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Volumn 8, Issue 8, 2008, Pages 632-645

The semaphorins: Versatile regulators of tumour progression and tumour angiogenesis

Author keywords

[No Author keywords available]

Indexed keywords

BEVACIZUMAB; NEUROPILIN; SEMAPHORIN; SEMAPHORIN 3A; SEMAPHORIN 3B; SEMAPHORIN 3D; SEMAPHORIN 3E; SEMAPHORIN 3F;

EID: 47949102937     PISSN: 1474175X     EISSN: 14741768     Source Type: Journal    
DOI: 10.1038/nrc2404     Document Type: Review
Times cited : (345)

References (170)
  • 1
    • 0027373701 scopus 로고
    • Collapsin: A protein in brain that induces the collapse and paralysis of neuronal growth cones
    • This is the first description of a semaphorin
    • Luo, Y., Raible, D. & Raper, J. A. Collapsin: a protein in brain that induces the collapse and paralysis of neuronal growth cones. Cell 75, 217-227 (1993). This is the first description of a semaphorin.
    • (1993) Cell , vol.75 , pp. 217-227
    • Luo, Y.1    Raible, D.2    Raper, J.A.3
  • 4
    • 0030886550 scopus 로고    scopus 로고
    • Koppel, A. M., Feiner, L., Kobayashi, H. & Raper, J. A. A 70 amino acid region within the semaphorin domain activates specific cellular response of semaphorin family members. Neuron 19, 531-537 (1997).
    • Koppel, A. M., Feiner, L., Kobayashi, H. & Raper, J. A. A 70 amino acid region within the semaphorin domain activates specific cellular response of semaphorin family members. Neuron 19, 531-537 (1997).
  • 5
    • 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. 24, 261-263 (1999).
    • (1999) Trends Biochem. Sci , vol.24 , pp. 261-263
    • Bork, P.1    Doerks, T.2    Springer, T.A.3    Snel, B.4
  • 6
    • 0141756154 scopus 로고    scopus 로고
    • Interactions between growth factor receptors and adhesion molecules: Breaking the rules
    • Comoglio, P. M., Boccaccio, C. & Trusolino, L. Interactions between growth factor receptors and adhesion molecules: breaking the rules. Curr. Opin. Cell Biol. 15, 565-571 (2003).
    • (2003) Curr. Opin. Cell Biol , vol.15 , pp. 565-571
    • Comoglio, P.M.1    Boccaccio, C.2    Trusolino, L.3
  • 7
    • 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. 273, 15708-15713 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 15708-15713
    • Koppel, A.M.1    Raper, J.A.2
  • 8
    • 0032571382 scopus 로고    scopus 로고
    • The chemorepulsive activity of the axonal guidance signal semaphorin D requires dimerization
    • Klostermann, A., Lohrum, M., Adams, R. H. & Puschel, A. W. The chemorepulsive activity of the axonal guidance signal semaphorin D requires dimerization. J. Biol. Chem. 273, 7326-7331 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 7326-7331
    • Klostermann, A.1    Lohrum, M.2    Adams, R.H.3    Puschel, A.W.4
  • 9
    • 34250307200 scopus 로고    scopus 로고
    • Basile, J. R., Holmbeck, K., Bugge, T. H. & Gutkind, J. S. MT1-MMP controls tumor-induced angiogenesis through the release of semaphorin 4D. J. Biol. Chem. 282, 6899-6905 (2007).
    • Basile, J. R., Holmbeck, K., Bugge, T. H. & Gutkind, J. S. MT1-MMP controls tumor-induced angiogenesis through the release of semaphorin 4D. J. Biol. Chem. 282, 6899-6905 (2007).
  • 10
    • 3843065433 scopus 로고    scopus 로고
    • The Semaphorin 4D receptor Plexin-B1 is a GTPase activating protein for R-Ras
    • The first paper in which it was found that plexins have a functional GAP domain that controls integrin function
    • Oinuma, I., Ishikawa, Y., Katoh, H. & Negishi, M. The Semaphorin 4D receptor Plexin-B1 is a GTPase activating protein for R-Ras. Science 305, 862-865 (2004). The first paper in which it was found that plexins have a functional GAP domain that controls integrin function.
    • (2004) Science , vol.305 , pp. 862-865
    • Oinuma, I.1    Ishikawa, Y.2    Katoh, H.3    Negishi, M.4
  • 11
    • 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. et al. Binding of Rac1, Rnd1 and RhoD to a novel Rho GTPase interaction motif destabilizes dimerization of the plexin-B1 effector domain. J. Biol. Chem. 282, 37215-37224 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 37215-37224
    • Tong, Y.1
  • 12
    • 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. et al. Plexin-B semaphorin receptors interact directly with active Rac and regulate the actin cytoskeleton by activating Rho. Curr. Biol. 11, 339-344 (2001).
    • (2001) Curr. Biol , vol.11 , pp. 339-344
    • Driessens, M.H.1
  • 13
    • 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. & Puschel, A. W. The semaphorin 3A receptor may directly regulate the activity of small GTPases. FEBS Lett. 486, 68-72 (2000).
    • (2000) FEBS Lett , vol.486 , pp. 68-72
    • Rohm, B.1    Rahim, B.2    Kleiber, B.3    Hovatta, I.4    Puschel, A.W.5
  • 14
    • 0036206649 scopus 로고    scopus 로고
    • The plexin-B1/Rac interaction inhibits PAK activation and enhances Sema4D ligand binding
    • Vikis, H. G., Li, W. & Guan, K. L. The plexin-B1/Rac interaction inhibits PAK activation and enhances Sema4D ligand binding. Genes Dev. 16, 836-845 (2002).
    • (2002) Genes Dev , vol.16 , pp. 836-845
    • Vikis, H.G.1    Li, W.2    Guan, K.L.3
  • 15
    • 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. USA 99, 12085-12090 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 12085-12090
    • Aurandt, J.1    Vikis, H.G.2    Gutkind, J.S.3    Ahn, N.4    Guan, K.L.5
  • 16
    • 0037044715 scopus 로고    scopus 로고
    • Plexin B regulates Rho through the guanine nucleotide exchange factors Leukemia-associated RhoGEF (LARG) and PDZ-RhoGEF
    • Perrot, V., Vazquez-Prado, J. & Gutkind, J. S. Plexin B regulates Rho through the guanine nucleotide exchange factors Leukemia-associated RhoGEF (LARG) and PDZ-RhoGEF. J. Biol. Chem. 278, 26111-26119 (2002).
    • (2002) J. Biol. Chem , vol.278 , pp. 26111-26119
    • Perrot, V.1    Vazquez-Prado, J.2    Gutkind, J.S.3
  • 17
    • 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 35, 51-63 (2002).
    • (2002) Neuron , vol.35 , pp. 51-63
    • Swiercz, J.M.1    Kuner, R.2    Behrens, J.3    Offermanns, S.4
  • 18
    • 0038532245 scopus 로고    scopus 로고
    • Functional regulation of semaphorin receptors by proprotein convertases
    • Artigiani, S. et al. Functional regulation of semaphorin receptors by proprotein convertases. J. Biol. Chem. 278, 10094-10101 (2003).
    • (2003) J. Biol. Chem , vol.278 , pp. 10094-10101
    • Artigiani, S.1
  • 19
    • 0033214312 scopus 로고    scopus 로고
    • Plexin-neuropilin-1 complexes form functional semaphorin-3A receptors
    • The first description of the role of plexins in neuropilin-mediated signal transduction
    • Takahashi, T. et al. Plexin-neuropilin-1 complexes form functional semaphorin-3A receptors. Cell 99, 59-69 (1999). The first description of the role of plexins in neuropilin-mediated signal transduction.
    • (1999) Cell , vol.99 , pp. 59-69
    • Takahashi, T.1
  • 20
    • 20244364929 scopus 로고    scopus 로고
    • Plexins are a large family of receptors for transmembrane, secreted, and GPI-anchored semaphorins in vertebrates
    • The first description of the role of plexins in neuropilin-mediated signal transduction
    • Tamagnone, L. et al. Plexins are a large family of receptors for transmembrane, secreted, and GPI-anchored semaphorins in vertebrates. Cell 99, 71-80 (1999). The first description of the role of plexins in neuropilin-mediated signal transduction.
    • (1999) Cell , vol.99 , pp. 71-80
    • Tamagnone, L.1
  • 21
    • 0025866476 scopus 로고
    • The A5 antigen, a candidate for the neuronal recognition molecule, has homologies to complement components and coagulation factors
    • Takagi, S. et al. The A5 antigen, a candidate for the neuronal recognition molecule, has homologies to complement components and coagulation factors. Neuron 7, 295-307 (1991).
    • (1991) Neuron , vol.7 , pp. 295-307
    • Takagi, S.1
  • 22
    • 0030847193 scopus 로고    scopus 로고
    • Neuropilin is a receptor for the axonal chemorepellent Semaphorin III
    • He, Z. & Tessier-Lavigne, M. Neuropilin is a receptor for the axonal chemorepellent Semaphorin III. Cell 90, 739-751 (1997).
    • (1997) Cell , vol.90 , pp. 739-751
    • He, Z.1    Tessier-Lavigne, M.2
  • 23
    • 0030829388 scopus 로고    scopus 로고
    • Neuropilin is a semaphorin III receptor
    • References 22 and 23 are the first descriptions of neuropilin 1 as a SEMA3A receptor
    • Kolodkin, A. L. et al. Neuropilin is a semaphorin III receptor. Cell 90, 753-762 (1997). References 22 and 23 are the first descriptions of neuropilin 1 as a SEMA3A receptor.
