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Volumn 3 AUG, Issue , 2013, Pages

Tumor-penetrating peptides

Author keywords

v integrins; C end Rule; Homing peptide; Neuropilin 1; Synaphic targeting; Tumor penetrating peptide

Indexed keywords

CELL PENETRATING PEPTIDE; DOXORUBICIN; IRGD PEPTIDE; LYP 1 PEPTIDE; NEUROPILIN 1; PACLITAXEL; SEMAPHORIN; TRASTUZUMAB; TUFTSIN; TUMOR PENETRATING PEPTIDE; UNCLASSIFIED DRUG; VASCULOTROPIN;

EID: 84891128382     PISSN: None     EISSN: 2234943X     Source Type: Journal    
DOI: 10.3389/fonc.2013.00216     Document Type: Review
Times cited : (173)

References (62)
  • 1
    • 77949762340 scopus 로고    scopus 로고
    • Targeting of drugs and nanoparticles to tumors
    • doi:10.1083/jcb.200910104
    • Ruoslahti E, Bhatia SN, Sailor MJ. Targeting of drugs and nanoparticles to tumors. J Cell Biol (2010) 188:759-68. doi:10.1083/jcb.200910104
    • (2010) J Cell Biol , vol.188 , pp. 759-768
    • Ruoslahti, E.1    Bhatia, S.N.2    Sailor, M.J.3
  • 2
    • 0032710319 scopus 로고    scopus 로고
    • Clinical applications of angiogenic growth factors and their inhibitors
    • doi:10.1038/9467
    • Ferrara N, Alitalo K. Clinical applications of angiogenic growth factors and their inhibitors. Nat Med (1999) 5:1359-64. doi:10.1038/9467
    • (1999) Nat Med , vol.5 , pp. 1359-1364
    • Ferrara, N.1    Alitalo, K.2
  • 3
    • 13844315323 scopus 로고    scopus 로고
    • Angiostatic peptides use plasma fibronectin to home to angiogenic vasculature
    • doi:10.1073/pnas.0409844102
    • Akerman ME, Pilch J, Peters D, Ruoslahti E. Angiostatic peptides use plasma fibronectin to home to angiogenic vasculature. Proc Natl Acad Sci U S A (2005) 102:2040-5. doi:10.1073/pnas.0409844102
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 2040-2045
    • Akerman, M.E.1    Pilch, J.2    Peters, D.3    Ruoslahti, E.4
  • 4
    • 84864125045 scopus 로고    scopus 로고
    • Peptides as targeting elements and tissue penetration devices for nanoparticles
    • doi:10.1002/adma.201200454
    • Ruoslahti E. Peptides as targeting elements and tissue penetration devices for nanoparticles. Adv Mater (2012) 24:3747-56. doi:10.1002/adma.201200454
    • (2012) Adv Mater , vol.24 , pp. 3747-3756
    • Ruoslahti, E.1
  • 5
    • 0029153736 scopus 로고
    • High endothelial venules (HEVs), specialized endothelium for lymphocyte migration
    • doi:10.1016/0167-5699(95)80023-9
    • Girard JP, Springer TA. High endothelial venules (HEVs), specialized endothelium for lymphocyte migration. Immunol Today (1995) 16:449-57. doi:10.1016/0167-5699(95)80023-9
    • (1995) Immunol Today , vol.16 , pp. 449-457
    • Girard, J.P.1    Springer, T.A.2
  • 6
    • 77953033326 scopus 로고    scopus 로고
    • The vascular biology of atherosclerosis and imaging targets
    • doi:10.2967/jnumed.109.069633
    • Libby P, DiCarli M, Weissleder R. The vascular biology of atherosclerosis and imaging targets. J Nucl Med (2010) 51(Suppl 1):33S-7. doi:10.2967/jnumed.109.069633
    • (2010) J Nucl Med , vol.51 , Issue.SUPPL. 1
    • Libby, P.1    DiCarli, M.2    Weissleder, R.3
  • 7
    • 52049123781 scopus 로고    scopus 로고
    • Mitochondrial/cell-surface protein p32/gC1qR as a molecular target in tumor cells and tumor stroma
    • doi:10.1158/0008-5472.CAN-07-6752
    • Fogal V, Zhang L, Krajewski S, Ruoslahti E. Mitochondrial/cell-surface protein p32/gC1qR as a molecular target in tumor cells and tumor stroma. Cancer Res (2008) 68:7210-8. doi:10.1158/0008-5472.CAN-07-6752
    • (2008) Cancer Res , vol.68 , pp. 7210-7218
    • Fogal, V.1    Zhang, L.2    Krajewski, S.3    Ruoslahti, E.4
  • 8
    • 0030325017 scopus 로고    scopus 로고
    • Tissue targeting with phage peptide libraries
    • Pasqualini R, Ruoslahti E. Tissue targeting with phage peptide libraries. Mol Psychiatry (1996) 1:423.
