메뉴 건너뛰기




Volumn 57, Issue 15, 2014, Pages 6301-6315

Strategies to inhibit tumor associated integrin receptors: Rationale for dual and multi-antagonists

Author keywords

[No Author keywords available]

Indexed keywords

ALPHAIIBBETA3 INTEGRIN; ALPHAVBETA5 INTEGRIN; ALPHAVBETA6 INTEGRIN; ALPHAVBETA8 INTEGRIN; ANTINEOPLASTIC AGENT; ARGINYLGLYCYLASPARTIC ACID; DISINTEGRIN; INTEGRIN RECEPTOR; UNCLASSIFIED DRUG; VERY LATE ACTIVATION ANTIGEN 5; VITRONECTIN RECEPTOR; ANGIOGENESIS INHIBITOR; ARGINYL-GLYCYL-ASPARTIC ACID; INTEGRIN; OLIGOPEPTIDE;

EID: 84906091809     PISSN: 00222623     EISSN: 15204804     Source Type: Journal    
DOI: 10.1021/jm5000547     Document Type: Review
Times cited : (75)

References (153)
  • 2
    • 8544259562 scopus 로고    scopus 로고
    • Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeutics
    • Xiao, T.; Takagi, J.; Coller, B. S.; Wang, J.-H.; Springer, T. A. Structural basis for allostery in integrins and binding to fibrinogen-mimetic therapeutics Nature 2004, 432, 59-67
    • (2004) Nature , vol.432 , pp. 59-67
    • Xiao, T.1    Takagi, J.2    Coller, B.S.3    Wang, J.-H.4    Springer, T.A.5
  • 11
    • 3142706142 scopus 로고    scopus 로고
    • Competition for talin results in trans-dominant inhibition of integrin activation
    • Calderwood, D. A.; Tai, V.; Di Paolo, G.; De Camilli, P.; Ginsberg, M. H. Competition for talin results in trans-dominant inhibition of integrin activation J. Biol. Chem. 2004, 279, 28889-28895
    • (2004) J. Biol. Chem. , vol.279 , pp. 28889-28895
    • Calderwood, D.A.1    Tai, V.2    Di Paolo, G.3    De Camilli, P.4    Ginsberg, M.H.5
  • 12
    • 77957363101 scopus 로고    scopus 로고
    • Integrins as therapeutic targets: Lessons and opportunities
    • Cox, D.; Brennan, M.; Moran, N. Integrins as therapeutic targets: lessons and opportunities Nat. Rev. Drug Discovery 2010, 9, 804-820
    • (2010) Nat. Rev. Drug Discovery , vol.9 , pp. 804-820
    • Cox, D.1    Brennan, M.2    Moran, N.3
  • 14
    • 21044454333 scopus 로고    scopus 로고
    • Dual antagonists of integrins
    • Nadrah, K.; Dolenc, M. S. Dual antagonists of integrins Curr. Med. Chem. 2005, 12, 1449-1466
    • (2005) Curr. Med. Chem. , vol.12 , pp. 1449-1466
    • Nadrah, K.1    Dolenc, M.S.2
  • 15
    • 34447292152 scopus 로고    scopus 로고
    • Alpha4-integrin antagonism-an effective approach for the treatment of inflammatory diseases?