    • (1997) Cell , vol.90 , pp. 753-762
    • Kolodkin, A.L.1
  • 24
    • 0032215144 scopus 로고    scopus 로고
    • Neuropilin-2 is a receptor for semaphorin IV: Insight into the structural basis of receptor function and specificity
    • Giger, R. J. et al. Neuropilin-2 is a receptor for semaphorin IV: insight into the structural basis of receptor function and specificity. Neuron 21, 1079-1092 (1998).
    • (1998) Neuron , vol.21 , pp. 1079-1092
    • Giger, R.J.1
  • 25
    • 0342872023 scopus 로고    scopus 로고
    • Neuropilin-2, a novel member of the neuropilin family, is a high affinity receptor for the semaphorins Sema E and Sema IV but not Sema III
    • Chen, H., Chedotal, A., He, Z., Goodman, C. S. & Tessier-Lavigne, M. Neuropilin-2, a novel member of the neuropilin family, is a high affinity receptor for the semaphorins Sema E and Sema IV but not Sema III. Neuron 19, 547-559 (1997).
    • (1997) Neuron , vol.19 , pp. 547-559
    • Chen, H.1    Chedotal, A.2    He, Z.3    Goodman, C.S.4    Tessier-Lavigne, M.5
  • 26
    • 0035923529 scopus 로고    scopus 로고
    • Inhibition of lung cancer cell growth and induction of apoptosis after reexpression of 3p21.3 candidate tumor suppressor gene SEMA3B
    • Tomizawa, Y. et al. Inhibition of lung cancer cell growth and induction of apoptosis after reexpression of 3p21.3 candidate tumor suppressor gene SEMA3B. Proc. Natl Acad. Sci. USA 98, 13954-13959 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 13954-13959
    • Tomizawa, Y.1
  • 27
    • 25644450430 scopus 로고    scopus 로고
    • Dual functional activity of semaphorin 3B is required for positioning the anterior commissure
    • Julien, F. et al. Dual functional activity of semaphorin 3B is required for positioning the anterior commissure. Neuron 48, 63-75 (2005).
    • (2005) Neuron , vol.48 , pp. 63-75
    • Julien, F.1
  • 28
    • 39449093684 scopus 로고    scopus 로고
    • Transmembrane domain interactions control biological functions neuropilin-1
    • Roth, L. et al. Transmembrane domain interactions control biological functions neuropilin-1. Mol. Biol. Cell 19 646-654 (2008).
    • (2008) Mol. Biol. Cell , vol.19 , pp. 646-654
    • Roth, L.1
  • 29
    • 0037124068 scopus 로고    scopus 로고
    • Characterization of neuropilin-1 structural features that confer binding to semaphorin 3A and vascular endothelial growth factor 165
    • Gu, C. et al. Characterization of neuropilin-1 structural features that confer binding to semaphorin 3A and vascular endothelial growth factor 165. J. Biol. Chem. 277, 18069-18076 (2002).
    • (2002) J. Biol. Chem , vol.277 , pp. 18069-18076
    • Gu, C.1
  • 30
    • 34547520925 scopus 로고    scopus 로고
    • Structural basis for ligand and heparin binding to neuropilin B domains
    • Vander Kooi, C. W. et al. Structural basis for ligand and heparin binding to neuropilin B domains. Proc. Natl Acad. Sci. USA 104, 6157-6152 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 6157-6152
    • Vander Kooi, C.W.1
  • 31
    • 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. B. & 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. 19, 6519-6527 (1999).
    • (1999) J. Neurosci , vol.19 , pp. 6519-6527
    • Cai, H.B.1    Reed, R.R.2
  • 32
    • 0033869852 scopus 로고    scopus 로고
    • Synectin, syndecan-4 cytoplasmic domain binding PDZ protein, inhibits cell migration
    • Gao, Y., Li, M., Chen, W. & Simons, M. Synectin, syndecan-4 cytoplasmic domain binding PDZ protein, inhibits cell migration. J. Cell Physiol. 184, 373-379 (2000).
    • (2000) J. Cell Physiol , vol.184 , pp. 373-379
    • Gao, Y.1    Li, M.2    Chen, W.3    Simons, M.4
  • 33
    • 33746320397 scopus 로고    scopus 로고
    • Glycosaminoglycan modification of neuropilin-1 modulates VEGFR2 signaling
    • Shintani, Y. et al. Glycosaminoglycan modification of neuropilin-1 modulates VEGFR2 signaling. EMBO J. 25, 3045-3055 (2006).
    • (2006) EMBO J , vol.25 , pp. 3045-3055
    • Shintani, Y.1
  • 34
    • 0029670002 scopus 로고    scopus 로고
    • Selective binding of VEGF121 to one of the three VEGF receptors of vascular endothelial cells
    • Gitay-Goren, H. et al. Selective binding of VEGF121 to one of the three VEGF receptors of vascular endothelial cells. J. Biol. Chem. 271, 5519-5523 (1996).
    • (1996) J. Biol. Chem , vol.271 , pp. 5519-5523
    • Gitay-Goren, H.1
  • 35
    • 0032549799 scopus 로고    scopus 로고
    • Neuropilin-1 is expressed by endothelial and tumor cells as an isoform specific receptor for vascular endothelial growth factor
    • The first description of neuropilin 1 as a functional VEGF receptor
    • Soker, S., Takashima, S., Miao, H. Q., Neufeld, G. & Klagsbrun, M. Neuropilin-1 is expressed by endothelial and tumor cells as an isoform specific receptor for vascular endothelial growth factor. Cell 92, 735-745 (1998). The first description of neuropilin 1 as a functional VEGF receptor.
    • (1998) Cell , vol.92 , pp. 735-745
    • Soker, S.1    Takashima, S.2    Miao, H.Q.3    Neufeld, G.4    Klagsbrun, M.5
  • 36
    • 0034674108 scopus 로고    scopus 로고
    • Neuropilin-2 and Neuropilin-1 are receptors for 165-amino acid long form of vascular endothelial growth factor (VEGF) and of placenta growth factor-2, but only neuropilin-2 functions as a receptor for the 145 amino acid form of VEGF
    • Gluzman-Poltorak, Z., Cohen, T., Herzog, Y. & Neufeld, G. Neuropilin-2 and Neuropilin-1 are receptors for 165-amino acid long form of vascular endothelial growth factor (VEGF) and of placenta growth factor-2, but only neuropilin-2 functions as a receptor for the 145 amino acid form of VEGF. J. Biol. Chem. 275, 18040-18045 (2000).
    • (2000) J. Biol. Chem , vol.275 , pp. 18040-18045
    • Gluzman-Poltorak, Z.1    Cohen, T.2    Herzog, Y.3    Neufeld, G.4
  • 37
    • 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. et al. 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. 146, 233-242 (1999).
    • (1999) J. Cell Biol , vol.146 , pp. 233-242
    • Miao, H.Q.1
  • 38
    • 0035377567 scopus 로고    scopus 로고
    • Vascular endothelial growth factor receptor-1 and neuropilin-2 form complexes
    • Gluzman-Poltorak, Z., Cohen, T., Shibuya, M. & Neufeld, G. Vascular endothelial growth factor receptor-1 and neuropilin-2 form complexes. J. Biol. Chem. 276, 18688-18694 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 18688-18694
    • Gluzman-Poltorak, Z.1    Cohen, T.2    Shibuya, M.3    Neufeld, G.4
  • 40
    • 33847343054 scopus 로고    scopus 로고
    • Neuropilin-1 and neuropilin-2 enhance VEGF121 stimulated signal transduction by the VEGFR-2 receptor
    • Shraga-Heled, N. et al. Neuropilin-1 and neuropilin-2 enhance VEGF121 stimulated signal transduction by the VEGFR-2 receptor. FASEB J. 21, 915-926 (2007).
    • (2007) FASEB J , vol.21 , pp. 915-926
    • Shraga-Heled, N.1
  • 41
    • 33747152506 scopus 로고    scopus 로고
    • Neuropilin-2 interacts with VEGFR-2 and VEGFR-3 and promotes human endothelial cell survival and migration
    • Favier, B. et al. Neuropilin-2 interacts with VEGFR-2 and VEGFR-3 and promotes human endothelial cell survival and migration. Blood 108, 1243-1250 (2006).
    • (2006) Blood , vol.108 , pp. 1243-1250
    • Favier, B.1
  • 42
    • 34548235938 scopus 로고    scopus 로고
    • Neuropilin-1 binds to VEGF121 and regulates endothelial cell migration and sprouting
    • Pan, Q. et al. Neuropilin-1 binds to VEGF121 and regulates endothelial cell migration and sprouting. J. Biol. Chem. 282, 24049-24056 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 24049-24056
    • Pan, Q.1
  • 43
    • 43149106665 scopus 로고    scopus 로고
    • Neuropilin-1 modulates p53/caspases axis to promote endothelial cell survival
    • Wang, L. et al. Neuropilin-1 modulates p53/caspases axis to promote endothelial cell survival. PLoS ONE 2, e1161 (2007).
    • (2007) PLoS ONE , vol.2
    • Wang, L.1
  • 44
    • 41049086388 scopus 로고    scopus 로고
    • Neuropilin-1 and neuropilin-2 act as coreceptors, potentiating proangiogenic activity
    • Characterization of neuropilins as receptors for HGF
    • Sulpice, E. et al. Neuropilin-1 and neuropilin-2 act as coreceptors, potentiating proangiogenic activity. Blood 111, 2036-2045 (2007). Characterization of neuropilins as receptors for HGF.
    • (2007) Blood , vol.111 , pp. 2036-2045
    • Sulpice, E.1
  • 45
    • 0034756449 scopus 로고    scopus 로고
    • Differential expression of neuropilin-1 and neuropilin-2 in arteries and veins
    • Herzog, Y., Kalcheim, C., Kahane, N., Reshef, R. & Neufeld, G. Differential expression of neuropilin-1 and neuropilin-2 in arteries and veins. Mech. Dev. 109, 115-119 (2001).