    • (1996) Mol Psychiatry , vol.1 , pp. 423
    • Pasqualini, R.1    Ruoslahti, E.2
  • 9
    • 84855582590 scopus 로고    scopus 로고
    • Mapping of vascular ZIP codes by phage display
    • doi:10.1016/B978-0-12-396962-0.00002-1
    • Teesalu T, Sugahara KN, Ruoslahti E. Mapping of vascular ZIP codes by phage display. Methods Enzymol (2012) 503:35-56. doi:10.1016/B978-0-12-396962-0.00002-1
    • (2012) Methods Enzymol , vol.503 , pp. 35-56
    • Teesalu, T.1    Sugahara, K.N.2    Ruoslahti, E.3
  • 10
    • 0036063778 scopus 로고    scopus 로고
    • A tumor-homing peptide with a targeting specificity related to lymphatic vessels
    • Laakkonen P, Porkka K, Hoffman JA, Ruoslahti E. A tumor-homing peptide with a targeting specificity related to lymphatic vessels. Nat Med (2002) 8:751-5.
    • (2002) Nat Med , vol.8 , pp. 751-755
    • Laakkonen, P.1    Porkka, K.2    Hoffman, J.A.3    Ruoslahti, E.4
  • 11
    • 3042687629 scopus 로고    scopus 로고
    • Antitumor activity of a homing peptide that targets tumor lymphatics and tumor cells
    • doi:10.1073/pnas.0403317101
    • Laakkonen P, Akerman ME, Biliran H, Yang M, Ferrer F, Karpanen T, et al. Antitumor activity of a homing peptide that targets tumor lymphatics and tumor cells. Proc Natl Acad Sci U S A (2004) 101:9381-6. doi:10.1073/pnas.0403317101
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 9381-9386
    • Laakkonen, P.1    Akerman, M.E.2    Biliran, H.3    Yang, M.4    Ferrer, F.5    Karpanen, T.6
  • 12
    • 70349482671 scopus 로고    scopus 로고
    • C-end rule peptides mediate neuropilin-1-dependent cell, vascular, and tissue penetration
    • doi:10.1073/pnas.0908201106
    • 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 U S A (2009) 106:16157-62. doi:10.1073/pnas.0908201106
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 16157-16162
    • Teesalu, T.1    Sugahara, K.N.2    Kotamraju, V.R.3    Ruoslahti, E.4
  • 13
    • 70749103751 scopus 로고    scopus 로고
    • Tissue-penetrating delivery of compounds and nanoparticles into tumors
    • doi:10.1016/j.ccr.2009.10.013
    • Sugahara KN, Teesalu T, Karmali PP, Kotamraju VR, Agemy L, Girard OM, et al. Tissue-penetrating delivery of compounds and nanoparticles into tumors. Cancer Cell (2009) 16:510-20. doi:10.1016/j.ccr.2009.10.013
    • (2009) Cancer Cell , vol.16 , pp. 510-520
    • Sugahara, K.N.1    Teesalu, T.2    Karmali, P.P.3    Kotamraju, V.R.4    Agemy, L.5    Girard, O.M.6
  • 14
    • 0025112794 scopus 로고
    • Searching for peptide ligands with an epitope library
    • doi:10.1126/science.1696028
    • Scott JK, Smith GP. Searching for peptide ligands with an epitope library. Science (1990) 249:386-90. doi:10.1126/science.1696028
    • (1990) Science , vol.249 , pp. 386-390
    • Scott, J.K.1    Smith, G.P.2
  • 15
    • 0021818675 scopus 로고
    • Filamentous fusion phage, novel expression vectors that display cloned antigens on the virion surface
    • doi:10.1126/science.4001944
    • Smith GP. Filamentous fusion phage, novel expression vectors that display cloned antigens on the virion surface. Science (1985) 228:1315-7. doi:10.1126/science.4001944
    • (1985) Science , vol.228 , pp. 1315-1317
    • Smith, G.P.1
  • 16
    • 0027267959 scopus 로고
    • Selection of peptides binding to the alpha 5 beta 1 integrin from phage display library
    • Koivunen E, Gay DA, Ruoslahti E. Selection of peptides binding to the alpha 5 beta 1 integrin from phage display library. J Biol Chem (1993) 268:20205-10.
