메뉴 건너뛰기




Volumn 3, Issue 9, 2012, Pages 921-939

Neuropilins are multifunctional coreceptors involved in tumor initiation, growth, metastasis and immunity

Author keywords

Anegiogenesis; Cancer stem cell; Growth factor; Neuropilin; Semaphorin; TGF beta; VEGF

Indexed keywords

ANTINEOPLASTIC AGENT; BEVACIZUMAB; CELL PENETRATING PEPTIDE; FIBROBLAST GROWTH FACTOR; INTEGRIN; MNRP 1685A; NEUROPILIN; NEUROPILIN 1; NEUROPILIN 2; NEUROPILIN 2B ANTIBODY; PACLITAXEL; PLATELET DERIVED GROWTH FACTOR; PLATELET DERIVED GROWTH FACTOR RECEPTOR; SCATTER FACTOR; SCATTER FACTOR RECEPTOR; SEMAPHORIN 3A; SONIC HEDGEHOG PROTEIN; TRANSFORMING GROWTH FACTOR BETA; TRANSFORMING GROWTH FACTOR BETA RECEPTOR 1; UNCLASSIFIED DRUG; VASCULOTROPIN; VASCULOTROPIN INHIBITOR;

EID: 84868616455     PISSN: None     EISSN: 19492553     Source Type: Journal    
DOI: 10.18632/oncotarget.626     Document Type: Review
Times cited : (240)

References (174)
  • 1
    • 42449148407 scopus 로고    scopus 로고
    • Neuropilins, structure, function and role in disease
    • Pellet-Many C, Frankel P, Jia H, Zachary I. Neuropilins: structure, function and role in disease. Biochem J. 2008; 411: 211-226.
    • (2008) Biochem J , vol.411 , pp. 211-226
    • Pellet-Many, C.1    Frankel, P.2    Jia, H.3    Zachary, I.4
  • 2
    • 42649132183 scopus 로고    scopus 로고
    • Neuropilins, a versatile partner of extracellular molecules that regulate development and disease
    • Uniewicz KA, Fernig DG. Neuropilins: a versatile partner of extracellular molecules that regulate development and disease. Front Biosci 2008; 13: 4339-4360.
    • (2008) Front Biosci , vol.13 , pp. 4339-4360
    • Uniewicz, K.A.1    Fernig, D.G.2
  • 6
    • 33745063095 scopus 로고    scopus 로고
    • The role of neuropilins in cancer
    • Ellis LM. The role of neuropilins in cancer. Mol Cancer Ther. 2006; 5: 1099-107.
    • (2006) Mol Cancer Ther , vol.5 , pp. 1099-1107
    • Ellis, L.M.1
  • 9
    • 34347332447 scopus 로고    scopus 로고
    • Neuropilins in physiological and pathological angiogenesis
    • Staton CA, Kumar I, Reed MW, Brown NJ. Neuropilins in physiological and pathological angiogenesis. J Pathol. 2007;,212: 237-248.
    • J Pathol , vol.2007 , Issue.212 , pp. 237-248
    • Staton, C.A.1    Kumar, I.2    Reed, M.W.3    Brown, N.J.4
  • 12
    • 84856259334 scopus 로고    scopus 로고
    • Neuropilin signalling in angiogenesis
    • Koch S. Neuropilin signalling in angiogenesis. Biochem Soc Trans. 2012; 40: 20-25.
    • (2012) Biochem Soc Trans , vol.40 , pp. 20-25
    • Koch, S.1
  • 13
    • 81855169496 scopus 로고    scopus 로고
    • How neuropilin-1 regulates receptor tyrosine kinase signalling, the knowns and known unknowns
    • Zachary IC. How neuropilin-1 regulates receptor tyrosine kinase signalling: the knowns and known unknowns. Biochem Soc Trans. 2011; 39: 1583-1591.
    • (2011) Biochem Soc Trans , vol.39 , pp. 1583-1591
    • Zachary, I.C.1
  • 17
    • 79961042374 scopus 로고    scopus 로고
    • VEGF binding to NRP1 is essential for VEGF stimulation of endothelial cell migration, complex formation between NRP1 and VEGFR2, and signaling via FAK Tyr407 phosphorylation
    • Herzog B, Pellet-Many C, Britton G, Hartzoulakis B, Zachary IC. VEGF binding to NRP1 is essential for VEGF stimulation of endothelial cell migration, complex formation between NRP1 and VEGFR2, and signaling via FAK Tyr407 phosphorylation. Mol Biol Cell. 2011; 22: 2766-2776.
    • (2011) Mol Biol Cell , vol.22 , pp. 2766-2776
    • Herzog, B.1    Pellet-Many, C.2    Britton, G.3    Hartzoulakis, B.4    Zachary, I.C.5
  • 19
    • 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. 1997; 90: 739- 751.
    • (1997) Cell , vol.90 , pp. 739-751
    • He, Z.1    Tessier-Lavigne, M.2
  • 20
    • 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 CS, 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. 1997; 19: 547-559.
    • (1997) Neuron , vol.19 , pp. 547-559
    • Chen, H.1    Chedotal, A.2    He, Z.3    Goodman, C.S.4    Tessier-Lavigne, M.5
  • 21
    • 0032215144 scopus 로고    scopus 로고
    • Neuropilin-2 is a receptor for semaphorin IV: Insight into the structural basis of receptor function and specificity
    • Giger RJ, Urquhart ER, Gillespie SK, Levengood DV, Ginty DD, Kolodkin AL. Neuropilin-2 is a receptor for semaphorin IV: Insight into the structural basis of receptor function and specificity. Neuron. 1998; 21: 1079-1092.
    • (1998) Neuron , vol.21 , pp. 1079-1092
    • Giger, R.J.1    Urquhart, E.R.2    Gillespie, S.K.3    Levengood, D.V.4    Ginty, D.D.5    Kolodkin, A.L.6
  • 23
    • 0030778454 scopus 로고    scopus 로고
    • Neuropilin-semaphorin III/D-mediated chemorepulsive signals play a crucial role in peripheral nerve projection in mice
    • Kitsukawa T, Shimizu M, Sanbo M, Hirata T, Taniguchi M, Bekku Y, Yagi T, Fujisawa H. Neuropilin-semaphorin III/D-mediated chemorepulsive signals play a crucial role in peripheral nerve projection in mice. Neuron. 1997; 19: 995-1005.
    • (1997) Neuron , vol.19 , pp. 995-1005
    • Kitsukawa, T.1    Shimizu, M.2    Sanbo, M.3    Hirata, T.4    Taniguchi, M.5    Bekku, Y.6    Yagi, T.7    Fujisawa, H.8
  • 24
    • 0034023548 scopus 로고    scopus 로고
    • Neuropilin-2 regulates the development of selective cranial and sensory nerves and hippocampal mossy fiber projections
    • Chen H, Bagri A, Zupicich JA. Neuropilin-2 regulates the development of selective cranial and sensory nerves and hippocampal mossy fiber projections. Neuron. 2000; 25: 43-56.
