Peptide Fragments of Odin-Sam1: Conformational Analysis and Interaction Studies with EphA2-Sam (358 views visite)
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-4227linking), 2015; 16(11): 1629-1636.
Export to Esporta in BibTeX Export to Esporta in EndNote
Paper type Tipo di articolo: Journal Article,
Impact factor: 2.85, 5-year impact factor Impact factor a 5 anni: 2.9
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84937250988&partnerID=40&md5=e59e17b9e68c7ae88cc167efd7760438
Keywords Parole chiave: Epha2, Nmr Spectroscopy, Peptides, Sam Domain, Surface Plasmon Resonance, Antineoplastic Agent, Buffer, Ephrin Receptor A2, Ephrin Receptor A2 Inhibitor, Odin Protein, Peptide Fragment, Protein Inhibitor, Sam Inhibitor, Sam1 Protein, Trifluoroethanol, Unclassified Drug, Amino Acid Sequence, Article, Controlled Study, Dissociation Constant, Nuclear Magnetic Resonance, Priority Journal, Protein Conformation,
Affiliations Affiliazioni:
*** IBB - CNR ***
Institute of Biostructures and Bioimaging, National Research Council, Via Mezzocannone 16, Naples, Italy
Department of Pharmacy, University of Naples federico II, Via Mezzocannone 16, Naples, Italy
Circmsb (Consorzio Interuniversitario di Ricerca in Chimica Dei Metalli Nei Sistemi Biologici), Via C. Ulpiani 27, Bari, Italy
Cirpeb (Centro Interuniversitario di Ricerca sui Peptidi Bioattivi), Via Mezzocannone 16, Naples, Italy
Institute of Crystallography, National Research Council, Via Giovanni Amendola 122/O, Bari, Italy
Center for Advanced Biomaterials for Health Care CRIB, Via Largo Barsanti e Matteucci 53, Naples, Italy
References Riferimenti:
Parthasarathi, L., Casey, F., Stein, A., Aloy, P., Shields, D.C., (2008) J. Chem. Inf. Model., 48, p. 194
Kim, C.A., Bowie, J.U., (2003) Trends Biochem. Sci., 28, p. 625
Ramachander, R., Bowie, J.U., (2004) J. Mol. Biol., 342, p. 1353
Leone, M., Cellitti, J., Pellecchia, M., (2008) Biochemistry, 47, p. 12721
Mercurio, F.A., Marasco, D., Pirone, L., Pedone, E.M., Pellecchia, M., Leone, M., (2012) Biochemistry, 51, p. 2136
Pandey, A., Blagoev, B., Kratchmarova, I., Fernandez, M., Nielsen, M., Kristiansen, T.Z., Ohara, O., Mann, M., (2002) Oncogene, 21, p. 8029
Kim, J., Lee, H., Kim, Y., Yoo, S., Park, E., Park, S., (2010) Mol. Cell. Biol., 30, p. 1582
Pasquale, E.B., (2010) Nat. Rev. Cancer, 10, p. 165
Zhuang, G., Brantley-Sieders, D.M., Vaught, D., Yu, J., Xie, L., Wells, S., Jackson, D., Chen, J., (2010) Cancer Res., 70, p. 299
Luo, P., Baldwin, R.L., (1997) Biochemistry, 36, p. 8413
Vuilleumier, S., Mutter, M., (1993) Biopolymers, 33, p. 389
Ha, S.-W., Asakura, T., Kishore, R., (2006) Biomacromolecules, 7, p. 18
Bax, A., Davis, D.G., (1985) J. Magn. Reson., 63, p. 207
Kjaergaard, M., Brander, S., Poulsen, F.M., (2011) J. Biomol. NMR, 49, p. 139
Pimenta, J., Viegas, A., Sardinha, J., Martins, I.C., Cabrita, E.J., Fontes, C.M.G.A., Prates, J.A., Pereira, R.M., (2013) Peptides, 49, p. 32
Kumar, A., Ernst, R.R., Wüthrich, K., (1980) Biochem. Biophys. Res. Commun., 95, p. 1
Wüthrich, K., (1986) NMR of Proteins and Nucleic Acids, , Wiley, New York
Griesinger, C., Otting, G., Wüthrich, K., Ernst, R.R., (1988) J. Am. Chem. Soc., 110, p. 7870
Piantini, U., Sorensen, O.W., Ernst, R.R., (1982) J. Am. Chem. Soc., 104, p. 6800
Merutka, G., Dyson, H.J., Wright, P.E., (1995) J. Biomol. NMR, 5, p. 14
Herrmann, T., Güntert, P., Wüthrich, K., (2002) J. Mol. Biol., 319, p. 209
Baxter, N.J., Williamson, M.P., (1997) J. Biomol. NMR, 9, p. 359
Rothemund, S., Weißhoff, H., Beyermann, M., Krause, E., Bienert, M., Mügge, C., Sykes, B.D., Sönnichsen, F.D., (1996) J. Biomol. NMR, 8, p. 93
Contreras, M.A., Haack, T., Royo, M., Giralt, E., Pons, M., (1997) Lett. Pept. Sci., 4, p. 29