    • Davenport, R. J.; Munday, J. R. Alpha4-integrin antagonism-an effective approach for the treatment of inflammatory diseases? Drug Discovery Today 2007, 12, 569-576
    • (2007) Drug Discovery Today , vol.12 , pp. 569-576
    • Davenport, R.J.1    Munday, J.R.2
  • 17
    • 0034699501 scopus 로고    scopus 로고
    • Platelet glycoprotein IIb-IIIa antagonists as prototypical integrin blockers: Novel parenteral and potential oral antithrombotic agents
    • Scarborough, R. M.; Gretler, D. D. Platelet glycoprotein IIb-IIIa antagonists as prototypical integrin blockers: novel parenteral and potential oral antithrombotic agents J. Med. Chem. 2000, 43, 3453-3473
    • (2000) J. Med. Chem. , vol.43 , pp. 3453-3473
    • Scarborough, R.M.1    Gretler, D.D.2
  • 18
    • 0033646764 scopus 로고    scopus 로고
    • Potential future clinical applications for the GPIIb/IIIa antagonist, abciximab in thrombosis, vascular and oncological indications
    • Cohen, S. A.; Trikha, M.; Mascelli, M. A. Potential future clinical applications for the GPIIb/IIIa antagonist, abciximab in thrombosis, vascular and oncological indications Pathol. Oncol. Res. 2000, 6, 163-174
    • (2000) Pathol. Oncol. Res. , vol.6 , pp. 163-174
    • Cohen, S.A.1    Trikha, M.2    Mascelli, M.A.3
  • 20
    • 0030919511 scopus 로고    scopus 로고
    • Randomised placebo-controlled trial of the effect of epifibatide on complications of percutaneous coronary intervention: IMPACT-II
    • The IMPACT-II Investigators
    • The IMPACT-II Investigators. Randomised placebo-controlled trial of the effect of epifibatide on complications of percutaneous coronary intervention: IMPACT-II Lancet 1997, 349, 1422-1428
    • (1997) Lancet , vol.349 , pp. 1422-1428
  • 28
    • 77953153938 scopus 로고    scopus 로고
    • Plasma fibronectin promotes lung metastasis by contributions to fibrin clots and tumor cell invasion
    • Malik, G.; Knowles, L. M.; Dhir, R.; Xu, S.; Yang, S.; Ruoslahti, E.; Pilch, J. Plasma fibronectin promotes lung metastasis by contributions to fibrin clots and tumor cell invasion Cancer Res. 2010, 70, 4327-4334
    • (2010) Cancer Res. , vol.70 , pp. 4327-4334
    • Malik, G.1    Knowles, L.M.2    Dhir, R.3    Xu, S.4    Yang, S.5    Ruoslahti, E.6    Pilch, J.7
  • 32
    • 78650304364 scopus 로고    scopus 로고
    • Integrins and bone metastasis: Integrating tumor cell and stromal cell interactions
    • Schneider, J. G.; Amend, S. H.; Weilbaecher, K. N. Integrins and bone metastasis: integrating tumor cell and stromal cell interactions Bone 2011, 48, 54-65
    • (2011) Bone , vol.48 , pp. 54-65
    • Schneider, J.G.1    Amend, S.H.2    Weilbaecher, K.N.3
  • 40
    • 0029008105 scopus 로고
    • Characterisation of tumor-induced platelet aggregation: The role of immunoregulated GPIb and GPIIb/IIIa expression by MCF-7 breast cancer cells
    • Oleksowicz, L.; Schwartz, Z. M. E.; Khorshidit, M.; Dutcher, J. P.; Puszkin, E. Characterisation of tumor-induced platelet aggregation: the role of immunoregulated GPIb and GPIIb/IIIa expression by MCF-7 breast cancer cells Thromb. Res. 1995, 79, 261-274
    • (1995) Thromb. Res. , vol.79 , pp. 261-274
    • Oleksowicz, L.1    Schwartz, Z.M.E.2    Khorshidit, M.3    Dutcher, J.P.4    Puszkin, E.5
  • 44
    • 11144230059 scopus 로고    scopus 로고
    • Platelets and fibrin(ogen) increase metastatic potential by impeding natural killer cell-mediated elimination of tumor cells
