HER2-mediated anticancer drug delivery: strategies to prepare targeting ligands highly specific for the receptor (571 views)
Curr Med Chem (ISSN: 0929-8673, 1875-533x, 1875-533xelectronic), 2015 May 20; 22(21): 2525-2538.
Export to BibTeX Export to EndNote
Paper type: Journal Article, Review,
Impact factor: 3.455, 5-year impact factor: 3.792
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84939838938&partnerID=40&md5=806cc51826aa79729f1fd348a5c9d55d
Keywords: Drug Delivery Systems, Her2 Receptor, Screening Methods, Selective Ligand, Synthetic Receptor Fragment, Targeted Cancer Therapy, Antineoplastic Agent, Epidermal Growth Factor Receptor 2, Monoclonal Antibody, Pertuzumab, Trastuzumab, Antigen Binding, Apparent Dissociation Constant, Article, Fluorescence In Situ Hybridization, Fluorescence Spectroscopy, Human, Immunohistochemistry, Molecular Dynamics, Molecularly Targeted Therapy, Nonhuman, Antineoplastic Agents Chemical Synthesis Chemistry Pharmacokinetics , Biomarkers, Tumor Antagonists, Inhibitors Metabolism , Breast Neoplasms Drug Therapy Metabolism , Female , Models, Molecular Targeted Therapy , Peptides Chemical Synthesis Chemistry Pharmacokinetics , Erbb-2 Antagonists, Structure-Activity Relationship,
Affiliations:
*** IBB - CNR ***
Institute of Biostructures and Bioimaging, National Research Council, 80138 Naples, Italy. stefania.deluca@cnr.it.,
Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO, United States
Institute of Crystallography, National Research Council, Bari, Italy
Consiglio Nazionale delle Ricerche
References:
Yarden, Y., Sliwkowski, M.X., Untangling the ERBB signalling network (2001) Nat. Rev. Mol. Cell. Biol., 2, pp. 127-13
Press, M.F., Cordon-Cardo, C., Slamon, D.J., Expression of the HER-2/neu proto-oncogene in normal human adult and fetal tissues (1990) Oncogene, 5, pp. 953-962
Dawood, S., Broglio, K., Buzdar, A.U., Hortobagyi, G.N., Giordano, S.H., Prognosis of women with metastatic breast cancer by HER2 status and trastuzumab treatment: An institutional-based review (2010) J. Clin. Oncol., 28, pp. 92-98
Ross, J.S., Slodkowska, E.A., Symmans, W.F., Pusztai, L., Ravdin, P.M., Hortobagyi, G.N., The HER-2 receptor and breast cancer: Ten years of targeted anti-HER-2 therapy and personalized medicine (2009) Oncologist, 14, pp. 320-368
Lax, I., Burgess, W.H., Bellot, F., Ullrich, A., Schlessinger, J., Givol, D., Localization of a major receptor-binding domain for epidermal growth factor by affinity labeling (1988) Mol. Cell. Biol., 8, pp. 1831-1834
Pietras, R.J., Arboleda, J., Reese, D.M., Wongvipat, N., Pegram, M.D., Ramos, L., Gorman, C.M., Slamon, D.J., HER-2 tyrosine kinase pathway targets estrogen receptor and promotes hormone-independent growth in human breast cancer cells (1995) Oncogene, 10, pp. 2435-2446
Garrett, T.P., McKern, N.M., Lou, M., Elleman, T.C., Adams, T.E., Lovrecz, G.O., Kofler, M., Ward, C.W., The crystal structure of a truncated ERBB2 ectodomain reveals an active conformation, poised to interact with other ERBB receptors (2003) Mol. Cell, 11, pp. 495-505
Neve, R.M., Lane, H.A., Hynes, N.E., The role of overexpressed HER2 intransformation (2001) Ann. Oncol., 12, pp. S9-S13
Slamon, D.J., Godolphin, W., Jones, L.A., Holt, J.A., Wong, S.G., Keith, D.E., Levin, W.J., Press, M.F., Studies of the HER-2/neu proto-ancogene in human breast and ovarian cancer (1989) Science, 244, pp. 707-712
Klapper, L.N., Kirschbaum, M.H., Sela, M., Yarden, Y., Biochemical and clinical implications of ERBB/HER signaling network of growth factor receptors (2000) Adv. Cancer Res., 77, pp. 25-79
Olayioye, M.A., Neve, R.M., Lane, H.A., Hynes, N.E., The ERBB sigaling network: Receptor heterodimerization in development and cancer (2000) EMBO J., 19, pp. 3159-3167
Niehans, G.A., Singleton, T.P., Dykoski, D., Kiang, D.T., Stability of HER-2/neu expression over time and at multiple metastatic sites (1993) J. Natl. Cancer Inst., 85, pp. 1230-1235
Cooke, T., What is HER2? (2000) Eur. J. Oncol. Nurs., 4, pp. 2-9
Spector, N., Xia, W., El-Hariry, I., Yarden, Y., Bacus, S., HER2 therapy. Small molecule HER-2 tyrosine kinase inhibitors (2007) Breast Cancer Res., 9, p. 205
Perez, E.A., Cortés, J., Gonzalez-Angulo, A.M., Bartlett, J.M.S., HER2 testing: Current status and future directions (2014) Cancer Treat. Rev., 40, pp. 276-284
Slamon, D.J., Leyland-Jones, B., Shak, S., Fuchs, H., Paton, V., Bajamonde, A., Fleming, T., Norton, L., Use of chemotherapy plus a monoclonal antibody against HER2 for metastatic breast cancer that overexpresses HER2 (2001) N. Engl. J. Med., 344, pp. 783-792
Smith, I., Procter, M., Gelberm, R.D., Guillaume, S., Feyereislova, A., Dowsett, M., Goldhirsch, A., Piccart-Gebhart, M.J., 2-year follow-up of trastuzumab after adjuvant chemotherapy in HER2-positive breast cancer: A randomised controlled trial (2007) Lancet, 369, pp. 29-36
Ghayad, S.E., Cohen, P.A., Inhibitors of the PI3K/Akt/mTOR pathway: New hope for breast cancer patients (2010) Recent Pat. Anticancer Drug Discov., 5, pp. 29-57
Iqbal, N., Iqbal, N., Human Epidermal Growth Factor Receptor 2 (HER2) in cancers: Overexpression and therapeutic implications (2014) Mol. Biol. Int., 9p. , http://dx.doi.org/10.1155/2014/852748
Romond, E.H., Perez, E.A., Bryant, J., Suman, V.J., Geyer, C.E., Jr., Davidson, N.E., Tan-Chiu, E., Wolmark, N., Trastuzumab plus adjuvant chemotherapy for operable HER2-positive breast cancer (2005) N. Engl. J. Med., 353, pp. 1673-1684
Adams, C.W., Allison, D.E., Flagella, K., Presta, L., Clarke, J., Dybdal, N., McKeever, K., Sliwkowski, M.X., Humanization of a recombinant monoclonal antibody to produce a therapeutic HER dimerization inhibitor, pertuzumab (2006) Cancer Immunol. Immunother., 55, pp. 717-727
Agus, D.B., Akita, R.W., Fox, W.D., Lewis, G.D., Higgins, B., Pisacane, P.I., Lofgren, J.A., Sliwkowski, M.X., Targeting ligand-activated ErbB2 signaling inhibits breast and prostate tumor growth (2002) Cancer Cell, 2, pp. 127-137
Cai, Z., Zhang, G., Zhou, Z., Bembas, K., Drebin, J.A., Greene, M.I., Zhang, H., Differential binding patterns of monoclonal antibody 2C4 to the ErbB3-p185her2/neu and the EGFR-p185her2/neu complexes (2008) Oncogene, 27, pp. 3870-3874
Scheuer, W., Friess, T., Burtscher, H., Bossenmaier, B., Endl, J., Hasmann, M., Strongly enhanced antitumor activity of trastuzumab and pertuzumab combination treatment on HER2-positive human xenograft tumor models (2009) Cancer Res., 69, pp. 9330-9336
Brockhoff, G., Heckel, B., Schmidt-Bruecken, E., Plander, M., Hofstaedter, F., Vollmann, A., Diermeier, S., Differential impact of Cetuximab, Pertuzumab and Trastuzumab on BT474 and SK-BR-3 breast cancer cell proliferation (2007) Cell Prolif., 40, pp. 488-507
Blattler, W.A., Chari, R.V.J., (2012) Methods of Treatment Using Anti-ERBB Antibody-maytansinoid Conjugates, , U. S. Patent
Lambert, J.M., Chari, R.V.J., Ado-trastuzumab Emtansine (TDM1): An Antibody-Drug Conjugate (ADC) for HER2-positive breast cancer (2014) J. Med. Chem.