    • (2000) Neuron , vol.25 , pp. 43-56
    • Chen, H.1    Bagri, A.2    Zupicich, J.A.3
  • 25
    • 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
  • 27
    • 0032549799 scopus 로고    scopus 로고
    • Neuropilin-1 is expressed by endothelial and tumor cells as an isoform-specific receptor for vascular endothelial growth factor
    • Soker S, Takashima S, Miao HQ, Neufeld G, Klagsbrun M. Neuropilin-1 is expressed by endothelial and tumor cells as an isoform-specific receptor for vascular endothelial growth factor. Cell. 1998; 92: 735-745.
    • (1998) Cell , vol.92 , pp. 735-745
    • Soker, S.1    Takashima, S.2    Miao, H.Q.3    Neufeld, G.4    Klagsbrun, M.5
  • 28
    • 0034282885 scopus 로고    scopus 로고
    • The interaction of neuropilin-1 with vascular endothelial growth factor and its receptor flt-1
    • Fuh G, Garcia KC, de Vos AM. The interaction of neuropilin-1 with vascular endothelial growth factor and its receptor flt-1. J. Biol. Chem. 2000; 275: 26690-26695.
    • (2000) J. Biol. Chem. , vol.275 , pp. 26690-26695
    • Fuh, G.1    Garcia, K.C.2    de Vos, A.M.3
  • 31
    • 0034674108 scopus 로고    scopus 로고
    • Neuropilin-2 and neuropilin-1 are receptors for the 165-amino acid 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 the 165-amino acid 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. 2000; 275: 18040-18045.
    • (2000) J Biol Chem , vol.275 , pp. 18040-18045
    • Gluzman-Poltorak, Z.1    Cohen, T.2    Herzog, Y.3    Neufeld, G.4
  • 33
    • 46949088806 scopus 로고    scopus 로고
    • Neuropilin-1 is a receptor for transforming growth factor beta-1, activates its latent form, and promotes regulatory T cell activity
    • GlinkaY, Prud'homme GJ. Neuropilin-1 is a receptor for transforming growth factor beta-1, activates its latent form, and promotes regulatory T cell activity. J Leukoc Biol. 2008; 84: 302-310.
    • (2008) J Leukoc Biol , vol.84 , pp. 302-310
    • Glinka, Y.1    Prud'homme, G.J.2
  • 34
    • 79953702245 scopus 로고    scopus 로고
    • Neuropilin-1 exerts co-receptor function for TGF-beta-1 on the membrane of cancer cells and enhances responses to both latent and active TGF-beta
    • Glinka Y, Stoilova S, Mohammed N, Prud'homme GJ. Neuropilin-1 exerts co-receptor function for TGF-beta-1 on the membrane of cancer cells and enhances responses to both latent and active TGF-beta. Carcinogenesis. 2011; 32: 613-621.
    • (2011) Carcinogenesis , vol.32 , pp. 613-621
    • Glinka, Y.1    Stoilova, S.2    Mohammed, N.3    Prud'homme, G.J.4
  • 38
    • 35948964766 scopus 로고    scopus 로고
    • Hepatocyte growth factor-mediated cell invasion in pancreatic cancer cells is dependent on neuropilin-1
    • Matsushita A, Götze T, Korc M. Hepatocyte growth factor-mediated cell invasion in pancreatic cancer cells is dependent on neuropilin-1. Cancer Res. 2007; 67: 10309- 10316.
    • (2007) Cancer Res , vol.67 , pp. 10309-10316
    • Matsushita, A.1    Götze, T.2    Korc, M.3
  • 39
    • 41049086388 scopus 로고    scopus 로고
    • Neuropilin-1 and neuropilin-2 act as coreceptors, potentiating proangiogenic activity
    • Sulpice E, Plouët J, Bergé M, Allanic D, Tobelem G, Merkulova-Rainon T. Neuropilin-1 and neuropilin-2 act as coreceptors, potentiating proangiogenic activity. Blood. 2008; 111: 2036-2045.
    • (2008) Blood , vol.111 , pp. 2036-2045
    • Sulpice, E.1    Plouët, J.2    Bergé, M.3    Allanic, D.4    Tobelem, G.5    Merkulova-Rainon, T.6
  • 40
    • 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, Sengupta K, Dhar K, Mehta S, D'Amore PA, Dhar G, Banerjee SK. Breast cancer cells secreted platelet-derived growth factor-induced motility of vascular smooth muscle cells is mediated through neuropilin-1. Mol Carcinog. 2006; 45: 871-880.
    • (2006) Mol Carcinog , vol.45 , pp. 871-880
    • Banerjee, S.1    Sengupta, K.2    Dhar, K.3    Mehta, S.4    D'Amore, P.A.5    Dhar, G.6    Banerjee, S.K.7
  • 42
    • 77950911871 scopus 로고    scopus 로고
    • Neuropilin-1 regulates platelet-derived growth factor receptor signalling in mesenchymal stem cells
    • Ball SG, Bayley C, Shuttleworth CA, Kielty CM. Neuropilin-1 regulates platelet-derived growth factor receptor signalling in mesenchymal stem cells. Biochem J. 2010; 427: 29-40.
    • (2010) Biochem J , vol.427 , pp. 29-40
    • Ball, S.G.1    Bayley, C.2    Shuttleworth, C.A.3    Kielty, C.M.4
  • 43
    • 77955225060 scopus 로고    scopus 로고
    • Tumor cell-derived PDGF-B potentiates mouse mesenchymal stem cells-pericytes transition and recruitment through an interaction with NRP-1
    • Dhar K, Dhar G, Majumder M, Haque I, Mehta S, Van Veldhuizen PJ, Banerjee SK, Banerjee S. Tumor cell-derived PDGF-B potentiates mouse mesenchymal stem cells-pericytes transition and recruitment through an interaction with NRP-1. Mol Cancer. 2010; 9: 209.
    • (2010) Mol Cancer , vol.9 , pp. 209
    • Dhar, K.1    Dhar, G.2    Majumder, M.3    Haque, I.4    Mehta, S.5    Van Veldhuizen, P.J.6    Banerjee, S.K.7    Banerjee, S.8
  • 44
    • 79954559053 scopus 로고    scopus 로고
    • Neuropilin-1 mediates PDGF stimulation of Vascular Smooth Muscle Cell migration and signalling via p130Cas
    • Pellet-Many C, Frankel P, Evans IM, Herzog B, Jünemann-Ramírez M, Zachary I. Neuropilin-1 mediates PDGF stimulation of Vascular Smooth Muscle Cell migration and signalling via p130Cas. Biochem J. 2011; 435: 609-618.
