3K
    • Gallo G. Semaphorin 3A inhibits ERM protein phosphorylation in growth cone filopodia through inactivation of PI3K. Dev. Neurobiol. 2008, 68:926-933.
    • (2008) Dev. Neurobiol. , vol.68 , pp. 926-933
    • Gallo, G.1
  • 59
    • 41049099329 scopus 로고    scopus 로고
    • Neuropilin structure governs VEGF and semaphorin binding and regulates angiogenesis
    • Geretti E., Shimizu A., Klagsbrun M. Neuropilin structure governs VEGF and semaphorin binding and regulates angiogenesis. Angiogenesis 2008, 11:31-39.
    • (2008) Angiogenesis , vol.11 , pp. 31-39
    • Geretti, E.1    Shimizu, A.2    Klagsbrun, M.3
  • 63
    • 4344594556 scopus 로고    scopus 로고
    • PlexinD1 and semaphorin signaling are required in endothelial cells for cardiovascular development
    • Gitler A.D., Lu M.M., Epstein J.A. PlexinD1 and semaphorin signaling are required in endothelial cells for cardiovascular development. Dev. Cell 2004, 7:107-116.
    • (2004) Dev. Cell , vol.7 , pp. 107-116
    • Gitler, A.D.1    Lu, M.M.2    Epstein, J.A.3
  • 64
    • 11844304062 scopus 로고    scopus 로고
    • The role of the Rho GTPases in neuronal development
    • Govek E.-E., Newey S.E., Van Aelst L. The role of the Rho GTPases in neuronal development. Genes Dev. 2005, 19:1-49.
    • (2005) Genes Dev. , vol.19 , pp. 1-49
    • Govek, E.-E.1    Newey, S.E.2    Van Aelst, L.3
  • 65
    • 2942610866 scopus 로고    scopus 로고
    • Domain analysis of the tubulin cofactor system: a model for tubulin folding and dimerization
    • Grynberg M., Jaroszewski L., Godzik A. Domain analysis of the tubulin cofactor system: a model for tubulin folding and dimerization. BMC Bioinform. 2003, 4:46.
    • (2003) BMC Bioinform. , vol.4 , pp. 46
    • Grynberg, M.1    Jaroszewski, L.2    Godzik, A.3
  • 68
    • 33646504431 scopus 로고    scopus 로고
    • Autocrine class 3 semaphorin system regulates slit diaphragm proteins and podocyte survival
    • Guan F., Villegas G., Teichman J., Mundel P., Tufro A. Autocrine class 3 semaphorin system regulates slit diaphragm proteins and podocyte survival. Kidney Int. 2006, 69:1564-1569.
    • (2006) Kidney Int. , vol.69 , pp. 1564-1569
    • Guan, F.1    Villegas, G.2    Teichman, J.3    Mundel, P.4    Tufro, A.5
  • 69
    • 85029435751 scopus 로고    scopus 로고
    • Caracterizacion biologica de la leucemia mieloide aguda con translocacion t(8;16)(p11;p13) y reordenamiento MYST3-CREBBP.
    • Guijosa, M.C., 2007. Caracterizacion biologica de la leucemia mieloide aguda con translocacion t(8;16)(p11;p13) y reordenamiento MYST3-CREBBP. 1-55.
    • (2007) , pp. 1-55
    • Guijosa, M.C.1
  • 70
    • 26444442014 scopus 로고    scopus 로고
    • Plexin B3 promotes neurite outgrowth, interacts homophilically, and interacts with Rin
    • Hartwig C., Veske A., Krejcova S., Rosenberger G., Finckh U. Plexin B3 promotes neurite outgrowth, interacts homophilically, and interacts with Rin. BMC Neurosci. 2005, 6:53.
    • (2005) BMC Neurosci. , vol.6 , pp. 53
    • Hartwig, C.1    Veske, A.2    Krejcova, S.3    Rosenberger, G.4    Finckh, U.5
  • 71
    • 70349453563 scopus 로고    scopus 로고
    • Crystal structure of the plexin A3 intracellular region reveals an autoinhibited conformation through active site sequestration
    • He H., Yang T., Terman J.R., Zhang X. Crystal structure of the plexin A3 intracellular region reveals an autoinhibited conformation through active site sequestration. Proc. Natl. Acad. Sci. U. S. A. 2009, 106:15610-15615.
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 15610-15615
    • He, H.1    Yang, T.2    Terman, J.R.3    Zhang, X.4
  • 73
    • 78649448187 scopus 로고    scopus 로고
    • Plexin D1 signals via the cytoskeletal scaffold protein filamin A
    • Horowitz A. Plexin D1 signals via the cytoskeletal scaffold protein filamin A. FASEB J. 2007, 21:872-879.
    • (2007) FASEB J. , vol.21 , pp. 872-879
    • Horowitz, A.1
  • 74
    • 0034783680 scopus 로고    scopus 로고
    • Plexin B mediates axon guidance in Drosophila by simultaneously inhibiting active Rac and enhancing RhoA signaling
    • Hu H., Marton T.F., Goodman C.S. Plexin B mediates axon guidance in Drosophila by simultaneously inhibiting active Rac and enhancing RhoA signaling. Neuron 2001, 32:39-51.
    • (2001) Neuron , vol.32 , pp. 39-51
    • Hu, H.1    Marton, T.F.2    Goodman, C.S.3
  • 75
    • 0038505967 scopus 로고    scopus 로고
    • GIPC interacts with the beta1-adrenergic receptor and regulates beta1-adrenergic receptor-mediated ERK activation
    • β
    • Hu L.A., Chen W., Martin N.P., Whalen E.J., Premont R.T., Lefkowitz R.J. GIPC interacts with the beta1-adrenergic receptor and regulates beta1-adrenergic receptor-mediated ERK activation. J. Biol. Chem. 2003, 278:26295-26301. β.
    • (2003) J. Biol. Chem. , vol.278 , pp. 26295-26301
    • Hu, L.A.1    Chen, W.2    Martin, N.P.3    Whalen, E.J.4    Premont, R.T.5    Lefkowitz, R.J.6
  • 77
    • 63749113783 scopus 로고    scopus 로고
    • Tyrosine phosphorylation: thirty years and counting
    • Hunter T. Tyrosine phosphorylation: thirty years and counting. Curr. Opin. Cell Biol. 2009, 21:140-146.
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 140-146
    • Hunter, T.1
  • 79
    • 71749121849 scopus 로고    scopus 로고
    • Identification and characterization of multiple similar ligand-binding repeats in filamin: implication on filamin-mediated receptor clustering and cross-talk
    • Ithychanda S.S., Hsu D., Li H., Yan L., Liu D., Das M., Plow E.F., Qin J. Identification and characterization of multiple similar ligand-binding repeats in filamin: implication on filamin-mediated receptor clustering and cross-talk. J. Biol. Chem. 2009, 284:35113-35121.