Gianolio, D.A., Rouleau, C., Bauta, W.E., Lovett, D., Cantrell, W.R., Jr., Recio, A.I., Wolstenholme-Hogg, P., Teicher, B.A., Targeting HER2-positive cancer with dolastatin 15 derivatives conjugated to trastuzumab, novel antibody-drug conjugates (2012) Cancer Chemother. Pharmacol., 70, pp. 439-449
Jia, L.T., Zhang, L.H., Yu, C.J., Zhao, J., Xu, Y.M., Gui, J.H., Jin, M., Yang, A.G., Specific tumoricidal activity of a secreted proapoptotic protein consisting of HER2 antibody and constitutively active caspase-3 (2003) Cancer Res., 63, pp. 3257-3262
Cho, H.M., Rosenblatt, J.D., Kang, Y.S., Iruela-Arispe, M.L., Morrison, S.L., Penichet, M.L., Kwon, Y.G., Shin, S.U., Enhanced inhibition of murine tumor and human breast tumor xenografts using targeted delivery of an antibody-endostatin fusion protein (2005) Mol. Cancer Ther., 4, pp. 956-967
Xia, W.Y., Lien, H.C., Wang, S.C., Pan, Y., Sahin, A., Kuo, Y.H., Chang, K.J., Hung, M.C., Expression of PEA3 and lack of correlation between PEA3 and HER-2/neu expression in breast cancer (2006) Breast Cancer Res. Treat., 98, pp. 295-301
Helguera, G., Rodriguez, J.A., Daniels, T.R., Penichet, M.L., Longterm immunity elicited by antibody-cytokine fusion proteins protects against sequential challenge with murine mammary and colon malignancies (2007) Cancer Immunol. Immunother., 56, pp. 1507-1512
Vivek, R., Thangam, R., NipunBabu, V., Rejeeth, C., Sivasubramanian, S., Gunasekaran, P., Muthuchelian, K., Kannan, S., Multifunctional HER2-antibody conjugated polymeric nanocarrier-based drug delivery system for multi-drug-resistant breast cancer therapy (2014) ACS Appl. Mater. Interfaces, 6, pp. 6469-6480
Hapuarachchige, S., Zhu, W., Kato, Y., Artemov, D., Bioorthogonal, two-component delivery systems based on antibody and drugutics (2014) Biomaterials, 35, pp. 2346-2354
Lu, H., Wang, D., Kazane, S., Javahishvili, T., Tian, F., Song, F., Sellers, A., Schultz, P.G., Site-specific antibody. Polymer conjugates for siRNA delivery (2013) J. Am. Chem. Soc., 135, pp. 13885-13891
Nord, K., Gunneriusson, E., Ringdahl, J., Stahl, S., Uhlen, M., Nygren, P.A., Binding proteins selected from combinatorial libraries of an a-helical bacterial receptor domain (1997) Nat. Biotechnol., 15, pp. 772-777
Ronnmark, J., Gronlund, H., Uhlen, M., Nygren, P.A., Human immunoglobulin A (IgA)-specific ligands from combinatorial engineering of protein A (2002) Eur. J. Biochem., 269, pp. 2647-2655
Steffen, A.C., Wikman, M., Tolmachev, V., Adams, G.P., Nilsson, F.Y., Stahl, S., Carlsson, J., In vitro characterization of a bivalent anti-HER-2 affibody with potential for radionuclide-based diagnostics (2005) Cancer Biother. Radiopharm., 20, pp. 239-248
Alexis, F., Basto, P., Levy-Nissenbaum, E., Radovic-Moreno, A.F., Zhang, L., Pridgen, E., Wang, A.Z., Farokhzad, O.C., HER-2-targeted nanoparticleaffibody bioconjugates for cancer therapy (2008) Chem. Med. Chem., 3, pp. 1839-1843
Park, B.W., Zhang, H.T., Wu, C., Berezov, A., Zhang, X., Dua, R., Wang, Q., Murali, R., Rationally designed anti-HER2/neu peptide mimetic disables P185HER2/neu tyrosine kinases in vitro and in vivo (2000) Nat. Biotechnol., 18, pp. 194-198
Shadidi, M., Sioud, M., Identification of novel carrier peptides for the specific delivery of therapeutics into cancer cells (2003) FASEB J., 17, pp. 256-258
Newton, J., Deutscher, S.L., Phage peptide display (2008) Handb. Exp. Pharmacol., pp. 145-163
Nakajima, H., Mizuta, N., Sakaguchi, K., Fujiwara, I., Yoshimori, A., Takahashi, S., Takasawa, R., Tanuma, S., Development of HER2-antagonistic peptides as novel antibreast cancer drugs by in silico methods (2008) Breast Cancer, 15, pp. 65-72
Fantin, V.R., Berardi, M.J., Babbe, H., Michelman, M.V., Manning, C.M., Leder, P., A bifunctional targeted peptide that blocks HER-2 tyrosine kinase and disables mitochondrial function in HER-2-positive carcinoma cells (2005) Cancer Res., 65, pp. 6891-6900
