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Volumn 5, Issue JUN, 2015, Pages

Neuropilin-1 as therapeutic target for malignant melanoma

Author keywords

Angiogenesis; Cell penetrating peptides; Melanoma; Metastasis; Neuropilin 1; Peptidomimetics; T regulatory cells

Indexed keywords

B RAF KINASE INHIBITOR; CELL PENETRATING PEPTIDE; FIBROBLAST GROWTH FACTOR; INTEGRIN; MATRIX METALLOPROTEINASE; MICRORNA; NEUROPILIN 1; PLACENTAL GROWTH FACTOR; PLATELET DERIVED GROWTH FACTOR; SCATTER FACTOR; SEMAPHORIN; SMALL INTERFERING RNA; TRANSFORMING GROWTH FACTOR BETA; VASCULOTROPIN;

EID: 84934277040     PISSN: None     EISSN: 2234943X     Source Type: Journal    
DOI: 10.3389/fonc.2015.00125     Document Type: Short Survey
Times cited : (64)

References (105)
  • 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) 411:211-26. doi:10.1042/BJ20071639
    • (2008) Biochem J , vol.411 , pp. 211-226
    • Pellet-Many, C.1    Frankel, P.2    Jia, H.3    Zachary, I.4
  • 3
    • 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) 90:739-51. doi:10.1016/S0092-8674(00)80534-6
    • (1997) Cell , vol.90 , pp. 739-751
    • He, Z.1    Tessier-Lavigne, M.2
  • 4
    • 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) 8:632-45. doi:10.1038/nrc2404
    • (2008) Nat Rev Cancer , vol.8 , pp. 632-645
    • Neufeld, G.1    Kessler, O.2
  • 5
    • 72549108629 scopus 로고    scopus 로고
    • Role of class 3 semaphorins and their receptors in tumor growth and angiogenesis
    • Gaur P, Bielenberg DR, Samuel S, Bose D, Zhou Y, Gray MJ, et al. Role of class 3 semaphorins and their receptors in tumor growth and angiogenesis. Clin Cancer Res (2009) 15:6763-70. doi:10.1158/1078-0432.CCR-09-1810
    • (2009) Clin Cancer Res , vol.15 , pp. 6763-6770
    • Gaur, P.1    Bielenberg, D.R.2    Samuel, S.3    Bose, D.4    Zhou, Y.5    Gray, M.J.6
  • 6
    • 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) 121:4309-18.
    • (1995) Development , vol.121 , pp. 4309-4318
    • Kitsukawa, T.1    Shimono, A.2    Kawakami, A.3    Kondoh, H.4    Fujisawa, H.5
  • 9
    • 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) 92:735-45. doi:10.1016/S0092-8674(00)81402-6
    • (1998) Cell , vol.92 , pp. 735-745
    • Soker, S.1    Takashima, S.2    Miao, H.Q.3    Neufeld, G.4    Klagsbrun, M.5
  • 10
    • 0033597813 scopus 로고    scopus 로고
    • Differential binding of vascular endothelial growth factor B splice and proteolytic isoforms to neuropilin-1
    • Mäkinen T, Olofsson B, Karpanen T, Hellman U, Soker S, Klagsbrun M, et al. Differential binding of vascular endothelial growth factor B splice and proteolytic isoforms to neuropilin-1. J Biol Chem (1999) 274:21217-22. doi:10.1074/jbc.274.30.21217
    • (1999) J Biol Chem , vol.274 , pp. 21217-21222
    • Mäkinen, T.1    Olofsson, B.2    Karpanen, T.3    Hellman, U.4    Soker, S.5    Klagsbrun, M.6
  • 11
    • 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) 275:26690-5. doi:10.1074/jbc.M003955200
    • (2000) J Biol Chem , vol.275 , pp. 26690-26695
    • Fuh, G.1    Garcia, K.C.2    de Vos, A.M.3
  • 12
    • 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) 275:18040-5. doi:10.1074/jbc.M909259199
    • (2000) J Biol Chem , vol.275 , pp. 18040-18045
    • Gluzman-Poltorak, Z.1    Cohen, T.2    Herzog, Y.3    Neufeld, G.4
  • 13
    • 33746503288 scopus 로고    scopus 로고
    • Functional interaction of VEGF-C and VEGF-D with neuropilin receptors
    • Kärpänen T, Heckman CA, Keskitalo S, Jeltsch M, Ollila H, Neufeld G, et al. Functional interaction of VEGF-C and VEGF-D with neuropilin receptors. FASEB J (2006) 20:1462-72. doi:10.1096/fj.05-5646com
    • (2006) FASEB J , vol.20 , pp. 1462-1472
    • Kärpänen, T.1    Heckman, C.A.2    Keskitalo, S.3    Jeltsch, M.4    Ollila, H.5    Neufeld, G.6
  • 14
    • 79960690759 scopus 로고    scopus 로고
    • Neuropilin-1 promotes VEGFR-2 trafficking through Rab11 vesicles thereby specifying signal output
    • Ballmer-Hofer K, Andersson AE, Ratcliffe LE, Berger P. Neuropilin-1 promotes VEGFR-2 trafficking through Rab11 vesicles thereby specifying signal output. Blood (2011) 118:816-26. doi:10.1182/blood-2011-01-328773
    • (2011) Blood , vol.118 , pp. 816-826
    • Ballmer-Hofer, K.1    Andersson, A.E.2    Ratcliffe, L.E.3    Berger, P.4
  • 16
    • 84868616455 scopus 로고    scopus 로고
    • Neuropilins are multifunctional coreceptors involved in tumor initiation, growth, metastasis and immunity
    • Prud'homme GJ, Glinka Y. Neuropilins are multifunctional coreceptors involved in tumor initiation, growth, metastasis and immunity. Oncotarget (2012) 3:921-39.