    • (1993) J Biol Chem , vol.268 , pp. 20205-20210
    • Koivunen, E.1    Gay, D.A.2    Ruoslahti, E.3
  • 18
    • 75749124699 scopus 로고    scopus 로고
    • Neuropilin-2 mediates VEGF-C-induced lymphatic sprouting together with VEGFR3
    • doi:10.1083/jcb.200903137
    • Xu Y, Yuan L, Mak J, Pardanaud L, Caunt M, Kasman I, et al. Neuropilin-2 mediates VEGF-C-induced lymphatic sprouting together with VEGFR3. J Cell Biol (2010) 188:115-30. doi:10.1083/jcb.200903137
    • (2010) J Cell Biol , vol.188 , pp. 115-130
    • Xu, Y.1    Yuan, L.2    Mak, J.3    Pardanaud, L.4    Caunt, M.5    Kasman, I.6
  • 19
    • 0030847193 scopus 로고    scopus 로고
    • Neuropilin is a receptor for the axonal chemorepellent semaphorin III
    • doi:10.1016/S0092-8674(00)80534-6
    • 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
  • 20
    • 0032549799 scopus 로고    scopus 로고
    • Neuropilin-1 is expressed by endothelial and tumor cells as an isoform-specific receptor for vascular endothelial growth factor
    • doi:10.1016/S0092-8674(00)81402-6
    • 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
  • 21
    • 33646822526 scopus 로고    scopus 로고
    • Tuftsin binds neuropilin-1 through a sequence similar to that encoded by exon 8 of vascular endothelial growth factor
    • doi:10.1074/jbc.M511941200
    • von Wronski MA, Raju N, Pillai R, Bogdan NJ, Marinelli ER, Nanjappan P, et al. Tuftsin binds neuropilin-1 through a sequence similar to that encoded by exon 8 of vascular endothelial growth factor. J Biol Chem (2006) 281:5702-10. doi:10.1074/jbc.M511941200
    • (2006) J Biol Chem , vol.281 , pp. 5702-5710
    • von Wronski, M.A.1    Raju, N.2    Pillai, R.3    Bogdan, N.J.4    Marinelli, E.R.5    Nanjappan, P.6
  • 22
    • 0020569813 scopus 로고
    • Structural requirements for microvascular permeability-increasing ability of peptides. Studies on analogues of a fibrinogen pentapeptide fragment
    • doi:10.1016/0304-4165(83)90063-6
    • Gerdin B, Lindeberg G, Ragnarsson U, Saldeen T, Wallin R. Structural requirements for microvascular permeability-increasing ability of peptides. Studies on analogues of a fibrinogen pentapeptide fragment. Biochim Biophys Acta (1983) 757:366-70. doi:10.1016/0304-4165(83)90063-6
    • (1983) Biochim Biophys Acta , vol.757 , pp. 366-370
    • Gerdin, B.1    Lindeberg, G.2    Ragnarsson, U.3    Saldeen, T.4    Wallin, R.5
  • 24
    • 79952407244 scopus 로고    scopus 로고
    • Binding of a C-end rule peptide to the neuropilin-1 receptor, a molecular modeling approach
    • doi:10.1021/bi101662j
    • 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) 50:1755-62. doi:10.1021/bi101662j
    • (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
  • 25
    • 84876719609 scopus 로고    scopus 로고
    • Sequence dependence of C-end rule peptides in binding and activation of neuropilin-1 receptor
    • doi:10.1016/j.jsb.2013.02.006