    • (2009) J. Biol. Chem. , vol.284 , pp. 35113-35121
    • Ithychanda, S.S.1    Hsu, D.2    Li, H.3    Yan, L.4    Liu, D.5    Das, M.6    Plow, E.F.7    Qin, J.8
  • 80
    • 33745603987 scopus 로고    scopus 로고
    • Sema4D/plexin-B1 activates GSK-3beta through R-Ras GAP activity, inducing growth cone collapse
    • Ito Y., Oinuma I., Katoh H., Kaibuchi K., Negishi M. Sema4D/plexin-B1 activates GSK-3beta through R-Ras GAP activity, inducing growth cone collapse. EMBO Rep. 2006, 7:704-709.
    • (2006) EMBO Rep. , vol.7 , pp. 704-709
    • Ito, Y.1    Oinuma, I.2    Katoh, H.3    Kaibuchi, K.4    Negishi, M.5
  • 81
    • 0038376002 scopus 로고    scopus 로고
    • Molecular regulation of vessel maturation
    • Jain R.K. Molecular regulation of vessel maturation. Nat. Med. 2003, 9:685-693.
    • (2003) Nat. Med. , vol.9 , pp. 685-693
    • Jain, R.K.1
  • 87
    • 0034599768 scopus 로고    scopus 로고
    • An epidermal plakin that integrates actin and microtubule networks at cellular junctions
    • Karakesisoglou I., Yang Y., Fuchs E. An epidermal plakin that integrates actin and microtubule networks at cellular junctions. J. Cell Biol. 2000, 149:195-208.
    • (2000) J. Cell Biol. , vol.149 , pp. 195-208
    • Karakesisoglou, I.1    Yang, Y.2    Fuchs, E.3
  • 88
    • 53749086983 scopus 로고    scopus 로고
    • Successful inhibition of tumor development by specific class-3 semaphorins is associated with expression of appropriate semaphorin receptors by tumor cells
    • Kigel B., Varshavsky A., Kessler O., Neufeld G. Successful inhibition of tumor development by specific class-3 semaphorins is associated with expression of appropriate semaphorin receptors by tumor cells. PLoS ONE 2008, 3:e3287.
    • (2008) PLoS ONE , vol.3
    • Kigel, B.1    Varshavsky, A.2    Kessler, O.3    Neufeld, G.4
  • 89
    • 0030723061 scopus 로고    scopus 로고
    • Identification and characterization of R-ras3: a novel member of the RAS gene family with a non-ubiquitous pattern of tissue distribution
    • Kimmelman A., Tolkacheva T., Lorenzi M.V., Osada M., Chan A.M. Identification and characterization of R-ras3: a novel member of the RAS gene family with a non-ubiquitous pattern of tissue distribution. Oncogene 1997, 15:2675-2685.
    • (1997) Oncogene , vol.15 , pp. 2675-2685
    • Kimmelman, A.1    Tolkacheva, T.2    Lorenzi, M.V.3    Osada, M.4    Chan, A.M.5
  • 91
    • 0032571382 scopus 로고    scopus 로고
    • The chemorepulsive activity of the axonal guidance signal semaphorin D requires dimerization
    • Klostermann A., Lohrum M., Adams R.H., Püschel A.W. The chemorepulsive activity of the axonal guidance signal semaphorin D requires dimerization. J. Biol. Chem. 1998, 273:7326-7331.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7326-7331
    • Klostermann, A.1    Lohrum, M.2    Adams, R.H.3    Püschel, A.W.4
  • 92
    • 84934441397 scopus 로고    scopus 로고
    • MICAL flavoprotein monooxygenases: structure, function and role in semaphorin signaling
    • Kolk S.M., Pasterkamp R.J. MICAL flavoprotein monooxygenases: structure, function and role in semaphorin signaling. Adv. Exp. Med. Biol. 2007, 600:38-51.
    • (2007) Adv. Exp. Med. Biol. , vol.600 , pp. 38-51
    • Kolk, S.M.1    Pasterkamp, R.J.2
  • 93
    • 28644439947 scopus 로고    scopus 로고
    • R-Ras is a global regulator of vascular regeneration that suppresses intimal hyperplasia and tumor angiogenesis
    • Komatsu M., Ruoslahti E. R-Ras is a global regulator of vascular regeneration that suppresses intimal hyperplasia and tumor angiogenesis. Nat. Med. 2005, 11:1346-1350.
    • (2005) Nat. Med. , vol.11 , pp. 1346-1350
    • Komatsu, M.1    Ruoslahti, E.2
  • 94
    • 0032546965 scopus 로고    scopus 로고
    • Collapsin-1 covalently dimerizes, and dimerization is necessary for collapsing activity
    • Koppel A.M., Raper J.A. Collapsin-1 covalently dimerizes, and dimerization is necessary for collapsing activity. J. Biol. Chem. 1998, 273:15708-15713.
    • (1998) J. Biol. Chem. , vol.273 , pp. 15708-15713
    • Koppel, A.M.1    Raper, J.A.2
  • 98
    • 67549089499 scopus 로고    scopus 로고
    • Antagonistic interactions among Plexins regulate the timing of intersegmental vessel formation
    • Lamont R.E., Lamont E.J., Childs S.J. Antagonistic interactions among Plexins regulate the timing of intersegmental vessel formation. Dev. Biol. 2009, 331:199-209.
    • (2009) Dev. Biol. , vol.331 , pp. 199-209
    • Lamont, R.E.1    Lamont, E.J.2    Childs, S.J.3
  • 100
    • 0033552634 scopus 로고    scopus 로고
    • Microtubule actin cross-linking factor (MACF): a hybrid of dystonin and dystrophin that can interact with the actin and microtubule cytoskeletons
    • Leung C.L., Sun D., Zheng M., Knowles D.R., Liem R.K. Microtubule actin cross-linking factor (MACF): a hybrid of dystonin and dystrophin that can interact with the actin and microtubule cytoskeletons. J. Cell Biol. 1999, 147:1275-1286.
    • (1999) J. Cell Biol. , vol.147 , pp. 1275-1286
    • Leung, C.L.1    Sun, D.2    Zheng, M.3    Knowles, D.R.4    Liem, R.K.5
  • 102
    • 29144459934 scopus 로고    scopus 로고
    • Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry
    • Liu T., Qian W.-J., Gritsenko M.A., Camp D.G., Monroe M.E., Moore R.J., Smith R.D. Human plasma N-glycoproteome analysis by immunoaffinity subtraction, hydrazide chemistry, and mass spectrometry. J. Proteome Res. 2005, 4:2070-2080.