Afshar, S., Asai, T., Morrison, S.L., Humanized ADEPT comprised of an engineered human purine nucleoside phosphorylase and a tumor targeting peptide for treatment of cancer (2009) Mol. Cancer Ther., 8, pp. 185-193
Tan, M., Lan, K.H., Yao, J., Lu, C.H., Sun, M., Neal, C.L., Lu, J., Yu, D., Selective inhibition of ErbB2-overexpressing breast cancer in vivo by a novel TAT-based ErbB2-targeting signal transducers and activators of transcription 3-blocking peptide (2006) Cancer Res., 66, pp. 3764-3772
Javadpour, M.M., Juban, M.M., Lo, W.C., Bishop, S.M., Alberty, J.B., Cowell, S.M., Becker, C.L., McLaughlin, M.L., De novo antimicrobial peptides with low mammalian cell toxicity (1996) J. Med. Chem., 39, pp. 3107-3713
Ellerby, H.M., Martin, S.J., Ellerby, L.M., Naiem, S.S., Rabizadeh, S., Salvesen, G.S., Casiano, C.A., Bredesen, D.E., Establishment of a cell-free system of neuronal apoptosis: Comparison of premitochondrial, mitochondrial, and postmitochondrial phases (1997) J. Neurosci., 17, pp. 6165-6178
Del Rio, G., Castro-Obregon, S., Rao, R., Ellerby, H.M., Bredesen, D.E., APAP, a sequence-pattern recognition approach identifies substance P as a potential apoptotic peptide (2001) FEBS Lett., 494, pp. 213-219
Fernandes, A., Hamburger, A.W., Gerwin, B.I., ERBB-2 kinase is required for constitutive stat 3 activation in malignant human lung epithelial cells (1999) Int. J. Cancer, 83, pp. 564-570
Ren, Z., Schaefer, T.S., ERBB-2activates Stat3 alpha in a Src- and JAK2-dependent manner (2002) J. Biol. Chem., 277, pp. 38486-38493
Olayioye, M.A., Beuvink, I., Horsch, K., Daly, J.M., Hynes, N.E., ERBB receptor-induced activation of stat transcription factors is mediated by src tyrosine kinases (1999) J. Biol. Chem., 274, pp. 17209-17218
Turkson, J., Ryan, D., Kim, J.S., Zhang, Y., Chen, Z., Haura, E., Laudano, A., Jove, R., Phosphotyrosyl peptides block Stat3-mediated DNA binding activity, gene regulation, and cell transformation (2001) J. Biol. Chem., 276, pp. 45443-45455
Landon, L.A., Deutscher, S.L., Combinatorial discovery of tumor targeting peptides using phage display (2003) J. Cell Biochem., 90, pp. 509-517
Cho, H.S., Mason, K., Ramyar, K.X., Stanley, A.M., Gabelli, S.B., Denney, D.W., Leahy, D.J., Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab (2003) Nature, 421, pp. 756-760
Monfregola, L., Vitale, R.M., Amodeo, P., De Luca, S., A SPR strategy for high-throughput ligand screenings based on synthetic peptides mimicking a selected subdomain of the target protein: A proof of concept on HER2 receptor (2009) Bioorg. Med. Chem., 17, pp. 7015-7020
Murzin, A.G., Brenner, S.E., Hubbard, T., Chothia, C.J., SCOP: A structural classification of proteins database for the investigation of sequences and structures (1995) Mol. Biol., 247, p. 536
Calce, E., Monfregola, L., Sandomenico, A., Saviano, M., De Luca, S., Fluorescence study for selecting specific ligands toward HER2 receptor: An example of receptor fragment approach (2013) Eur. J. Med. Chem., 61, pp. 116-121
Calce, E., Sandomenico, A., Saviano, M., Ruvo, M., De Luca, S., Cysteine co-oxidation process driven by native peptide folding: An example on HER2 receptor model system (2014) Amino Acids, 46, pp. 1197-1206
Rabanal, F., DeGrado, W.F., Dutton, P.L., Use of 2, 2'-dithiobis (5-nitropyridine) for the heterodimerization of cysteine-containing peptides.introduction of the 5-nitro-2-pyridinesulfenyl group (1996) Tetrahedron Lett., 37, pp. 1347-1350
Hahnefeld, C., Drewianka, S., Herberg, F.W., Determination of kinetic data using surface plasmon resonance biosensors (2004) Methods Mol. Med., 94, pp. 299-320
Rich, R.L., Myszka, D.G., Survey of the year 2003 commercial optical biosensor literature (2005) J. Mol. Recognit., 18, pp. 1-39
Schuck, P., Minton, A.P., Analysis of mass transport-limited binding kinetics in evanescent wave biosensors (1996) Anal. Biochem., 240, pp. 262-272
Wu, S.J., Chaiken, I., Biosensor analysis of receptor-ligand interaction (2004) Methods Mol. Biol., 249, pp. 93-110
Curr Med Chem (ISSN: 0929-8673, 1875-533x, 1875-533xelectronic), 2015 May 20; 22(21): 2525-2538.