    • Palumbo, J. S.; Talmage, K. E.; Massari, J. V.; La Jeunesse, C. M.; Flick, M. J.; Kombrinck, K. W.; Jirouskova, M.; Degen, J. L. Platelets and fibrin(ogen) increase metastatic potential by impeding natural killer cell-mediated elimination of tumor cells Blood 2005, 105, 178-185
    • (2005) Blood , vol.105 , pp. 178-185
    • Palumbo, J.S.1    Talmage, K.E.2    Massari, J.V.3    La Jeunesse, C.M.4    Flick, M.J.5    Kombrinck, K.W.6    Jirouskova, M.7    Degen, J.L.8
  • 45
    • 84893676358 scopus 로고    scopus 로고
    • 3 integrins in MDA-MB-231 cell invasion and shear flow-induced cancer cell mechanotransduction
    • 3 integrins in MDA-MB-231 cell invasion and shear flow-induced cancer cell mechanotransduction Cancer Lett. 2014, 344, 62-73
    • (2014) Cancer Lett. , vol.344 , pp. 62-73
    • Zhao, F.1    Li, L.2    Guan, L.3    Yang, H.4    Wu, C.5    Liu, Y.6
  • 48
    • 84867306135 scopus 로고    scopus 로고
    • 3 integrin inhibits pulmonary metastasis by preferentially fragmenting activated platelets in the tumor microenvironment
    • 3 integrin inhibits pulmonary metastasis by preferentially fragmenting activated platelets in the tumor microenvironment Blood 2012, 120, 2889-2898
    • (2012) Blood , vol.120 , pp. 2889-2898
    • Zhang, W.1    Dang, S.2    Hong, T.3    Tang, J.4    Fan, J.5    Bu, D.6    Sun, Y.7    Wang, Z.8    Wisniewski, T.9
  • 49
    • 0032836245 scopus 로고    scopus 로고
    • Blockade of GpIIb/IIIa inhibits the release of vascular endothelial growth factor (VEGF) from tumor cell-activated platelets and experimental metastasis
    • Amirkhosravi, A.; Amaya, M.; Siddiqui, F.; Biggerstaff, J. P.; Meyer, T. V.; Francis, J. L. Blockade of GpIIb/IIIa inhibits the release of vascular endothelial growth factor (VEGF) from tumor cell-activated platelets and experimental metastasis Platelets 1999, 10, 285-292
    • (1999) Platelets , vol.10 , pp. 285-292
    • Amirkhosravi, A.1    Amaya, M.2    Siddiqui, F.3    Biggerstaff, J.P.4    Meyer, T.V.5    Francis, J.L.6
  • 51
    • 71149111643 scopus 로고    scopus 로고
    • 3 integrins during HeLa cells adhesion, migration, and invasion to monolayer endothelium under static and dynamic shear flow
    • 3 integrins during HeLa cells adhesion, migration, and invasion to monolayer endothelium under static and dynamic shear flow J. Biomed. Biotechnol. 2009, 2009, 829243
    • (2009) J. Biomed. Biotechnol. , vol.2009 , pp. 829243
    • Liu, Y.1    Zhao, F.2    Gu, W.3    Yang, H.4    Meng, Q.5    Zhang, Y.6    Yang, H.7    Duan, Q.8
  • 54
    • 0034681464 scopus 로고    scopus 로고
    • Synthesis and biological evaluation of integrin antagonists containing trans-and cis-2,5-disubstituted THF rings
    • Osterkamp, F.; Ziemer, B.; Koert, U.; Weisner, M.; Raddatz, P.; Goodman, S. L. Synthesis and biological evaluation of integrin antagonists containing trans-and cis-2,5-disubstituted THF rings Chem.-Eur. J. 2000, 6, 666-683
    • (2000) Chem.-Eur. J. , vol.6 , pp. 666-683
    • Osterkamp, F.1    Ziemer, B.2    Koert, U.3    Weisner, M.4    Raddatz, P.5    Goodman, S.L.6
  • 56
    • 0027944516 scopus 로고
    • Inhibition of integrin function by a cyclic RGD-containing peptide prevents neointima formation
    • Matsuno, H.; Stassen, J. M.; Vermylen, J.; Deckmyn, H. Inhibition of integrin function by a cyclic RGD-containing peptide prevents neointima formation Circulation 1994, 90, 2203-2206