    • (2005) J. Proteome Res. , vol.4 , pp. 2070-2080
    • Liu, T.1    Qian, W.-J.2    Gritsenko, M.A.3    Camp, D.G.4    Monroe, M.E.5    Moore, R.J.6    Smith, R.D.7
  • 107
    • 68349088106 scopus 로고    scopus 로고
    • Deal breaker: semaphorin and specificity in the spinal stretch reflex circuit
    • Maro G.S., Shen K., Cheng H.J. Deal breaker: semaphorin and specificity in the spinal stretch reflex circuit. Neuron 2009, 63:8-11.
    • (2009) Neuron , vol.63 , pp. 8-11
    • Maro, G.S.1    Shen, K.2    Cheng, H.J.3
  • 109
    • 3242876311 scopus 로고    scopus 로고
    • BLAST: at the core of a powerful and diverse set of sequence analysis tools
    • McGinnis S., Madden T.L. BLAST: at the core of a powerful and diverse set of sequence analysis tools. Nucleic Acids Res. 2004, 32:W20-W25.
    • (2004) Nucleic Acids Res. , vol.32
    • McGinnis, S.1    Madden, T.L.2
  • 110
    • 33644959471 scopus 로고    scopus 로고
    • Distinct roles of beta1 integrins during angiogenesis
    • Mettouchi A., Meneguzzi G. Distinct roles of beta1 integrins during angiogenesis. Eur. J. Cell Biol. 2006, 85:243-247.
    • (2006) Eur. J. Cell Biol. , vol.85 , pp. 243-247
    • Mettouchi, A.1    Meneguzzi, G.2
  • 111
    • 0033549556 scopus 로고    scopus 로고
    • Neuropilin-1 mediates collapsin-1/semaphorin III inhibition of endothelial cell motility: functional competition of collapsin-1 and vascular endothelial growth factor-165
    • Miao H.Q., Soker S., Feiner L., Alonso J.L., Raper J.A., Klagsbrun M. Neuropilin-1 mediates collapsin-1/semaphorin III inhibition of endothelial cell motility: functional competition of collapsin-1 and vascular endothelial growth factor-165. J. Cell Biol. 1999, 146:233-242.
    • (1999) J. Cell Biol. , vol.146 , pp. 233-242
    • Miao, H.Q.1    Soker, S.2    Feiner, L.3    Alonso, J.L.4    Raper, J.A.5    Klagsbrun, M.6
  • 113
    • 0035136029 scopus 로고    scopus 로고
    • Expression of metastasis-associated mts1 gene is co-induced with membrane type-1 matrix metalloproteinase (MT1-MMP) during oncogenic transformation and tubular formation of Madin Darby canine kidney (MDCK) epithelial cells
    • Miyamori H., Hasegawa K., Kim K.R., Sato H. Expression of metastasis-associated mts1 gene is co-induced with membrane type-1 matrix metalloproteinase (MT1-MMP) during oncogenic transformation and tubular formation of Madin Darby canine kidney (MDCK) epithelial cells. Clin. Exp. Metastasis 2000, 18:51-56.
    • (2000) Clin. Exp. Metastasis , vol.18 , pp. 51-56
    • Miyamori, H.1    Hasegawa, K.2    Kim, K.R.3    Sato, H.4
  • 116
    • 58249089943 scopus 로고    scopus 로고
    • Evolution of protein phosphatases in plants and animals
    • Moorhead G.B.G., De Wever V., Templeton G., Kerk D. Evolution of protein phosphatases in plants and animals. Biochem. J. 2009, 417:401-409.
    • (2009) Biochem. J. , vol.417 , pp. 401-409
    • Moorhead, G.B.G.1    De Wever, V.2    Templeton, G.3    Kerk, D.4
  • 119
    • 43249083763 scopus 로고    scopus 로고
    • Involvement of actinin-4 in the recruitment of JRAB/MICAL-L2 to cell-cell junctions and the formation of functional tight junctions
    • Nakatsuji H., Nishimura N., Yamamura R., Kanayama H.-O., Sasaki T. Involvement of actinin-4 in the recruitment of JRAB/MICAL-L2 to cell-cell junctions and the formation of functional tight junctions. Mol. Cell. Biol. 2008, 28:3324-3335.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 3324-3335
    • Nakatsuji, H.1    Nishimura, N.2    Yamamura, R.3    Kanayama, H.-O.4    Sasaki, T.5
  • 120
    • 0036851301 scopus 로고    scopus 로고
    • Protein-protein interactions between large proteins: two-hybrid screening using a functionally classified library composed of long cDNAs
    • Nakayama M., Kikuno R., Ohara O. Protein-protein interactions between large proteins: two-hybrid screening using a functionally classified library composed of long cDNAs. Genome Res. 2002, 12:1773-1784.
    • (2002) Genome Res. , vol.12 , pp. 1773-1784
    • Nakayama, M.1    Kikuno, R.2    Ohara, O.3
  • 121
    • 47949102937 scopus 로고    scopus 로고
    • The semaphorins: versatile regulators of tumour progression and tumour angiogenesis
    • Neufeld G., Kessler O. The semaphorins: versatile regulators of tumour progression and tumour angiogenesis. Nat. Rev. Cancer 2008, 8:632-645.
    • (2008) Nat. Rev. Cancer , vol.8 , pp. 632-645
    • Neufeld, G.1    Kessler, O.2
  • 123
    • 0032489841 scopus 로고    scopus 로고
    • A new member of the Rho family, Rnd1, promotes disassembly of actin filament structures and loss of cell adhesion
    • Nobes C.D., Lauritzen I., Mattei M.G., Paris S., Hall A., Chardin P. A new member of the Rho family, Rnd1, promotes disassembly of actin filament structures and loss of cell adhesion. J. Cell Biol. 1998, 141:187-197.
    • (1998) J. Cell Biol. , vol.141 , pp. 187-197
    • Nobes, C.D.1    Lauritzen, I.2    Mattei, M.G.3    Paris, S.4    Hall, A.5    Chardin, P.6
  • 124
    • 0029018485 scopus 로고
    • Plexin: a novel neuronal cell surface molecule that mediates cell adhesion via a homophilic binding mechanism in the presence of calcium ions
    • Ohta K., Mizutani A., Kawakami A., Murakami Y., Kasuya Y., Takagi S., Tanaka H., Fujisawa H. Plexin: a novel neuronal cell surface molecule that mediates cell adhesion via a homophilic binding mechanism in the presence of calcium ions. Neuron 1995, 14:1189-1199.
    • (1995) Neuron , vol.14 , pp. 1189-1199
    • Ohta, K.1    Mizutani, A.2    Kawakami, A.3    Murakami, Y.4    Kasuya, Y.5    Takagi, S.6    Tanaka, H.7    Fujisawa, H.8
  • 125
    • 0026637781 scopus 로고
    • Involvement of neuronal cell surface molecule B2 in the formation of retinal plexiform layers
    • Ohta K., Takagi S., Asou H., Fujisawa H. Involvement of neuronal cell surface molecule B2 in the formation of retinal plexiform layers. Neuron 1992, 9:151-161.