Export to BibTeX Export to EndNote
Paper type: Journal Article, Review,
Impact factor: 3.455, 5-year impact factor: 3.792
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84939838938&partnerID=40&md5=806cc51826aa79729f1fd348a5c9d55d
Keywords: Drug Delivery Systems, Her2 Receptor, Screening Methods, Selective Ligand, Synthetic Receptor Fragment, Targeted Cancer Therapy, Antineoplastic Agent, Epidermal Growth Factor Receptor 2, Monoclonal Antibody, Pertuzumab, Trastuzumab, Antigen Binding, Apparent Dissociation Constant, Article, Fluorescence In Situ Hybridization, Fluorescence Spectroscopy, Human, Immunohistochemistry, Molecular Dynamics, Molecularly Targeted Therapy, Nonhuman, Antineoplastic Agents Chemical Synthesis Chemistry Pharmacokinetics , Biomarkers, Tumor Antagonists, Inhibitors Metabolism , Breast Neoplasms Drug Therapy Metabolism , Female , Models, Molecular Targeted Therapy , Peptides Chemical Synthesis Chemistry Pharmacokinetics , Erbb-2 Antagonists, Structure-Activity Relationship,
Affiliations:
*** IBB - CNR ***
Institute of Biostructures and Bioimaging, National Research Council, 80138 Naples, Italy. stefania.deluca@cnr.it.,
Department of Chemistry and Biochemistry, University of Colorado, Boulder, CO, United States
Institute of Crystallography, National Research Council, Bari, Italy
Consiglio Nazionale delle Ricerche
References:
Yarden, Y., Sliwkowski, M.X., Untangling the ERBB signalling network (2001) Nat. Rev. Mol. Cell. Biol., 2, pp. 127-13
Press, M.F., Cordon-Cardo, C., Slamon, D.J., Expression of the HER-2/neu proto-oncogene in normal human adult and fetal tissues (1990) Oncogene, 5, pp. 953-962
Dawood, S., Broglio, K., Buzdar, A.U., Hortobagyi, G.N., Giordano, S.H., Prognosis of women with metastatic breast cancer by HER2 status and trastuzumab treatment: An institutional-based review (2010) J. Clin. Oncol., 28, pp. 92-98
Ross, J.S., Slodkowska, E.A., Symmans, W.F., Pusztai, L., Ravdin, P.M., Hortobagyi, G.N., The HER-2 receptor and breast cancer: Ten years of targeted anti-HER-2 therapy and personalized medicine (2009) Oncologist, 14, pp. 320-368
Lax, I., Burgess, W.H., Bellot, F., Ullrich, A., Schlessinger, J., Givol, D., Localization of a major receptor-binding domain for epidermal growth factor by affinity labeling (1988) Mol. Cell. Biol., 8, pp. 1831-1834
Pietras, R.J., Arboleda, J., Reese, D.M., Wongvipat, N., Pegram, M.D., Ramos, L., Gorman, C.M., Slamon, D.J., HER-2 tyrosine kinase pathway targets estrogen receptor and promotes hormone-independent growth in human breast cancer cells (1995) Oncogene, 10, pp. 2435-2446
Garrett, T.P., McKern, N.M., Lou, M., Elleman, T.C., Adams, T.E., Lovrecz, G.O., Kofler, M., Ward, C.W., The crystal structure of a truncated ERBB2 ectodomain reveals an active conformation, poised to interact with other ERBB receptors (2003) Mol. Cell, 11, pp. 495-505
Neve, R.M., Lane, H.A., Hynes, N.E., The role of overexpressed HER2 intransformation (2001) Ann. Oncol., 12, pp. S9-S13
Slamon, D.J., Godolphin, W., Jones, L.A., Holt, J.A., Wong, S.G., Keith, D.E., Levin, W.J., Press, M.F., Studies of the HER-2/neu proto-ancogene in human breast and ovarian cancer (1989) Science, 244, pp. 707-712
Klapper, L.N., Kirschbaum, M.H., Sela, M., Yarden, Y., Biochemical and clinical implications of ERBB/HER signaling network of growth factor receptors (2000) Adv. Cancer Res., 77, pp. 25-79
Olayioye, M.A., Neve, R.M., Lane, H.A., Hynes, N.E., The ERBB sigaling network: Receptor heterodimerization in development and cancer (2000) EMBO J., 19, pp. 3159-3167
Niehans, G.A., Singleton, T.P., Dykoski, D., Kiang, D.T., Stability of HER-2/neu expression over time and at multiple metastatic sites (1993) J. Natl. Cancer Inst., 85, pp. 1230-1235
Cooke, T., What is HER2? (2000) Eur. J. Oncol. Nurs., 4, pp. 2-9
Spector, N., Xia, W., El-Hariry, I., Yarden, Y., Bacus, S., HER2 therapy. Small molecule HER-2 tyrosine kinase inhibitors (2007) Breast Cancer Res., 9, p. 205
Perez, E.A., Cortés, J., Gonzalez-Angulo, A.M., Bartlett, J.M.S., HER2 testing: Current status and future directions (2014) Cancer Treat. Rev., 40, pp. 276-284
Slamon, D.J., Leyland-Jones, B., Shak, S., Fuchs, H., Paton, V., Bajamonde, A., Fleming, T., Norton, L., Use of chemotherapy plus a monoclonal antibody against HER2 for metastatic breast cancer that overexpresses HER2 (2001) N. Engl. J. Med., 344, pp. 783-792
Smith, I., Procter, M., Gelberm, R.D., Guillaume, S., Feyereislova, A., Dowsett, M., Goldhirsch, A., Piccart-Gebhart, M.J., 2-year follow-up of trastuzumab after adjuvant chemotherapy in HER2-positive breast cancer: A randomised controlled trial (2007) Lancet, 369, pp. 29-36
Ghayad, S.E., Cohen, P.A., Inhibitors of the PI3K/Akt/mTOR pathway: New hope for breast cancer patients (2010) Recent Pat. Anticancer Drug Discov., 5, pp. 29-57
Iqbal, N., Iqbal, N., Human Epidermal Growth Factor Receptor 2 (HER2) in cancers: Overexpression and therapeutic implications (2014) Mol. Biol. Int., 9p. , http://dx.doi.org/10.1155/2014/852748
Romond, E.H., Perez, E.A., Bryant, J., Suman, V.J., Geyer, C.E., Jr., Davidson, N.E., Tan-Chiu, E., Wolmark, N., Trastuzumab plus adjuvant chemotherapy for operable HER2-positive breast cancer (2005) N. Engl. J. Med., 353, pp. 1673-1684
Adams, C.W., Allison, D.E., Flagella, K., Presta, L., Clarke, J., Dybdal, N., McKeever, K., Sliwkowski, M.X., Humanization of a recombinant monoclonal antibody to produce a therapeutic HER dimerization inhibitor, pertuzumab (2006) Cancer Immunol. Immunother., 55, pp. 717-727
Agus, D.B., Akita, R.W., Fox, W.D., Lewis, G.D., Higgins, B., Pisacane, P.I., Lofgren, J.A., Sliwkowski, M.X., Targeting ligand-activated ErbB2 signaling inhibits breast and prostate tumor growth (2002) Cancer Cell, 2, pp. 127-137
Cai, Z., Zhang, G., Zhou, Z., Bembas, K., Drebin, J.A., Greene, M.I., Zhang, H., Differential binding patterns of monoclonal antibody 2C4 to the ErbB3-p185her2/neu and the EGFR-p185her2/neu complexes (2008) Oncogene, 27, pp. 3870-3874
Scheuer, W., Friess, T., Burtscher, H., Bossenmaier, B., Endl, J., Hasmann, M., Strongly enhanced antitumor activity of trastuzumab and pertuzumab combination treatment on HER2-positive human xenograft tumor models (2009) Cancer Res., 69, pp. 9330-9336
Brockhoff, G., Heckel, B., Schmidt-Bruecken, E., Plander, M., Hofstaedter, F., Vollmann, A., Diermeier, S., Differential impact of Cetuximab, Pertuzumab and Trastuzumab on BT474 and SK-BR-3 breast cancer cell proliferation (2007) Cell Prolif., 40, pp. 488-507
Blattler, W.A., Chari, R.V.J., (2012) Methods of Treatment Using Anti-ERBB Antibody-maytansinoid Conjugates, , U. S. Patent
Lambert, J.M., Chari, R.V.J., Ado-trastuzumab Emtansine (TDM1): An Antibody-Drug Conjugate (ADC) for HER2-positive breast cancer (2014) J. Med. Chem.