    • Zanuy D, Kotla R, Nussinov R, Teesalu T, Sugahara KN, Aleman C, et al. Sequence dependence of C-end rule peptides in binding and activation of neuropilin-1 receptor. J Struct Biol (2013) 182:78-86. doi:10.1016/j.jsb.2013.02.006
    • (2013) J Struct Biol , vol.182 , pp. 78-86
    • Zanuy, D.1    Kotla, R.2    Nussinov, R.3    Teesalu, T.4    Sugahara, K.N.5    Aleman, C.6
  • 26
    • 84879005229 scopus 로고    scopus 로고
    • Design of a Cyclotide antagonist of neuropilin-1 and-2 that potently inhibits endothelial cell migration
    • doi:10.1021/cb4000585
    • Getz JA, Cheneval O, Craik DJ, Daugherty PS. Design of a Cyclotide antagonist of neuropilin-1 and-2 that potently inhibits endothelial cell migration. ACS Chem Biol (2013) 8:1147-54. doi:10.1021/cb4000585
    • (2013) ACS Chem Biol , vol.8 , pp. 1147-1154
    • Getz, J.A.1    Cheneval, O.2    Craik, D.J.3    Daugherty, P.S.4
  • 27
    • 42649132183 scopus 로고    scopus 로고
    • Neuropilins, a versatile partner of extracellular molecules that regulate development and disease
    • doi:10.2741/3008
    • Uniewicz KA, Fernig DG. Neuropilins, a versatile partner of extracellular molecules that regulate development and disease. Front Biosci (2008) 13:4339-60. doi:10.2741/3008
    • (2008) Front Biosci , vol.13 , pp. 4339-4360
    • Uniewicz, K.A.1    Fernig, D.G.2
  • 28
    • 63449090307 scopus 로고    scopus 로고
    • Neuropilins in tumor biology
    • doi:10.1158/1078-0432.CCR-08-0563
    • Bagri A, Tessier-Lavigne M, Watts RJ. Neuropilins in tumor biology. Clin Cancer Res (2009) 15:1860-4. doi:10.1158/1078-0432.CCR-08-0563
    • (2009) Clin Cancer Res , vol.15 , pp. 1860-1864
    • Bagri, A.1    Tessier-Lavigne, M.2    Watts, R.J.3
  • 29
    • 42449148407 scopus 로고    scopus 로고
    • Neuropilins, structure, function and role in disease
    • doi:10.1042/BJ20071639
    • 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
  • 30
    • 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
    • doi:10.1074/jbc.M512121200
    • Jia H, Bagherzadeh A, Hartzoulakis B, Jarvis A, Lohr 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    Lohr, M.5    Shaikh, S.6
  • 31
    • 34548064808 scopus 로고    scopus 로고
    • Targeting neuropilin 1 as an antitumor strategy in lung cancer
    • doi:10.1158/1078-0432.CCR-07-0001
    • 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
  • 32
    • 33845969276 scopus 로고    scopus 로고
    • Function blocking antibodies to neuropilin-1 generated from a designed human synthetic antibody phage library
    • doi:10.1016/j.jmb.2006.11.021
    • 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
  • 34
    • 77951622512 scopus 로고    scopus 로고
    • Peptide-based interference of the transmembrane domain of neuropilin-1 inhibits glioma growth in vivo
    • doi:10.1038/onc.2010.9
    • Nasarre C, Roth M, Jacob L, Roth L, Koncina E, Thien A, et al. Peptide-based interference of the transmembrane domain of neuropilin-1 inhibits glioma growth in vivo. Oncogene (2010) 29:2381-92. doi:10.1038/onc.2010.9