    • (1992) Neuron , vol.9 , pp. 151-161
    • Ohta, K.1    Takagi, S.2    Asou, H.3    Fujisawa, H.4
  • 126
    • 3843065433 scopus 로고    scopus 로고
    • The Semaphorin 4D receptor Plexin-B1 is a GTPase activating protein for R-Ras
    • Oinuma I., Ishikawa Y., Katoh H., Negishi M. The Semaphorin 4D receptor Plexin-B1 is a GTPase activating protein for R-Ras. Science 2004, 305:862-865.
    • (2004) Science , vol.305 , pp. 862-865
    • Oinuma, I.1    Ishikawa, Y.2    Katoh, H.3    Negishi, M.4
  • 127
    • 0038491273 scopus 로고    scopus 로고
    • Direct interaction of Rnd1 with Plexin-B1 regulates PDZ-RhoGEF-mediated Rho activation by Plexin-B1 and induces cell contraction in COS-7 cells
    • Oinuma I., Katoh H., Harada A., Negishi M. Direct interaction of Rnd1 with Plexin-B1 regulates PDZ-RhoGEF-mediated Rho activation by Plexin-B1 and induces cell contraction in COS-7 cells. J. Biol. Chem. 2003, 278:25671-25677.
    • (2003) J. Biol. Chem. , vol.278 , pp. 25671-25677
    • Oinuma, I.1    Katoh, H.2    Harada, A.3    Negishi, M.4
  • 128
    • 10644250013 scopus 로고    scopus 로고
    • Molecular dissection of the semaphorin 4D receptor plexin-B1-stimulated R-Ras GTPase-activating protein activity and neurite remodeling in hippocampal neurons
    • Oinuma I., Katoh H., Negishi M. Molecular dissection of the semaphorin 4D receptor plexin-B1-stimulated R-Ras GTPase-activating protein activity and neurite remodeling in hippocampal neurons. J. Neurosci. 2004, 24:11473-11480.
    • (2004) J. Neurosci. , vol.24 , pp. 11473-11480
    • Oinuma, I.1    Katoh, H.2    Negishi, M.3
  • 129
    • 33646788001 scopus 로고    scopus 로고
    • Semaphorin 4D/Plexin-B1-mediated R-Ras GAP activity inhibits cell migration by regulating beta(1) integrin activity
    • Oinuma I., Katoh H., Negishi M. Semaphorin 4D/Plexin-B1-mediated R-Ras GAP activity inhibits cell migration by regulating beta(1) integrin activity. J. Cell Biol. 2006, 173:601-613.
    • (2006) J. Cell Biol. , vol.173 , pp. 601-613
    • Oinuma, I.1    Katoh, H.2    Negishi, M.3
  • 130
    • 36849036806 scopus 로고    scopus 로고
    • Regulation of actomyosin contractility by PI3K in sensory axons
    • Orlova I., Silver L., Gallo G. Regulation of actomyosin contractility by PI3K in sensory axons. Dev. Neurobiol. 2007, 67:1843-1851.
    • (2007) Dev. Neurobiol. , vol.67 , pp. 1843-1851
    • Orlova, I.1    Silver, L.2    Gallo, G.3
  • 131
    • 0019425377 scopus 로고
    • Coloboma, congenital heart disease, and choanal atresia with multiple anomalies: CHARGE association
    • Pagon R.A., Graham J.M., Zonana J., Yong S.L. Coloboma, congenital heart disease, and choanal atresia with multiple anomalies: CHARGE association. J. Pediatr. 1981, 99:223-227.
    • (1981) J. Pediatr. , vol.99 , pp. 223-227
    • Pagon, R.A.1    Graham, J.M.2    Zonana, J.3    Yong, S.L.4
  • 132
    • 73949110776 scopus 로고    scopus 로고
    • Sonic hedgehog induces response of commissural axons to Semaphorin repulsion during midline crossing
    • Parra L.M., Zou Y. Sonic hedgehog induces response of commissural axons to Semaphorin repulsion during midline crossing. Nat. Neurosci. 2010, 13:29-35.
    • (2010) Nat. Neurosci. , vol.13 , pp. 29-35
    • Parra, L.M.1    Zou, Y.2
  • 133
    • 13244268383 scopus 로고    scopus 로고
    • R-Ras fills another GAP in semaphorin signalling
    • Pasterkamp R.J. R-Ras fills another GAP in semaphorin signalling. Trends Cell Biol. 2005, 15:61-64.
    • (2005) Trends Cell Biol. , vol.15 , pp. 61-64
    • Pasterkamp, R.J.1
  • 134
    • 68649124073 scopus 로고    scopus 로고
    • Semaphorin function in neural plasticity and disease
    • Pasterkamp R.J., Giger R.J. Semaphorin function in neural plasticity and disease. Curr. Opin. Neurobiol. 2009, 19:263-274.
    • (2009) Curr. Opin. Neurobiol. , vol.19 , pp. 263-274
    • Pasterkamp, R.J.1    Giger, R.J.2
  • 135
    • 67349159339 scopus 로고    scopus 로고
    • Specificity of sensory-motor connections encoded by Sema3e-Plxnd1 recognition
    • Pecho-Vrieseling E., Sigrist M., Yoshida Y., Jessell T.M., Arber S. Specificity of sensory-motor connections encoded by Sema3e-Plxnd1 recognition. Nature 2009, 459:842-846.
    • (2009) Nature , vol.459 , pp. 842-846
    • Pecho-Vrieseling, E.1    Sigrist, M.2    Yoshida, Y.3    Jessell, T.M.4    Arber, S.5
  • 136
    • 0037044715 scopus 로고    scopus 로고
    • Plexin B regulates Rho through the guanine nucleotide exchange factors leukemia-associated Rho GEF (LARG) and PDZ-RhoGEF
    • Perrot V., Vazquez-Prado J., Gutkind J.S. Plexin B regulates Rho through the guanine nucleotide exchange factors leukemia-associated Rho GEF (LARG) and PDZ-RhoGEF. J. Biol. Chem. 2002, 277:43115-43120.
    • (2002) J. Biol. Chem. , vol.277 , pp. 43115-43120
    • Perrot, V.1    Vazquez-Prado, J.2    Gutkind, J.S.3
  • 138
    • 0742306892 scopus 로고    scopus 로고
    • Stimulation-dependent recycling of integrin beta1 regulated by ARF6 and Rab11
    • Powelka A.M., Sun J., Li J., Gao M., Shaw L.M., Sonnenberg A., Hsu V.W. Stimulation-dependent recycling of integrin beta1 regulated by ARF6 and Rab11. Traffic 2004, 5:20-36.