    • (2012) Oncotarget , vol.3 , pp. 921-939
    • Prud'homme, G.J.1    Glinka, Y.2
  • 17
    • 84921282496 scopus 로고    scopus 로고
    • Novel expression of neuropilin 1 on human tumor-infiltrating lymphocytes in colorectal cancer liver metastases
    • Chaudhary B, Elkord E. Novel expression of neuropilin 1 on human tumor-infiltrating lymphocytes in colorectal cancer liver metastases. Expert Opin Ther Targets (2014) 29:1-15. doi:10.1517/14728222.2014.977784
    • (2014) Expert Opin Ther Targets , vol.29 , pp. 1-15
    • Chaudhary, B.1    Elkord, E.2
  • 18
    • 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 (2007) 67:10309-16. doi:10.1158/0008-5472.CAN-07-3256
    • (2007) Cancer Res , vol.67 , pp. 10309-10316
    • Matsushita, A.1    Gotze, T.2    Korc, M.3
  • 19
    • 84858256282 scopus 로고    scopus 로고
    • Neuropilins: expression and roles in the epithelium
    • Wild JRL, Staton CA, Chapple K, Corfe BM. Neuropilins: expression and roles in the epithelium. Int J Exp Pathol (2012) 93:81-103. doi:10.1111/j.1365-2613.2012.00810.x
    • (2012) Int J Exp Pathol , vol.93 , pp. 81-103
    • Wild, J.R.L.1    Staton, C.A.2    Chapple, K.3    Corfe, B.M.4
  • 20
    • 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) 6:1173-80. doi:10.4161/cbt.6.8.4363
    • (2007) Cancer Biol Ther , vol.6 , pp. 1173-1180
    • Fukasawa, M.1    Matsushita, A.2    Korc, M.3
  • 21
    • 71749099202 scopus 로고    scopus 로고
    • Alphav beta3 integrin limits the contribution of neuropilin-1 to vascular endothelial growth factor-induced angiogenesis
    • Robinson SD, Reynolds LE, Kostourou V, Reynolds AR, da Silva RG, Tavora B, et al. Alphav beta3 integrin limits the contribution of neuropilin-1 to vascular endothelial growth factor-induced angiogenesis. J Biol Chem (2009) 284:33966-81. doi:10.1074/jbc.M109.030700
    • (2009) J Biol Chem , vol.284 , pp. 33966-33981
    • Robinson, S.D.1    Reynolds, L.E.2    Kostourou, V.3    Reynolds, A.R.4    da Silva, R.G.5    Tavora, B.6
  • 22
    • 58849090461 scopus 로고    scopus 로고
    • Neuropilin-1/GIPC1 signaling regulates alpha5beta1 integrin traffic and function in endothelial cells
    • Valdembri D, Caswell PT, Anderson KI, Schwarz JP, König I, Astanina E, et al. Neuropilin-1/GIPC1 signaling regulates alpha5beta1 integrin traffic and function in endothelial cells. PLoS Biol (2009) 7:e1000025. doi:10.1371/journal.pbio.1000025
    • (2009) PLoS Biol , vol.7
    • Valdembri, D.1    Caswell, P.T.2    Anderson, K.I.3    Schwarz, J.P.4    König, I.5    Astanina, E.6
  • 23
    • 84865140752 scopus 로고    scopus 로고
    • Neuropilin-1 stimulates tumor growth by increasing fibronectin fibril assembly in the tumor microenvironment
    • Yaqoob U, Cao S, Shergill U, Jagavelu K, Geng Z, Yin M, et al. Neuropilin-1 stimulates tumor growth by increasing fibronectin fibril assembly in the tumor microenvironment. Cancer Res (2012) 72:4047-59. doi:10.1158/0008-5472.CAN-11-3907
    • (2012) Cancer Res , vol.72 , pp. 4047-4059
    • Yaqoob, U.1    Cao, S.2    Shergill, U.3    Jagavelu, K.4    Geng, Z.5    Yin, M.6
  • 24
    • 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, et al. Breast cancer cells secreted platelet-derived growth factor-induced motility of vascular smooth muscle cells is mediated through neuropilin-1. Mol Carcinog (2006) 45:871-80. doi:10.1002/mc.20248
    • (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
  • 25
    • 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, et al. 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. doi:10.1186/1476-4598-9-209
    • (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
  • 26
    • 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, Junemann-Ramirez M, Zachary IC. Neuropilin-1 mediates PDGF stimulation of vascular smooth muscle cell migration and signalling via p130Cas. Biochem J (2011) 435:609-18. doi:10.1042/BJ20100580
    • (2011) Biochem J , vol.435 , pp. 609-618
    • Pellet-Many, C.1    Frankel, P.2    Evans, I.M.3    Herzog, B.4    Junemann-Ramirez, M.5    Zachary, I.C.6
  • 27
    • 84874760414 scopus 로고    scopus 로고
    • Targeting placental growth factor/neuropilin 1 pathway inhibits growth and spread of medulloblastoma
    • Snuderl M, Batista A, Kirkpatrick ND, Ruiz de Almodovar C, Riedemann L, Walsh EC, et al. Targeting placental growth factor/neuropilin 1 pathway inhibits growth and spread of medulloblastoma. Cell (2013) 152:1065-76. doi:10.1016/j.cell.2013.01.036
    • (2013) Cell , vol.152 , pp. 1065-1076
    • Snuderl, M.1    Batista, A.2    Kirkpatrick, N.D.3    Ruiz de Almodovar, C.4    Riedemann, L.5    Walsh, E.C.6
  • 28
    • 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, et al. Neuropilin-1 signaling through p130Cas tyrosine phosphorylation is essential for growth factor-dependent migration of glioma and endothelial cells. Mol Cell Biol (2011) 31:1174-85. doi:10.1128/MCB.00903-10
    • (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
  • 29
    • 84879651682 scopus 로고    scopus 로고
    • Neuropilin-1 expression promotes invasiveness of melanoma cells through vascular endothelial growth factor receptor-2-dependent and -independent mechanisms
    • Ruffini F, D'Atri S, Lacal PM. Neuropilin-1 expression promotes invasiveness of melanoma cells through vascular endothelial growth factor receptor-2-dependent and -independent mechanisms. Int J Oncol (2013) 43:297-306. doi:10.3892/ijo.2013.1948
    • (2013) Int J Oncol , vol.43 , pp. 297-306
    • Ruffini, F.1    D'Atri, S.2    Lacal, P.M.3
  • 30
    • 84901760004 scopus 로고    scopus 로고
    • Imatinib inhibits VEGF-independent angiogenesis by targeting neuropilin 1-dependent ABL1 activation in endothelial cells
    • Raimondi C, Fantin A, Lampropoulou A, Denti L, Chikh A, Ruhrberg C. Imatinib inhibits VEGF-independent angiogenesis by targeting neuropilin 1-dependent ABL1 activation in endothelial cells. J Exp Med (2014) 211:1167-83. doi:10.1084/jem.20132330
    • (2014) J Exp Med , vol.211 , pp. 1167-1183
    • Raimondi, C.1    Fantin, A.2    Lampropoulou, A.3    Denti, L.4    Chikh, A.5    Ruhrberg, C.6
  • 31
    • 0142245808 scopus 로고    scopus 로고
    • Characterization of a new alternatively spliced neuropilin-1 isoform
    • Tao Q, Spring SC, Terman BI. Characterization of a new alternatively spliced neuropilin-1 isoform. Angiogenesis (2003) 6:39-45. doi:10.1023/A:1025884628155
    • (2003) Angiogenesis , vol.6 , pp. 39-45
    • Tao, Q.1    Spring, S.C.2    Terman, B.I.3
  • 32
    • 2942625876 scopus 로고    scopus 로고
    • Identification of two novel alternatively spliced neuropilin-1 isoforms
    • Cackowski FC, Xu L, Hu B, Cheng SY. Identification of two novel alternatively spliced neuropilin-1 isoforms. Genomics (2004) 84:82-94. doi:10.1016/j.ygeno.2004.02.001
    • (2004) Genomics , vol.84 , pp. 82-94
    • Cackowski, F.C.1    Xu, L.2    Hu, B.3    Cheng, S.Y.4
  • 34
    • 79959729771 scopus 로고    scopus 로고
    • Neuropilins: a new target for cancer therapy
    • Grandclement C, Borg C. Neuropilins: a new target for cancer therapy. Cancers (2011) 3:1899-928. doi:10.3390/cancers3021899
    • (2011) Cancers , vol.3 , pp. 1899-1928
    • Grandclement, C.1    Borg, C.2
  • 35
    • 1442329388 scopus 로고    scopus 로고
    • Expression of neuropilin-1 in high-grade dysplasia, invasive cancer, and metastases of the human gastrointestinal tract
    • Hansel DE, Wilentz RE, Yeo CJ, Schulick RD, Montgomery E, Maitra A. Expression of neuropilin-1 in high-grade dysplasia, invasive cancer, and metastases of the human gastrointestinal tract. Am J Surg Pathol (2004) 28:347-56. doi:10.1097/00000478-200403000-00007
    • (2004) Am J Surg Pathol , vol.28 , pp. 347-356
    • Hansel, D.E.1    Wilentz, R.E.2    Yeo, C.J.3    Schulick, R.D.4    Montgomery, E.5    Maitra, A.6
  • 36
    • 0035422178 scopus 로고    scopus 로고
    • Vascular endothelial growth factor is an autocrine survival factor for neuropilin-expressing breast carcinoma cells
    • Bachelder RE, Crago A, Chung J, Wendt MA, Shaw LM, Robinson G, et al. Vascular endothelial growth factor is an autocrine survival factor for neuropilin-expressing breast carcinoma cells. Cancer Res (2001) 61:5736-40.