Gianolio, D.A., Rouleau, C., Bauta, W.E., Lovett, D., Cantrell, W.R., Jr., Recio, A.I., Wolstenholme-Hogg, P., Teicher, B.A., Targeting HER2-positive cancer with dolastatin 15 derivatives conjugated to trastuzumab, novel antibody-drug conjugates (2012) Cancer Chemother. Pharmacol., 70, pp. 439-449
Jia, L.T., Zhang, L.H., Yu, C.J., Zhao, J., Xu, Y.M., Gui, J.H., Jin, M., Yang, A.G., Specific tumoricidal activity of a secreted proapoptotic protein consisting of HER2 antibody and constitutively active caspase-3 (2003) Cancer Res., 63, pp. 3257-3262
Cho, H.M., Rosenblatt, J.D., Kang, Y.S., Iruela-Arispe, M.L., Morrison, S.L., Penichet, M.L., Kwon, Y.G., Shin, S.U., Enhanced inhibition of murine tumor and human breast tumor xenografts using targeted delivery of an antibody-endostatin fusion protein (2005) Mol. Cancer Ther., 4, pp. 956-967
Xia, W.Y., Lien, H.C., Wang, S.C., Pan, Y., Sahin, A., Kuo, Y.H., Chang, K.J., Hung, M.C., Expression of PEA3 and lack of correlation between PEA3 and HER-2/neu expression in breast cancer (2006) Breast Cancer Res. Treat., 98, pp. 295-301
Helguera, G., Rodriguez, J.A., Daniels, T.R., Penichet, M.L., Longterm immunity elicited by antibody-cytokine fusion proteins protects against sequential challenge with murine mammary and colon malignancies (2007) Cancer Immunol. Immunother., 56, pp. 1507-1512
Vivek, R., Thangam, R., NipunBabu, V., Rejeeth, C., Sivasubramanian, S., Gunasekaran, P., Muthuchelian, K., Kannan, S., Multifunctional HER2-antibody conjugated polymeric nanocarrier-based drug delivery system for multi-drug-resistant breast cancer therapy (2014) ACS Appl. Mater. Interfaces, 6, pp. 6469-6480
Hapuarachchige, S., Zhu, W., Kato, Y., Artemov, D., Bioorthogonal, two-component delivery systems based on antibody and drugutics (2014) Biomaterials, 35, pp. 2346-2354
Lu, H., Wang, D., Kazane, S., Javahishvili, T., Tian, F., Song, F., Sellers, A., Schultz, P.G., Site-specific antibody. Polymer conjugates for siRNA delivery (2013) J. Am. Chem. Soc., 135, pp. 13885-13891
Nord, K., Gunneriusson, E., Ringdahl, J., Stahl, S., Uhlen, M., Nygren, P.A., Binding proteins selected from combinatorial libraries of an a-helical bacterial receptor domain (1997) Nat. Biotechnol., 15, pp. 772-777
Ronnmark, J., Gronlund, H., Uhlen, M., Nygren, P.A., Human immunoglobulin A (IgA)-specific ligands from combinatorial engineering of protein A (2002) Eur. J. Biochem., 269, pp. 2647-2655
Steffen, A.C., Wikman, M., Tolmachev, V., Adams, G.P., Nilsson, F.Y., Stahl, S., Carlsson, J., In vitro characterization of a bivalent anti-HER-2 affibody with potential for radionuclide-based diagnostics (2005) Cancer Biother. Radiopharm., 20, pp. 239-248
Alexis, F., Basto, P., Levy-Nissenbaum, E., Radovic-Moreno, A.F., Zhang, L., Pridgen, E., Wang, A.Z., Farokhzad, O.C., HER-2-targeted nanoparticleaffibody bioconjugates for cancer therapy (2008) Chem. Med. Chem., 3, pp. 1839-1843
Park, B.W., Zhang, H.T., Wu, C., Berezov, A., Zhang, X., Dua, R., Wang, Q., Murali, R., Rationally designed anti-HER2/neu peptide mimetic disables P185HER2/neu tyrosine kinases in vitro and in vivo (2000) Nat. Biotechnol., 18, pp. 194-198
Shadidi, M., Sioud, M., Identification of novel carrier peptides for the specific delivery of therapeutics into cancer cells (2003) FASEB J., 17, pp. 256-258
Newton, J., Deutscher, S.L., Phage peptide display (2008) Handb. Exp. Pharmacol., pp. 145-163
Nakajima, H., Mizuta, N., Sakaguchi, K., Fujiwara, I., Yoshimori, A., Takahashi, S., Takasawa, R., Tanuma, S., Development of HER2-antagonistic peptides as novel antibreast cancer drugs by in silico methods (2008) Breast Cancer, 15, pp. 65-72
Fantin, V.R., Berardi, M.J., Babbe, H., Michelman, M.V., Manning, C.M., Leder, P., A bifunctional targeted peptide that blocks HER-2 tyrosine kinase and disables mitochondrial function in HER-2-positive carcinoma cells (2005) Cancer Res., 65, pp. 6891-6900
Afshar, S., Asai, T., Morrison, S.L., Humanized ADEPT comprised of an engineered human purine nucleoside phosphorylase and a tumor targeting peptide for treatment of cancer (2009) Mol. Cancer Ther., 8, pp. 185-193
Tan, M., Lan, K.H., Yao, J., Lu, C.H., Sun, M., Neal, C.L., Lu, J., Yu, D., Selective inhibition of ErbB2-overexpressing breast cancer in vivo by a novel TAT-based ErbB2-targeting signal transducers and activators of transcription 3-blocking peptide (2006) Cancer Res., 66, pp. 3764-3772
Javadpour, M.M., Juban, M.M., Lo, W.C., Bishop, S.M., Alberty, J.B., Cowell, S.M., Becker, C.L., McLaughlin, M.L., De novo antimicrobial peptides with low mammalian cell toxicity (1996) J. Med. Chem., 39, pp. 3107-3713
Ellerby, H.M., Martin, S.J., Ellerby, L.M., Naiem, S.S., Rabizadeh, S., Salvesen, G.S., Casiano, C.A., Bredesen, D.E., Establishment of a cell-free system of neuronal apoptosis: Comparison of premitochondrial, mitochondrial, and postmitochondrial phases (1997) J. Neurosci., 17, pp. 6165-6178
Del Rio, G., Castro-Obregon, S., Rao, R., Ellerby, H.M., Bredesen, D.E., APAP, a sequence-pattern recognition approach identifies substance P as a potential apoptotic peptide (2001) FEBS Lett., 494, pp. 213-219
Fernandes, A., Hamburger, A.W., Gerwin, B.I., ERBB-2 kinase is required for constitutive stat 3 activation in malignant human lung epithelial cells (1999) Int. J. Cancer, 83, pp. 564-570
Ren, Z., Schaefer, T.S., ERBB-2activates Stat3 alpha in a Src- and JAK2-dependent manner (2002) J. Biol. Chem., 277, pp. 38486-38493
Olayioye, M.A., Beuvink, I., Horsch, K., Daly, J.M., Hynes, N.E., ERBB receptor-induced activation of stat transcription factors is mediated by src tyrosine kinases (1999) J. Biol. Chem., 274, pp. 17209-17218
Turkson, J., Ryan, D., Kim, J.S., Zhang, Y., Chen, Z., Haura, E., Laudano, A., Jove, R., Phosphotyrosyl peptides block Stat3-mediated DNA binding activity, gene regulation, and cell transformation (2001) J. Biol. Chem., 276, pp. 45443-45455
Landon, L.A., Deutscher, S.L., Combinatorial discovery of tumor targeting peptides using phage display (2003) J. Cell Biochem., 90, pp. 509-517