    • (1994) Circulation , vol.90 , pp. 2203-2206
    • Matsuno, H.1    Stassen, J.M.2    Vermylen, J.3    Deckmyn, H.4
  • 58
    • 13444291204 scopus 로고    scopus 로고
    • 3 integrin loop" regulates breast cancer cell survival and chemosensitivity through activation of ERK1/ERK2 MAPK signaling pathway
    • 3 integrin loop" regulates breast cancer cell survival and chemosensitivity through activation of ERK1/ERK2 MAPK signaling pathway Oncogene 2005, 24, 761-779
    • (2005) Oncogene , vol.24 , pp. 761-779
    • Menendez, J.A.1    Vellon, L.2    Mehmi, I.3    Teng, P.K.4    Griggs, D.W.5    Lupu, R.6
  • 67
    • 84964875096 scopus 로고    scopus 로고
    • 3-LIBS epitope, and permit routine staining of archival paraffin samples of human tumors
    • 3-LIBS epitope, and permit routine staining of archival paraffin samples of human tumors Biol. Open 2012, 1, 329-340
    • (2012) Biol. Open , vol.1 , pp. 329-340
    • Goodman, S.L.1    Grote, H.J.2    Wilm, C.3
  • 68
    • 84893680442 scopus 로고    scopus 로고
    • Integrins and their ligands are expressed in non-small cell lung cancer but not correlated with parameters of disease progression
    • Böger, C.; Kalthoff, H.; Goodman, S. L.; Behrens, H. M.; Röcken, C. Integrins and their ligands are expressed in non-small cell lung cancer but not correlated with parameters of disease progression Virchows Arch. 2014, 464, 69-78
    • (2014) Virchows Arch. , vol.464 , pp. 69-78
    • Böger, C.1    Kalthoff, H.2    Goodman, S.L.3    Behrens, H.M.4    Röcken, C.5
  • 72
    • 84879414971 scopus 로고    scopus 로고
    • 5 contributes to the tumorigenic potential of breast cancer cells through the Src-FAK and MEK-ERK signaling pathways
    • 5 contributes to the tumorigenic potential of breast cancer cells through the Src-FAK and MEK-ERK signaling pathways Oncogene 2013, 32, 3049-3058
    • (2013) Oncogene , vol.32 , pp. 3049-3058
    • Bianchi-Smiraglia, A.1    Paesante, S.2    Bakin, A.V.3
  • 75
    • 77957926274 scopus 로고    scopus 로고
    • Click-chemistry-derived triazole ligands of arginine-glycine-aspartate (RGD) integrins with a broad capacity to inhibit adhesion of melanoma cells and both in vitro and in vivo angiogenesis
    • Trabocchi, A.; Menchi, G.; Cini, N.; Bianchini, F.; Raspanti, S.; Bottoncetti, A.; Pupi, A.; Calorini, L.; Guarna, A. Click-chemistry-derived triazole ligands of arginine-glycine-aspartate (RGD) integrins with a broad capacity to inhibit adhesion of melanoma cells and both in vitro and in vivo angiogenesis J. Med. Chem. 2010, 53, 7119-7128
    • (2010) J. Med. Chem. , vol.53 , pp. 7119-7128
    • Trabocchi, A.1    Menchi, G.2    Cini, N.3    Bianchini, F.4    Raspanti, S.5    Bottoncetti, A.6    Pupi, A.7    Calorini, L.8    Guarna, A.9
  • 79
    • 0038441393 scopus 로고    scopus 로고
    • Decrease in survival threshold of quiescent colon carcinoma cells in the presence of a small molecule integrin antagonist
    • Burbridge, M. F.; Venot, V.; Casara, P. J.; Perron-Sierra, F.; Hickman, J. A.; Tucker, G. C. Decrease in survival threshold of quiescent colon carcinoma cells in the presence of a small molecule integrin antagonist Mol. Pharmacol. 2003, 63, 1281-1288
    • (2003) Mol. Pharmacol. , vol.63 , pp. 1281-1288
    • Burbridge, M.F.1    Venot, V.2    Casara, P.J.3    Perron-Sierra, F.4    Hickman, J.A.5    Tucker, G.C.6
  • 81
    • 79952741178 scopus 로고    scopus 로고