    • (2001) Cancer Res , vol.61 , pp. 5736-5740
    • Bachelder, R.E.1    Crago, A.2    Chung, J.3    Wendt, M.A.4    Shaw, L.M.5    Robinson, G.6
  • 37
    • 0033674846 scopus 로고    scopus 로고
    • Neuropilin-1 expression by tumor cells promotes tumor angiogenesis and progression
    • Miao HQ, Lee P, Lin H, Soker S, Klagsbrun M. Neuropilin-1 expression by tumor cells promotes tumor angiogenesis and progression. FASEB J (2000) 14:2532-9. doi:10.1096/fj.00-0250com
    • (2000) FASEB J , vol.14 , pp. 2532-2539
    • Miao, H.Q.1    Lee, P.2    Lin, H.3    Soker, S.4    Klagsbrun, M.5
  • 38
    • 0141816865 scopus 로고    scopus 로고
    • Competing autocrine pathways involving alternative neuropilin-1 ligands regulate chemotaxis of carcinoma cells
    • Bachelder RE, Lipscomb EA, Lin X, Wendt MA, Chadborn NH, Eickholt BJ, et al. Competing autocrine pathways involving alternative neuropilin-1 ligands regulate chemotaxis of carcinoma cells. Cancer Res (2003) 63:5230-3.
    • (2003) Cancer Res , vol.63 , pp. 5230-5233
    • Bachelder, R.E.1    Lipscomb, E.A.2    Lin, X.3    Wendt, M.A.4    Chadborn, N.H.5    Eickholt, B.J.6
  • 39
    • 14844320026 scopus 로고    scopus 로고
    • A peptide corresponding to the neuropilin-1-binding site on VEGF(165) induces apoptosis of neuropilin-1-expressing breast tumour cells
    • Barr MP, Byrne AM, Duffy AM, Condron CM, Devocelle M, Harriott P, et al. A peptide corresponding to the neuropilin-1-binding site on VEGF(165) induces apoptosis of neuropilin-1-expressing breast tumour cells. Br J Cancer (2005) 92:328-33.
    • (2005) Br J Cancer , vol.92 , pp. 328-333
    • Barr, M.P.1    Byrne, A.M.2    Duffy, A.M.3    Condron, C.M.4    Devocelle, M.5    Harriott, P.6
  • 41
    • 34548064808 scopus 로고    scopus 로고
    • Targeting neuropilin 1 as an antitumor strategy in lung cancer
    • Hong TM, Chen YL, Wu YY, Yuan A, Chao YC, Chung YC, et al. Targeting neuropilin 1 as an antitumor strategy in lung cancer. Clin Cancer Res (2007) 13:4759-68. doi:10.1158/1078-0432.CCR-07-0001
    • (2007) Clin Cancer Res , vol.13 , pp. 4759-4768
    • Hong, T.M.1    Chen, Y.L.2    Wu, Y.Y.3    Yuan, A.4    Chao, Y.C.5    Chung, Y.C.6
  • 42
    • 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, et al. Neuropilin-1 upholds dedifferentiation and propagation phenotypes of renal cell carcinoma cells by activating Akt and sonic hedgehog axes. Cancer Res (2008) 68:8667-72. doi:10.1158/0008-5472.CAN-08-2614
    • (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
  • 43
    • 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) 102:541-52. doi:10.1038/sj.bjc.6605539
    • (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
  • 44
    • 79958044393 scopus 로고    scopus 로고
    • VEGF signaling through neuropilin 1 guides commissural axon crossing at the optic chiasm
    • Erskine L, Reijntjes S, Pratt T, Denti L, Schwarz Q, Vieira JM, et al. VEGF signaling through neuropilin 1 guides commissural axon crossing at the optic chiasm. Neuron (2011) 70:951-65. doi:10.1016/j.neuron.2011.02.052
    • (2011) Neuron , vol.70 , pp. 951-965
    • Erskine, L.1    Reijntjes, S.2    Pratt, T.3    Denti, L.4    Schwarz, Q.5    Vieira, J.M.6
  • 45
    • 0034518226 scopus 로고    scopus 로고
    • Human melanoma cells secrete and respond to placenta growth factor and vascular endothelial growth factor
    • Lacal PM, Failla CM, Pagani E, Odorisio T, Schietroma C, Falcinelli S, et al. Human melanoma cells secrete and respond to placenta growth factor and vascular endothelial growth factor. J Invest Dermatol (2000) 115:1000-7. doi:10.1046/j.1523-1747.2000.00199.x
    • (2000) J Invest Dermatol , vol.115 , pp. 1000-1007
    • Lacal, P.M.1    Failla, C.M.2    Pagani, E.3    Odorisio, T.4    Schietroma, C.5    Falcinelli, S.6
  • 46
    • 33644829930 scopus 로고    scopus 로고
    • An autocrine loop directed by the vascular endothelial growth factor promotes invasiveness of human melanoma cells
    • Lacal PM, Ruffini F, Pagani E, D'Atri S. An autocrine loop directed by the vascular endothelial growth factor promotes invasiveness of human melanoma cells. Int J Oncol (2005) 27:1625-32. doi:10.3892/ijo.27.6.1625
    • (2005) Int J Oncol , vol.27 , pp. 1625-1632
    • Lacal, P.M.1    Ruffini, F.2    Pagani, E.3    D'Atri, S.4
  • 47
    • 84944964277 scopus 로고    scopus 로고
    • Cilengitide down-modulates invasiveness and vasculogenic mimicry of neuropilin-1 expressing melanoma cells through the inhibition of avß5 integrin
    • Ruffini F, Graziani G, Levati L, Tentori L, D'Atri S, Lacal PM. Cilengitide down-modulates invasiveness and vasculogenic mimicry of neuropilin-1 expressing melanoma cells through the inhibition of avß5 integrin. Int J Cancer (2015) 136:E545-58. doi:10.1002/ijc.29252
    • (2015) Int J Cancer , vol.136 , pp. E545-E558
    • Ruffini, F.1    Graziani, G.2    Levati, L.3    Tentori, L.4    D'Atri, S.5    Lacal, P.M.6
  • 48
    • 84892384905 scopus 로고    scopus 로고
    • Platelet derived growth factor C and calpain-3 are modulators of human melanoma cell invasiveness
    • Ruffini F, Tentori L, Dorio AS, Arcelli D, d'Amati G, D'Atri S, et al. Platelet derived growth factor C and calpain-3 are modulators of human melanoma cell invasiveness. Oncol Rep (2013) 30:2887-96. doi:10.3892/or.2013.2791