    • (2004) Traffic , vol.5 , pp. 20-36
    • Powelka, A.M.1    Sun, J.2    Li, J.3    Gao, M.4    Shaw, L.M.5    Sonnenberg, A.6    Hsu, V.W.7
  • 141
    • 19444368524 scopus 로고    scopus 로고
    • Filamin A: phenotypic diversity
    • Robertson S.P. Filamin A: phenotypic diversity. Curr. Opin. Genet. Dev. 2005, 15:301-307.
    • (2005) Curr. Opin. Genet. Dev. , vol.15 , pp. 301-307
    • Robertson, S.P.1
  • 142
    • 0034550281 scopus 로고    scopus 로고
    • The semaphorin 3A receptor may directly regulate the activity of small GTPases
    • Rohm B., Rahim B., Kleiber B., Hovatta I., Püschel A.W. The semaphorin 3A receptor may directly regulate the activity of small GTPases. FEBS Lett. 2000, 486:68-72.
    • (2000) FEBS Lett. , vol.486 , pp. 68-72
    • Rohm, B.1    Rahim, B.2    Kleiber, B.3    Hovatta, I.4    Püschel, A.W.5
  • 145
    • 70349861793 scopus 로고    scopus 로고
    • Plexin D1 is ubiquitously expressed on tumor vessels and tumor cells in solid malignancies
    • Roodink I., Verrijp K., Raats J., Leenders W.P.J. Plexin D1 is ubiquitously expressed on tumor vessels and tumor cells in solid malignancies. BMC Cancer 2009, 9:297.
    • (2009) BMC Cancer , vol.9 , pp. 297
    • Roodink, I.1    Verrijp, K.2    Raats, J.3    Leenders, W.P.J.4
  • 148
    • 75749094781 scopus 로고    scopus 로고
    • Rab13 regulates neurite outgrowth in PC12 cells through its effector protein, JRAB/MICAL-L2
    • Sakane A., Honda K., Sasaki T. Rab13 regulates neurite outgrowth in PC12 cells through its effector protein, JRAB/MICAL-L2. Mol. Cell. Biol. 2010, 30:1077-1087.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 1077-1087
    • Sakane, A.1    Honda, K.2    Sasaki, T.3
  • 150
    • 0028876585 scopus 로고
    • Differential expression of two cell surface proteins, neuropilin and plexin, in Xenopus olfactory axon subclasses
    • Satoda M., Takagi S., Ohta K., Hirata T., Fujisawa H. Differential expression of two cell surface proteins, neuropilin and plexin, in Xenopus olfactory axon subclasses. J. Neurosci. 1995, 15:942-955.
    • (1995) J. Neurosci. , vol.15 , pp. 942-955
    • Satoda, M.1    Takagi, S.2    Ohta, K.3    Hirata, T.4    Fujisawa, H.5
  • 151
    • 0025604399 scopus 로고
    • Bullous pemphigoid antigen (BPAG1): cDNA cloning and mapping of the gene to the short arm of human chromosome 6
    • Sawamura D., Nomura K., Sugita Y., Mattei M.G., Chu M.L., Knowlton R., Uitto J. Bullous pemphigoid antigen (BPAG1): cDNA cloning and mapping of the gene to the short arm of human chromosome 6. Genomics 1990, 8:722-726.
    • (1990) Genomics , vol.8 , pp. 722-726
    • Sawamura, D.1    Nomura, K.2    Sugita, Y.3    Mattei, M.G.4    Chu, M.L.5    Knowlton, R.6    Uitto, J.7
  • 152
    • 84934436620 scopus 로고    scopus 로고
    • The CRMP family of proteins and their role in Sema3A signaling
    • Schmidt E.F., Strittmatter S.M. The CRMP family of proteins and their role in Sema3A signaling. Adv. Exp. Med. Biol. 2007, 600:1-11.
    • (2007) Adv. Exp. Med. Biol. , vol.600 , pp. 1-11
    • Schmidt, E.F.1    Strittmatter, S.M.2
  • 153
    • 77449085256 scopus 로고    scopus 로고
    • Neuropilin, you gotta let me know: should I stay or should I go?
    • Schwarz Q., Ruhrberg C. Neuropilin, you gotta let me know: should I stay or should I go?. Cell adhesion & migration 4 2010.
    • (2010) Cell adhesion & migration 4
    • Schwarz, Q.1    Ruhrberg, C.2
  • 155
    • 73849118696 scopus 로고    scopus 로고
    • MICAL-L1 links EHD1 to tubular recycling endosomes and regulates receptor recycling
    • Sharma M., Giridharan S.S.P., Rahajeng J., Naslavsky N., Caplan S. MICAL-L1 links EHD1 to tubular recycling endosomes and regulates receptor recycling. Mol. Biol. Cell 2009, 20:5181-5194.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 5181-5194
    • Sharma, M.1    Giridharan, S.S.P.2    Rahajeng, J.3    Naslavsky, N.4    Caplan, S.5
  • 157
    • 84934443084 scopus 로고    scopus 로고
    • Signaling of secreted semaphorins in growth cone steering
    • Shim S., Ming G.-l. Signaling of secreted semaphorins in growth cone steering. Adv. Exp. Med. Biol. 2007, 600:52-60.
    • (2007) Adv. Exp. Med. Biol. , vol.600 , pp. 52-60
    • Shim, S.1    Ming, G.-L.2
  • 158
    • 55249110412 scopus 로고    scopus 로고
    • ABL2/ARG tyrosine kinase mediates SEMA3F-induced RhoA inactivation and cytoskeleton collapse in human glioma cells
    • Shimizu A., Mammoto A., Italiano J.E., Pravda E., Dudley A.C., Ingber D.E., Klagsbrun M. ABL2/ARG tyrosine kinase mediates SEMA3F-induced RhoA inactivation and cytoskeleton collapse in human glioma cells. J. Biol. Chem. 2008, 283:27230-27238.
    • (2008) J. Biol. Chem. , vol.283 , pp. 27230-27238
    • Shimizu, A.1    Mammoto, A.2    Italiano, J.E.3    Pravda, E.4    Dudley, A.C.5    Ingber, D.E.6    Klagsbrun, M.7
  • 159
    • 0041402828 scopus 로고    scopus 로고
    • Semaphorin3a1 regulates angioblast migration and vascular development in zebrafish embryos
    • Shoji W., Isogai S., Sato-Maeda M., Obinata M., Kuwada J.Y. Semaphorin3a1 regulates angioblast migration and vascular development in zebrafish embryos. Development 2003, 130:3227-3236.
    • (2003) Development , vol.130 , pp. 3227-3236
    • Shoji, W.1    Isogai, S.2    Sato-Maeda, M.3    Obinata, M.4    Kuwada, J.Y.5
  • 160
    • 0031898879 scopus 로고    scopus 로고
    • Zebrafish semaphorin Z1a collapses specific growth cones and alters their pathway in vivo
    • Shoji W., Yee C.S., Kuwada J.Y. Zebrafish semaphorin Z1a collapses specific growth cones and alters their pathway in vivo. Development 1998, 125:1275-1283.