    • Cilengitide: The first anti-angiogenic small molecule drug candidate. Design, synthesis and clinical evaluation
    • Mas-Moruno, C.; Rechenmacher, F.; Kessler, H. Cilengitide: the first anti-angiogenic small molecule drug candidate. Design, synthesis and clinical evaluation Anti-Cancer Agents Med. Chem. 2010, 10, 753-768
    • (2010) Anti-Cancer Agents Med. Chem. , vol.10 , pp. 753-768
    • Mas-Moruno, C.1    Rechenmacher, F.2    Kessler, H.3
  • 82
    • 0025880146 scopus 로고
    • Arg-Gly-Asp constrained within cyclic pentapeptides. Strong and selective inhibitors of cell adhesion to vitronectin and laminin fragments
    • Aumailley, M.; Gurrath, M.; Müller, G.; Calvete, J.; Timpl, R.; Kessler, H. Arg-Gly-Asp constrained within cyclic pentapeptides. Strong and selective inhibitors of cell adhesion to vitronectin and laminin fragments FEBS Lett. 1991, 291, 50-54
    • (1991) FEBS Lett. , vol.291 , pp. 50-54
    • Aumailley, M.1    Gurrath, M.2    Müller, G.3    Calvete, J.4    Timpl, R.5    Kessler, H.6
  • 85
    • 84867830537 scopus 로고    scopus 로고
    • Integrin inhibitor cilengitide for the treatment of glioblastoma: A brief overview of current clinical results
    • Scaringi, C.; Minniti, G.; Caporello, P.; Enrici, R. M. Integrin inhibitor cilengitide for the treatment of glioblastoma: a brief overview of current clinical results Anticancer Res. 2012, 32, 4213-4223
    • (2012) Anticancer Res. , vol.32 , pp. 4213-4223
    • Scaringi, C.1    Minniti, G.2    Caporello, P.3    Enrici, R.M.4
  • 87
    • 84868193304 scopus 로고    scopus 로고
    • A safety run-in and randomized phase 2 study of cilengitide combined with chemoradiation for newly diagnosed glioblastoma (NABTT 0306)
    • New Approaches to Brain Tumor Therapy Central Nervous System Consortium
    • Nabors, L. B.; Mikkelsen, T.; Hegi, M. E.; Ye, X.; Batchelor, T.; Lesser, G.; Peereboom, D.; Rosenfeld, M. R.; Olsen, J.; Brem, S.; Fisher, J. D.; Grossman, S. A.; New Approaches to Brain Tumor Therapy Central Nervous System Consortium. A safety run-in and randomized phase 2 study of cilengitide combined with chemoradiation for newly diagnosed glioblastoma (NABTT 0306) Cancer 2012, 118, 5601-5607
    • (2012) Cancer , vol.118 , pp. 5601-5607
    • Nabors, L.B.1    Mikkelsen, T.2    Hegi, M.E.3    Ye, X.4    Batchelor, T.5    Lesser, G.6    Peereboom, D.7    Rosenfeld, M.R.8    Olsen, J.9    Brem, S.10    Fisher, J.D.11    Grossman, S.A.12
  • 88
    • 79957671402 scopus 로고    scopus 로고
    • Phase I/II trial of cilengitide with cetuximab, cisplatin and 5-fluorouracil in recurrent and/or metastatic squamous cell cancer of the head and neck: Findings of the phase i part
    • Vermorken, J. B.; Guigay, J.; Mesia, R.; Trigo, J. M.; Keilholz, U.; Kerber, A.; Bethe, U.; Picard, M.; Brummendorf, T. H. Phase I/II trial of cilengitide with cetuximab, cisplatin and 5-fluorouracil in recurrent and/or metastatic squamous cell cancer of the head and neck: findings of the phase I part Br. J. Cancer 2011, 104, 1691-1696
    • (2011) Br. J. Cancer , vol.104 , pp. 1691-1696
    • Vermorken, J.B.1    Guigay, J.2    Mesia, R.3    Trigo, J.M.4    Keilholz, U.5    Kerber, A.6    Bethe, U.7    Picard, M.8    Brummendorf, T.H.9
  • 91
    • 84903445620 scopus 로고    scopus 로고
    • Integrins and p53 pathways in glioblastoma resistance to temozolomide