    • (2001) Mech. Dev , vol.109 , pp. 115-119
    • Herzog, Y.1    Kalcheim, C.2    Kahane, N.3    Reshef, R.4    Neufeld, G.5
  • 46
    • 0036803751 scopus 로고    scopus 로고
    • Abnormal lymphatic vessel development in neuropilin 2 mutant mice
    • Yuan, L. et al. Abnormal lymphatic vessel development in neuropilin 2 mutant mice. Development 129, 4797-4806 (2002).
    • (2002) Development , vol.129 , pp. 4797-4806
    • Yuan, L.1
  • 47
    • 0034794689 scopus 로고    scopus 로고
    • Plasticity of endothelial cells during arterial-venous differentiation in the avian embryo
    • Moyon, D., Pardanaud, L., Yuan, L., Breant, C. & Eichmann, A. Plasticity of endothelial cells during arterial-venous differentiation in the avian embryo. Development 128, 3359-3370 (2001).
    • (2001) Development , vol.128 , pp. 3359-3370
    • Moyon, D.1    Pardanaud, L.2    Yuan, L.3    Breant, C.4    Eichmann, A.5
  • 48
    • 0029006696 scopus 로고
    • Failure of blood-island formation and vasculogenesis in Flk-1-deficient mice
    • Shalaby, F. et al. Failure of blood-island formation and vasculogenesis in Flk-1-deficient mice. Nature 376, 62-66 (1995).
    • (1995) Nature , vol.376 , pp. 62-66
    • Shalaby, F.1
  • 49
    • 0037133617 scopus 로고    scopus 로고
    • Targeting of both mouse neuropilin-1 and neuropilin-2 genes severely impairs developmental yolk sac and embryonic angiogenesis
    • A paper showing that neuropilins are essential for vasculogenesis
    • Takashima, S. et al. Targeting of both mouse neuropilin-1 and neuropilin-2 genes severely impairs developmental yolk sac and embryonic angiogenesis. Proc. Natl Acad. Sci. USA 99, 3657-3662 (2002). A paper showing that neuropilins are essential for vasculogenesis.
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 3657-3662
    • Takashima, S.1
  • 50
    • 0033597813 scopus 로고    scopus 로고
    • Differential binding of vascular endothelial growth factor B splice and proteolytic isoforms to neuropilin-1
    • Makinen, T. et al. Differential binding of vascular endothelial growth factor B splice and proteolytic isoforms to neuropilin-1. J. Biol. Chem. 274, 21217-21222 (1999).
    • (1999) J. Biol. Chem , vol.274 , pp. 21217-21222
    • Makinen, T.1
  • 51
    • 0032575576 scopus 로고    scopus 로고
    • Neuropilin-1 is a placenta growth factor-2 receptor
    • Migdal, M. et al. Neuropilin-1 is a placenta growth factor-2 receptor. J. Biol. Chem. 273, 22272-22278 (1998).
    • (1998) J. Biol. Chem , vol.273 , pp. 22272-22278
    • Migdal, M.1
  • 52
    • 0035940403 scopus 로고    scopus 로고
    • A model for gene therapy of human hereditary lymphedema
    • Karkkainen, M. J. et al. A model for gene therapy of human hereditary lymphedema. Proc. Natl Acad. Sci. USA 98, 12677-12682 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 12677-12682
    • Karkkainen, M.J.1
  • 53
    • 33746503288 scopus 로고    scopus 로고
    • Functional interaction of VEGF-C and VEGF-D with neuropilin receptors
    • Karpanen, T. et al. Functional interaction of VEGF-C and VEGF-D with neuropilin receptors. FASEB J. 20, 1462-1472 (2006).
    • (2006) FASEB J , vol.20 , pp. 1462-1472
    • Karpanen, T.1
  • 54
    • 33750457687 scopus 로고    scopus 로고
    • Breast cancer cells secreted platelet-derived growth factor-induced motility of vascular smooth muscle cells is mediated through neuropilin-1
    • Banerjee, S. et al. Breast cancer cells secreted platelet-derived growth factor-induced motility of vascular smooth muscle cells is mediated through neuropilin-1. Mol. Carcinog. 45, 871-880 (2006).
    • (2006) Mol. Carcinog , vol.45 , pp. 871-880
    • Banerjee, S.1
  • 55
    • 25444463573 scopus 로고    scopus 로고
    • Endothelial/pericyte interactions
    • Armulik, A., Abramsson, A. & Betsholtz, C. Endothelial/pericyte interactions. Circ. Res. 97, 512-523 (2005).
    • (2005) Circ. Res , vol.97 , pp. 512-523
    • Armulik, A.1    Abramsson, A.2    Betsholtz, C.3
  • 56
    • 20244362645 scopus 로고    scopus 로고
    • Interactions of multiple heparin-binding growth factors with neuropilin-1 and potentiation of the activity of fibroblast growth factor-2
    • West, D. C. et al. Interactions of multiple heparin-binding growth factors with neuropilin-1 and potentiation of the activity of fibroblast growth factor-2. J. Biol. Chem. 280, 13457-13464 (2005).
    • (2005) J. Biol. Chem , vol.280 , pp. 13457-13464
    • West, D.C.1
  • 57
    • 45949085841 scopus 로고    scopus 로고
    • Galectin-1, a novel ligand of neuropilin-1, activates VEGFR-2 signaling and modulates the migration of vascular endothelial cells
    • 28 Jan, doi: 10.1038/sj.onc.1211029
    • Hsieh, S. H. et al. Galectin-1, a novel ligand of neuropilin-1, activates VEGFR-2 signaling and modulates the migration of vascular endothelial cells. Oncogene 28 Jan 2008 (doi: 10.1038/sj.onc.1211029).
    • (2008) Oncogene
    • Hsieh, S.H.1
  • 58
    • 0033678716 scopus 로고    scopus 로고
    • Analysis of the L1-deficient mouse phenotype reveals cross-talk between Sema3A and L1 signaling pathways in axonal guidance
    • A paper showing that SEMA3A is turned from a repulsive agent into an attractive agent in the presence of the extracellular domain of L1CAM
    • Castellani, V., Chedotal, A., Schachner, M., Faivre-Sarrailh, C. & Rougon, G. Analysis of the L1-deficient mouse phenotype reveals cross-talk between Sema3A and L1 signaling pathways in axonal guidance. Neuron 27, 237-249 (2000). A paper showing that SEMA3A is turned from a repulsive agent into an attractive agent in the presence of the extracellular domain of L1CAM.
    • (2000) Neuron , vol.27 , pp. 237-249
    • Castellani, V.1    Chedotal, A.2    Schachner, M.3    Faivre-Sarrailh, C.4    Rougon, G.5
  • 59
    • 0037011182 scopus 로고    scopus 로고
    • Cis and trans interactions of L1 with neuropilin-1 control axonal responses to semaphorin 3A
    • Castellani, V., De Angelis, E., Kenwrick, S. & Rougon, G. Cis and trans interactions of L1 with neuropilin-1 control axonal responses to semaphorin 3A. EMBO J. 21, 6348-6357 (2002).
    • (2002) EMBO J , vol.21 , pp. 6348-6357
    • Castellani, V.1    De Angelis, E.2    Kenwrick, S.3    Rougon, G.4
  • 60
    • 37249007666 scopus 로고    scopus 로고
    • Close homolog of L1 and neuropilin 1 mediate guidance of thalamocortical axons at the ventral telencephalon
    • Wright, A. G. et al. Close homolog of L1 and neuropilin 1 mediate guidance of thalamocortical axons at the ventral telencephalon. J. Neurosci. 27, 13667-13679 (2007).
    • (2007) J. Neurosci , vol.27 , pp. 13667-13679
    • Wright, A.G.1
  • 61
    • 38049184323 scopus 로고    scopus 로고
    • CHL1 promotes Sema3A-induced growth cone collapse and neurite elaboration through a motif required for recruitment of ERM proteins to the plasma membrane
    • Schlatter, M. C., Buhusi, M., Wright, A. G. & Maness, P. F. CHL1 promotes Sema3A-induced growth cone collapse and neurite elaboration through a motif required for recruitment of ERM proteins to the plasma membrane. J. Neurochem. 104, 731-744 (2008).
    • (2008) J. Neurochem , vol.104 , pp. 731-744
    • Schlatter, M.C.1    Buhusi, M.2    Wright, A.G.3    Maness, P.F.4
  • 62
    • 35948965519 scopus 로고    scopus 로고
    • Neuropilin-1 interacts with integrin β1 and modulates pancreatic cancer cell growth, survival and invasion
    • Fukasawa, M., Matsushita, A. & Korc, M. Neuropilin-1 interacts with integrin β1 and modulates pancreatic cancer cell growth, survival and invasion. Cancer Biol. Ther. 6, (2007).
    • (2007) Cancer Biol. Ther , vol.6
    • Fukasawa, M.1    Matsushita, A.2    Korc, M.3
  • 63
    • 33745063095 scopus 로고    scopus 로고
    • The role of neuropilins in cancer
    • Ellis, L. M. The role of neuropilins in cancer. Mol. Cancer Ther. 5, 1099-1107 (2006).
    • (2006) Mol. Cancer Ther , vol.5 , pp. 1099-1107
    • Ellis, L.M.1
  • 64
    • 0033674846 scopus 로고    scopus 로고
    • Neuropilin-1 expression by tumor cells promotes tumor angiogenesis and progression
    • Miao, H. Q., Lee, P., Lin, H., Soker, S. & Klagsbrun, M. Neuropilin-1 expression by tumor cells promotes tumor angiogenesis and progression. FASEB J. 14, 2532-2539 (2000).