    • (2011) Biochem J , vol.435 , pp. 609-618
    • Pellet-Many, C.1    Frankel, P.2    Evans, I.M.3    Herzog, B.4    Jünemann-Ramírez, M.5    Zachary, I.6
  • 45
    • 79952255709 scopus 로고    scopus 로고
    • Neuropilin-1 Signaling through p130Cas Tyrosine Phosphorylation Is Essential for Growth Factor-Dependent Migration of Glioma and Endothelial Cells
    • Evans IM, Yamaji M, Britton G, Pellet-Many C, Lockie C, Zachary IC, Frankel P. Neuropilin-1 Signaling through p130Cas Tyrosine Phosphorylation Is Essential for Growth Factor-Dependent Migration of Glioma and Endothelial Cells. Mol Cell Biol. 2011; 31: 1174-1185.
    • (2011) Mol Cell Biol , vol.31 , pp. 1174-1185
    • Evans, I.M.1    Yamaji, M.2    Britton, G.3    Pellet-Many, C.4    Lockie, C.5    Zachary, I.C.6    Frankel, P.7
  • 47
    • 35948965519 scopus 로고    scopus 로고
    • Neuropilin-1 interacts with integrin beta1 and modulates pancreatic cancer cell growth, survival and invasion
    • Fukasawa M, Matsushita A, Korc M. Neuropilin-1 interacts with integrin beta1 and modulates pancreatic cancer cell growth, survival and invasion. Cancer Biol Ther. 2007; 6: 1173-1180.
    • (2007) Cancer Biol Ther , vol.6 , pp. 1173-1180
    • Fukasawa, M.1    Matsushita, A.2    Korc, M.3
  • 49
    • 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
    • Hsieh SH, Ying NW, Wu MH, Chiang WF, Hsu CL, Wong TY, Jin YT, Hong TM, Chen YL. Galectin-1, a novel ligand of neuropilin-1, activates VEGFR-2 signaling and modulates the migration of vascular endothelial cells. Oncogene. 2008; 27: 3746-3753
    • (2008) Oncogene , vol.27 , pp. 3746-3753
    • Hsieh, S.H.1    Ying, N.W.2    Wu, M.H.3    Chiang, W.F.4    Hsu, C.L.5    Wong, T.Y.6    Jin, Y.T.7    Hong, T.M.8    Chen, Y.L.9
  • 50
    • 0033678716 scopus 로고    scopus 로고
    • Analysis of the L1-deficient mouse phenotype reveals cross-talk between Sema3A and L1 signaling pathways in axonal guidance
    • Castellani V, Chédotal 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. 2000; 27: 237-249.
    • (2000) Neuron , vol.27 , pp. 237-249
    • Castellani, V.1    Chédotal, A.2    Schachner, M.3    Faivre-Sarrailh, C.4    Rougon, G.5
  • 51
    • 2342504645 scopus 로고    scopus 로고
    • Semaphorin3A-induced receptor endocytosis during axon guidance responses is mediated by L1 CAM
    • Castellani V, Falk J, Rougon G. Semaphorin3A-induced receptor endocytosis during axon guidance responses is mediated by L1 CAM. Mol Cell Neurosci. 2004; 26: 89- 100.
    • (2004) Mol Cell Neurosci , vol.26 , pp. 89-100
    • Castellani, V.1    Falk, J.2    Rougon, G.3
  • 53
    • 70349482671 scopus 로고    scopus 로고
    • C-end rule peptides mediate neuropilin-1-dependent cell, vascular, and tissue penetration
    • Teesalu T, Sugahara KN, Kotamraju VR, Ruoslahti E. C-end rule peptides mediate neuropilin-1-dependent cell, vascular, and tissue penetration. Proc Natl Acad Sci USA. 2009; 106: 16157-16162.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 16157-16162
    • Teesalu, T.1    Sugahara, K.N.2    Kotamraju, V.R.3    Ruoslahti, E.4
  • 56
    • 79952407244 scopus 로고    scopus 로고
    • Binding of a C-end rule peptide to the neuropilin-1 receptor, a molecular modeling approach
    • Haspel N, Zanuy D, Nussinov R, Teesalu T, Ruoslahti E, Aleman C. Binding of a C-end rule peptide to the neuropilin-1 receptor: a molecular modeling approach. Biochemistry. 2011; 50: 1755-1762
    • (2011) Biochemistry , vol.50 , pp. 1755-1762
    • Haspel, N.1    Zanuy, D.2    Nussinov, R.3    Teesalu, T.4    Ruoslahti, E.5    Aleman, C.6
  • 59
  • 60
    • 33751091501 scopus 로고    scopus 로고
    • Antiangiogenic and antitumor activities of peptide inhibiting the vascular endothelial growth factor binding to neuropilin-1
    • Starzec A, Vassy R, Martin A, Lecouvey M, Di Benedetto M, Crépin M, Perret GY. Antiangiogenic and antitumor activities of peptide inhibiting the vascular endothelial growth factor binding to neuropilin-1. Life Sci. 2006; 79: 2370-2381.
    • (2006) Life Sci , vol.79 , pp. 2370-2381
    • Starzec, A.1    Vassy, R.2    Martin, A.3    Lecouvey, M.4    Di Benedetto, M.5    Crépin, M.6    Perret, G.Y.7
  • 61
    • 76349096681 scopus 로고    scopus 로고
    • Neuropilin-1 antagonism in human carcinoma cells inhibits migration and enhances chemosensitivity
    • Jia H, Cheng L, Tickner M, Bagherzadeh A, Selwood D, Zachary I. Neuropilin-1 antagonism in human carcinoma cells inhibits migration and enhances chemosensitivity. Br J Cancer. 2010; 102: 541-552.
    • (2010) Br J Cancer , vol.102 , pp. 541-552
    • Jia, H.1    Cheng, L.2    Tickner, M.3    Bagherzadeh, A.4    Selwood, D.5    Zachary, I.6
  • 63
    • 36348954513 scopus 로고    scopus 로고
    • Modulation of semaphorin3A activity by p75 neurotrophin receptor influences peripheral axon patterning
    • Ben-Zvi, A, Ben-Gigi L, Klein H, Behar O. Modulation of semaphorin3A activity by p75 neurotrophin receptor influences peripheral axon patterning. J Neurosci. 2007; 27: 13000-13011.
    • (2007) J Neurosci , vol.27 , pp. 13000-13011
    • Ben-Zvi, A.1    Ben-Gigi, L.2    Klein, H.3    Behar, O.4
  • 64
    • 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, Shraga-Heled N, Varshavsky A, Guimaraes-Sternberg C, Kessler O, Neufeld G. Semaphorin-3A and semaphorin-3F work together to repel endothelial cells and to inhibit their survival by induction of apoptosis. J Biol Chem. 2007; 282: 26294-26305.