    • Martin, S.; Janouskova, H.; Dontenwill, M. Integrins and p53 pathways in glioblastoma resistance to temozolomide Front. Oncol. 2012, 2, 157
    • (2012) Front. Oncol. , vol.2 , pp. 157
    • Martin, S.1    Janouskova, H.2    Dontenwill, M.3
  • 92
    • 84875258658 scopus 로고    scopus 로고
    • 1, the fibronectin receptor, as a pertinent therapeutic target in solid tumors
    • 1, the fibronectin receptor, as a pertinent therapeutic target in solid tumors Cancers 2013, 5, 27-47
    • (2013) Cancers , vol.5 , pp. 27-47
    • Schaffner, F.1    Ray, A.M.2    Dontenwill, M.3
  • 93
    • 0033119722 scopus 로고    scopus 로고
    • RGD-recognizing integrins mediate interactions of human prostate carcinoma cells with endothelial cells in vitro
    • Romanov, V. I.; Goligorsky, M. S. RGD-recognizing integrins mediate interactions of human prostate carcinoma cells with endothelial cells in vitro Prostate 1999, 39, 108-118
    • (1999) Prostate , vol.39 , pp. 108-118
    • Romanov, V.I.1    Goligorsky, M.S.2
  • 94
    • 84867178220 scopus 로고    scopus 로고
    • 3 integrins in relation to adhesion and spreading dynamics of prostate cancer cells interacting with fibronectin under in vitro conditions
    • 3 integrins in relation to adhesion and spreading dynamics of prostate cancer cells interacting with fibronectin under in vitro conditions Cell Biol. Int. 2012, 36, 883-892
    • (2012) Cell Biol. Int. , vol.36 , pp. 883-892
    • Stachurska, A.1    Elbanowski, J.2    Kowalczyñska, H.M.3
  • 113
    • 25144501954 scopus 로고    scopus 로고
    • Targeting ECM-integrin interaction with liposome-encapsulated small interfering RNAs inhibits the growth of human prostate cancer in a bone xenograft imaging model
    • Bisanz, K.; Yu, J.; Edlund, M.; Spohn, B.; Hung, M.-C.; Chung, L. W. K.; Hsieh, C.-L. Targeting ECM-integrin interaction with liposome-encapsulated small interfering RNAs inhibits the growth of human prostate cancer in a bone xenograft imaging model Mol. Ther. 2005, 12, 634-643
    • (2005) Mol. Ther. , vol.12 , pp. 634-643
    • Bisanz, K.1    Yu, J.2    Edlund, M.3    Spohn, B.4    Hung, M.-C.5    Chung, L.W.K.6    Hsieh, C.-L.7
  • 122
    • 79959735566 scopus 로고    scopus 로고
    • A phase 1, multicenter, open-label study of the safety of two dose levels of a human monoclonal antibody to human α(v) integrins, intetumumab, in combination with docetaxel and prednisone in patients with castrate-resistant metastatic prostate cancer
    • Chu, F. M.; Picus, J.; Fracasso, P. M.; Dreicer, R.; Lang, Z.; Foster, B. A phase 1, multicenter, open-label study of the safety of two dose levels of a human monoclonal antibody to human α(v) integrins, intetumumab, in combination with docetaxel and prednisone in patients with castrate-resistant metastatic prostate cancer Invest. New Drugs 2011, 29, 674-679
    • (2011) Invest. New Drugs , vol.29 , pp. 674-679
    • Chu, F.M.1    Picus, J.2    Fracasso, P.M.3    Dreicer, R.4    Lang, Z.5    Foster, B.6
  • 125
    • 84896402978 scopus 로고    scopus 로고
    • v-integrin antibody EMD 525797 (DI17E6) in healthy subjects after ascending single intravenous doses
    • [Online early access]. DOI: 10.1007/s10637-013-038-5. Published Online: November 19
    • v- integrin antibody EMD 525797 (DI17E6) in healthy subjects after ascending single intravenous doses. Invest. New Drugs [Online early access]. DOI: 10.1007/s10637-013-038-5. Published Online: November 19, 2013.