    • (2013) Oncol Rep , vol.30 , pp. 2887-2896
    • Ruffini, F.1    Tentori, L.2    Dorio, A.S.3    Arcelli, D.4    d'Amati, G.5    D'Atri, S.6
  • 49
    • 33746602209 scopus 로고    scopus 로고
    • Increased melanoma growth and metastasis spreading in mice overexpressing placenta growth factor
    • Marcellini M, De Luca N, Riccioni T, Ciucci A, Orecchia A, Lacal PM, et al. Increased melanoma growth and metastasis spreading in mice overexpressing placenta growth factor. Am J Pathol (2006) 169:643-54. doi:10.2353/ajpath.2006.051041
    • (2006) Am J Pathol , vol.169 , pp. 643-654
    • Marcellini, M.1    De Luca, N.2    Riccioni, T.3    Ciucci, A.4    Orecchia, A.5    Lacal, P.M.6
  • 50
    • 78650841055 scopus 로고    scopus 로고
    • Placenta growth factor induces melanoma resistance to temozolomide through a mechanism that involves the activation of the transcription factor NF-?B
    • Levati L, Ruffini F, Muzi A, Umezawa K, Graziani G, D'Atri S, et al. Placenta growth factor induces melanoma resistance to temozolomide through a mechanism that involves the activation of the transcription factor NF-?B. Int J Oncol (2011) 38:241-7. doi:10.3892/ijo_00000844
    • (2011) Int J Oncol , vol.38 , pp. 241-247
    • Levati, L.1    Ruffini, F.2    Muzi, A.3    Umezawa, K.4    Graziani, G.5    D'Atri, S.6
  • 51
    • 85045872410 scopus 로고    scopus 로고
    • Neuropilin-1 expressing melanoma cells as a model to study the aggressiveness of metastatic melanoma
    • Ruffini F, Graziani G, Levati L, Tentori L, Caporali S, D'Atri S, et al. Neuropilin-1 expressing melanoma cells as a model to study the aggressiveness of metastatic melanoma. J Transl Med (2015) 13:2074. doi:10.1186/1479-5876-13-S1-P6
    • (2015) J Transl Med , vol.13 , pp. 2074
    • Ruffini, F.1    Graziani, G.2    Levati, L.3    Tentori, L.4    Caporali, S.5    D'Atri, S.6
  • 53
    • 1542571789 scopus 로고    scopus 로고
    • Neuropilin-1-mediated vascular permeability factor/vascular endothelial growth factor-dependent endothelial cell migration
    • Wang L, Zeng H, Wang P, Soker S, Mukhopadhyay D. Neuropilin-1-mediated vascular permeability factor/vascular endothelial growth factor-dependent endothelial cell migration. J Biol Chem (2003) 278:48848-60. doi:10.1074/jbc.M310047200
    • (2003) J Biol Chem , vol.278 , pp. 48848-48860
    • Wang, L.1    Zeng, H.2    Wang, P.3    Soker, S.4    Mukhopadhyay, D.5
  • 54
  • 55
    • 84907891290 scopus 로고    scopus 로고
    • Immunohistological insight into the correlation between neuropilin-1 and epithelial-mesenchymal transition markers in epithelial ovarian cancer
    • Adham SA, Al Harrasi I, Al Haddabi I, Al Rashdi A, Al Sinawi S, Al Maniri A, et al. Immunohistological insight into the correlation between neuropilin-1 and epithelial-mesenchymal transition markers in epithelial ovarian cancer. J Histochem Cytochem (2014) 62:619-31. doi:10.1369/0022155414538821
    • (2014) J Histochem Cytochem , vol.62 , pp. 619-631
    • Adham, S.A.1    Al Harrasi, I.2    Al Haddabi, I.3    Al Rashdi, A.4    Al Sinawi, S.5    Al Maniri, A.6
  • 56
    • 84904297060 scopus 로고    scopus 로고
    • Neuropilin-1 promotes epithelial-to-mesenchymal transition by stimulating nuclear factor-kappa B and is associated with poor prognosis in human oral squamous cell carcinoma
    • Chu W, Song X, Yang X, Ma L, Zhu J, He M, et al. Neuropilin-1 promotes epithelial-to-mesenchymal transition by stimulating nuclear factor-kappa B and is associated with poor prognosis in human oral squamous cell carcinoma. PLoS One (2014) 9:e101931. doi:10.1371/journal.pone.0101931
    • (2014) PLoS One , vol.9
    • Chu, W.1    Song, X.2    Yang, X.3    Ma, L.4    Zhu, J.5    He, M.6
  • 57
    • 0034646262 scopus 로고    scopus 로고
    • Identification of a natural soluble neuropilin-1 that binds vascular endothelial growth factor: in vivo expression and antitumor activity
    • Gagnon ML, Bielenberg DR, Gechtman Z, Miao HQ, Takashima S, Soker S, et al. Identification of a natural soluble neuropilin-1 that binds vascular endothelial growth factor: in vivo expression and antitumor activity. Proc Natl Acad Sci USA (2000) 97:2573-8. doi:10.1073/pnas.040337597
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 2573-2578
    • Gagnon, M.L.1    Bielenberg, D.R.2    Gechtman, Z.3    Miao, H.Q.4    Takashima, S.5    Soker, S.6
  • 58
    • 84903542048 scopus 로고    scopus 로고
    • Regulation of soluble neuropilin 1, an endogenous angiogenesis inhibitor, in liver development and regeneration
    • Panigrahy D, Adini I, Mamluk R, Levonyak N, Bruns CJ, D'Amore PA, et al. Regulation of soluble neuropilin 1, an endogenous angiogenesis inhibitor, in liver development and regeneration. Pathology (2014) 46:416-23. doi:10.1097/PAT.0000000000000121
    • (2014) Pathology , vol.46 , pp. 416-423
    • Panigrahy, D.1    Adini, I.2    Mamluk, R.3    Levonyak, N.4    Bruns, C.J.5    D'Amore, P.A.6
  • 59
    • 0037114642 scopus 로고    scopus 로고
    • In vivo administration of vascular endothelial growth factor (VEGF) and its antagonist, soluble neuropilin-1, predicts a role of VEGF in the progression of acute myeloid leukemia in vivo