    • (2007) J Biol Chem , vol.282 , pp. 26294-26305
    • Guttmann-Raviv, N.1    Shraga-Heled, N.2    Varshavsky, A.3    Guimaraes-Sternberg, C.4    Kessler, O.5    Neufeld, G.6
  • 65
    • 0034688995 scopus 로고    scopus 로고
    • Determination of cell adhesion sites of neuropilin-1
    • Shimizu M, Murakami Y, Suto F, Fujisawa H. Determination of cell adhesion sites of neuropilin-1. J Cell Biol. 2000; 148:1283-1293.
    • (2000) J Cell Biol , vol.148 , pp. 1283-1293
    • Shimizu, M.1    Murakami, Y.2    Suto, F.3    Fujisawa, H.4
  • 66
    • 55349113212 scopus 로고    scopus 로고
    • Neuropilin-1 upholds dedifferentiation and propagation phenotypes of renal cell carcinoma cells by activating Akt and sonic hedgehog axes
    • Cao Y, Wang L, Nandy D, Zhang Y, Basu A, Radisky D, Mukhopadhyay D. Neuropilin-1 upholds dedifferentiation and propagation phenotypes of renal cell carcinoma cells by activating Akt and sonic hedgehog axes. Cancer Res. 2008; 68: 8667-8672.
    • (2008) Cancer Res , vol.68 , pp. 8667-8672
    • Cao, Y.1    Wang, L.2    Nandy, D.3    Zhang, Y.4    Basu, A.5    Radisky, D.6    Mukhopadhyay, D.7
  • 70
    • 84862565810 scopus 로고    scopus 로고
    • Cancer Stem Cells and Novel Targets for Antitumor Strategies
    • Prud'homme GJ. Cancer Stem Cells and Novel Targets for Antitumor Strategies. Curr Pharm Des. 2012; 18: 2838- 2849.
    • (2012) Curr Pharm Des , vol.18 , pp. 2838-2849
    • Prud'homme, G.J.1
  • 74
    • 84868191136 scopus 로고    scopus 로고
    • Semaphorins and neuropilins, new players in the neuroendocrine control of the intrathymic T-cell migration in humans
    • [Epub ahead of print
    • Mendes-da-Cruz DA, Linhares-Lacerda L, Smaniotto S, Dardenne M, Savino W. Semaphorins and neuropilins: new players in the neuroendocrine control of the intrathymic T-cell migration in humans. Exp Physiol. 2012 Feb 10. [Epub ahead of print..
    • (2012) Exp Physiol
    • Mendes-da-Cruz, D.A.1    Linhares-Lacerda, L.2    Smaniotto, S.3    Dardenne, M.4    Savino, W.5
  • 76
    • 34447132255 scopus 로고    scopus 로고
    • Anti-BDCA-4 (neuropilin-1) antibody can suppress virus-induced IFN-alpha production of plasmacytoid dendritic cells
    • Grage-Griebenow E, Löseke S, Kauth M, Gehlhar K, Zawatzky R, Bufe A. Anti-BDCA-4 (neuropilin-1) antibody can suppress virus-induced IFN-alpha production of plasmacytoid dendritic cells. Immunol Cell Biol. 2007; 85: 383-390.
    • (2007) Immunol Cell Biol , vol.85 , pp. 383-390
    • Grage-Griebenow, E.1    Löseke, S.2    Kauth, M.3    Gehlhar, K.4    Zawatzky, R.5    Bufe, A.6
  • 77
    • 37149048411 scopus 로고    scopus 로고
    • Fattorossi A Neuropilin-1 expression identifies a subset of regulatory T cells in human lymph nodes that is modulated by preoperative chemoradiation therapy in cervical cancer
    • Battaglia A, Buzzonetti A, Monego G, Peri L, Ferrandina G, Fanfani F, Scambia G, Fattorossi A Neuropilin-1 expression identifies a subset of regulatory T cells in human lymph nodes that is modulated by preoperative chemoradiation therapy in cervical cancer. Immunology. 2008; 123: 129- 138
    • (2008) Immunology , vol.123 , pp. 129-138
    • Battaglia, A.1    Buzzonetti, A.2    Monego, G.3    Peri, L.4    Ferrandina, G.5    Fanfani, F.6    Scambia, G.7
  • 78
    • 40249108222 scopus 로고    scopus 로고
    • Neuropilin-1 expression on regulatory T cells enhances their interactions with dendritic cells during antigen recognition
    • Sarris M, Andersen KG, Randow F, Mayr L, Betz AG. Neuropilin-1 expression on regulatory T cells enhances their interactions with dendritic cells during antigen recognition. Immunity. 2008; 28: 402-413.
    • (2008) Immunity , vol.28 , pp. 402-413
    • Sarris, M.1    Andersen, K.G.2    Randow, F.3    Mayr, L.4    Betz, A.G.5
  • 80
    • 65049086413 scopus 로고    scopus 로고
    • Therapeutic potential of FOXP3(+) regulatory T cells and their interactions with dendritic cells
    • Tran DQ, Shevach EM. Therapeutic potential of FOXP3(+) regulatory T cells and their interactions with dendritic cells. Hum Immunol. 2009; 70: 294-299.
    • (2009) Hum Immunol , vol.70 , pp. 294-299
    • Tran, D.Q.1    Shevach, E.M.2
  • 82
    • 80052923989 scopus 로고    scopus 로고
    • IL-17-producing invariant NKT cells in lymphoid organs are recent thymic emigrants identified by neuropilin-1 expression
    • Milpied P, Massot B, Renand A, Diem S, Herbelin A, Leite-de-Moraes M, Rubio MT, Hermine O. IL-17-producing invariant NKT cells in lymphoid organs are recent thymic emigrants identified by neuropilin-1 expression. Blood. 2011; 118: 2993-3002.
    • (2011) Blood , vol.118 , pp. 2993-3002
    • Milpied, P.1    Massot, B.2    Renand, A.3    Diem, S.4    Herbelin, A.5    Leite-de-Moraes, M.6    Rubio, M.T.7    Hermine, O.8
  • 84
    • 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 RR. 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(15): 6519-27.
    • (1999) J Neurosci , vol.19 , Issue.15 , pp. 6519-6527
    • Cai, H.1    Reed, R.R.2
  • 85
    • 0036618202 scopus 로고    scopus 로고
    • GIPC gene family
    • Katoh M. GIPC gene family. Int J Mol Med. 2002; 9: 585- 589.