    • (2013) Invest. New Drugs
    • Uhl, W.1    Zühlsdorf, M.2    Koernicke, T.3    Forssmann, U.4    Kovar, A.5
  • 127
    • 0032728451 scopus 로고    scopus 로고
    • Development of eptifibatide
    • Scarborough, R. M. Development of eptifibatide Am. Heart J. 1999, 138, 1093-1104
    • (1999) Am. Heart J. , vol.138 , pp. 1093-1104
    • Scarborough, R.M.1
  • 128
    • 84872496139 scopus 로고    scopus 로고
    • The continuing saga of snake venom disintegrins
    • Calvete, J. J. The continuing saga of snake venom disintegrins Toxicon 2013, 62, 40-49
    • (2013) Toxicon , vol.62 , pp. 40-49
    • Calvete, J.J.1
  • 130
    • 62349084228 scopus 로고    scopus 로고
    • Colombistatin: A disintegrin isolated from the venom of the South American snake (Bothrops colombiensis) that effectively inhibits platelet aggregation and SK-Mel-28 cell adhesion
    • Sánchez, E. E.; Rodríguez-Acosta, A.; Palomar, R.; Lucena, S. E.; Bashir, S.; Soto, J. G.; Pérez, J. C. Colombistatin: a disintegrin isolated from the venom of the South American snake (Bothrops colombiensis) that effectively inhibits platelet aggregation and SK-Mel-28 cell adhesion Arch. Toxicol. 2009, 83, 271-279
    • (2009) Arch. Toxicol. , vol.83 , pp. 271-279
    • Sánchez, E.E.1    Rodríguez-Acosta, A.2    Palomar, R.3    Lucena, S.E.4    Bashir, S.5    Soto, J.G.6    Pérez, J.C.7
  • 131
    • 84859383536 scopus 로고    scopus 로고
    • Anti-invasive and anti-adhesive activities of a recombinant disintegrin, r-viridistatin 2, derived from the Prairie rattlesnake (Crotalus viridis viridis)
    • Lucena, S. E.; Jia, Y.; Soto, J. G.; Parral, J.; Cantu, E.; Brannon, J.; Lardner, K.; Ramos, C. J.; Seoane, A. I.; Sánchez, E. E. Anti-invasive and anti-adhesive activities of a recombinant disintegrin, r-viridistatin 2, derived from the Prairie rattlesnake (Crotalus viridis viridis) Toxicon 2012, 60, 31-39
    • (2012) Toxicon , vol.60 , pp. 31-39
    • Lucena, S.E.1    Jia, Y.2    Soto, J.G.3    Parral, J.4    Cantu, E.5    Brannon, J.6    Lardner, K.7    Ramos, C.J.8    Seoane, A.I.9    Sánchez, E.E.10
  • 132
    • 84855225404 scopus 로고    scopus 로고
    • Recombinant rubistatin (r-Rub), an MVD disintegrin, inhibits cell migration and proliferation, and is a strong apoptotic inducer of the human melanoma cell line SK-Mel-28
    • Carey, C. M.; Bueno, R.; Gutierrez, D. A.; Petro, C.; Lucena, S. E.; Sanchez, E. E.; Soto, J. G. Recombinant rubistatin (r-Rub), an MVD disintegrin, inhibits cell migration and proliferation, and is a strong apoptotic inducer of the human melanoma cell line SK-Mel-28 Toxicon 2012, 59, 241-248
    • (2012) Toxicon , vol.59 , pp. 241-248
    • Carey, C.M.1    Bueno, R.2    Gutierrez, D.A.3    Petro, C.4    Lucena, S.E.5    Sanchez, E.E.6    Soto, J.G.7
  • 133
    • 84876819507 scopus 로고    scopus 로고
    • 5-dependent functions in melanoma cells by an ECD-disintegrin acurhagin-C
    • 5-dependent functions in melanoma cells by an ECD-disintegrin acurhagin-C Matrix Biol. 2013, 32, 152-159
    • (2013) Matrix Biol. , vol.32 , pp. 152-159
    • Shih, C.-H.1    Chiang, T.-B.2    Wang, W.-J.3
  • 134
    • 0034683048 scopus 로고    scopus 로고