    • (2000) FASEB J , vol.14 , pp. 2532-2539
    • Miao, H.Q.1    Lee, P.2    Lin, H.3    Soker, S.4    Klagsbrun, M.5
  • 65
    • 2442639176 scopus 로고    scopus 로고
    • Neuropilin-1 in human colon cancer: Expression, regulation, and role in induction of angiogenesis
    • Parikh, A. A. et al. Neuropilin-1 in human colon cancer: expression, regulation, and role in induction of angiogenesis. Am. J. Pathol. 164, 2139-2151 (2004).
    • (2004) Am. J. Pathol , vol.164 , pp. 2139-2151
    • Parikh, A.A.1
  • 66
    • 18144427143 scopus 로고    scopus 로고
    • Neuropilin-1 suppresses tumorigenic properties in a human pancreatic adenocarcinoma cell line lacking neuropilin-1 coreceptors
    • Gray, M. J. et al. Neuropilin-1 suppresses tumorigenic properties in a human pancreatic adenocarcinoma cell line lacking neuropilin-1 coreceptors. Cancer Res. 65, 3664-3670 (2005).
    • (2005) Cancer Res , vol.65 , pp. 3664-3670
    • Gray, M.J.1
  • 67
    • 33744474889 scopus 로고    scopus 로고
    • The preserved expression of neuropilin (NRP) 1 contributes to a better prognosis in colon cancer
    • Kamiya, T. et al. The preserved expression of neuropilin (NRP) 1 contributes to a better prognosis in colon cancer. Oncol. Rep. 15, 369-373 (2006).
    • (2006) Oncol. Rep , vol.15 , pp. 369-373
    • Kamiya, T.1
  • 68
    • 38449095310 scopus 로고    scopus 로고
    • Therapeutic targeting of neuropilin-2 on colorectal carcinoma cells implanted in the murine liver
    • Gray, M. J. et al. Therapeutic targeting of neuropilin-2 on colorectal carcinoma cells implanted in the murine liver. J. Natl Cancer Inst. 100, 109-120 (2008).
    • (2008) J. Natl Cancer Inst , vol.100 , pp. 109-120
    • Gray, M.J.1
  • 69
    • 24944581963 scopus 로고    scopus 로고
    • Plexin d1 expression is induced on tumor vasculature and tumor cells: A novel target for diagnosis and therapy?
    • Roodink, I. et al. Plexin d1 expression is induced on tumor vasculature and tumor cells: a novel target for diagnosis and therapy? Cancer Res. 65, 8317-8323 (2005).
    • (2005) Cancer Res , vol.65 , pp. 8317-8323
    • Roodink, I.1
  • 70
    • 0141816865 scopus 로고    scopus 로고
    • Competing autocrine pathways involving alternative neuropilin-1 ligands regulate chemotaxis of carcinoma cells
    • Bachelder, R. E. et al. Competing autocrine pathways involving alternative neuropilin-1 ligands regulate chemotaxis of carcinoma cells. Cancer Res. 63, 5230-5233 (2003).
    • (2003) Cancer Res , vol.63 , pp. 5230-5233
    • Bachelder, R.E.1
  • 71
    • 0038458973 scopus 로고    scopus 로고
    • Human malignant glioma cells express semaphorins and their receptors, neuropilins and plexins
    • Rieger, J., Wick, W. & Weller, M. Human malignant glioma cells express semaphorins and their receptors, neuropilins and plexins. Glia 42, 379-389 (2003).
    • (2003) Glia , vol.42 , pp. 379-389
    • Rieger, J.1    Wick, W.2    Weller, M.3
  • 72
    • 28744439266 scopus 로고    scopus 로고
    • Profiling estrogen-regulated gene expression changes in normal and malignant human ovarian surface epithelial cells
    • Syed, V. et al. Profiling estrogen-regulated gene expression changes in normal and malignant human ovarian surface epithelial cells. Oncogene 24, 8128-8143 (2005).
    • (2005) Oncogene , vol.24 , pp. 8128-8143
    • Syed, V.1
  • 73
    • 33748336510 scopus 로고    scopus 로고
    • Inhibition of vascular endothelial growth factor (VEGF)-165 and semaphorin 3A-mediated cellular invasion and tumor growth by the VEGF signaling inhibitor ZD4190 in human colon cancer cells and xenografts
    • Nguyen, Q. D. et al. Inhibition of vascular endothelial growth factor (VEGF)-165 and semaphorin 3A-mediated cellular invasion and tumor growth by the VEGF signaling inhibitor ZD4190 in human colon cancer cells and xenografts. Mol. Cancer Ther. 5, 2070-2077 (2006).
    • (2006) Mol. Cancer Ther , vol.5 , pp. 2070-2077
    • Nguyen, Q.D.1
  • 74
    • 37649009370 scopus 로고    scopus 로고
    • Plexin-B1 mutations in prostate cancer
    • Wong, O. G. et al. Plexin-B1 mutations in prostate cancer. Proc. Natl Acad. Sci. USA 48, 19040-19045 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.48 , pp. 19040-19045
    • Wong, O.G.1
  • 75
    • 33947202804 scopus 로고    scopus 로고
    • Poor outcome in estrogen receptor-positive breast cancers predicted by loss of plexin b1
    • Rody, A. et al. Poor outcome in estrogen receptor-positive breast cancers predicted by loss of plexin b1. Clin. Cancer Res. 13, 1115-1122 (2007).
    • (2007) Clin. Cancer Res , vol.13 , pp. 1115-1122
    • Rody, A.1
  • 76
    • 0038068926 scopus 로고    scopus 로고
    • Allelic loss on chromosome 3p21.3 and promoter hypermethylation of semaphorin 3b in nonsmall cell lung cancer
    • Kuroki, T. et al. Allelic loss on chromosome 3p21.3 and promoter hypermethylation of semaphorin 3b in nonsmall cell lung cancer. Cancer Res. 63, 3352-3355 (2003).
    • (2003) Cancer Res , vol.63 , pp. 3352-3355
    • Kuroki, T.1
  • 77
    • 20144371437 scopus 로고    scopus 로고
    • Allele loss and epigenetic inactivation of 3p21.3 in malignant liver tumors
    • Tischoff, I. et al. Allele loss and epigenetic inactivation of 3p21.3 in malignant liver tumors. Int. J. Cancer 115, 684-689 (2005).
    • (2005) Int. J. Cancer , vol.115 , pp. 684-689
    • Tischoff, I.1
  • 78
    • 34247181069 scopus 로고    scopus 로고
    • High-resolution analysis of 3p deletion in neuroblastoma and differential methylation of the SEMA3B tumor suppressor gene
    • Nair, P. N., McArdle, L., Cornell, J., Cohn, S. L. & Stallings, R. L. High-resolution analysis of 3p deletion in neuroblastoma and differential methylation of the SEMA3B tumor suppressor gene. Cancer Genet. Cytogenet. 174, 100-110 (2007).
    • (2007) Cancer Genet. Cytogenet , vol.174 , pp. 100-110
    • Nair, P.N.1    McArdle, L.2    Cornell, J.3    Cohn, S.L.4    Stallings, R.L.5
  • 79
    • 24944474931 scopus 로고    scopus 로고
    • The race associated allele of semaphorin 3B (SEMA3B) T415I and its role in lung cancer in African-Americans and Latino-Americans
    • Marsit, C. J., Wiencke, J. K., Liu, M. & Kelsey, K. T. The race associated allele of semaphorin 3B (SEMA3B) T415I and its role in lung cancer in African-Americans and Latino-Americans. Carcinogenesis 26, 1446-1449 (2005).
    • (2005) Carcinogenesis , vol.26 , pp. 1446-1449
    • Marsit, C.J.1    Wiencke, J.K.2    Liu, M.3    Kelsey, K.T.4
  • 80
    • 18544371321 scopus 로고    scopus 로고
    • Null and conditional semaphorin 3B alleles using a flexible puroΔtk loxP/FRT vector
    • van der Weyden, L. et al. Null and conditional semaphorin 3B alleles using a flexible puroΔtk loxP/FRT vector. Genesis 41, 171-178 (2005).
    • (2005) Genesis , vol.41 , pp. 171-178
    • van der Weyden, L.1
  • 81
    • 3843113186 scopus 로고    scopus 로고
    • Semaphorin 3B (SEMA3B) induces apoptosis in lung and breast cancer, whereas VEGF165 antagonizes this effect
    • Castro-Rivera, E., Ran, S., Thorpe, P. & Minna, J. D. Semaphorin 3B (SEMA3B) induces apoptosis in lung and breast cancer, whereas VEGF165 antagonizes this effect. Proc. Natl Acad. Sci. USA 101, 11432-11437 (2004).
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 11432-11437
    • Castro-Rivera, E.1    Ran, S.2    Thorpe, P.3    Minna, J.D.4
  • 82
    • 0029871193 scopus 로고    scopus 로고
    • Isolation of the human semaphorin III/F gene (SEMA3F) at chromosome 3p21, a region deleted in lung cancer
    • Xiang, R. H. et al. Isolation of the human semaphorin III/F gene (SEMA3F) at chromosome 3p21, a region deleted in lung cancer. Genomics 32, 39-48 (1996).
    • (1996) Genomics , vol.32 , pp. 39-48
    • Xiang, R.H.1
  • 83
    • 9244251007 scopus 로고    scopus 로고
    • Distinct 3p21.3 deletions in lung cancer and identification of a new human semaphorin
    • Roche, J. et al. Distinct 3p21.3 deletions in lung cancer and identification of a new human semaphorin. Oncogene 12, 1289-1297 (1996).