    • (2010) Oncogene , vol.29 , pp. 2381-2392
    • Nasarre, C.1    Roth, M.2    Jacob, L.3    Roth, L.4    Koncina, E.5    Thien, A.6
  • 35
    • 0027051024 scopus 로고
    • Bradykinin-degrading enzymes, structure, function, distribution, and potential roles in cardiovascular pharmacology
    • doi:10.1097/00005344-199206209-00002
    • Skidgel RA. Bradykinin-degrading enzymes, structure, function, distribution, and potential roles in cardiovascular pharmacology. J Cardiovasc Pharmacol (1992) 20(Suppl 9):S4-9. doi:10.1097/00005344-199206209-00002
    • (1992) J Cardiovasc Pharmacol , vol.20 , Issue.SUPPL. 9
    • Skidgel, R.A.1
  • 36
    • 0035074497 scopus 로고    scopus 로고
    • The vesiculo-vacuolar organelle (VVO). A new endothelial cell permeability organelle
    • doi:10.1177/002215540104900401
    • Dvorak AM, Feng D. The vesiculo-vacuolar organelle (VVO). A new endothelial cell permeability organelle. J Histochem Cytochem (2001) 49:419-32. doi:10.1177/002215540104900401
    • (2001) J Histochem Cytochem , vol.49 , pp. 419-432
    • Dvorak, A.M.1    Feng, D.2
  • 37
    • 84865258883 scopus 로고    scopus 로고
    • Transtumoral targeting enabled by a novel neuropilin-binding peptide
    • doi:10.1038/onc.2011.537
    • Roth L, Agemy L, Kotamraju VR, Braun G, Teesalu T, Sugahara KN, et al. Transtumoral targeting enabled by a novel neuropilin-binding peptide. Oncogene (2012) 31:3754-63. doi:10.1038/onc.2011.537
    • (2012) Oncogene , vol.31 , pp. 3754-3763
    • Roth, L.1    Agemy, L.2    Kotamraju, V.R.3    Braun, G.4    Teesalu, T.5    Sugahara, K.N.6
  • 38
    • 77952901022 scopus 로고    scopus 로고
    • Coadministration of a tumor-penetrating peptide enhances the efficacy of cancer drugs
    • doi:10.1126/science.1183057
    • 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
  • 39
    • 0025201350 scopus 로고
    • Evidence that the N-terminal domain of nonstructural protein NS3 from yellow fever virus is a serine protease responsible for site-specific cleavages in the viral polyprotein
    • doi:10.1073/pnas.87.22.8898
    • Chambers TJ, Weir RC, Grakoui A, McCourt DW, Bazan JF, Fletterick RJ, et al. Evidence that the N-terminal domain of nonstructural protein NS3 from yellow fever virus is a serine protease responsible for site-specific cleavages in the viral polyprotein. Proc Natl Acad Sci U S A (1990) 87:8898-902. doi:10.1073/pnas.87.22.8898
    • (1990) Proc Natl Acad Sci U S A , vol.87 , pp. 8898-8902
    • Chambers, T.J.1    Weir, R.C.2    Grakoui, A.3    McCourt, D.W.4    Bazan, J.F.5    Fletterick, R.J.6
  • 40
    • 0032949982 scopus 로고    scopus 로고
    • Endoproteolytic processing of the ebola virus envelope glycoprotein, cleavage is not required for function
    • Wool-Lewis RJ, Bates P. Endoproteolytic processing of the ebola virus envelope glycoprotein, cleavage is not required for function. J Virol (1999) 73:1419-26.