    • (1998) Development , vol.125 , pp. 1275-1283
    • Shoji, W.1    Yee, C.S.2    Kuwada, J.Y.3
  • 163
    • 54249131103 scopus 로고    scopus 로고
    • Capturing protein tails by CAP-Gly domains
    • Steinmetz M.O., Akhmanova A. Capturing protein tails by CAP-Gly domains. Trends Biochem. Sci. 2008, 33:535-545.
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 535-545
    • Steinmetz, M.O.1    Akhmanova, A.2
  • 164
    • 0037139533 scopus 로고    scopus 로고
    • A novel gene encoding a putative transmembrane protein with two extracellular CUB domains and a low-density lipoprotein class A module: isolation of alternatively spliced isoforms in retina and brain
    • Stöhr H., Berger C., Fröhlich S., Weber B.H.F. A novel gene encoding a putative transmembrane protein with two extracellular CUB domains and a low-density lipoprotein class A module: isolation of alternatively spliced isoforms in retina and brain. Gene 2002, 286:223-231.
    • (2002) Gene , vol.286 , pp. 223-231
    • Stöhr, H.1    Berger, C.2    Fröhlich, S.3    Weber, B.H.F.4
  • 166
    • 67449096531 scopus 로고    scopus 로고
    • Tyrosine dephosphorylation of the Syndecan-1 PDZ binding domain regulates Syntenin-1 recruitment
    • Sulka B., Lortat-Jacob H., Terreux R., Letourneur F., Rousselle P. Tyrosine dephosphorylation of the Syndecan-1 PDZ binding domain regulates Syntenin-1 recruitment. J. Biol. Chem. 2009, 284:10659-10671.
    • (2009) J. Biol. Chem. , vol.284 , pp. 10659-10671
    • Sulka, B.1    Lortat-Jacob, H.2    Terreux, R.3    Letourneur, F.4    Rousselle, P.5
  • 170
    • 0037014472 scopus 로고    scopus 로고
    • Plexin-B1 directly interacts with PDZ-RhoGEF/LARG to regulate RhoA and growth cone morphology
    • Swiercz J.M., Kuner R., Behrens J., Offermanns S. Plexin-B1 directly interacts with PDZ-RhoGEF/LARG to regulate RhoA and growth cone morphology. Neuron 2002, 35:51-63.
    • (2002) Neuron , vol.35 , pp. 51-63
    • Swiercz, J.M.1    Kuner, R.2    Behrens, J.3    Offermanns, S.4
  • 171
    • 3042546082 scopus 로고    scopus 로고
    • Plexin-B1/RhoGEF-mediated RhoA activation involves the receptor tyrosine kinase ErbB-2
    • Swiercz J.M., Kuner R., Offermanns S. Plexin-B1/RhoGEF-mediated RhoA activation involves the receptor tyrosine kinase ErbB-2. J. Cell Biol. 2004, 165:869-880.
    • (2004) J. Cell Biol. , vol.165 , pp. 869-880
    • Swiercz, J.M.1    Kuner, R.2    Offermanns, S.3
  • 172
    • 38349167245 scopus 로고    scopus 로고
    • ErbB-2 and met reciprocally regulate cellular signaling via plexin-B1
    • Swiercz J.M., Worzfeld T., Offermanns S. ErbB-2 and met reciprocally regulate cellular signaling via plexin-B1. J. Biol. Chem. 2008, 283:1893-1901.
    • (2008) J. Biol. Chem. , vol.283 , pp. 1893-1901
    • Swiercz, J.M.1    Worzfeld, T.2    Offermanns, S.3
  • 173
    • 71949106010 scopus 로고    scopus 로고
    • Semaphorin 4D signaling requires the recruitment of phospholipase C gamma into the plexin-B1 receptor complex
    • Swiercz J.M., Worzfeld T., Offermanns S. Semaphorin 4D signaling requires the recruitment of phospholipase C gamma into the plexin-B1 receptor complex. Mol. Cell. Biol. 2009, 29:6321-6334.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 6321-6334
    • Swiercz, J.M.1    Worzfeld, T.2    Offermanns, S.3
  • 174
    • 0035105491 scopus 로고    scopus 로고
    • Plexina1 autoinhibition by the plexin sema domain
    • Takahashi T., Strittmatter S.M. Plexina1 autoinhibition by the plexin sema domain. Neuron 2001, 29:429-439.
    • (2001) Neuron , vol.29 , pp. 429-439
    • Takahashi, T.1    Strittmatter, S.M.2
  • 177
    • 33744549035 scopus 로고    scopus 로고
    • Pragmin, a novel effector of Rnd2 GTPase, stimulates RhoA activity
    • Tanaka H., Katoh H., Negishi M. Pragmin, a novel effector of Rnd2 GTPase, stimulates RhoA activity. J. Biol. Chem. 2006, 281:10355-10364.
    • (2006) J. Biol. Chem. , vol.281 , pp. 10355-10364
    • Tanaka, H.1    Katoh, H.2    Negishi, M.3
  • 178
    • 35548965485 scopus 로고    scopus 로고
    • Novel mutations affecting axon guidance in zebrafish and a role for plexin signalling in the guidance of trigeminal and facial nerve axons
    • Tanaka H., Maeda R., Shoji W., Wada H., Masai I., Shiraki T., Kobayashi M., Nakayama R., Okamoto H. Novel mutations affecting axon guidance in zebrafish and a role for plexin signalling in the guidance of trigeminal and facial nerve axons. Development 2007, 134:3259-3269.
    • (2007) Development , vol.134 , pp. 3259-3269
    • Tanaka, H.1    Maeda, R.2    Shoji, W.3    Wada, H.4    Masai, I.5    Shiraki, T.6    Kobayashi, M.7    Nakayama, R.8    Okamoto, H.9
  • 179
    • 33745754458 scopus 로고    scopus 로고
    • JRAB/MICAL-L2 is a junctional Rab13-binding protein mediating the endocytic recycling of occludin
    • Terai T., Nishimura N., Kanda I., Yasui N., Sasaki T. JRAB/MICAL-L2 is a junctional Rab13-binding protein mediating the endocytic recycling of occludin. Mol. Biol. Cell 2006, 17:2465-2475.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2465-2475
    • Terai, T.1    Nishimura, N.2    Kanda, I.3    Yasui, N.4    Sasaki, T.5
  • 180
    • 23044471849 scopus 로고    scopus 로고
    • Response to comment on "Nervy Links Protein Kinase A to Plexin-Mediated Semaphorin Repulsion"
    • Terman J., Kolodkin A.L. Response to comment on "Nervy Links Protein Kinase A to Plexin-Mediated Semaphorin Repulsion". Science 2005, 309:558c.