    • Schuch G, Machluf M, Bartsch G Jr, Nomi M, Richard H, Atala A, et al. In vivo administration of vascular endothelial growth factor (VEGF) and its antagonist, soluble neuropilin-1, predicts a role of VEGF in the progression of acute myeloid leukemia in vivo. Blood (2002) 100:4622-8. doi:10.1182/blood.V100.13.4622
    • (2002) Blood , vol.100 , pp. 4622-4628
    • Schuch, G.1    Machluf, M.2    Bartsch, G.3    Nomi, M.4    Richard, H.5    Atala, A.6
  • 60
    • 41049096239 scopus 로고    scopus 로고
    • Neuropilins: novel targets for anti-angiogenesis therapies
    • Geretti E, Klagsbrun M. Neuropilins: novel targets for anti-angiogenesis therapies. Cell Adh Migr (2007) 1:56-61. doi:10.4161/cam.1.2.4490
    • (2007) Cell Adh Migr , vol.1 , pp. 56-61
    • Geretti, E.1    Klagsbrun, M.2
  • 61
    • 77953659997 scopus 로고    scopus 로고
    • Identification of circulating neuropilin-1 and dose-dependent elevation following anti-neuropilin-1 antibody administration
    • Lu Y, Xiang H, Liu P, Tong RR, Watts RJ, Koch AW, et al. Identification of circulating neuropilin-1 and dose-dependent elevation following anti-neuropilin-1 antibody administration. MAbs (2009) 1:364-9. doi:10.4161/mabs.1.4.8885
    • (2009) MAbs , vol.1 , pp. 364-369
    • Lu, Y.1    Xiang, H.2    Liu, P.3    Tong, R.R.4    Watts, R.J.5    Koch, A.W.6
  • 62
    • 84897421093 scopus 로고    scopus 로고
    • NRP1 presented in trans to the endothelium arrests VEGFR2 endocytosis, preventing angiogenic signaling and tumor initiation
    • Koch S, van Meeteren LA, Morin E, Testini C, Westörm S, Björkelund H, et al. NRP1 presented in trans to the endothelium arrests VEGFR2 endocytosis, preventing angiogenic signaling and tumor initiation. Dev Cell (2014) 28:633-46. doi:10.1016/j.devcel.2014.02.010
    • (2014) Dev Cell , vol.28 , pp. 633-646
    • Koch, S.1    van Meeteren, L.A.2    Morin, E.3    Testini, C.4    Westörm, S.5    Björkelund, H.6
  • 63
    • 76649115312 scopus 로고    scopus 로고
    • Hormonal regulation and distinct functions of semaphorin-3B and semaphorin-3F in ovarian cancer
    • Joseph D, Ho SM, Syed V. Hormonal regulation and distinct functions of semaphorin-3B and semaphorin-3F in ovarian cancer. Mol Cancer Ther (2010) 9:499-509. doi:10.1158/1535-7163.MCT-09-0664
    • (2010) Mol Cancer Ther , vol.9 , pp. 499-509
    • Joseph, D.1    Ho, S.M.2    Syed, V.3
  • 64
    • 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) 122:1723-36. doi:10.1242/jcs.030197
    • (2009) J Cell Sci. , vol.122 , pp. 1723-1736
    • Capparuccia, L.1    Tamagnone, L.2
  • 65
    • 40049103902 scopus 로고    scopus 로고
    • Semaphorin3a disrupts podocyte foot processes causing acute proteinuria
    • Tapia R, Guan F, Gershin I, Teichman J, Villegas G, Tufro A. Semaphorin3a disrupts podocyte foot processes causing acute proteinuria. Kidney Int (2008) 73:733-40. doi:10.1038/sj.ki.5002726
    • (2008) Kidney Int , vol.73 , pp. 733-740
    • Tapia, R.1    Guan, F.2    Gershin, I.3    Teichman, J.4    Villegas, G.5    Tufro, A.6
  • 66
    • 36549056078 scopus 로고    scopus 로고
    • Structural studies of neuropilin/antibody complexes provide insights into semaphorin and VEGF binding
    • Appleton BA, Wu P, Maloney J, Yin J, Liang WC, Stawicki S, et al. Structural studies of neuropilin/antibody complexes provide insights into semaphorin and VEGF binding. EMBO J (2007) 26:4902-12. doi:10.1038/sj.emboj.7601906
    • (2007) EMBO J , vol.26 , pp. 4902-4912
    • Appleton, B.A.1    Wu, P.2    Maloney, J.3    Yin, J.4    Liang, W.C.5    Stawicki, S.6
  • 67
    • 33845969276 scopus 로고    scopus 로고
    • Function blocking antibodies to neuropilin-1 generated from a designed human synthetic antibody phage library
    • Liang WC, Dennis MS, Stawicki S, Chanthery Y, Pan Q, Chen Y, et al. Function blocking antibodies to neuropilin-1 generated from a designed human synthetic antibody phage library. J Mol Biol (2007) 366:815-29. doi:10.1016/j.jmb.2006.11.021
    • (2007) J Mol Biol , vol.366 , pp. 815-829
    • Liang, W.C.1    Dennis, M.S.2    Stawicki, S.3    Chanthery, Y.4    Pan, Q.5    Chen, Y.6
  • 68
    • 33845991161 scopus 로고    scopus 로고
    • Blocking neuropilin-1 function has an additive effect with anti-VEGF to inhibit tumor growth
    • Pan Q, Chanthery Y, Liang WC, Stawicki S, Mak J, Rathore N, et al. Blocking neuropilin-1 function has an additive effect with anti-VEGF to inhibit tumor growth. Cancer Cell (2007) 11:53-67. doi:10.1016/j.ccr.2006.10.018
    • (2007) Cancer Cell , vol.11 , pp. 53-67
    • Pan, Q.1    Chanthery, Y.2    Liang, W.C.3    Stawicki, S.4    Mak, J.5    Rathore, N.6
  • 69
    • 84868528828 scopus 로고    scopus 로고
    • Pharmacokinetic and pharmacodynamic analysis of circulating biomarkers of anti-NRP1, a novel antiangiogenesis agent, in two phase I trials in patients with advanced solid tumors
    • Xin Y, Li J, Wu J, Kinard R, Weekes CD, Patnaik A, et al. Pharmacokinetic and pharmacodynamic analysis of circulating biomarkers of anti-NRP1, a novel antiangiogenesis agent, in two phase I trials in patients with advanced solid tumors. Clin. Cancer Res (2012) 18:6040-8.