    • (2002) Int J Mol Med , vol.9 , pp. 585-589
    • Katoh, M.1
  • 86
    • 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
  • 87
    • 30944451158 scopus 로고    scopus 로고
    • RGS proteins have a signalling complex, interactions between RGS proteins and GPCRs, effectors, and auxiliary proteins
    • Abramow-Newerly M, Roy AA, Nunn C, Chidiac P. RGS proteins have a signalling complex: interactions between RGS proteins and GPCRs, effectors, and auxiliary proteins. Cell Signal. 2006; 18: 579-591.
    • (2006) Cell Signal , vol.18 , pp. 579-591
    • Abramow-Newerly, M.1    Roy, A.A.2    Nunn, C.3    Chidiac, P.4
  • 91
    • 0037598870 scopus 로고    scopus 로고
    • Distinct endocytic pathways regulate TGF-beta receptor signalling and turnover
    • Di Guglielmo GM, Le Roy C, Goodfellow AF, Wrana JL. Distinct endocytic pathways regulate TGF-beta receptor signalling and turnover. Nat Cell Biol. 2003; 5: 410-421.
    • (2003) Nat Cell Biol , vol.5 , pp. 410-421
    • Di Guglielmo, G.M.1    Le Roy, C.2    Goodfellow, A.F.3    Wrana, J.L.4
  • 92
    • 13444263549 scopus 로고    scopus 로고
    • Clathrin- and non-clathrin-mediated endocytic regulation of cell signalling
    • Le Roy C, Wrana JL. Clathrin- and non-clathrin-mediated endocytic regulation of cell signalling. Nat Rev Mol Cell Biol. 2005; 6: 112-126.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 112-126
    • Le Roy, C.1    Wrana, J.L.2
  • 94
    • 0041327729 scopus 로고    scopus 로고
    • Myosin VI, two distinct roles in endocytosis
    • Hasson T. Myosin VI: two distinct roles in endocytosis. J Cell Sci. 2003; 116(Pt 17): 3453-61.
    • (2003) J Cell Sci , vol.116 , Issue.PART 17 , pp. 3453-3461
    • Hasson, T.1
  • 95
    • 0030778454 scopus 로고    scopus 로고
    • Neuropilin-semaphorin III/D-mediated chemorepulsive signals play a crucial role in peripheral nerve projection in mice
    • Kitsukawa T, Shimizu M, Sanbo M, Hirata T, Taniguchi M, Bekku Y, Yagi T, Fujisawa H. Neuropilin-semaphorin III/D-mediated chemorepulsive signals play a crucial role in peripheral nerve projection in mice. Neuron. 1997; 19: 995-1005.
    • (1997) Neuron , vol.19 , pp. 995-1005
    • Kitsukawa, T.1    Shimizu, M.2    Sanbo, M.3    Hirata, T.4    Taniguchi, M.5    Bekku, Y.6    Yagi, T.7    Fujisawa, H.8
  • 97
    • 16844380415 scopus 로고    scopus 로고
    • Peripheral nerve-derived VEGF promotes arterial differentiation via neuropilin 1-mediated positive feedback
    • Mukouyama YS, Gerber HP, Ferrara N, Gu C, Anderson DJ. Peripheral nerve-derived VEGF promotes arterial differentiation via neuropilin 1-mediated positive feedback. Development. 2005; 32: 941-52.
    • (2005) Development , vol.32 , pp. 941-952
    • Mukouyama, Y.S.1    Gerber, H.P.2    Ferrara, N.3    Gu, C.4    Anderson, D.J.5
  • 99
    • 0029562097 scopus 로고
    • Overexpression of a membrane protein, neuropilin, in chimeric mice causes anomalies in the cardiovascular system, nervous system and limbs
    • Kitsukawa T, Shimono A, Kawakami A, Kondoh H, Fujisawa H. Overexpression of a membrane protein, neuropilin, in chimeric mice causes anomalies in the cardiovascular system, nervous system and limbs. Development. 1995; 121: 4309-4318.
    • (1995) Development , vol.121 , pp. 4309-4318
    • Kitsukawa, T.1    Shimono, A.2    Kawakami, A.3    Kondoh, H.4    Fujisawa, H.5
  • 102
    • 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 HQ, Soker S, Feiner L, Alonso JL, Raper JA, Klagsbrun MJ. Neuropilin-1 mediates collapsin-1/ semaphorin III inhibition of endothelial cell motility: functional competition of collapsin-1 and vascular endothelial growth factor-165. Cell Biol. 1999; 146: 233- 242.
    • (1999) 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.J.6
  • 103
    • 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, Limberg BJ, Whitaker GB, Perman B, Leahy DJ, Rosenbaum JS, Ginty DD, Kolodkin AL. Characterization of neuropilin-1 structural features that confer binding to semaphorin 3A and vascular endothelial growth factor 165. J Biol Chem. 2002; 277: 18069-18076.
    • (2002) J Biol Chem , vol.277 , pp. 18069-18076
    • Gu, C.1    Limberg, B.J.2    Whitaker, G.B.3    Perman, B.4    Leahy, D.J.5    Rosenbaum, J.S.6    Ginty, D.D.7    Kolodkin, A.L.8
  • 108
    • 84859488831 scopus 로고    scopus 로고
    • Structural basis for the selective vascular endothelial growth factor-A (VEGF-A) binding to neuropilin-1
    • Parker MW, Xu P, Li X, Vander Kooi CW. Structural basis for the selective vascular endothelial growth factor-A (VEGF-A) binding to neuropilin-1. J Biol Chem. 2012; 287: 11082-11089.
    • (2012) J Biol Chem , vol.287 , pp. 11082-11089
    • Parker, M.W.1    Xu, P.2    Li, X.3    Vander Kooi, C.W.4
  • 112
    • 77956925423 scopus 로고    scopus 로고
    • Neuropilins and semaphorins - from angiogenesis to autoimmunity
    • Vadasz Z, Attias D, Kessel A, Toubi E. Neuropilins and semaphorins - from angiogenesis to autoimmunity. Autoimmun Rev. 2010; 9(12): 825-829.
    • (2010) Autoimmun Rev , vol.9 , Issue.12 , pp. 825-829
    • Vadasz, Z.1    Attias, D.2    Kessel, A.3    Toubi, E.4
  • 113
    • 78650632039 scopus 로고    scopus 로고
    • The neuroimmune semaphorin-3A reduces inflammation and progression of experimental autoimmune arthritis
    • Catalano A. The neuroimmune semaphorin-3A reduces inflammation and progression of experimental autoimmune arthritis. J Immunol. 2010; 185: 6373-83.