    • (2005) Science , vol.309
    • Terman, J.1    Kolodkin, A.L.2
  • 181
    • 1242284592 scopus 로고    scopus 로고
    • Nervy links protein kinase a to plexin-mediated semaphorin repulsion
    • Terman J.R., Kolodkin A.L. Nervy links protein kinase a to plexin-mediated semaphorin repulsion. Science 2004, 303:1204-1207.
    • (2004) Science , vol.303 , pp. 1204-1207
    • Terman, J.R.1    Kolodkin, A.L.2
  • 182
    • 0037188897 scopus 로고    scopus 로고
    • MICALs, a family of conserved flavoprotein oxidoreductases, function in plexin-mediated axonal repulsion
    • Terman J.R., Mao T., Pasterkamp R.J., Yu H.-H., Kolodkin A.L. MICALs, a family of conserved flavoprotein oxidoreductases, function in plexin-mediated axonal repulsion. Cell 2002, 109:887-900.
    • (2002) Cell , vol.109 , pp. 887-900
    • Terman, J.R.1    Mao, T.2    Pasterkamp, R.J.3    Yu, H.-H.4    Kolodkin, A.L.5
  • 183
    • 33646916006 scopus 로고    scopus 로고
    • RanBPM contributes to Semaphorin3A signaling through plexin-A receptors
    • Togashi H., Schmidt E.F., Strittmatter S.M. RanBPM contributes to Semaphorin3A signaling through plexin-A receptors. J. Neurosci. 2006, 26:4961-4969.
    • (2006) J. Neurosci. , vol.26 , pp. 4961-4969
    • Togashi, H.1    Schmidt, E.F.2    Strittmatter, S.M.3
  • 184
    • 23144465799 scopus 로고    scopus 로고
    • 1H, 15N and 13C Resonance assignments and secondary structure determination reveal that the minimal Rac1 GTPase binding domain of plexin-B1 has a ubiquitin fold
    • Tong Y., Buck M. 1H, 15N and 13C Resonance assignments and secondary structure determination reveal that the minimal Rac1 GTPase binding domain of plexin-B1 has a ubiquitin fold. J. Biomol. NMR 2005, 31:369-370.
    • (2005) J. Biomol. NMR , vol.31 , pp. 369-370
    • Tong, Y.1    Buck, M.2
  • 185
    • 37549021146 scopus 로고    scopus 로고
    • Binding of Rac1, Rnd1, and RhoD to a novel Rho GTPase interaction motif destabilizes dimerization of the plexin-B1 effector domain
    • Tong Y., Chugha P., Hota P.K., Alviani R.S., Li M., Tempel W., Shen L., Park H.-W., Buck M. Binding of Rac1, Rnd1, and RhoD to a novel Rho GTPase interaction motif destabilizes dimerization of the plexin-B1 effector domain. J. Biol. Chem. 2007, 282:37215-37224.
    • (2007) J. Biol. Chem. , vol.282 , pp. 37215-37224
    • Tong, Y.1    Chugha, P.2    Hota, P.K.3    Alviani, R.S.4    Li, M.5    Tempel, W.6    Shen, L.7    Park, H.-W.8    Buck, M.9
  • 187
    • 33947129779 scopus 로고    scopus 로고
    • Semaphorin-4A, an activator for T-cell-mediated immunity, suppresses angiogenesis via Plexin-D1
    • Toyofuku T., Yabuki M., Kamei J., Kamei M., Makino N., Kumanogoh A., Hori M. Semaphorin-4A, an activator for T-cell-mediated immunity, suppresses angiogenesis via Plexin-D1. EMBO J. 2007, 26:1373-1384.
    • (2007) EMBO J. , vol.26 , pp. 1373-1384
    • Toyofuku, T.1    Yabuki, M.2    Kamei, J.3    Kamei, M.4    Makino, N.5    Kumanogoh, A.6    Hori, M.7
  • 190
    • 12144285611 scopus 로고    scopus 로고
    • Dual roles of Sema6D in cardiac morphogenesis through region-specific association of its receptor, Plexin-A1, with off-track and vascular endothelial growth factor receptor type 2
    • Toyofuku T., Zhang H., Kumanogoh A., Takegahara N., Suto F., Kamei J., Aoki K., Yabuki M., Hori M., Fujisawa H., Kikutani H. Dual roles of Sema6D in cardiac morphogenesis through region-specific association of its receptor, Plexin-A1, with off-track and vascular endothelial growth factor receptor type 2. Genes Dev. 2004, 18:435-447.
    • (2004) Genes Dev. , vol.18 , pp. 435-447
    • Toyofuku, T.1    Zhang, H.2    Kumanogoh, A.3    Takegahara, N.4    Suto, F.5    Kamei, J.6    Aoki, K.7    Yabuki, M.8    Hori, M.9    Fujisawa, H.10    Kikutani, H.11
  • 192
    • 4043105621 scopus 로고    scopus 로고
    • The activity of the plexin-A1 receptor is regulated by Rac
    • Turner L.J., Nicholls S., Hall A. The activity of the plexin-A1 receptor is regulated by Rac. J. Biol. Chem. 2004, 279:33199-33205.
    • (2004) J. Biol. Chem. , vol.279 , pp. 33199-33205
    • Turner, L.J.1    Nicholls, S.2    Hall, A.3
  • 193
    • 65449122789 scopus 로고    scopus 로고
    • Different requirement for Rnd GTPases of R-Ras GAP activity of Plexin-C1 and Plexin-D1
    • Uesugi K., Oinuma I., Katoh H., Negishi M. Different requirement for Rnd GTPases of R-Ras GAP activity of Plexin-C1 and Plexin-D1. J. Biol. Chem. 2008, 284:6743-6751.
    • (2008) J. Biol. Chem. , vol.284 , pp. 6743-6751
    • Uesugi, K.1    Oinuma, I.2    Katoh, H.3    Negishi, M.4
  • 196
    • 34250662228 scopus 로고    scopus 로고
    • Selective requirements for NRP1 ligands during neurovascular patterning
    • Vieira J.M., Schwarz Q., Ruhrberg C. Selective requirements for NRP1 ligands during neurovascular patterning. Development 2007, 134:1833-1843.
    • (2007) Development , vol.134 , pp. 1833-1843
    • Vieira, J.M.1    Schwarz, Q.2    Ruhrberg, C.3
  • 197
    • 0033739987 scopus 로고    scopus 로고
    • The semaphorin receptor plexin-B1 specifically interacts with active Rac in a ligand-dependent manner
    • Vikis H.G., Li W., He Z., Guan K.L. The semaphorin receptor plexin-B1 specifically interacts with active Rac in a ligand-dependent manner. Proc. Natl. Acad. Sci. U. S. A. 2000, 97:12457-12462.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 12457-12462
    • Vikis, H.G.1    Li, W.2    He, Z.3    Guan, K.L.4
  • 199
    • 33845678052 scopus 로고    scopus 로고
    • C terminus of RGS-GAIP-interacting protein conveys neuropilin-1-mediated signaling during angiogenesis
    • Wang L., Mukhopadhyay D., Xu X. C terminus of RGS-GAIP-interacting protein conveys neuropilin-1-mediated signaling during angiogenesis. FASEB J. 2006, 20:1513-1515.