    • Suppressive mechanism of salmosin, a novel disintegrin in B16 melanoma cell metastasis
    • Kang, I.-C.; Kim, D.-S.; Jang, Y.; Chung, K.-H. Suppressive mechanism of salmosin, a novel disintegrin in B16 melanoma cell metastasis Biochem. Biophys. Res. Commun. 2000, 275, 169-173
    • (2000) Biochem. Biophys. Res. Commun. , vol.275 , pp. 169-173
    • Kang, I.-C.1    Kim, D.-S.2    Jang, Y.3    Chung, K.-H.4
  • 135
    • 0028111866 scopus 로고
    • 1 integrin-mediated human metastatic melanoma cell adhesion and blocks experimental metastasis
    • 1 integrin-mediated human metastatic melanoma cell adhesion and blocks experimental metastasis Cancer Res. 1994, 54, 4993-4998
    • (1994) Cancer Res. , vol.54 , pp. 4993-4998
    • Trikha, M.1    De Clerck, Y.A.2    Markland, F.S.3
  • 136
    • 77955223245 scopus 로고    scopus 로고
    • Vicrostatin-an anti-invasive multi-integrin targeting chimeric disintegrin with tumor anti-angiogenic and pro-apoptotic activities
    • Minea, R. O.; Helchowski, C. M.; Zidovetzki, S. J.; Costa, F. K.; Swenson, S. D.; Markland, F. S. J. Vicrostatin-an anti-invasive multi-integrin targeting chimeric disintegrin with tumor anti-angiogenic and pro-apoptotic activities PLoS One 2010, 5, e10929
    • (2010) PLoS One , vol.5 , pp. 10929
    • Minea, R.O.1    Helchowski, C.M.2    Zidovetzki, S.J.3    Costa, F.K.4    Swenson, S.D.5    Markland, F.S.J.6
  • 137
    • 33646794420 scopus 로고    scopus 로고
    • Development of a novel recombinant disintegrin, contortrostatin, as an effective anti-tumor and anti-angiogenic agent
    • Minea, R.; Swenson, S.; Costa, F.; Chen, T. C.; Markland, F. S. Development of a novel recombinant disintegrin, contortrostatin, as an effective anti-tumor and anti-angiogenic agent Pathophysiol. Haemostasis Thromb. 2005, 34, 177-183
    • (2005) Pathophysiol. Haemostasis Thromb. , vol.34 , pp. 177-183
    • Minea, R.1    Swenson, S.2    Costa, F.3    Chen, T.C.4    Markland, F.S.5
  • 138
  • 140
    • 77956371198 scopus 로고    scopus 로고
    • The disintegrin contortrostatin in combination with docetaxel is a potent inhibitor of prostate cancer in vitro and in vivo
    • Lin, E.; Wang, Q.; Swenson, S.; Jadvar, H.; Groshen, S.; Ye, W.; Markland, F. S.; Pinski, J. The disintegrin contortrostatin in combination with docetaxel is a potent inhibitor of prostate cancer in vitro and in vivo Prostate 2010, 70, 1359-1370
    • (2010) Prostate , vol.70 , pp. 1359-1370
    • Lin, E.1    Wang, Q.2    Swenson, S.3    Jadvar, H.4    Groshen, S.5    Ye, W.6    Markland, F.S.7    Pinski, J.8
  • 142
    • 84870523333 scopus 로고    scopus 로고
    • Effect of the disintegrin eristostatin on melanoma-natural killer cell interactions
    • Hailey, S.; Adams, E.; Penn, R.; Wong, A.; McLane, M. A. Effect of the disintegrin eristostatin on melanoma-natural killer cell interactions Toxicon 2013, 61, 83-93
    • (2013) Toxicon , vol.61 , pp. 83-93
    • Hailey, S.1    Adams, E.2    Penn, R.3    Wong, A.4    McLane, M.A.5
  • 153
    • 84906087549 scopus 로고    scopus 로고
    • Clinicaltrials.gov. (accessed Nov 27, 2013)
    • Clinicaltrials.gov. www.clinicaltrials.gov (accessed Nov 27, 2013).


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.