    • (2012) Clin. Cancer Res , vol.18 , pp. 6040-6048
    • Xin, Y.1    Li, J.2    Wu, J.3    Kinard, R.4    Weekes, C.D.5    Patnaik, A.6
  • 70
    • 84901627424 scopus 로고    scopus 로고
    • A monoclonal antibody targeting neuropilin-1 inhibits adhesion of MCF7 breast cancer cells to fibronectin by suppressing the FAK/p130cas signaling pathway
    • Zeng F, Luo F, Lv S, Zhang H, Cao C, Chen X, et al. A monoclonal antibody targeting neuropilin-1 inhibits adhesion of MCF7 breast cancer cells to fibronectin by suppressing the FAK/p130cas signaling pathway. Anticancer Drugs (2014) 25:663-72. doi:10.1097/CAD.0000000000000091
    • (2014) Anticancer Drugs , vol.25 , pp. 663-672
    • Zeng, F.1    Luo, F.2    Lv, S.3    Zhang, H.4    Cao, C.5    Chen, X.6
  • 71
    • 84863801928 scopus 로고    scopus 로고
    • Anti-angiogenesis therapies: their potential in cancer management
    • Eichholz A, Merchant S, Gaya AM. Anti-angiogenesis therapies: their potential in cancer management. Onco Targets Ther. (2010) 3:69-82. doi:10.2147/OTT.S5256
    • (2010) Onco Targets Ther. , vol.3 , pp. 69-82
    • Eichholz, A.1    Merchant, S.2    Gaya, A.M.3
  • 72
    • 84904569660 scopus 로고    scopus 로고
    • A phase I study of the human monoclonal anti-NRP1 antibody MNRP1685A in patients with advanced solid tumors
    • Weekes CD, Beeram M, Tolcher AW, Papadopoulos KP, Gore L, Hegde P, et al. A phase I study of the human monoclonal anti-NRP1 antibody MNRP1685A in patients with advanced solid tumors. Invest New Drugs (2014) 32:653-60. doi:10.1007/s10637-014-0071-z
    • (2014) Invest New Drugs , vol.32 , pp. 653-660
    • Weekes, C.D.1    Beeram, M.2    Tolcher, A.W.3    Papadopoulos, K.P.4    Gore, L.5    Hegde, P.6
  • 73
    • 84900798650 scopus 로고    scopus 로고
    • A Phase Ib study evaluating MNRP1685A, a fully human anti-NRP1 monoclonal antibody, in combination with bevacizumab and paclitaxel in patients with advanced solid tumors
    • Patnaik A, LoRusso PM, Messersmith WA, Papadopoulos KP, Gore L, Beeram M, et al. A Phase Ib study evaluating MNRP1685A, a fully human anti-NRP1 monoclonal antibody, in combination with bevacizumab and paclitaxel in patients with advanced solid tumors. Cancer Chemother Pharmacol (2014) 73:951-60. doi:10.1007/s00280-014-2426-8
    • (2014) Cancer Chemother Pharmacol , vol.73 , pp. 951-960
    • Patnaik, A.1    LoRusso, P.M.2    Messersmith, W.A.3    Papadopoulos, K.P.4    Gore, L.5    Beeram, M.6
  • 74
    • 0037025311 scopus 로고    scopus 로고
    • Neuropilin-1 binds vascular endothelial growth factor 165, placenta growth factor-2, and heparin via its b1b2 domain
    • Mamluk R, Gechtman Z, Kutcher ME, Gasiunas N, Gallagher J, Klagsbrun M. Neuropilin-1 binds vascular endothelial growth factor 165, placenta growth factor-2, and heparin via its b1b2 domain. J Biol Chem (2002) 277:24818-25. doi:10.1074/jbc.M200730200
    • (2002) J Biol Chem , vol.277 , pp. 24818-24825
    • Mamluk, R.1    Gechtman, Z.2    Kutcher, M.E.3    Gasiunas, N.4    Gallagher, J.5    Klagsbrun, M.6
  • 75
    • 33744965754 scopus 로고    scopus 로고
    • Characterization of a bicyclic peptide neuropilin-1 (NP-1) antagonist (EG3287) reveals importance of vascular endothelial growth factor exon 8 for NP-1 binding and role of NP-1 in KDR signaling
    • Jia H, Bagherzadeh A, Hartzoulakis B, Jarvis A, Löhr M, Shaikh S, et al. Characterization of a bicyclic peptide neuropilin-1 (NP-1) antagonist (EG3287) reveals importance of vascular endothelial growth factor exon 8 for NP-1 binding and role of NP-1 in KDR signaling. J Biol Chem (2006) 281:13493-502. doi:10.1074/jbc.M512121200
    • (2006) J Biol Chem , vol.281 , pp. 13493-13502
    • Jia, H.1    Bagherzadeh, A.2    Hartzoulakis, B.3    Jarvis, A.4    Löhr, M.5    Shaikh, S.6
  • 76
    • 0031438075 scopus 로고    scopus 로고
    • Inhibition of vascular endothelial growth factor (VEGF)-induced endothelial cell proliferation by a peptide corresponding to the exon 7-encoded domain of VEGF165
    • Soker S, Gollamudi-Payne S, Fidder H, Charmahelli H, Klagsbrun M. Inhibition of vascular endothelial growth factor (VEGF)-induced endothelial cell proliferation by a peptide corresponding to the exon 7-encoded domain of VEGF165. J Biol Chem (1997) 272:31582-8. doi:10.1074/jbc.272.50.31582
    • (1997) J Biol Chem , vol.272 , pp. 31582-31588
    • Soker, S.1    Gollamudi-Payne, S.2    Fidder, H.3    Charmahelli, H.4    Klagsbrun, M.5
  • 77
    • 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, et al. Antiangiogenic and antitumor activities of peptide inhibiting the vascular endothelial growth factor binding to neuropilin-1. Life Sci (2006) 79:2370-81. doi:10.1016/j.lfs.2006.08.005
    • (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
  • 78
    • 77950398570 scopus 로고    scopus 로고
    • From combinatorial peptide selection to drug prototype (I): targeting the vascular endothelial growth factor receptor pathway
    • Giordano RJ, Cardó-Vila M, Salameh A, Anobom CD, Zeitlin BD, Hawke DH, et al. From combinatorial peptide selection to drug prototype (I): targeting the vascular endothelial growth factor receptor pathway. Proc Natl Acad Sci U. S. A. (2010) 107:5112-7. doi:10.1073/pnas.0915141107
    • (2010) Proc Natl Acad Sci U. S. A. , vol.107 , pp. 5112-5117
    • Giordano, R.J.1    Cardó-Vila, M.2    Salameh, A.3    Anobom, C.D.4    Zeitlin, B.D.5    Hawke, D.H.6
  • 79
    • 77949342169 scopus 로고    scopus 로고
    • Small molecule inhibitors of the neuropilin-1 vascular endothelial growth factor A (VEGF-A) interaction
    • Jarvis A, Allerston CK, Jia H, Herzog B, Garza-Garcia A, Winfield N, et al. Small molecule inhibitors of the neuropilin-1 vascular endothelial growth factor A (VEGF-A) interaction. J Med Chem (2010) 53:2215-26. doi:10.1021/jm901755g
    • (2010) J Med Chem , vol.53 , pp. 2215-2226
    • Jarvis, A.1    Allerston, C.K.2    Jia, H.3    Herzog, B.4    Garza-Garcia, A.5    Winfield, N.6