    • (1999) J Virol , vol.73 , pp. 1419-1426
    • Wool-Lewis, R.J.1    Bates, P.2
  • 41
    • 33646729280 scopus 로고    scopus 로고
    • Furin cleavage potentiates the membrane fusion-controlling intersubunit disulfide bond isomerization activity of leukemia virus Env
    • doi:10.1128/JVI.01851-05
    • Sjöberg M, Wallin M, Lindqvist B, Garoff H. Furin cleavage potentiates the membrane fusion-controlling intersubunit disulfide bond isomerization activity of leukemia virus Env. J Virol (2006) 80:5540-51. doi:10.1128/JVI.01851-05
    • (2006) J Virol , vol.80 , pp. 5540-5551
    • Sjöberg, M.1    Wallin, M.2    Lindqvist, B.3    Garoff, H.4
  • 42
    • 33645967164 scopus 로고    scopus 로고
    • Crimean-congo hemorrhagic fever virus glycoprotein precursor is cleaved by furin-like and SKI-1 proteases to generate a novel 38-kilodalton glycoprotein
    • doi:10.1128/JVI.80.1.514-525.2006
    • Sanchez AJ, Vincent MJ, Erickson BR, Nichol ST. Crimean-congo hemorrhagic fever virus glycoprotein precursor is cleaved by furin-like and SKI-1 proteases to generate a novel 38-kilodalton glycoprotein. J Virol (2006) 80:514-25. doi:10.1128/JVI.80.1.514-525.2006
    • (2006) J Virol , vol.80 , pp. 514-525
    • Sanchez, A.J.1    Vincent, M.J.2    Erickson, B.R.3    Nichol, S.T.4
  • 43
    • 0026775916 scopus 로고
    • Human furin is a calcium-dependent serine endoprotease that recognizes the sequence arg-X-X-arg and efficiently cleaves anthrax toxin protective antigen
    • Molloy SS, Bresnahan PA, Leppla SH, Klimpel KR, Thomas G. Human furin is a calcium-dependent serine endoprotease that recognizes the sequence arg-X-X-arg and efficiently cleaves anthrax toxin protective antigen. J Biol Chem (1992) 267:16396-402.
    • (1992) J Biol Chem , vol.267 , pp. 16396-16402
    • Molloy, S.S.1    Bresnahan, P.A.2    Leppla, S.H.3    Klimpel, K.R.4    Thomas, G.5
  • 44
    • 0032535999 scopus 로고    scopus 로고
    • Cancer treatment by targeted drug delivery to tumor vasculature in a mouse model
    • doi:10.1126/science.279.5349.377
    • Arap W, Pasqualini R, Ruoslahti E. Cancer treatment by targeted drug delivery to tumor vasculature in a mouse model. Science (1998) 279:377-80. doi:10.1126/science.279.5349.377
    • (1998) Science , vol.279 , pp. 377-380
    • Arap, W.1    Pasqualini, R.2    Ruoslahti, E.3
  • 45
    • 0028899525 scopus 로고
    • Phage libraries displaying cyclic peptides with different ring sizes, ligand specificities of the RGD-directed integrins
    • doi:10.1038/nbt0395-265
    • Koivunen E, Wang B, Ruoslahti E. Phage libraries displaying cyclic peptides with different ring sizes, ligand specificities of the RGD-directed integrins. Biotechnology (N Y) (1995) 13:265-70. doi:10.1038/nbt0395-265
    • (1995) Biotechnology (N Y) , vol.13 , pp. 265-270
    • Koivunen, E.1    Wang, B.2    Ruoslahti, E.3
  • 46
    • 0033950895 scopus 로고    scopus 로고
    • Aminopeptidase N is a receptor for tumor-homing peptides and a target for inhibiting angiogenesis
    • Pasqualini R, Koivunen E, Kain R, Lahdenranta J, Sakamoto M, Stryhn A, et al. Aminopeptidase N is a receptor for tumor-homing peptides and a target for inhibiting angiogenesis. Cancer Res (2000) 60:722-7.