    • (2006) FASEB J. , vol.20 , pp. 1513-1515
    • Wang, L.1    Mukhopadhyay, D.2    Xu, X.3
  • 200
    • 27844560722 scopus 로고    scopus 로고
    • Gigaxonin interacts with tubulin folding cofactor B and controls its degradation through the ubiquitin-proteasome pathway
    • Wang W., Ding J., Allen E., Zhu P., Zhang L., Vogel H., Yang Y. Gigaxonin interacts with tubulin folding cofactor B and controls its degradation through the ubiquitin-proteasome pathway. Curr. Biol. 2005, 15:2050-2055.
    • (2005) Curr. Biol. , vol.15 , pp. 2050-2055
    • Wang, W.1    Ding, J.2    Allen, E.3    Zhu, P.4    Zhang, L.5    Vogel, H.6    Yang, Y.7
  • 201
    • 38349043891 scopus 로고    scopus 로고
    • The C. elegans L1CAM homologue LAD-2 functions as a coreceptor in MAB-20/Sema2 mediated axon guidance
    • Wang X., Zhang W., Cheever T., Schwarz V., Opperman K., Hutter H., Koepp D., Chen L. The C. elegans L1CAM homologue LAD-2 functions as a coreceptor in MAB-20/Sema2 mediated axon guidance. J. Cell Biol. 2008, 180:233-246.
    • (2008) J. Cell Biol. , vol.180 , pp. 233-246
    • Wang, X.1    Zhang, W.2    Cheever, T.3    Schwarz, V.4    Opperman, K.5    Hutter, H.6    Koepp, D.7    Chen, L.8
  • 202
    • 33749034202 scopus 로고    scopus 로고
    • Binding and complementary expression patterns of semaphorin 3E and plexin D1 in the mature neocortices of mice and monkeys
    • Watakabe A., Ohsawa S., Hashikawa T., Yamamori T. Binding and complementary expression patterns of semaphorin 3E and plexin D1 in the mature neocortices of mice and monkeys. J. Comp. Neurol. 2006, 499:258-273.
    • (2006) J. Comp. Neurol. , vol.499 , pp. 258-273
    • Watakabe, A.1    Ohsawa, S.2    Hashikawa, T.3    Yamamori, T.4
  • 204
    • 0032953340 scopus 로고    scopus 로고
    • What guides early embryonic blood vessel formation?
    • Weinstein B.M. What guides early embryonic blood vessel formation?. Dev. Dyn. 1999, 215:2-11.
    • (1999) Dev. Dyn. , vol.215 , pp. 2-11
    • Weinstein, B.M.1
  • 205
    • 26644431823 scopus 로고    scopus 로고
    • Evidence that nervy, the Drosophila homolog of ETO/MTG8, promotes mechanosensory organ development by enhancing Notch signaling
    • Wildonger J., Mann R.S. Evidence that nervy, the Drosophila homolog of ETO/MTG8, promotes mechanosensory organ development by enhancing Notch signaling. Dev. Biol. 2005, 286:507-520.
    • (2005) Dev. Biol. , vol.286 , pp. 507-520
    • Wildonger, J.1    Mann, R.S.2
  • 207
    • 0034782822 scopus 로고    scopus 로고
    • The transmembrane protein Off-track associates with Plexins and functions downstream of Semaphorin signaling during axon guidance
    • Winberg M.L., Tamagnone L., Bai J., Comoglio P.M., Montell D., Goodman C.S. The transmembrane protein Off-track associates with Plexins and functions downstream of Semaphorin signaling during axon guidance. Neuron 2001, 32:53-62.
    • (2001) Neuron , vol.32 , pp. 53-62
    • Winberg, M.L.1    Tamagnone, L.2    Bai, J.3    Comoglio, P.M.4    Montell, D.5    Goodman, C.S.6
  • 208
    • 52949098421 scopus 로고    scopus 로고
    • ACF7 regulates cytoskeletal-focal adhesion dynamics and migration and has ATPase activity
    • Wu X., Kodama A., Fuchs E. ACF7 regulates cytoskeletal-focal adhesion dynamics and migration and has ATPase activity. Cell 2008, 135:137-148.
    • (2008) Cell , vol.135 , pp. 137-148
    • Wu, X.1    Kodama, A.2    Fuchs, E.3
  • 209
    • 13544268336 scopus 로고    scopus 로고
    • Unraveling the mechanism of protein N-glycosylation
    • Yan A., Lennarz W.J. Unraveling the mechanism of protein N-glycosylation. J. Biol. Chem. 2005, 280:3121-3124.
    • (2005) J. Biol. Chem. , vol.280 , pp. 3121-3124
    • Yan, A.1    Lennarz, W.J.2
  • 211
    • 34249712685 scopus 로고    scopus 로고
    • PlexinA1 signaling directs the segregation of proprioceptive sensory axons in the developing spinal cord
    • Yoshida Y., Han B., Mendelsohn M., Jessell T.M. PlexinA1 signaling directs the segregation of proprioceptive sensory axons in the developing spinal cord. Neuron 2006, 52:775-788.
    • (2006) Neuron , vol.52 , pp. 775-788
    • Yoshida, Y.1    Han, B.2    Mendelsohn, M.3    Jessell, T.M.4
  • 212
    • 0037080330 scopus 로고    scopus 로고
    • Antagonistic effects of Rnd1 and RhoD GTPases regulate receptor activity in Semaphorin 3A-induced cytoskeletal collapse
    • Zanata S.M., Hovatta I., Rohm B., Püschel A.W. Antagonistic effects of Rnd1 and RhoD GTPases regulate receptor activity in Semaphorin 3A-induced cytoskeletal collapse. J. Neurosci. 2002, 22:471-477.
    • (2002) J. Neurosci. , vol.22 , pp. 471-477
    • Zanata, S.M.1    Hovatta, I.2    Rohm, B.3    Püschel, A.W.4
  • 213
    • 57849120401 scopus 로고    scopus 로고
    • Tie2Cre-mediated inactivation of plexinD1 results in congenital heart, vascular and skeletal defects
    • Zhang Y., Singh M., Degenhardt K., Lu M., Bennett J., Yoshida Y., Epstein J. Tie2Cre-mediated inactivation of plexinD1 results in congenital heart, vascular and skeletal defects. Dev. Biol. 2008, 325(1):82-93.
    • (2008) Dev. Biol. , vol.325 , Issue.1 , pp. 82-93
    • Zhang, Y.1    Singh, M.2    Degenhardt, K.3    Lu, M.4    Bennett, J.5    Yoshida, Y.6    Epstein, J.7


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