    • (2010) J Immunol , vol.185 , pp. 6373-6383
    • Catalano, A.1
  • 115
    • 33645751561 scopus 로고    scopus 로고
    • Semaphorin-3A is expressed by tumor cells and alters T-cell signal transduction and function
    • Catalano A, Caprari P, Moretti S, Faronato M, Tamagnone L, Procopio A. Semaphorin-3A is expressed by tumor cells and alters T-cell signal transduction and function. Blood. 2006; 107: 3321-3329.
    • (2006) Blood , vol.107 , pp. 3321-3329
    • Catalano, A.1    Caprari, P.2    Moretti, S.3    Faronato, M.4    Tamagnone, L.5    Procopio, A.6
  • 116
    • 35348940144 scopus 로고    scopus 로고
    • Pathobiology of transforming growth factor beta in cancer, fibrosis and immunologic disease, and therapeutic considerations
    • Prud'homme GJ. (2007) Pathobiology of transforming growth factor beta in cancer, fibrosis and immunologic disease, and therapeutic considerations. Lab Invest. 87; 1077-1091.
    • (2007) Lab Invest , vol.87 , pp. 1077-1091
    • Prud'homme, G.J.1
  • 118
    • 69449085219 scopus 로고    scopus 로고
    • GARP (LRRC32) is essential for the surface expression of latent TGF-beta on platelets and activated FOXP3+ regulatory T cells
    • Tran DQ, Andersson J, Wang R, Ramsey H, Unutmaz D, Shevach EM. GARP (LRRC32) is essential for the surface expression of latent TGF-beta on platelets and activated FOXP3+ regulatory T cells. Proc Natl Acad Sci U S A, 2009; 106: 13445-13450.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 13445-13450
    • Tran, D.Q.1    Andersson, J.2    Wang, R.3    Ramsey, H.4    Unutmaz, D.5    Shevach, E.M.6
  • 119
  • 120
    • 73249123203 scopus 로고    scopus 로고
    • Membrane protein GARP is a receptor for latent TGF-beta on the surface of activated human Treg
    • Stockis J, Colau D, Coulie PG, Lucas S. Membrane protein GARP is a receptor for latent TGF-beta on the surface of activated human Treg. Eur J Immunol. 2009; 39: 3315- 3322.
    • (2009) Eur J Immunol , vol.39 , pp. 3315-3322
    • Stockis, J.1    Colau, D.2    Coulie, P.G.3    Lucas, S.4
  • 121
  • 123
    • 44449109208 scopus 로고    scopus 로고
    • Differential control of T regulatory cell proliferation and suppressive activity by mature plasmacytoid versus conventional spleen dendritic cells
    • Ouabed A, Hubert FX, Chabannes D, Gautreau L, Heslan M, Josien R. Differential control of T regulatory cell proliferation and suppressive activity by mature plasmacytoid versus conventional spleen dendritic cells. J Immunol. 2008; 180: 5862-5870.
    • (2008) J Immunol , vol.180 , pp. 5862-5870
    • Ouabed, A.1    Hubert, F.X.2    Chabannes, D.3    Gautreau, L.4    Heslan, M.5    Josien, R.6
  • 125
    • 79953903119 scopus 로고    scopus 로고
    • Polysialic acid is required for neuropilin-2a/b-mediated control of CCL21- driven chemotaxis of mature dendritic cells and for their migration in vivo
    • Rey-Gallardo A, Delgado-Martín C, Gerardy-Schahn R, Rodríguez-Fernández JL, Vega MA. Polysialic acid is required for neuropilin-2a/b-mediated control of CCL21- driven chemotaxis of mature dendritic cells and for their migration in vivo. Glycobiology. 2011; 21: 655-662.
    • (2011) Glycobiology , vol.21 , pp. 655-662
    • Rey-Gallardo, A.1    Delgado-Martín, C.2    Gerardy-Schahn, R.3    Rodríguez-Fernández, J.L.4    Vega, M.A.5
  • 126
    • 27644538315 scopus 로고    scopus 로고
    • Integrin-mediated activation of latent transforming growth factor beta
    • Sheppard D. Integrin-mediated activation of latent transforming growth factor beta. Cancer Metastasis Rev. 2005; 24: 395-402.
    • (2005) Cancer Metastasis Rev , vol.24 , pp. 395-402
    • Sheppard, D.1
  • 127
    • 4444338819 scopus 로고    scopus 로고
    • Molecular interactions that confer latency to transforming growth factor-beta
    • Young GD, Murphy-Ullrich JE. Molecular interactions that confer latency to transforming growth factor-beta. J Biol Chem. 2004; 279: 38032-38039
    • (2004) J Biol Chem , vol.279 , pp. 38032-38039
    • Young, G.D.1    Murphy-Ullrich, J.E.2
  • 129
    • 49049110677 scopus 로고    scopus 로고
    • Integrins and the activation of latent transforming growth factor beta1 - an intimate relationship
    • Wipff PJ, Hinz B. Integrins and the activation of latent transforming growth factor beta1 - an intimate relationship. Eur J Cell Biol. 2008; 87: 601-615.
    • (2008) Eur J Cell Biol , vol.87 , pp. 601-615
    • Wipff, P.J.1    Hinz, B.2
  • 130
    • 76649126441 scopus 로고    scopus 로고
    • PGF isoforms, PLGF-1 and PGF-2 and the PGF receptor, neuropilin, in human breast cancer, prognostic significance
    • Escudero-Esparza A, Martin TA, Douglas-Jones A, Mansel RE, Jiang WG. PGF isoforms, PLGF-1 and PGF-2 and the PGF receptor, neuropilin, in human breast cancer: prognostic significance. Oncol Rep. 2010; 23: 537-544.
    • (2010) Oncol Rep , vol.23 , pp. 537-544
    • Escudero-Esparza, A.1    Martin, T.A.2    Douglas-Jones, A.3    Mansel, R.E.4    Jiang, W.G.5
  • 131
    • 55949098114 scopus 로고    scopus 로고
    • High levels of vascular endothelial growth factor and its receptors (VEGFR-1, VEGFR-2, neuropilin-1) are associated with worse outcome in breast cancer
    • Ghosh S, Sullivan CA, Zerkowski MP, Molinaro AM, Rimm DL, Camp RL, Chung GG. High levels of vascular endothelial growth factor and its receptors (VEGFR-1, VEGFR-2, neuropilin-1) are associated with worse outcome in breast cancer. Hum Pathol. 2008; 39: 1835-1843.
    • (2008) Hum Pathol , vol.39 , pp. 1835-1843
    • Ghosh, S.1    Sullivan, C.A.2    Zerkowski, M.P.3    Molinaro, A.M.4    Rimm, D.L.5    Camp, R.L.6    Chung, G.G.7
  • 138
    • 58149213801 scopus 로고    scopus 로고
    • Non-Smad pathways in TGF-beta signaling
    • Zhang YE. Non-Smad pathways in TGF-beta signaling. Cell Res. 2009; 19: 128-139.