    • (2000) Cancer Res , vol.60 , pp. 722-727
    • Pasqualini, R.1    Koivunen, E.2    Kain, R.3    Lahdenranta, J.4    Sakamoto, M.5    Stryhn, A.6
  • 47
    • 53449088574 scopus 로고    scopus 로고
    • The neovasculature homing motif NGR, more than meets the eye
    • doi:10.1182/blood-2008-04-150862
    • Corti A, Curnis F, Arap W, Pasqualini R. The neovasculature homing motif NGR, more than meets the eye. Blood (2008) 112:2628-35. doi:10.1182/blood-2008-04-150862
    • (2008) Blood , vol.112 , pp. 2628-2635
    • Corti, A.1    Curnis, F.2    Arap, W.3    Pasqualini, R.4
  • 49
    • 38949104405 scopus 로고    scopus 로고
    • Design of a tumor-homing cell-penetrating peptide
    • doi:10.1021/bc0701139
    • Myrberg H, Zhang L, Mae M, Langel U. Design of a tumor-homing cell-penetrating peptide. Bioconjug Chem (2008) 19(1):70-5. doi:10.1021/bc0701139
    • (2008) Bioconjug Chem , vol.19 , Issue.1 , pp. 70-75
    • Myrberg, H.1    Zhang, L.2    Mae, M.3    Langel, U.4
  • 50
    • 35148881028 scopus 로고    scopus 로고
    • Drug resistance and the solid tumor microenvironment
    • doi:10.1093/jnci/djm135
    • Tredan O, Galmarini CM, Patel K, Tannock IF. Drug resistance and the solid tumor microenvironment. J Natl Cancer Inst (2007) 99:1441-54. doi:10.1093/jnci/djm135
    • (2007) J Natl Cancer Inst , vol.99 , pp. 1441-1454
    • Tredan, O.1    Galmarini, C.M.2    Patel, K.3    Tannock, I.F.4
  • 51
    • 29344443251 scopus 로고    scopus 로고
    • The distribution of the anticancer drug doxorubicin in relation to blood vessels in solid tumors
    • doi:10.1158/1078-0432.CCR-05-1664
    • Primeau AJ, Rendon A, Hedley D, Lilge L, Tannock IF. The distribution of the anticancer drug doxorubicin in relation to blood vessels in solid tumors. Clin Cancer Res (2005) 11:8782-8. doi:10.1158/1078-0432.CCR-05-1664
    • (2005) Clin Cancer Res , vol.11 , pp. 8782-8788
    • Primeau, A.J.1    Rendon, A.2    Hedley, D.3    Lilge, L.4    Tannock, I.F.5
  • 52
    • 42249103840 scopus 로고    scopus 로고
    • Direct visualization of heterogeneous extravascular distribution of trastuzumab in human epidermal growth factor receptor type 2 overexpressing xenografts
    • doi:10.1158/1078-0432.CCR-07-4465
    • Baker JH, Lindquist KE, Huxham LA, Kyle AH, Sy JT, Minchinton AI. Direct visualization of heterogeneous extravascular distribution of trastuzumab in human epidermal growth factor receptor type 2 overexpressing xenografts. Clin Cancer Res (2008) 14:2171-9. doi:10.1158/1078-0432.CCR-07-4465
    • (2008) Clin Cancer Res , vol.14 , pp. 2171-2179
    • Baker, J.H.1    Lindquist, K.E.2    Huxham, L.A.3    Kyle, A.H.4    Sy, J.T.5    Minchinton, A.I.6
  • 53
    • 4544333732 scopus 로고    scopus 로고
    • Targeting the tumor vascular compartment to improve conventional cancer therapy
    • doi:10.1016/j.tips.2004.08.008
    • Feron O. Targeting the tumor vascular compartment to improve conventional cancer therapy. Trends Pharmacol Sci (2004) 25:536-42. doi:10.1016/j.tips.2004.08.008
    • (2004) Trends Pharmacol Sci , vol.25 , pp. 536-542
    • Feron, O.1
  • 54
    • 34249294519 scopus 로고    scopus 로고
    • The effect of collagenase and hyaluronidase on transient perfusion in human osteosarcoma xenografts grown orthotopically and in dorsal skinfold chambers
    • Tufto I, Hansen R, Byberg D, Nygaard KHH, Tufto J, Davies CDL. The effect of collagenase and hyaluronidase on transient perfusion in human osteosarcoma xenografts grown orthotopically and in dorsal skinfold chambers. Anticancer Res (2007) 27:1475-81.