Cho, H.S., Mason, K., Ramyar, K.X., Stanley, A.M., Gabelli, S.B., Denney, D.W., Leahy, D.J., Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab (2003) Nature, 421, pp. 756-760
Monfregola, L., Vitale, R.M., Amodeo, P., De Luca, S., A SPR strategy for high-throughput ligand screenings based on synthetic peptides mimicking a selected subdomain of the target protein: A proof of concept on HER2 receptor (2009) Bioorg. Med. Chem., 17, pp. 7015-7020
Murzin, A.G., Brenner, S.E., Hubbard, T., Chothia, C.J., SCOP: A structural classification of proteins database for the investigation of sequences and structures (1995) Mol. Biol., 247, p. 536
Calce, E., Monfregola, L., Sandomenico, A., Saviano, M., De Luca, S., Fluorescence study for selecting specific ligands toward HER2 receptor: An example of receptor fragment approach (2013) Eur. J. Med. Chem., 61, pp. 116-121
Calce, E., Sandomenico, A., Saviano, M., Ruvo, M., De Luca, S., Cysteine co-oxidation process driven by native peptide folding: An example on HER2 receptor model system (2014) Amino Acids, 46, pp. 1197-1206
Rabanal, F., DeGrado, W.F., Dutton, P.L., Use of 2, 2'-dithiobis (5-nitropyridine) for the heterodimerization of cysteine-containing peptides.introduction of the 5-nitro-2-pyridinesulfenyl group (1996) Tetrahedron Lett., 37, pp. 1347-1350
Hahnefeld, C., Drewianka, S., Herberg, F.W., Determination of kinetic data using surface plasmon resonance biosensors (2004) Methods Mol. Med., 94, pp. 299-320
Rich, R.L., Myszka, D.G., Survey of the year 2003 commercial optical biosensor literature (2005) J. Mol. Recognit., 18, pp. 1-39
Schuck, P., Minton, A.P., Analysis of mass transport-limited binding kinetics in evanescent wave biosensors (1996) Anal. Biochem., 240, pp. 262-272
Wu, S.J., Chaiken, I., Biosensor analysis of receptor-ligand interaction (2004) Methods Mol. Biol., 249, pp. 93-110
HER2-mediated anticancer drug delivery: strategies to prepare targeting ligands highly specific for the receptor
HER2 receptor, for its involvement in tumorigenesis, has been largely studied as topic in cancer research. In particular, the employment of trastuzumab (Herceptin), a humanized anti-HER2 antibody, showed several clinical benefits in the therapy against the breast cancer. Moreover, for its accessible extracellular domain, this receptor is considered an ideal target to deliver anticancer drugs for the receptormediated anticancer therapy. By now, monoclonal antibody and its fragments, affibody, and some peptides have been employed as targeting agents in order to deliver various drugs to HER2 positive tumor cells. In particular, the ability to perform a fast and reliable screening of a large number of peptide molecules would make possible the selection of highly specific compounds to the receptor target. In this regard, the availability of preparing a simplified synthetic model which is a good mimetic of the receptor target and can be used in a reliable screening method of ligands would be of a strategic importance for the development of selective HER2-targeting peptide molecules. Herein, we illustrate the importance of HER2-targeted anticancer therapies. We also report on a synthetic and effective mimetic of the receptor, which revealed to be a useful tool for the selection of specific HER2 ligands. © 2015 Bentham Science Publishers.
HER2 receptor, for its involvement in tumorigenesis, has been largely studied as topic in cancer research. In particular, the employment of trastuzumab (Herceptin), a humanized anti-HER2 antibody, showed several clinical benefits in the therapy against the breast cancer. Moreover, for its accessible extracellular domain, this receptor is considered an ideal target to deliver anticancer drugs for the receptormediated anticancer therapy. By now, monoclonal antibody and its fragments, affibody, and some peptides have been employed as targeting agents in order to deliver various drugs to HER2 positive tumor cells. In particular, the ability to perform a fast and reliable screening of a large number of peptide molecules would make possible the selection of highly specific compounds to the receptor target. In this regard, the availability of preparing a simplified synthetic model which is a good mimetic of the receptor target and can be used in a reliable screening method of ligands would be of a strategic importance for the development of selective HER2-targeting peptide molecules. Herein, we illustrate the importance of HER2-targeted anticancer therapies. We also report on a synthetic and effective mimetic of the receptor, which revealed to be a useful tool for the selection of specific HER2 ligands. © 2015 Bentham Science Publishers.
HER2-mediated anticancer drug delivery: strategies to prepare targeting ligands highly specific for the receptor
HER2-mediated anticancer drug delivery: strategies to prepare targeting ligands highly specific for the receptor
Other filter: ([btitle,keywords] "Drug Delivery System ...
De Luca S, Verdoliva V, Saviano M
* Peptide Ligands Specifically Targeting HER2 Receptor and the Role Played by a Synthetic Model System of the Receptor Extracellular Domain: Hypothesized Future Perspectives (54 views)
J Med Chem (ISSN: 0022-2623linking, 0022-2623print), 2020 Dec 24; 63(24): 15333-15343.
Impact Factor: 6.205
View Export to BibTeX Export to EndNote
De Luca S, Verdoliva V, Saviano M, Fattorusso R, Diana D
* SPR and NMR characterization of the molecular interaction between A9 peptide and a model system of HER2 receptor: A fragment approach for selecting peptide structures specific for their target (135 views)
J Pept Sci (ISSN: 1075-2617linking, 1099-1387electronic), 2020 Feb; 26(2): e3231-e3231.
Impact Factor: 1.877
View Export to BibTeX Export to EndNote
Honarvar H, Calce E, Doti N, Langella E, Orlova A, Buijs J, D’amato V, Bianco R, Saviano M, Tolmachev V, De Luca S
* Evaluation of HER2-specific peptide ligand for its employment as radiolabeled imaging probe (297 views)
Sci Rep (ISSN: 2045-2322linking, 2045-2322electronic), 2018 Feb 14; 8(1): 2998-2998.