    • (1996) Oncogene , vol.12 , pp. 1289-1297
    • Roche, J.1
  • 84
    • 0036569936 scopus 로고    scopus 로고
    • Semaphorin 3F gene from human 3p21.3 suppresses tumor formation in nude mice
    • Xiang, R. et al. Semaphorin 3F gene from human 3p21.3 suppresses tumor formation in nude mice. Cancer Res. 62, 2637-2643 (2002).
    • (2002) Cancer Res , vol.62 , pp. 2637-2643
    • Xiang, R.1
  • 85
    • 12244313025 scopus 로고    scopus 로고
    • Semaphorin SEMA3F and VEGF have opposing effects on cell attachment and spreading
    • Nasarre, P. et al. Semaphorin SEMA3F and VEGF have opposing effects on cell attachment and spreading. Neoplasia 5, 83-92 (2003).
    • (2003) Neoplasia , vol.5 , pp. 83-92
    • Nasarre, P.1
  • 86
    • 14644416543 scopus 로고    scopus 로고
    • Semaphorin SEMA3F has a repulsing activity on breast cancer cells and inhibits E-cadherin-mediated cell adhesion
    • Nasarre, P. et al. Semaphorin SEMA3F has a repulsing activity on breast cancer cells and inhibits E-cadherin-mediated cell adhesion. Neoplasia 7, 180-189 (2005).
    • (2005) Neoplasia , vol.7 , pp. 180-189
    • Nasarre, P.1
  • 87
    • 85047693077 scopus 로고    scopus 로고
    • Semaphorin 3F, a chemorepulsant for endothelial cells, induces a poorly vascularized, encapsulated, nonmetastatic tumor phenotype
    • Bielenberg, D. R. et al. Semaphorin 3F, a chemorepulsant for endothelial cells, induces a poorly vascularized, encapsulated, nonmetastatic tumor phenotype. J. Clin. Invest. 114, 1260-1271 (2004).
    • (2004) J. Clin. Invest , vol.114 , pp. 1260-1271
    • Bielenberg, D.R.1
  • 88
    • 34548735409 scopus 로고    scopus 로고
    • Semaphorin SEMA3F affects multiple signaling pathways in lung cancer cells
    • Potiron, V. A. et al. Semaphorin SEMA3F affects multiple signaling pathways in lung cancer cells. Cancer Res. 67, 8708-8715 (2007).
    • (2007) Cancer Res , vol.67 , pp. 8708-8715
    • Potiron, V.A.1
  • 89
    • 20344381552 scopus 로고    scopus 로고
    • Selective suppression of in vivo tumorigenicity by semaphorin SEMA3F in lung cancer cells
    • Kusy, S. et al. Selective suppression of in vivo tumorigenicity by semaphorin SEMA3F in lung cancer cells. Neoplasia 7, 457-465 (2005).
    • (2005) Neoplasia , vol.7 , pp. 457-465
    • Kusy, S.1
  • 90
    • 33750069768 scopus 로고    scopus 로고
    • Expression of semaphorins, vascular endothelial growth factor, and their common receptor neuropilins and alleic loss of semaphorin locus in epithelial ovarian neoplasms: Increased ratio of vascular endothelial growth factor to semaphorin is a poor prognostic factor in ovarian carcinomas
    • Osada, R. et al. Expression of semaphorins, vascular endothelial growth factor, and their common receptor neuropilins and alleic loss of semaphorin locus in epithelial ovarian neoplasms: increased ratio of vascular endothelial growth factor to semaphorin is a poor prognostic factor in ovarian carcinomas. Hum. Pathol. 37, 1414-1425 (2006).
    • (2006) Hum. Pathol , vol.37 , pp. 1414-1425
    • Osada, R.1
  • 91
    • 34447345999 scopus 로고    scopus 로고
    • Increased class 3 semaphorin expression modulates the invasive and adhesive properties of prostate cancer cells
    • Herman, J. G. & Meadows, G. G. Increased class 3 semaphorin expression modulates the invasive and adhesive properties of prostate cancer cells. Int. J. Oncol. 30, 1231-1238 (2007).
    • (2007) Int. J. Oncol , vol.30 , pp. 1231-1238
    • Herman, J.G.1    Meadows, G.G.2
  • 92
    • 35649009802 scopus 로고    scopus 로고
    • Association of axon guidance factor semaphorin 3A with poor outcome in pancreatic cancer
    • Muller, M. W. et al. Association of axon guidance factor semaphorin 3A with poor outcome in pancreatic cancer. Int. J. Cancer 121, 2421-2433 (2007).
    • (2007) Int. J. Cancer , vol.121 , pp. 2421-2433
    • Muller, M.W.1
  • 93
    • 1442265710 scopus 로고    scopus 로고
    • Cross-talk between vascular endothelial growth factor and semaphorin-3A pathway in the regulation of normal and malignant mesothelial cell proliferation
    • Catalano, A. et al. Cross-talk between vascular endothelial growth factor and semaphorin-3A pathway in the regulation of normal and malignant mesothelial cell proliferation. FASEB J. 18, 358-360 (2004).
    • (2004) FASEB J , vol.18 , pp. 358-360
    • Catalano, A.1
  • 94
    • 41949129114 scopus 로고    scopus 로고
    • Semaphorin 3A suppresses VEGF-mediated angiogenesis yet acts as a vascular permeability factor
    • Acevedo, L. M., Barillas, S., Weis, S. M., Gothert, J. R. & Cheresh, D. A. Semaphorin 3A suppresses VEGF-mediated angiogenesis yet acts as a vascular permeability factor. Blood 111, 2674-2680 (2008).
    • (2008) Blood , vol.111 , pp. 2674-2680
    • Acevedo, L.M.1    Barillas, S.2    Weis, S.M.3    Gothert, J.R.4    Cheresh, D.A.5
  • 95
    • 0345466647 scopus 로고    scopus 로고
    • Identification of semaphorin E gene expression in metastatic human lung adenocarcinoma cells by mRNA differential display
    • Martin-Satue, M. & Blanco, J. Identification of semaphorin E gene expression in metastatic human lung adenocarcinoma cells by mRNA differential display. J. Surg. Oncol. 72, 18-23 (1999).
    • (1999) J. Surg. Oncol , vol.72 , pp. 18-23
    • Martin-Satue, M.1    Blanco, J.2
  • 96
    • 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. 20, 2150-2152 (2006).
    • (2006) FASEB J , vol.20 , pp. 2150-2152
    • Banu, N.1    Teichman, J.2    Dunlap-Brown, M.3    Villegas, G.4    Tufro, A.5
  • 97
    • 0036711644 scopus 로고    scopus 로고
    • The Semaphorin 4D receptor controls invasive growth by coupling with Met
    • The first description of plexin-mediated activation of a tyrosine kinase receptor by a semaphorin
    • Giordano, S. et al. The Semaphorin 4D receptor controls invasive growth by coupling with Met. Nature Cell Biol. 4, 720-724 (2002). The first description of plexin-mediated activation of a tyrosine kinase receptor by a semaphorin.
    • (2002) Nature Cell Biol , vol.4 , pp. 720-724
    • Giordano, S.1
  • 98
    • 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 23, 5131-5137 (2004).
    • (2004) Oncogene , vol.23 , pp. 5131-5137
    • Conrotto, P.1    Corso, S.2    Gamberini, S.3    Comoglio, P.M.4    Giordano, S.5
  • 99
    • 34547931473 scopus 로고    scopus 로고
    • Neuropilin-1 promotes human glioma progression through potentiating the activity of the HGF/SF autocrine pathway
    • Hu, B. et al. Neuropilin-1 promotes human glioma progression through potentiating the activity of the HGF/SF autocrine pathway. Oncogene 26, 5577-5586 (2007).
    • (2007) Oncogene , vol.26 , pp. 5577-5586
    • Hu, B.1
  • 100
    • 33745828702 scopus 로고    scopus 로고
    • EGF-ERBB signalling: Towards the systems level
    • Citri, A. & Yarden, Y. EGF-ERBB signalling: towards the systems level. Nature Rev. Mol. Cell Biol. 7, 505-516 (2006).
    • (2006) Nature Rev. Mol. Cell Biol , vol.7 , pp. 505-516
    • Citri, A.1    Yarden, Y.2
  • 101
    • 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. 165, 869-880 (2004).
    • (2004) J. Cell Biol , vol.165 , pp. 869-880
    • Swiercz, J.M.1    Kuner, R.2    Offermanns, S.3
  • 102
    • 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. 283, 1893-1901 (2008).
    • (2008) J. Biol. Chem , vol.283 , pp. 1893-1901
    • Swiercz, J.M.1    Worzfeld, T.2    Offermanns, S.3
  • 103
    • 4444252172 scopus 로고    scopus 로고
    • Plexin-B3 is a functional receptor for semaphorin 5A
    • 710-714
    • Artigiani, S. et al. Plexin-B3 is a functional receptor for semaphorin 5A. EMBO Rep. 5, 710-714 (2004).
    • (2004) EMBO Rep , vol.5
    • Artigiani, S.1
  • 104
    • 34249016907 scopus 로고    scopus 로고
    • Genome-wide gene expression profiles of clear cell renal cell carcinoma: Identification of molecular targets for treatment of renal cell carcinoma
    • Hirota, E. et al. Genome-wide gene expression profiles of clear cell renal cell carcinoma: Identification of molecular targets for treatment of renal cell carcinoma. Int. J. Oncol. 29, 799-827 (2006).
    • (2006) Int. J. Oncol , vol.29 , pp. 799-827
    • Hirota, E.1
  • 105
    • 34249977586 scopus 로고    scopus 로고
    • CLCP1 interacts with semaphorin 4B and regulates motility of lung cancer cells
    • Nagai, H. et al. CLCP1 interacts with semaphorin 4B and regulates motility of lung cancer cells. Oncogene 26, 4025-4031 (2007).