  • 80
    • 84905100973 scopus 로고    scopus 로고
    • Discovery of novel inhibitors of vascular endothelial growth factor-A-Neuropilin-1 interaction by structure-based virtual screening
    • Starzec A, Miteva MA, Ladam P, Villoutreix BO, Perret GY. Discovery of novel inhibitors of vascular endothelial growth factor-A-Neuropilin-1 interaction by structure-based virtual screening. Bioorg Med Chem (2014) 22:4042-8. doi:10.1016/j.bmc.2014.05.068
    • (2014) Bioorg Med Chem , vol.22 , pp. 4042-4048
    • Starzec, A.1    Miteva, M.A.2    Ladam, P.3    Villoutreix, B.O.4    Perret, G.Y.5
  • 81
    • 78650188526 scopus 로고    scopus 로고
    • Small interfering RNAs induce target-independent inhibition of tumor growth and vasculature remodeling in a mouse model of hepatocellular carcinoma
    • Bergé M, Bonnin P, Sulpice E, Vilar J, Allanic D, Silvestre JS, et al. Small interfering RNAs induce target-independent inhibition of tumor growth and vasculature remodeling in a mouse model of hepatocellular carcinoma. Am J Pathol (2010) 177:3192-201. doi:10.2353/ajpath.2010.100157
    • (2010) Am J Pathol , vol.177 , pp. 3192-3201
    • Bergé, M.1    Bonnin, P.2    Sulpice, E.3    Vilar, J.4    Allanic, D.5    Silvestre, J.S.6
  • 82
    • 76549103146 scopus 로고    scopus 로고
    • Inhibition of neuropilin-1 by RNA-interference and its angiostatic potential in the treatment of hepatocellular carcinoma
    • Raskopf E, Vogt A, Standop J, Sauerbruch T, Schmitz V. Inhibition of neuropilin-1 by RNA-interference and its angiostatic potential in the treatment of hepatocellular carcinoma. Z Gastroenterol (2010) 48:21-7. doi:10.1055/s-0028-1109907
    • (2010) Z Gastroenterol , vol.48 , pp. 21-27
    • Raskopf, E.1    Vogt, A.2    Standop, J.3    Sauerbruch, T.4    Schmitz, V.5
  • 83
    • 38849094477 scopus 로고    scopus 로고
    • Neuropilin-1 in acute myeloid leukemia: expression and role in proliferation and migration of leukemia cells
    • Lu L, Zhang L, Xiao Z, Lu S, Yang R, Han ZC. Neuropilin-1 in acute myeloid leukemia: expression and role in proliferation and migration of leukemia cells. Leuk Lymphoma (2008) 49:331-8. doi:10.1080/10428190701809149
    • (2008) Leuk Lymphoma , vol.49 , pp. 331-338
    • Lu, L.1    Zhang, L.2    Xiao, Z.3    Lu, S.4    Yang, R.5    Han, Z.C.6
  • 84
    • 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 DC, Rees CG, Duchesne L, Patey SJ, Terry CJ, Turnbull JE, 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 (2005) 280:13457-64. doi:10.1074/jbc.M410924200
    • (2005) J Biol Chem , vol.280 , pp. 13457-13464
    • West, D.C.1    Rees, C.G.2    Duchesne, L.3    Patey, S.J.4    Terry, C.J.5    Turnbull, J.E.6
  • 85
    • 82155192283 scopus 로고    scopus 로고
    • MicroRNA-181b and microRNA-9 mediate arsenic-induced angiogenesis via NRP1
    • Cui Y, Han Z, Hu Y, Song G, Hao C, Xia H, et al. MicroRNA-181b and microRNA-9 mediate arsenic-induced angiogenesis via NRP1. J Cell Physiol. (2012) 227:772-83. doi:10.1002/jcp.22789
    • (2012) J Cell Physiol. , vol.227 , pp. 772-783
    • Cui, Y.1    Han, Z.2    Hu, Y.3    Song, G.4    Hao, C.5    Xia, H.6
  • 86
    • 84892736489 scopus 로고    scopus 로고
    • miR-320 regulates tumor angiogenesis driven by vascular endothelial cells in oral cancer by silencing neuropilin 1
    • Wu YY, Chen YL, Jao YC, Hsieh IS, Chang KC, Hong TM. miR-320 regulates tumor angiogenesis driven by vascular endothelial cells in oral cancer by silencing neuropilin 1. Angiogenes1is (2014) 17:247-60. doi:10.1007/s10456-013-9394-1
    • (2014) Angiogenes1is , vol.17 , pp. 247-260
    • Wu, Y.Y.1    Chen, Y.L.2    Jao, Y.C.3    Hsieh, I.S.4    Chang, K.C.5    Hong, T.M.6
  • 87
    • 84863032564 scopus 로고    scopus 로고
    • microRNA-320a inhibits tumor invasion by targeting neuropilin1 and is associated with liver metastasis in colorectal cancer
    • Zhang Y, He X, Liu Y, Ye Y, Zhang H, He P, et al. microRNA-320a inhibits tumor invasion by targeting neuropilin1 and is associated with liver metastasis in colorectal cancer. Oncol Rep (2012) 27:685-94. doi:10.3892/or.2011.1561
    • (2012) Oncol Rep , vol.27 , pp. 685-694
    • Zhang, Y.1    He, X.2    Liu, Y.3    Ye, Y.4    Zhang, H.5    He, P.6
  • 89
    • 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) 106:16157-62. doi:10.1073/pnas.0908201106
    • (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
  • 91
    • 84865258883 scopus 로고    scopus 로고
    • Transtumoral targeting enabled by a novel neuropilin-binding peptide
    • Roth L, Agemy L, Kotamraju VR, Braun G, Teesalu T, Sugahara KN, et al. Transtumoral targeting enabled by a novel neuropilin-binding peptide. Oncogene (2011) 31(33):3754-63. doi:10.1038/onc.2011.537
    • (2011) Oncogene , vol.31 , Issue.33 , pp. 3754-3763
    • Roth, L.1    Agemy, L.2    Kotamraju, V.R.3    Braun, G.4    Teesalu, T.5    Sugahara, K.N.6
  • 92
    • 77952901022 scopus 로고    scopus 로고
    • Coadministration of a tumor-penetrating peptide enhances the efficacy of cancer drugs
    • Sugahara KN, Teesalu T, Karmali PP, Kotamraju VR, Agemy L, Greenwald DR, et al. Coadministration of a tumor-penetrating peptide enhances the efficacy of cancer drugs. Science (2010) 328:1031-5. doi:10.1126/science.1183057
    • (2010) Science , vol.328 , pp. 1031-1035
    • Sugahara, K.N.1    Teesalu, T.2    Karmali, P.P.3    Kotamraju, V.R.4    Agemy, L.5    Greenwald, D.R.6
  • 93
    • 84920271862 scopus 로고    scopus 로고
    • A comprehensive study of iRGD-modified liposomes with improved chemotherapeutic efficacy on B16 melanoma
    • Dai W, Fan Y, Zhang H, Wang X, Zhang Q, Wang X. A comprehensive study of iRGD-modified liposomes with improved chemotherapeutic efficacy on B16 melanoma. Drug Del. (2015) 22:10-20. doi:10.3109/10717544.2014.903580
    • (2015) Drug Del. , vol.22 , pp. 10-20
    • Dai, W.1    Fan, Y.2    Zhang, H.3    Wang, X.4    Zhang, Q.5    Wang, X.6
  • 94