    • (2007) Anticancer Res , vol.27 , pp. 1475-1481
    • Tufto, I.1    Hansen, R.2    Byberg, D.3    Nygaard, K.H.H.4    Tufto, J.5    Davies, C.D.L.6
  • 55
    • 77951233373 scopus 로고    scopus 로고
    • Cancer associated fibroblasts (CAFs) in tumor microenvironment
    • doi:10.2741/3613
    • Xing F, Saidou J, Watabe K. Cancer associated fibroblasts (CAFs) in tumor microenvironment. Front Biosci (2010) 15:166-79. doi:10.2741/3613
    • (2010) Front Biosci , vol.15 , pp. 166-179
    • Xing, F.1    Saidou, J.2    Watabe, K.3
  • 57
  • 58
    • 33745107170 scopus 로고    scopus 로고
    • Strategies to improve plasma half life time of peptide and protein drugs
    • doi:10.1007/s00726-005-0289-3
    • Werle M, Bernkop-Schnurch A. Strategies to improve plasma half life time of peptide and protein drugs. Amino Acids (2006) 30:351-67. doi:10.1007/s00726-005-0289-3
    • (2006) Amino Acids , vol.30 , pp. 351-367
    • Werle, M.1    Bernkop-Schnurch, A.2
  • 59
    • 59849110112 scopus 로고    scopus 로고
    • Targeting of albumin-embedded paclitaxel nanoparticles to tumors
    • doi:10.1016/j.nano.2008.07.007
    • Karmali PP, Kotamraju VR, Kastantin M, Black M, Missirlis D, Tirrell M, et al. Targeting of albumin-embedded paclitaxel nanoparticles to tumors. Nanomedicine (2009) 5:73-82. doi:10.1016/j.nano.2008.07.007
    • (2009) Nanomedicine , vol.5 , pp. 73-82
    • Karmali, P.P.1    Kotamraju, V.R.2    Kastantin, M.3    Black, M.4    Missirlis, D.5    Tirrell, M.6
  • 60
    • 79955462137 scopus 로고    scopus 로고
    • Protein cage nanoparticles bearing the LyP-1 peptide for enhanced imaging of macrophage-rich vascular lesions
    • doi:10.1021/nn102863y
    • Uchida M, Kosuge H, Terashima M, Willits DA, Liepold LO, Young MJ, et al. Protein cage nanoparticles bearing the LyP-1 peptide for enhanced imaging of macrophage-rich vascular lesions. ACS Nano (2011) 5:2493-502. doi:10.1021/nn102863y
    • (2011) ACS Nano , vol.5 , pp. 2493-2502
    • Uchida, M.1    Kosuge, H.2    Terashima, M.3    Willits, D.A.4    Liepold, L.O.5    Young, M.J.6
  • 61
    • 79955552146 scopus 로고    scopus 로고
    • Specific penetration and accumulation of a homing peptide within atherosclerotic plaques of apolipoprotein E-deficient mice
    • doi:10.1073/pnas.1104540108
    • Hamzah J, Kotamraju VR, Seo JW, Agemy L, Fogal V, Mahakian LM, et al. Specific penetration and accumulation of a homing peptide within atherosclerotic plaques of apolipoprotein E-deficient mice. Proc Natl Acad Sci U S A (2011) 108:7154-9. doi:10.1073/pnas.1104540108
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 7154-7159
    • Hamzah, J.1    Kotamraju, V.R.2    Seo, J.W.3    Agemy, L.4    Fogal, V.5    Mahakian, L.M.6
  • 62
    • 84862770584 scopus 로고    scopus 로고
    • Imaging tumor-induced sentinel lymph node lymphangiogenesis with LyP-1 peptide
    • doi:10.1007/s00726-011-0976-1
    • Zhang F, Niu G, Lin X, Jacobson O, Ma Y, Eden HS, et al. Imaging tumor-induced sentinel lymph node lymphangiogenesis with LyP-1 peptide. Amino Acids (2012) 42:2343-51. doi:10.1007/s00726-011-0976-1
    • (2012) Amino Acids , vol.42 , pp. 2343-2351
    • Zhang, F.1    Niu, G.2    Lin, X.3    Jacobson, O.4    Ma, Y.5    Eden, H.S.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.