Impact Factor: 4.259
View Export to BibTeX Export to EndNote
Caraci F, Bruno V, Copani A, Matrisciano F, Nicoletti F, Battaglia G
* The impact of metabotropic glutamate receptors into active neurodegenerative processes: A "dark side" in the development of new symptomatic treatments for neurologic and psychiatric disorders (291 views)
Neuropharm (ISSN: 0028-3908, 1873-7064electronic, 0028-3908linking), 2017 Mar 15; 115: 180-192.
Impact Factor: 5.012
View Export to BibTeX Export to EndNote
Greco A, Albanese S, Auletta L, De Carlo F, Salvatore M, Howard CM, Claudio PP
* Advances in molecular preclinical therapy mediated by imaging (268 views) (PDF 207 views)
Q J Nucl Med Mol Im (ISSN: 1824-4785, 1824-4478, 1827-1936), 2017 Mar; 61(1): 76-94.
Impact Factor: 2.368
View Export to BibTeX Export to EndNote
Langella E, Calce E, Saviano M, De Luca S
* Structural identification of an HER2 receptor model binding pocket to optimize lead compounds: a combined experimental and computational approach (310 views)
Mol Biosyst (ISSN: 1742-206x), 2016 Jun 21; 12(7): 2159-2167.
Impact Factor: 2.781
View Export to BibTeX Export to EndNote
Calce E, Saviano M, De Luca S
* Development of Targeting Ligands for HER2 Receptor: Simplified Receptor Model Employed for Selecting Highly Specific Molecules (261 views)
International Journal Of Peptide Research And Therapeutics, 2015 Dec; N/D: N/D-N/D.
Impact Factor: 0.99
View Export to BibTeX Export to EndNote
Ringhieri P, Diaferia C, Galdiero S, Palumbo R, Morelli G, Accardo A
* Liposomal doxorubicin doubly functionalized with CCK8 and R8 peptide sequences for selective intracellular drug delivery (451 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617linking), 2015; 21(5): 415-425.
Impact Factor: 1.951
View Export to BibTeX Export to EndNote
Calce E, Sandomenico A, Saviano M, Ruvo M, De Luca S
* Cysteine Co-Oxidation Process Driven By Native Peptide Folding: An Example On Her2 Receptor Model System (366 views)
Amino Acids (ISSN: 0939-4451, 1438-2199, 1438-2199electronic), 2014; 46(5): 1197-1206.
Impact Factor: 3.293
View Export to BibTeX Export to EndNote
Nande R, Greco A, Gossman MS, Lopez JP, Claudio L, Salvatore M, Brunetti A, Denvir J, Howard CM, Claudio PP
* Microbubble-assisted p53, RB, and p130 gene transfer in combination with radiation therapy in prostate cancer (457 views)
Current Gene Therapy (ISSN: 1875-5631, 1566-5232), 2013 Jun 1; 13(3): 163-174.
Impact Factor: 4.906
View Export to BibTeX Export to EndNote
Calce E, Monfregola L, Sandomenico A, Saviano M, De Luca S
* Fluorescence study for selecting specific ligands toward HER2 receptor: An example of receptor fragment approach (438 views)
Eur J Med Chem (ISSN: 0223-5234, 1768-3254, 1768-3254electronic), 2013 Mar; 61: 116-121.
Impact Factor: 3.432
View Export to BibTeX Export to EndNote
Accardo A, Morisco A, Tesauro D, Pedone C, Morelli G
* Naposomes: A new class of peptide-derivatized, target-selective multimodal nanoparticles for imaging and therapeutic applications (408 views)
Ther Deliv (ISSN: 2041-5990), 2011 Feb; 2(2): 235-257.
Impact Factor: 0
View Export to BibTeX Export to EndNote
Monfregola L, Vitale RM, Amodeo P, De Luca S
* A SPR strategy for high-throughput ligand screenings based on synthetic peptides mimicking a selected subdomain of the target protein: A proof of concept on HER2 receptor (425 views)
Bioorg Med Chem (ISSN: 0968-0896, 1464-3391, 1464-3391electronic), 2009 Oct 1; 17(19): 7015-7020.
Impact Factor: 2.822
View Export to BibTeX Export to EndNote
Zaccaro L, Del Gatto A, Pedone C, Saviano M
* Peptides for tumour therapy and diagnosis: current status and future directions (1011 views)
Curr Med Chem (ISSN: 0929-8673, 1875-533x, 1875-533xelectronic), 2009 Mar; 16(7): 780-795.
Impact Factor: 4.708
View Export to BibTeX Export to EndNote
Del Vecchio S, Zannetti A, Fonti R, Pace L, Salvatore M
* Nuclear imaging in cancer theranostics (616 views)
Q J Nucl Med Mol Im (ISSN: 1824-4785, 1824-4478, 1824-4785linking), 2007 Jun; 51(2): 152-163.
Impact Factor: 1.724
View Export to BibTeX Export to EndNote
Pappalardo M, Milardi D, Grasso D, La Rosa C
* Phase behaviour of polymer-grafted DPPC membranes for drug delivery systems design (302 views)
Journal Of Thermal Analysis And Calorimetry (ISSN: 1388-6150), 2005 May; 80(2): 413-418.
Impact Factor: 1.425
View Export to BibTeX Export to EndNote
Benedetti E, Morelli G, Della Moglie R, De Luca S, Saviano M, Aloj L
* A cyclic and branched peptide as a new selective ligand for the CCKA receptor (356 views)
Peptide Revolution, 2004; N/D: N/D-N/D.
Impact Factor: 4.659
View Export to BibTeX Export to EndNote
Borgatti M, Breda L, Cortesi R, Nastruzzi C, Romanelli A, Saviano M, Bianchi N, Mischiati C, Pedone C, Gambari R
* Cationic Liposomes As Delivery Systems For Double-Stranded Pna-Dna Chimeras Exhibiting Decoy Activity Against Nf-Kappab Transcription Factors (416 views)
Biochem Pharmacol Biochemical Pharmacology (ISSN: 1873-2968, 0006-2952), 2002 Sep 15; 64(4): 609-616.
Impact Factor: 3.542
View Export to BibTeX Export to EndNote
* Peptide Ligands Specifically Targeting HER2 Receptor and the Role Played by a Synthetic Model System of the Receptor Extracellular Domain: Hypothesized Future Perspectives (54 views)
J Med Chem (ISSN: 0022-2623linking, 0022-2623print), 2020 Dec 24; 63(24): 15333-15343.
Impact Factor: 6.205
View Export to BibTeX Export to EndNote
De Luca S, Verdoliva V, Saviano M, Fattorusso R, Diana D
* SPR and NMR characterization of the molecular interaction between A9 peptide and a model system of HER2 receptor: A fragment approach for selecting peptide structures specific for their target (135 views)
J Pept Sci (ISSN: 1075-2617linking, 1099-1387electronic), 2020 Feb; 26(2): e3231-e3231.