    • (2007) Oncogene , vol.26 , pp. 4025-4031
    • Nagai, H.1
  • 106
    • 0041530325 scopus 로고    scopus 로고
    • Class 3 semaphorins control vascular morphogenesis by inhibiting integrin function
    • First description of semaphorins as modulators of integrin function
    • Serini, G. et al. Class 3 semaphorins control vascular morphogenesis by inhibiting integrin function. Nature 424, 391-397 (2003). First description of semaphorins as modulators of integrin function.
    • (2003) Nature , vol.424 , pp. 391-397
    • Serini, G.1
  • 107
    • 34548839104 scopus 로고    scopus 로고
    • Semaphorin-3A and semaphorin-3F work together to repel endothelial cells and to inhibit their survival by induction of apoptosis
    • Guttmann-Raviv, N. et al. Semaphorin-3A and semaphorin-3F work together to repel endothelial cells and to inhibit their survival by induction of apoptosis. J. Biol. Chem. 282, 26294-26305 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 26294-26305
    • Guttmann-Raviv, N.1
  • 108
    • 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 134, 1833-1843 (2007).
    • (2007) Development , vol.134 , pp. 1833-1843
    • Vieira, J.M.1    Schwarz, Q.2    Ruhrberg, C.3
  • 109
    • 0038686623 scopus 로고    scopus 로고
    • Neuropilin-1 conveys semaphorin and VEGF signaling during neural and cardiovascular development
    • Gu, C. et al. Neuropilin-1 conveys semaphorin and VEGF signaling during neural and cardiovascular development. Dev. Cell 5, 45-57 (2003).
    • (2003) Dev. Cell , vol.5 , pp. 45-57
    • Gu, C.1
  • 110
    • 0842304286 scopus 로고    scopus 로고
    • Kessler, O. et al. Semaphorin-3F is an inhibitor of tumor angiogenesis. Cancer Res. 64, 1008-1015 (2004). The first description of a semaphorin as an inhibitor of tumour angiogenesis.
    • Kessler, O. et al. Semaphorin-3F is an inhibitor of tumor angiogenesis. Cancer Res. 64, 1008-1015 (2004). The first description of a semaphorin as an inhibitor of tumour angiogenesis.
  • 111
    • 33847766123 scopus 로고    scopus 로고
    • Possible role of semaphorin 3F, a candidate tumor suppressor gene at 3p21.3, in p53-regulated tumor angiogenesis suppression
    • Futamura, M. et al. Possible role of semaphorin 3F, a candidate tumor suppressor gene at 3p21.3, in p53-regulated tumor angiogenesis suppression. Cancer Res. 67, 1451-1460 (2007).
    • (2007) Cancer Res , vol.67 , pp. 1451-1460
    • Futamura, M.1
  • 112
    • 19944430075 scopus 로고    scopus 로고
    • Semaphorin 3E and plexin-D1 control vascular pattern independently of neuropilins
    • This paper changes a dogma by showing that the class 3 semaphorin SEMA3E signals directly through plexin D1 and repels blood vessels during embryonic development
    • Gu, C. et al. Semaphorin 3E and plexin-D1 control vascular pattern independently of neuropilins. Science 307, 265-268 (2005). This paper changes a dogma by showing that the class 3 semaphorin SEMA3E signals directly through plexin D1 and repels blood vessels during embryonic development.
    • (2005) Science , vol.307 , pp. 265-268
    • Gu, C.1
  • 113
    • 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 7, 107-116 (2004).
    • (2004) Dev. Cell , vol.7 , pp. 107-116
    • Gitler, A.D.1    Lu, M.M.2    Epstein, J.A.3
  • 114
    • 36549073637 scopus 로고    scopus 로고
    • Gating of Sema3E/PlexinD1 signaling by neuropilin-1 switches axonal repulsion to attraction during brain development
    • Chauvet, S. et al. Gating of Sema3E/PlexinD1 signaling by neuropilin-1 switches axonal repulsion to attraction during brain development. Neuron 56, 807-822 (2007).
    • (2007) Neuron , vol.56 , pp. 807-822
    • Chauvet, S.1
  • 115
    • 33947129779 scopus 로고    scopus 로고
    • Semaphorin-4A, an activator for T-cell-mediated immunity, suppresses angiogenesis via plexin-D1
    • Toyofuku, T. et al. Semaphorin-4A, an activator for T-cell-mediated immunity, suppresses angiogenesis via plexin-D1. EMBO J. 26, 1373-1384 (2007).
    • (2007) EMBO J , vol.26 , pp. 1373-1384
    • Toyofuku, T.1
  • 116
    • 25144490134 scopus 로고    scopus 로고
    • Recombinant semaphorin 6A-1 ectodomain inhibits in vivo growth factor and tumor cell line-induced angiogenesis
    • Dhanabal, M. et al. Recombinant semaphorin 6A-1 ectodomain inhibits in vivo growth factor and tumor cell line-induced angiogenesis. Cancer Biol. Ther. 4, 659-668 (2005).
    • (2005) Cancer Biol. Ther , vol.4 , pp. 659-668
    • Dhanabal, M.1
  • 117
    • 41249088330 scopus 로고    scopus 로고
    • Caunt, M. et al. Blocking neuropilin-2 function inhibits tumor cell metastasis. Cancer Cell 13, 331-342 (2008). This manuscript demonstrates that antibodies to neuropilin 2 can inhibit tumour metastasis through inhibition of lymphangiogenesis.
    • Caunt, M. et al. Blocking neuropilin-2 function inhibits tumor cell metastasis. Cancer Cell 13, 331-342 (2008). This manuscript demonstrates that antibodies to neuropilin 2 can inhibit tumour metastasis through inhibition of lymphangiogenesis.
  • 118
    • 33846850498 scopus 로고    scopus 로고
    • Regulated surface expression and shedding support a dual role for semaphorin 4D in platelet responses to vascular injury
    • Zhu, L. et al. Regulated surface expression and shedding support a dual role for semaphorin 4D in platelet responses to vascular injury. Proc. Natl Acad. Sci. USA 104, 1621-1626 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 1621-1626
    • Zhu, L.1
  • 119
    • 3442897353 scopus 로고    scopus 로고
    • Class IV semaphorins promote angiogenesis by stimulating Rho-initiated pathways through plexin-B
    • Basile, J. R., Barac, A., Zhu, T., Guan, K. L. & Gutkind, J. S. Class IV semaphorins promote angiogenesis by stimulating Rho-initiated pathways through plexin-B. Cancer Res. 64, 5212-5224 (2004).
    • (2004) Cancer Res , vol.64 , pp. 5212-5224
    • Basile, J.R.1    Barac, A.2    Zhu, T.3    Guan, K.L.4    Gutkind, J.S.5
  • 120
    • 33745176581 scopus 로고    scopus 로고
    • Semaphorin 4D provides a link between axon guidance processes and tumor-induced angiogenesis
    • The first demonstration that a semaphorin can promote tumour progression through induction of 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. USA 103, 9017-9022 (2006). The first demonstration that a semaphorin can promote tumour progression through induction of angiogenesis.
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 9017-9022
    • Basile, J.R.1    Castilho, R.M.2    Williams, V.P.3    Gutkind, J.S.4
  • 121
    • 19344364598 scopus 로고    scopus 로고
    • Sema4D induces angiogenesis through Met recruitment by Plexin B1
    • Conrotto, P. et al. Sema4D induces angiogenesis through Met recruitment by Plexin B1. Blood 105, 4321-4329 (2005).
    • (2005) Blood , vol.105 , pp. 4321-4329
    • Conrotto, P.1
  • 122
    • 34250194655 scopus 로고    scopus 로고
    • PlexinB1 plays a redundant role during mouse development and in tumour angiogenesis
    • Fazzari, P. et al. PlexinB1 plays a redundant role during mouse development and in tumour angiogenesis. BMC Dev. Biol. 7, 55 (2007).
    • (2007) BMC Dev. Biol , vol.7 , pp. 55
    • Fazzari, P.1
  • 123
    • 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. et al. 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. 18, 435-447 (2004).
    • (2004) Genes Dev , vol.18 , pp. 435-447
    • Toyofuku, T.1
  • 124
    • 33845991161 scopus 로고    scopus 로고
    • Blocking neuropilin-1 function has an additive effect with anti-VEGF to inhibit tumor growth
    • This paper shows that antibodies directed against neuropilins have a potential use as supressors of tumour development
    • Pan, Q. et al. Blocking neuropilin-1 function has an additive effect with anti-VEGF to inhibit tumor growth. Cancer Cell 11, 53-67 (2007). This paper shows that antibodies directed against neuropilins have a potential use as supressors of tumour development.
    • (2007) Cancer Cell , vol.11 , pp. 53-67
    • Pan, Q.1
  • 125
    • 35948964766 scopus 로고    scopus 로고
    • Hepatocyte growth factor-mediated cell invasion in pancreatic cancer cells is dependent on neuropilin-1
    • Matsushita, A., Gotze, T. & Korc, M. Hepatocyte growth factor-mediated cell invasion in pancreatic cancer cells is dependent on neuropilin-1. Cancer Res. 67, 10309-10316 (2007).
    • (2007) Cancer Res , vol.67 , pp. 10309-10316
    • Matsushita, A.1    Gotze, T.2    Korc, M.3
  • 126
    • 17044406054 scopus 로고    scopus 로고
    • CD38 and CD100 lead a network of surface receptors relaying positive signals for B-CLL growth and survival
    • Deaglio, S. et al. CD38 and CD100 lead a network of surface receptors relaying positive signals for B-CLL growth and survival. Blood 105, 3042-3050 (2005).