    • 81355122667 scopus 로고    scopus 로고
    • Gold nanoparticles functionalized with therapeutic andtargeted peptides for cancer treatment
    • Kumar A, Ma H, Zhang X, Huang K, Jin S, Liu J, et al. Gold nanoparticles functionalized with therapeutic andtargeted peptides for cancer treatment. Biomaterials (2012) 33:1180-9. doi:10.1016/j.biomaterials.2011.10.058
    • (2012) Biomaterials , vol.33 , pp. 1180-1189
    • Kumar, A.1    Ma, H.2    Zhang, X.3    Huang, K.4    Jin, S.5    Liu, J.6
  • 95
    • 84889091074 scopus 로고    scopus 로고
    • Challenging resistance mechanisms to therapies for metastatic melanoma
    • Tentori L, Lacal PM, Graziani G. Challenging resistance mechanisms to therapies for metastatic melanoma. Trends Pharmacol Sci (2013) 34:656-66. doi:10.1016/j.tips.2013.10.003
    • (2013) Trends Pharmacol Sci , vol.34 , pp. 656-666
    • Tentori, L.1    Lacal, P.M.2    Graziani, G.3
  • 96
    • 73349134996 scopus 로고    scopus 로고
    • Spontaneous regression of metastases from melanoma: review of the literature
    • Kalialis LV, Drzewiecki KT, Klyver H. Spontaneous regression of metastases from melanoma: review of the literature. Melanoma Res (2009) 19:275-82. doi:10.1097/CMR.0b013e32832eabd5
    • (2009) Melanoma Res , vol.19 , pp. 275-282
    • Kalialis, L.V.1    Drzewiecki, K.T.2    Klyver, H.3
  • 97
    • 84865559786 scopus 로고    scopus 로고
    • Melanoma as a model tumour for immuno-oncology
    • Maio M. Melanoma as a model tumour for immuno-oncology. Ann Oncol (2012) 8:viii10-4. doi:10.1093/annonc/mds257
    • (2012) Ann Oncol , vol.8 , pp. 810-814
    • Maio, M.1
  • 98
    • 77956934219 scopus 로고    scopus 로고
    • Effect of vascular endothelial growth factor and its receptor KDR on the transendothelial migration and local trafficking of human T cells in vitro and in vivo
    • Edelbauer M, Datta D, Vos IH, Basu A, Stack MP, Reinders ME, et al. Effect of vascular endothelial growth factor and its receptor KDR on the transendothelial migration and local trafficking of human T cells in vitro and in vivo. Blood (2010) 116:1980-9. doi:10.1182/blood-2009-11-252460
    • (2010) Blood , vol.116 , pp. 1980-1989
    • Edelbauer, M.1    Datta, D.2    Vos, I.H.3    Basu, A.4    Stack, M.P.5    Reinders, M.E.6
  • 99
    • 84897107439 scopus 로고    scopus 로고
    • VEGF-A promotes IL-17A-producing γ?δ T cell accumulation in mouse skin and serves as a chemotactic factor for plasmacytoid dendritic cells
    • Suzuki T, Hirakawa S, Shimauchi T, Ito T, Sakabe J, Detmar M, et al. VEGF-A promotes IL-17A-producing γ?δ T cell accumulation in mouse skin and serves as a chemotactic factor for plasmacytoid dendritic cells. J Dermatol Sci (2014) 74:116-24. doi:10.1016/j.jdermsci.2013.12.013
    • (2014) J Dermatol Sci , vol.74 , pp. 116-124
    • Suzuki, T.1    Hirakawa, S.2    Shimauchi, T.3    Ito, T.4    Sakabe, J.5    Detmar, M.6
  • 100
    • 84869777544 scopus 로고    scopus 로고
    • Neuropilin 1 deficiency on CD4+Foxp3+ regulatory T cells impairs mouse melanoma growth
    • Hansen W, Hutzler M, Abel S, Alter C, Stockmann C, Kliche S, et al. Neuropilin 1 deficiency on CD4+Foxp3+ regulatory T cells impairs mouse melanoma growth. J Exp Med (2012) 209:2001-16. doi:10.1084/jem.20111497
    • (2012) J Exp Med , vol.209 , pp. 2001-2016
    • Hansen, W.1    Hutzler, M.2    Abel, S.3    Alter, C.4    Stockmann, C.5    Kliche, S.6
  • 101
    • 84939251884 scopus 로고    scopus 로고
    • Prognostic and predictive significance of immune cells infiltrating cutaneous melanoma
    • Ladányi A. Prognostic and predictive significance of immune cells infiltrating cutaneous melanoma. Pigment Cell Melanoma Res (2015). doi:10.1111/pcmr.12371
    • (2015) Pigment Cell Melanoma Res
    • Ladányi, A.1
  • 102
    • 0037057655 scopus 로고    scopus 로고
    • Class IV semaphorin Sema4A enhances T-cell activation and interacts with Tim-2
    • Kumanogoh A, Marukawa S, Suzuki K, Takegahara N, Watanabe C, Ch'ng E, et al. Class IV semaphorin Sema4A enhances T-cell activation and interacts with Tim-2. Nature (2002) 419:629-33. doi:10.1038/nature01037
    • (2002) Nature , vol.419 , pp. 629-633
    • Kumanogoh, A.1    Marukawa, S.2    Suzuki, K.3    Takegahara, N.4    Watanabe, C.5    Ch'ng, E.6
  • 103
    • 84884206864 scopus 로고    scopus 로고
    • Stability and function of regulatory T cells is maintained by a neuropilin-1-semaphorin-4a axis
    • Delgoffe GM, Woo SR, Turnis ME, Gravano DM, Guy C, Overacre AE, et al. Stability and function of regulatory T cells is maintained by a neuropilin-1-semaphorin-4a axis. Nature (2013) 501:252-6. doi:10.1038/nature12428
    • (2013) Nature , vol.501 , pp. 252-256
    • Delgoffe, G.M.1    Woo, S.R.2    Turnis, M.E.3    Gravano, D.M.4    Guy, C.5    Overacre, A.E.6
  • 104
    • 84859708396 scopus 로고    scopus 로고
    • Maximizing tumour exposure to anti-neuropilin-1 antibody requires saturation of non-tumour tissue antigenic sinks in mice
    • Bumbaca D, Xiang H, Boswell CA, Port RE, Stainton SL, Mundo EE, et al. Maximizing tumour exposure to anti-neuropilin-1 antibody requires saturation of non-tumour tissue antigenic sinks in mice. Br J Pharmacol (2012) 166:368-77. doi:10.1111/j.1476-5381.2011.01777.x
    • (2012) Br J Pharmacol , vol.166 , pp. 368-377
    • Bumbaca, D.1    Xiang, H.2    Boswell, C.A.3    Port, R.E.4    Stainton, S.L.5    Mundo, E.E.6
  • 105
    • 80053380547 scopus 로고    scopus 로고
    • Advanced glycation end products inhibit adhesion ability of differentiated podocytes in a neuropilin-1-dependent manner
    • Bondeva T, Wojciech S, Wolf G. Advanced glycation end products inhibit adhesion ability of differentiated podocytes in a neuropilin-1-dependent manner. Am J Physiol Renal Physiol (2011) 301:F852-70. doi:10.1152/ajprenal.00575.2010
    • (2011) Am J Physiol Renal Physiol , vol.301 , pp. F852-F870
    • Bondeva, T.1    Wojciech, S.2    Wolf, G.3


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