Impact Factor: 1.877
View Export to BibTeX Export to EndNote
Honarvar H, Calce E, Doti N, Langella E, Orlova A, Buijs J, D’amato V, Bianco R, Saviano M, Tolmachev V, De Luca S
* Evaluation of HER2-specific peptide ligand for its employment as radiolabeled imaging probe (297 views)
Sci Rep (ISSN: 2045-2322linking, 2045-2322electronic), 2018 Feb 14; 8(1): 2998-2998.
Impact Factor: 4.259
View Export to BibTeX Export to EndNote
Caraci F, Bruno V, Copani A, Matrisciano F, Nicoletti F, Battaglia G
* The impact of metabotropic glutamate receptors into active neurodegenerative processes: A "dark side" in the development of new symptomatic treatments for neurologic and psychiatric disorders (291 views)
Neuropharm (ISSN: 0028-3908, 1873-7064electronic, 0028-3908linking), 2017 Mar 15; 115: 180-192.
Impact Factor: 5.012
View Export to BibTeX Export to EndNote
Greco A, Albanese S, Auletta L, De Carlo F, Salvatore M, Howard CM, Claudio PP
* Advances in molecular preclinical therapy mediated by imaging (268 views) (PDF 207 views)
Q J Nucl Med Mol Im (ISSN: 1824-4785, 1824-4478, 1827-1936), 2017 Mar; 61(1): 76-94.
Impact Factor: 2.368
View Export to BibTeX Export to EndNote
Langella E, Calce E, Saviano M, De Luca S
* Structural identification of an HER2 receptor model binding pocket to optimize lead compounds: a combined experimental and computational approach (310 views)
Mol Biosyst (ISSN: 1742-206x), 2016 Jun 21; 12(7): 2159-2167.
Impact Factor: 2.781
View Export to BibTeX Export to EndNote
Calce E, Saviano M, De Luca S
* Development of Targeting Ligands for HER2 Receptor: Simplified Receptor Model Employed for Selecting Highly Specific Molecules (261 views)
International Journal Of Peptide Research And Therapeutics, 2015 Dec; N/D: N/D-N/D.
Impact Factor: 0.99
View Export to BibTeX Export to EndNote
Ringhieri P, Diaferia C, Galdiero S, Palumbo R, Morelli G, Accardo A
* Liposomal doxorubicin doubly functionalized with CCK8 and R8 peptide sequences for selective intracellular drug delivery (451 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617linking), 2015; 21(5): 415-425.
Impact Factor: 1.951
View Export to BibTeX Export to EndNote
Calce E, Sandomenico A, Saviano M, Ruvo M, De Luca S
* Cysteine Co-Oxidation Process Driven By Native Peptide Folding: An Example On Her2 Receptor Model System (366 views)
Amino Acids (ISSN: 0939-4451, 1438-2199, 1438-2199electronic), 2014; 46(5): 1197-1206.
Impact Factor: 3.293
View Export to BibTeX Export to EndNote
Nande R, Greco A, Gossman MS, Lopez JP, Claudio L, Salvatore M, Brunetti A, Denvir J, Howard CM, Claudio PP
* Microbubble-assisted p53, RB, and p130 gene transfer in combination with radiation therapy in prostate cancer (457 views)
Current Gene Therapy (ISSN: 1875-5631, 1566-5232), 2013 Jun 1; 13(3): 163-174.
Impact Factor: 4.906
View Export to BibTeX Export to EndNote
Calce E, Monfregola L, Sandomenico A, Saviano M, De Luca S
* Fluorescence study for selecting specific ligands toward HER2 receptor: An example of receptor fragment approach (438 views)
Eur J Med Chem (ISSN: 0223-5234, 1768-3254, 1768-3254electronic), 2013 Mar; 61: 116-121.
Impact Factor: 3.432
View Export to BibTeX Export to EndNote
Accardo A, Morisco A, Tesauro D, Pedone C, Morelli G
* Naposomes: A new class of peptide-derivatized, target-selective multimodal nanoparticles for imaging and therapeutic applications (408 views)
Ther Deliv (ISSN: 2041-5990), 2011 Feb; 2(2): 235-257.
Impact Factor: 0
View Export to BibTeX Export to EndNote
Monfregola L, Vitale RM, Amodeo P, De Luca S
* A SPR strategy for high-throughput ligand screenings based on synthetic peptides mimicking a selected subdomain of the target protein: A proof of concept on HER2 receptor (425 views)
Bioorg Med Chem (ISSN: 0968-0896, 1464-3391, 1464-3391electronic), 2009 Oct 1; 17(19): 7015-7020.
Impact Factor: 2.822
View Export to BibTeX Export to EndNote
Zaccaro L, Del Gatto A, Pedone C, Saviano M
* Peptides for tumour therapy and diagnosis: current status and future directions (1011 views)
Curr Med Chem (ISSN: 0929-8673, 1875-533x, 1875-533xelectronic), 2009 Mar; 16(7): 780-795.
Impact Factor: 4.708
View Export to BibTeX Export to EndNote
Del Vecchio S, Zannetti A, Fonti R, Pace L, Salvatore M
* Nuclear imaging in cancer theranostics (616 views)
Q J Nucl Med Mol Im (ISSN: 1824-4785, 1824-4478, 1824-4785linking), 2007 Jun; 51(2): 152-163.
Impact Factor: 1.724
View Export to BibTeX Export to EndNote
Pappalardo M, Milardi D, Grasso D, La Rosa C
* Phase behaviour of polymer-grafted DPPC membranes for drug delivery systems design (302 views)
Journal Of Thermal Analysis And Calorimetry (ISSN: 1388-6150), 2005 May; 80(2): 413-418.
Impact Factor: 1.425
View Export to BibTeX Export to EndNote
Benedetti E, Morelli G, Della Moglie R, De Luca S, Saviano M, Aloj L
* A cyclic and branched peptide as a new selective ligand for the CCKA receptor (356 views)
Peptide Revolution, 2004; N/D: N/D-N/D.
Impact Factor: 4.659
View Export to BibTeX Export to EndNote
Borgatti M, Breda L, Cortesi R, Nastruzzi C, Romanelli A, Saviano M, Bianchi N, Mischiati C, Pedone C, Gambari R
* Cationic Liposomes As Delivery Systems For Double-Stranded Pna-Dna Chimeras Exhibiting Decoy Activity Against Nf-Kappab Transcription Factors (416 views)
Biochem Pharmacol Biochemical Pharmacology (ISSN: 1873-2968, 0006-2952), 2002 Sep 15; 64(4): 609-616.
Impact Factor: 3.542
View Export to BibTeX Export to EndNote
18 Records (16 excluding Abstracts).
Total impact factor: 55.954 (47.036 excluding Abstracts).
Total 5 year impact factor: 57.1 (46.784 excluding Abstracts).
Total impact factor: 55.954 (47.036 excluding Abstracts).
Total 5 year impact factor: 57.1 (46.784 excluding Abstracts).
571 views. Last view on Tuesday 28 February 2023, 8:32:43
ibb.cnr.it