    • (2005) Blood , vol.105 , pp. 3042-3050
    • Deaglio, S.1
  • 127
    • 0037369284 scopus 로고    scopus 로고
    • + B lymphocytes
    • + B lymphocytes. Blood 101, 1962-1969 (2003).
    • (2003) Blood , vol.101 , pp. 1962-1969
    • Granziero, L.1
  • 128
    • 27644521904 scopus 로고    scopus 로고
    • Proprotein convertases: "master switches" in the regulation of tumor growth and progression
    • Bassi, D. E., Fu, J., Lopez de, C. R. & Klein-Szanto, A. J. Proprotein convertases: "master switches" in the regulation of tumor growth and progression. Mol. Carcinog. 44, 151-161 (2005).
    • (2005) Mol. Carcinog , vol.44 , pp. 151-161
    • Bassi, D.E.1    Fu, J.2    Lopez de, C.R.3    Klein-Szanto, A.J.4
  • 129
    • 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. & Puschel, A. W. The chemorepulsive activity of secreted semaphorins is regulated by furin-dependent proteolytic processing. EMBO J. 16, 6077-6086 (1997).
    • (1997) EMBO J , vol.16 , pp. 6077-6086
    • Adams, R.H.1    Lohrum, M.2    Klostermann, A.3    Betz, H.4    Puschel, A.W.5
  • 130
    • 22244475429 scopus 로고    scopus 로고
    • Proteolytic processing converts the repelling signal sema3e into an inducer of invasive growth and lung metastasis
    • Christensen, C. et al. Proteolytic processing converts the repelling signal sema3e into an inducer of invasive growth and lung metastasis. Cancer Res. 65, 6167-6177 (2005).
    • (2005) Cancer Res , vol.65 , pp. 6167-6177
    • Christensen, C.1
  • 131
    • 37549050866 scopus 로고    scopus 로고
    • Semaphorin-3A guides radial migration of cortical neurons during development
    • Chen, G. et al. Semaphorin-3A guides radial migration of cortical neurons during development. Nature Neurosci. 11, 36-44 (2008).
    • (2008) Nature Neurosci , vol.11 , pp. 36-44
    • Chen, G.1
  • 132
    • 13844276582 scopus 로고    scopus 로고
    • Differential requirement for plexin-A3 and -A4 in mediating responses of sensory and sympathetic neurons to distinct class 3 semaphorins
    • Yaron, A., Huang, P. H., Cheng, H. J. & Tessier-Lavigne, M. Differential requirement for plexin-A3 and -A4 in mediating responses of sensory and sympathetic neurons to distinct class 3 semaphorins. Neuron 45, 513-523 (2005).
    • (2005) Neuron , vol.45 , pp. 513-523
    • Yaron, A.1    Huang, P.H.2    Cheng, H.J.3    Tessier-Lavigne, M.4
  • 133
    • 0035105491 scopus 로고    scopus 로고
    • Takahashi, T. & Strittmatter, S. M. PlexinA1 autoinhibition by the plexin sema domain. Neuron 29, 429-439 (2001). This manuscript demonstrates a role for the sema domain of plexin in the inhibition of plexin activity in the absence of semaphorins.
    • Takahashi, T. & Strittmatter, S. M. PlexinA1 autoinhibition by the plexin sema domain. Neuron 29, 429-439 (2001). This manuscript demonstrates a role for the sema domain of plexin in the inhibition of plexin activity in the absence of semaphorins.
  • 135
    • 28644439947 scopus 로고    scopus 로고
    • Komatsu, M. & Ruoslahti, E. R-Ras is a global regulator of vascular regeneration that suppresses intimal hyperplasia and tumor angiogenesis. Nature Med. 11, 1346-1350 (2005).
    • Komatsu, M. & Ruoslahti, E. R-Ras is a global regulator of vascular regeneration that suppresses intimal hyperplasia and tumor angiogenesis. Nature Med. 11, 1346-1350 (2005).
  • 136
    • 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. & Puschel, A. W. Antagonistic effects of Rnd1 and RhoD GTPases regulate receptor activity in Semaphorin 3A-induced cytoskeletal collapse. J. Neurosci. 22, 471-477 (2002).
    • (2002) J. Neurosci , vol.22 , pp. 471-477
    • Zanata, S.M.1    Hovatta, I.2    Rohm, B.3    Puschel, A.W.4
  • 137
    • 0141865705 scopus 로고    scopus 로고
    • Talin binding to integrin beta tails: A final common step in integrin activation
    • Tadokoro, S. et al. Talin binding to integrin beta tails: a final common step in integrin activation. Science 302, 103-106 (2003).
    • (2003) Science , vol.302 , pp. 103-106
    • Tadokoro, S.1
  • 138
    • 0035096551 scopus 로고    scopus 로고
    • Phosphorylation of cofilin by LIM-kinase is necessary for semaphorin 3A- induced growth cone collapse
    • Aizawa, H. et al. Phosphorylation of cofilin by LIM-kinase is necessary for semaphorin 3A- induced growth cone collapse. Nature Neurosci. 4, 367-373 (2001).
    • (2001) Nature Neurosci , vol.4 , pp. 367-373
    • Aizawa, H.1
  • 139
    • 34249315804 scopus 로고    scopus 로고
    • Lim kinases, regulators of actin dynamics
    • Bernard, O. Lim kinases, regulators of actin dynamics. Int. J. Biochem. Cell Biol. 39, 1071-1076 (2007).
    • (2007) Int. J. Biochem. Cell Biol , vol.39 , pp. 1071-1076
    • Bernard, O.1
  • 140
    • 0036645682 scopus 로고    scopus 로고
    • Involvement of Fes/Fps tyrosine kinase in semaphorin3A signaling
    • Mitsui, N. et al. Involvement of Fes/Fps tyrosine kinase in semaphorin3A signaling. EMBO J. 21, 3274-3285 (2002).
    • (2002) EMBO J , vol.21 , pp. 3274-3285
    • Mitsui, N.1
  • 141
    • 38849182799 scopus 로고    scopus 로고
    • The Fer tyrosine kinase regulates an axon retraction response to Semaphorin 3A in dorsal root ganglion neurons
    • Shapovalova, Z., Tabunshchyk, K. & Greer, P. A. The Fer tyrosine kinase regulates an axon retraction response to Semaphorin 3A in dorsal root ganglion neurons. BMC Dev. Biol. 7, 133 (2007).
    • (2007) BMC Dev. Biol , vol.7 , pp. 133
    • Shapovalova, Z.1    Tabunshchyk, K.2    Greer, P.A.3
  • 142
    • 18644374595 scopus 로고    scopus 로고
    • Fyn and Cdk5 mediate semaphorin-3A signaling, which is involved in regulation of dendrite orientation in cerebral cortex
    • Sasaki, Y. et al. Fyn and Cdk5 mediate semaphorin-3A signaling, which is involved in regulation of dendrite orientation in cerebral cortex. Neuron 35, 907-920 (2002).
    • (2002) Neuron , vol.35 , pp. 907-920
    • Sasaki, Y.1
  • 143
    • 20044370438 scopus 로고    scopus 로고
    • Semaphorin3A signalling is mediated via sequential Cdk5 and GSK3β phosphorylation of CRMP2: Implication of common phosphorylating mechanism underlying axon guidance and Alzheimer's disease
    • Uchida, Y. et al. Semaphorin3A signalling is mediated via sequential Cdk5 and GSK3β phosphorylation of CRMP2: implication of common phosphorylating mechanism underlying axon guidance and Alzheimer's disease. Genes Cells 10, 165-179 (2005).
    • (2005) Genes Cells , vol.10 , pp. 165-179
    • Uchida, Y.1
  • 144
    • 27644447928 scopus 로고    scopus 로고
    • Phosphorylation by Rho kinase regulates CRMP-2 activity in growth cones
    • Arimura, N. et al. Phosphorylation by Rho kinase regulates CRMP-2 activity in growth cones. Mol. Cell Biol. 25, 9973-9984 (2005).
    • (2005) Mol. Cell Biol , vol.25 , pp. 9973-9984
    • Arimura, N.1
  • 145
    • 0035900688 scopus 로고    scopus 로고
    • Collapsin response mediator protein switches RhoA and Rac1 morphology in N1E-115 neuroblastoma cells and is regulated by Rho kinase
    • Hall, C. et al. Collapsin response mediator protein switches RhoA and Rac1 morphology in N1E-115 neuroblastoma cells and is regulated by Rho kinase. J. Biol. Chem. 276, 43482-43486 (2001).
    • (2001) J. Biol. Chem , vol.276 , pp. 43482-43486
    • Hall, C.1
  • 146
    • 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 109, 887-900 (2002).
    • (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
  • 147
    • 30044443383 scopus 로고    scopus 로고
    • MICAL flavoprotein monooxygenases: Expression during neural development and following spinal cord injuries in the rat
    • Pasterkamp, R. J. et al. MICAL flavoprotein monooxygenases: Expression during neural development and following spinal cord injuries in the rat. Mol. Cell Neurosci. 31, 52-69 (2006).
    • (2006) Mol. Cell Neurosci , vol.31 , pp. 52-69
    • Pasterkamp, R.J.1
  • 148
    • 39849089206 scopus 로고    scopus 로고
    • Release of MICAL autoinhibition by semaphorin-plexin signaling promotes interaction with collapsin response mediator protein
    • Schmidt, E. F., Shim, S. O. & Strittmatter, S. M. Release of MICAL autoinhibition by semaphorin-plexin signaling promotes interaction with collapsin response mediator protein. J. Neurosci. 28, 2287-2297 (2008).