    • (2009) Cell Res , vol.19 , pp. 128-139
    • Zhang, Y.E.1
  • 139
    • 77649178841 scopus 로고    scopus 로고
    • The TAK1-TRAF6 signalling pathway
    • Landström M. The TAK1-TRAF6 signalling pathway. Int J Biochem Cell Biol. 2010; 42: 585-589.
    • (2010) Int J Biochem Cell Biol , vol.42 , pp. 585-589
    • Landström, M.1
  • 140
    • 24944439828 scopus 로고    scopus 로고
    • Identification and characterization of ERK MAP kinase phosphorylation sites in Smad3
    • Matsuura I, Wang G, He D, Liu F. Identification and characterization of ERK MAP kinase phosphorylation sites in Smad3. Biochemistry. 2005; 44: 12546-53.
    • (2005) Biochemistry , vol.44 , pp. 12546-12553
    • Matsuura, I.1    Wang, G.2    He, D.3    Liu, F.4
  • 141
    • 79952706985 scopus 로고    scopus 로고
    • Transforming growth factor-β and the hallmarks of cancer
    • Tian M, Neil JR, Schiemann WP. Transforming growth factor-β and the hallmarks of cancer. Cell Signal. 2011; 23: 951-962.
    • (2011) Cell Signal , vol.23 , pp. 951-962
    • Tian, M.1    Neil, J.R.2    Schiemann, W.P.3
  • 143
    • 84862992680 scopus 로고    scopus 로고
    • T cell- but not tumor cell-produced TGF-β1 promotes the development of spontaneous mammary cancer
    • Sarkar A, Donkor MK, Li MO. T cell- but not tumor cell-produced TGF-β1 promotes the development of spontaneous mammary cancer. Oncotarget. 2011; 2: 1339- 1351.
    • (2011) Oncotarget , vol.2 , pp. 1339-1351
    • Sarkar, A.1    Donkor, M.K.2    Li, M.O.3
  • 146
    • 84860292363 scopus 로고    scopus 로고
    • p130Cas substrate domain signaling promotes migration, invasion, and survival of estrogen receptor-negative breast cancer cells
    • (London)
    • Cunningham-Edmondson, A.C., Hanks SK. p130Cas substrate domain signaling promotes migration, invasion, and survival of estrogen receptor-negative breast cancer cells. Breast Cancer (London), 2009; 1: 39-52.
    • (2009) Breast Cancer , vol.1 , pp. 39-52
    • Cunningham-Edmondson, A.C.1    Hanks, S.K.2
  • 147
    • 48249136081 scopus 로고    scopus 로고
    • The integrin-coupled signaling adaptor p130Cas suppresses Smad3 function in transforming growth factor-beta signaling
    • Kim W, Seok Kang Y, Soo Kim J, Shin NY, Hanks SK, Song WK. The integrin-coupled signaling adaptor p130Cas suppresses Smad3 function in transforming growth factor-beta signaling. Mol Biol Cell. 2008; 19: 2135-2146.
    • (2008) Mol Biol Cell , vol.19 , pp. 2135-2146
    • Kim, W.1    Seok Kang, Y.2    Soo Kim, J.3    Shin, N.Y.4    Hanks, S.K.5    Song, W.K.6
  • 148
    • 71749099201 scopus 로고    scopus 로고
    • J p130Cas is required for mammary tumor growth and transforming growth factor-beta-mediated metastasis through regulation of Smad2/3 activity
    • Wendt MK, Smith JA, Schiemann WP.J p130Cas is required for mammary tumor growth and transforming growth factor-beta-mediated metastasis through regulation of Smad2/3 activity. Biol Chem. 2009; 284: 34145-34156.
    • (2009) Biol Chem , vol.284 , pp. 34145-34156
    • Wendt, M.K.1    Smith, J.A.2    Schiemann, W.P.3
  • 149
    • 78149487540 scopus 로고    scopus 로고
    • Breast cancer stem-like cells are inhibited by a non-toxic aryl hydrocarbon receptor agonist
    • Prud'homme GJ, Glinka Y, Toulina A, Ace O, Subramaniam V, Jothy S. Breast cancer stem-like cells are inhibited by a non-toxic aryl hydrocarbon receptor agonist. PLoS One. 2010; 5: e13831.
    • (2010) PLoS One , vol.5
    • Prud'homme, G.J.1    Glinka, Y.2    Toulina, A.3    Ace, O.4    Subramaniam, V.5    Jothy, S.6
  • 150
    • 66549111659 scopus 로고    scopus 로고
    • Neuropilin-1 identifies endothelial precursors in human and murine embryonic stem cells before CD34 expression
    • Cimato T, Beers J, Ding S, Ma M, McCoy JP, Boehm M, Nabel EG. Neuropilin-1 identifies endothelial precursors in human and murine embryonic stem cells before CD34 expression. Circulation. 2009; 119: 2170-2178.
    • (2009) Circulation , vol.119 , pp. 2170-2178
    • Cimato, T.1    Beers, J.2    Ding, S.3    Ma, M.4    McCoy, J.P.5    Boehm, M.6    Nabel, E.G.7
  • 151
    • 58249113838 scopus 로고    scopus 로고
    • Microenvironment drives the endothelial or neural fate of differentiating embryonic stem cells coexpressing neuropilin-1 and Flk-1
    • Gualandris A, Noghero A, Geuna M, Arese M, Valdembri D, Serini G, Bussolino F. Microenvironment drives the endothelial or neural fate of differentiating embryonic stem cells coexpressing neuropilin-1 and Flk-1. FASEB J. 2009; 23: 68-78.
    • (2009) FASEB J , vol.23 , pp. 68-78
    • Gualandris, A.1    Noghero, A.2    Geuna, M.3    Arese, M.4    Valdembri, D.5    Serini, G.6    Bussolino, F.7
  • 152
    • 84865992234 scopus 로고    scopus 로고
    • Neuropilin-1 is expressed by breast cancer stem-like cells and is linked to NF-κB activation and tumor sphere formation
    • Aug 2. [Epub ahead of print]
    • Glinka Y, Mohammed N, Subramaniam V, Jothy S, Prud'homme GJ. Neuropilin-1 is expressed by breast cancer stem-like cells and is linked to NF-κB activation and tumor sphere formation. Biochem Biophys Res Commun. 2012; Aug 2. [Epub ahead of print].
    • (2012) Biochem Biophys Res Commun
    • Glinka, Y.1    Mohammed, N.2    Subramaniam, V.3    Jothy, S.4    Prud'homme, G.J.5
  • 153
    • 77954167982 scopus 로고    scopus 로고
    • Transcriptional crosstalk between TGF-β and stem cell pathways in tumor cell invasion, role of EMT promoting Smad complexes
    • Fuxe J, Vincent T, Garcia de Herreros A. Transcriptional crosstalk between TGF-β and stem cell pathways in tumor cell invasion: role of EMT promoting Smad complexes. Cell Cycle. 2010; 9: 2363-2374.