    • (2008) J. Neurosci , vol.28 , pp. 2287-2297
    • Schmidt, E.F.1    Shim, S.O.2    Strittmatter, S.M.3
  • 149
    • 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. 26, 4961-4969 (2006).
    • (2006) J. Neurosci , vol.26 , pp. 4961-4969
    • Togashi, H.1    Schmidt, E.F.2    Strittmatter, S.M.3
  • 150
    • 0027192866 scopus 로고
    • The organization of F-actin and microtubules in growth cones exposed to a brain-derived collapsing factor
    • Fan, J., Mansfield, S. G., Redmond, T., Gordon-Weeks, P. R. & Raper, J. A. The organization of F-actin and microtubules in growth cones exposed to a brain-derived collapsing factor. J. Cell Biol. 121, 867-878 (1993).
    • (1993) J. Cell Biol , vol.121 , pp. 867-878
    • Fan, J.1    Mansfield, S.G.2    Redmond, T.3    Gordon-Weeks, P.R.4    Raper, J.A.5
  • 151
    • 0032817550 scopus 로고    scopus 로고
    • Shirvan, A. et al. Semaphorins as mediators of neuronal apoptosis. J. Neurochem. 73, 961-971 (1999). The first description of a semaphorin as an inducer of apoptosis.
    • Shirvan, A. et al. Semaphorins as mediators of neuronal apoptosis. J. Neurochem. 73, 961-971 (1999). The first description of a semaphorin as an inducer of apoptosis.
  • 152
    • 0035873074 scopus 로고    scopus 로고
    • Semaphorin 3A-vascular endothelial growth factor-165 balance mediates migration and apoptosis of neural progenitor cells by the recruitment of shared receptor
    • Bagnard, D. et al. Semaphorin 3A-vascular endothelial growth factor-165 balance mediates migration and apoptosis of neural progenitor cells by the recruitment of shared receptor. J. Neurosci. 21, 3332-3341 (2001).
    • (2001) J. Neurosci , vol.21 , pp. 3332-3341
    • Bagnard, D.1
  • 153
    • 36849022482 scopus 로고    scopus 로고
    • Plexin-B1 utilizes RhoA and Rho kinase to promote the integrin-dependent activation of Akt and ERK and endothelial cell motility
    • Basile, J. R., Gavard, J. & Gutkind, J. S. Plexin-B1 utilizes RhoA and Rho kinase to promote the integrin-dependent activation of Akt and ERK and endothelial cell motility. J. Biol. Chem. 282, 34888-34895 (2007).
    • (2007) J. Biol. Chem , vol.282 , pp. 34888-34895
    • Basile, J.R.1    Gavard, J.2    Gutkind, J.S.3
  • 154
    • 27844453850 scopus 로고    scopus 로고
    • p190 Rho-GTPase activating protein associates with plexins and it is required for semaphorin signalling
    • Barberis, D. et al. p190 Rho-GTPase activating protein associates with plexins and it is required for semaphorin signalling. J Cell Sci. 118, 4689-4700 (2005).
    • (2005) J Cell Sci , vol.118 , pp. 4689-4700
    • Barberis, D.1
  • 155
    • 33745603987 scopus 로고    scopus 로고
    • Sema4D/plexin-B1 activates GSK-3β through R-Ras GAP activity, inducing growth cone collapse
    • 704-709
    • Ito, Y., Oinuma, I., Katoh, H., Kaibuchi, K. & Negishi, M. Sema4D/plexin-B1 activates GSK-3β through R-Ras GAP activity, inducing growth cone collapse. EMBO Rep. 7, 704-709 (2006).
    • (2006) EMBO Rep , vol.7
    • Ito, Y.1    Oinuma, I.2    Katoh, H.3    Kaibuchi, K.4    Negishi, M.5
  • 156
    • 0036048640 scopus 로고    scopus 로고
    • CRMP-2 binds to tubulin heterodimers to promote microtubule assembly
    • Fukata, Y. et al. CRMP-2 binds to tubulin heterodimers to promote microtubule assembly. Nature Cell Biol. 4, 583-591 (2002).
    • (2002) Nature Cell Biol , vol.4 , pp. 583-591
    • Fukata, Y.1
  • 158
    • 33947417050 scopus 로고    scopus 로고
    • Immune semaphorins: Increasing members and their diverse roles
    • Kikutani, H., Suzuki, K. & Kumanogoh, A. Immune semaphorins: increasing members and their diverse roles. Adv. Immunol. 93, 121-143 (2007).
    • (2007) Adv. Immunol , vol.93 , pp. 121-143
    • Kikutani, H.1    Suzuki, K.2    Kumanogoh, A.3
  • 159
    • 33645751561 scopus 로고    scopus 로고
    • Semaphorin-3A is expressed by tumor cells and alters T-cell signal transduction and function
    • Catalano, A. et al. Semaphorin-3A is expressed by tumor cells and alters T-cell signal transduction and function. Blood 107, 3321-3329 (2006).
    • (2006) Blood , vol.107 , pp. 3321-3329
    • Catalano, A.1
  • 161
    • 0037057655 scopus 로고    scopus 로고
    • Class IV semaphorin Sema4A enhances T-cell activation and interacts with Tim-2
    • Kumanogoh, A. et al. Class IV semaphorin Sema4A enhances T-cell activation and interacts with Tim-2. Nature 419, 629-633 (2002).
    • (2002) Nature , vol.419 , pp. 629-633
    • Kumanogoh, A.1
  • 162
    • 0033636321 scopus 로고    scopus 로고
    • Identification of CD72 as a lymphocyte receptor for the class IV semaphorin CD100: A novel mechanism for regulating B cell signaling
    • Kumanogoh, A. et al. Identification of CD72 as a lymphocyte receptor for the class IV semaphorin CD100: a novel mechanism for regulating B cell signaling. Immunity 13, 621-631 (2000).
    • (2000) Immunity , vol.13 , pp. 621-631
    • Kumanogoh, A.1
  • 163
    • 10444257969 scopus 로고    scopus 로고
    • Semaphorin 5A is a bifunctional axon guidance cue regulated by heparan and chondroitin sulfate proteoglycans
    • Kantor, D. B. et al. Semaphorin 5A is a bifunctional axon guidance cue regulated by heparan and chondroitin sulfate proteoglycans. Neuron 44, 961-975 (2004).
    • (2004) Neuron , vol.44 , pp. 961-975
    • Kantor, D.B.1
  • 164
    • 22544470038 scopus 로고    scopus 로고
    • A role for axon guidance receptors and ligands in blood vessel development and tumor angiogenesis
    • Klagsbrun, M. & Eichmann, A. A role for axon guidance receptors and ligands in blood vessel development and tumor angiogenesis. Cytokine Growth Factor Rev. 16, 535-548 (2005).
    • (2005) Cytokine Growth Factor Rev , vol.16 , pp. 535-548
    • Klagsbrun, M.1    Eichmann, A.2
  • 165
    • 34250223116 scopus 로고    scopus 로고
    • Regulation of angiogenesis by Eph-ephrin interactions
    • Kuijper, S., Turner, C. J. & Adams, R. H. Regulation of angiogenesis by Eph-ephrin interactions. Trends Cardiovasc. Med. 17, 145-151 (2007).
    • (2007) Trends Cardiovasc. Med , vol.17 , pp. 145-151
    • Kuijper, S.1    Turner, C.J.2    Adams, R.H.3
  • 166
    • 34147094761 scopus 로고    scopus 로고
    • Neogenin: One receptor, many functions
    • Wilson, N. H. & Key, B. Neogenin: one receptor, many functions. Int. J. Biochem. Cell Biol. 39, 874-878 (2007).
    • (2007) Int. J. Biochem. Cell Biol , vol.39 , pp. 874-878
    • Wilson, N.H.1    Key, B.2
  • 167
    • 12344332651 scopus 로고    scopus 로고
    • Role of neural guidance signals in blood vessel navigation
    • Autiero, M., De Smet, F., Claes, F. & Carmeliet, P. Role of neural guidance signals in blood vessel navigation. Cardiovasc. Res. 65, 629-638 (2005).
    • (2005) Cardiovasc. Res , vol.65 , pp. 629-638
    • Autiero, M.1    De Smet, F.2    Claes, F.3    Carmeliet, P.4
  • 168
    • 23044459218 scopus 로고    scopus 로고
    • Role of netrin-1 and netrin-1 dependence receptors in colorectal cancers
    • Mehlen, P. & Llambi, F. Role of netrin-1 and netrin-1 dependence receptors in colorectal cancers. Br. J. Cancer. 93, 1-6 (2005).
    • (2005) Br. J. Cancer , vol.93 , pp. 1-6
    • Mehlen, P.1    Llambi, F.2
  • 169
    • 33746438460 scopus 로고    scopus 로고
    • Potential role of the Slit/Robo signal pathway in angiogenesis
    • Fujiwara, M., Ghazizadeh, M. & Kawanami, O. Potential role of the Slit/Robo signal pathway in angiogenesis. Vasc. Med. 11, 115-121 (2006).
    • (2006) Vasc. Med , vol.11 , pp. 115-121
    • Fujiwara, M.1    Ghazizadeh, M.2    Kawanami, O.3
  • 170
    • 47949102960 scopus 로고    scopus 로고
    • Neuropilin-1 is a receptor for transforming growth factorβ-1, activates its latent form, and promotes regulatory T cell activity
    • in the press
    • Glinka, Y. & Prud'homme, G. J. Neuropilin-1 is a receptor for transforming growth factorβ-1, activates its latent form, and promotes regulatory T cell activity. J. Leukoc. Biol. (in the press).
    • J. Leukoc. Biol
    • Glinka, Y.1    Prud'homme, G.J.2


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