    • (2010) Cell Cycle , vol.9 , pp. 2363-2374
    • Fuxe, J.1    Vincent, T.2    Garcia de Herreros, A.3
  • 154
    • 82855170853 scopus 로고    scopus 로고
    • TGFβ-induced c-Myb affects the expression of EMT-associated genes and promotes invasion of ER+ breast cancer cells
    • Cesi V, Casciati A, Sesti F, Tanno B, Calabretta B, Raschellà G. TGFβ-induced c-Myb affects the expression of EMT-associated genes and promotes invasion of ER+ breast cancer cells. Cell Cycle. 2011; 10: 4149-4161.
    • (2011) Cell Cycle , vol.10 , pp. 4149-4161
    • Cesi, V.1    Casciati, A.2    Sesti, F.3    Tanno, B.4    Calabretta, B.5    Raschellà, G.6
  • 155
    • 77953550880 scopus 로고    scopus 로고
    • Role of β5-integrin in epithelial-mesenchymal transition in response to TGF-β
    • Bianchi A, Gervasi ME, Bakin A. Role of β5-integrin in epithelial-mesenchymal transition in response to TGF-β. Cell Cycle. 2010; 9: 1647-1659.
    • (2010) Cell Cycle , vol.9 , pp. 1647-1659
    • Bianchi, A.1    Gervasi, M.E.2    Bakin, A.3
  • 156
    • 34249028607 scopus 로고    scopus 로고
    • PDGF essentially links TGF-beta signaling to nuclear beta-catenin accumulation in hepatocellular carcinoma progression
    • Fischer AN, Fuchs E, Mikula M, Huber H, Beug H, Mikulits W. PDGF essentially links TGF-beta signaling to nuclear beta-catenin accumulation in hepatocellular carcinoma progression. Oncogene. 2007; 26: 3395-3405.
    • (2007) Oncogene , vol.26 , pp. 3395-3405
    • Fischer, A.N.1    Fuchs, E.2    Mikula, M.3    Huber, H.4    Beug, H.5    Mikulits, W.6
  • 157
    • 76549114666 scopus 로고    scopus 로고
    • Platelet derived growth factor B and epithelial mesenchymal transition of peritoneal mesothelial cells
    • Patel P, West-Mays J, Kolb M, Rodrigues JC, Hoff CM, Margetts PJ. Platelet derived growth factor B and epithelial mesenchymal transition of peritoneal mesothelial cells. Matrix Biol. 2010; 29: 97-106.
    • (2010) Matrix Biol , vol.29 , pp. 97-106
    • Patel, P.1    West-Mays, J.2    Kolb, M.3    Rodrigues, J.C.4    Hoff, C.M.5    Margetts, P.J.6
  • 160
    • 84863209310 scopus 로고    scopus 로고
    • Epithelial-mesenchymal transition in breast cancer lines is mediated through PDGF-D released by tissue-resident stem cells
    • Devarajan E, Song YH, Krishnappa S, Alt E. Epithelial-mesenchymal transition in breast cancer lines is mediated through PDGF-D released by tissue-resident stem cells. Int J Cancer. 2012; 131: 1023-1031.
    • (2012) Int J Cancer , vol.131 , pp. 1023-1031
    • Devarajan, E.1    Song, Y.H.2    Krishnappa, S.3    Alt, E.4
  • 162
    • 80053104790 scopus 로고    scopus 로고
    • RNA interference targeting NRP-1 inhibits human glioma cell proliferation and enhances cell apoptosis
    • Li X, Tang T, Lu X, Zhou H, Huang Y. RNA interference targeting NRP-1 inhibits human glioma cell proliferation and enhances cell apoptosis. Mol Med Report. 2011; 4: 1261-1266.
    • (2011) Mol Med Report , vol.4 , pp. 1261-1266
    • Li, X.1    Tang, T.2    Lu, X.3    Zhou, H.4    Huang, Y.5
  • 163
    • 77955747734 scopus 로고    scopus 로고
    • A mutated soluble neuropilin-2 B domain antagonizes vascular endothelial growth factor bioactivity and inhibits tumor progression
    • Geretti E, van Meeteren LA, Shimizu A, Dudley AC, Claesson-Welsh L, Klagsbrun M. A mutated soluble neuropilin-2 B domain antagonizes vascular endothelial growth factor bioactivity and inhibits tumor progression. Mol Cancer Res. 2010; 8: 1063-1073.
    • (2010) Mol Cancer Res , vol.8 , pp. 1063-1073
    • Geretti, E.1    van Meeteren, L.A.2    Shimizu, A.3    Dudley, A.C.4    Claesson-Welsh, L.5    Klagsbrun, M.6
  • 171
    • 84860821068 scopus 로고    scopus 로고
    • Semaphorin signals tweaking the tumor microenvironment
    • Muratori C, Tamagnone L. Semaphorin signals tweaking the tumor microenvironment. Adv. Cancer Res. 2012; 114: 59-85.
    • (2012) Adv. Cancer Res. , vol.114 , pp. 59-85
    • Muratori, C.1    Tamagnone, L.2
  • 172
    • 69449097679 scopus 로고    scopus 로고
    • Semaphorin signaling in cancer cells and in cells of the tumor microenvironment- -two sides of a coin
    • Capparuccia L, Tamagnone L. Semaphorin signaling in cancer cells and in cells of the tumor microenvironment- -two sides of a coin. J. Cell Sci. 2009; 122(Pt 11): 1723- 1736.
    • (2009) J. Cell Sci. , vol.122 , Issue.PART 11 , pp. 1723-1736
    • Capparuccia, L.1    Tamagnone, L.2
  • 173
    • 84855486320 scopus 로고    scopus 로고
    • Semaphorin signaling in angiogenesis, lymphangiogenesis and cancer
    • Sakurai A, Doçi CL, Gutkind JS. Semaphorin signaling in angiogenesis, lymphangiogenesis and cancer. Cell Res. 2012; 22: 23-32.
    • (2012) Cell Res , vol.22 , pp. 23-32
    • Sakurai, A.1    Doçi, C.L.2    Gutkind, J.S.3
  • 174
    • 84865137629 scopus 로고    scopus 로고
    • Emerging role of semaphorins as major regulatory signals and potential therapeutic targets in cancer
    • Tamagnone L. Emerging role of semaphorins as major regulatory signals and potential therapeutic targets in cancer. Cancer Cell. 2012; 22: 145-152.
    • (2012) Cancer Cell , vol.22 , pp. 145-152
    • Tamagnone, L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.