Koradi, R., Billeter, M., Wüthrich, K., (1996) J. Mol. Graph., 14, p. 51
Sancho, J., Neira, J.L., Fersht, A.R., (1992) J. Mol. Biol., 224, p. 749
Sonnichsen, F.D., Van Eyk, J.E., Hodges, R.S., Sykes, B.D., (1992) Biochemistry, 31, p. 8790
Reymond, M.T., Merutka, G., Dyson, H.J., Wright, P.E., (1997) Protein Sci., 6, p. 706
Dyson, H.J., Rance, M., Houghten, R.A., Wright, P.E., Lerner, R.A., (1988) J. Mol. Biol., 201, p. 201
Mercurio, F.A., Scognamiglio, P.L., Di Natale, C., Marasco, D., Pellecchia, M., Leone, M., (2014) Biopolymers, 101, p. 1088
Neira, J.L., (2014) Arch. Biochem. Biophys., 558, p. 133
Villegas, V., Viguera, A.R., Avilés, F.X., Serrano, L., (1996) Fold Des., 1, p. 29
Buck, M., (1998) Q. Rev. Biophys., 31, p. 297
Buck, M., Schwalbe, H., Dobson, C.M., (1995) Biochemistry, 34, p. 13219
Lehrman, S.R., Tuls, J.L., Lund, M., (1990) Biochemistry, 29, p. 5590
Buck, M., Boyd, J., Redfield, C., Mackenzie, D.A., Jeenes, D.J., Archer, D.B., Dobson, C.M., (1995) Biochemistry, 34, p. 4041
Borthakur, S., Lee, H., Kim, S., Wang, B.-C., Buck, M., (2014) J. Biol. Chem., 289, p. 19694
Lee, H.J., Hota, P.K., Chugha, P., Guo, H., Miao, H., Zhang, L., Kim, S.-J., Buck, M., (2012) Structure, 20, p. 41
Leettola, C.N., Knight, M.J., Cascio, D., Hoffman, S., Bowie, J.U., (2014) BMC Struct. Biol., 14, p. 17
Thanos, C.D., Goodwill, K.E., Bowie, J.U., (1999) Science, 283, p. 833
Zhang, L., Buck, M., (2013) Biophys. J., 105, p. 2412
Hwang, T.L., Shaka, A.J., (1995) J. Magn. Reson. A, 112, p. 275
Bartels, C., Xia, T.H., Billeter, M., Güntert, P., Wüthrich, K., (1995) J. Biomol. NMR, 6, p. 1
Doreleijers, J.F., Sousa Da Silva, A.W., Krieger, E., Nabuurs, S.B., Spronk, C.A.E.M., Stevens, T.J., Vranken, W.F., Vuister, G.W., (2012) J. Biomol. NMR, 54, p. 267
Pettersen, E.F., Goddard, T.D., Huang, C.C., Couch, G.S., Greenblatt, D.M., Meng, E.C., Ferrin, T.E., (2004) J. Comput. Chem., 25, p. 1605
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-4227linking), 2015; 16(11): 1629-1636.
Export to Esporta in BibTeX Export to Esporta in EndNote
Paper type Tipo di articolo: Journal Article,
Impact factor: 2.85, 5-year impact factor Impact factor a 5 anni: 2.9
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84937250988&partnerID=40&md5=e59e17b9e68c7ae88cc167efd7760438
Keywords Parole chiave: Epha2, Nmr Spectroscopy, Peptides, Sam Domain, Surface Plasmon Resonance, Antineoplastic Agent, Buffer, Ephrin Receptor A2, Ephrin Receptor A2 Inhibitor, Odin Protein, Peptide Fragment, Protein Inhibitor, Sam Inhibitor, Sam1 Protein, Trifluoroethanol, Unclassified Drug, Amino Acid Sequence, Article, Controlled Study, Dissociation Constant, Nuclear Magnetic Resonance, Priority Journal, Protein Conformation,
Affiliations Affiliazioni:
*** IBB - CNR ***
Institute of Biostructures and Bioimaging, National Research Council, Via Mezzocannone 16, Naples, Italy
Department of Pharmacy, University of Naples federico II, Via Mezzocannone 16, Naples, Italy
Circmsb (Consorzio Interuniversitario di Ricerca in Chimica Dei Metalli Nei Sistemi Biologici), Via C. Ulpiani 27, Bari, Italy
Cirpeb (Centro Interuniversitario di Ricerca sui Peptidi Bioattivi), Via Mezzocannone 16, Naples, Italy
Institute of Crystallography, National Research Council, Via Giovanni Amendola 122/O, Bari, Italy
Center for Advanced Biomaterials for Health Care CRIB, Via Largo Barsanti e Matteucci 53, Naples, Italy
References Riferimenti:
Parthasarathi, L., Casey, F., Stein, A., Aloy, P., Shields, D.C., (2008) J. Chem. Inf. Model., 48, p. 194
Kim, C.A., Bowie, J.U., (2003) Trends Biochem. Sci., 28, p. 625
Ramachander, R., Bowie, J.U., (2004) J. Mol. Biol., 342, p. 1353
Leone, M., Cellitti, J., Pellecchia, M., (2008) Biochemistry, 47, p. 12721
Mercurio, F.A., Marasco, D., Pirone, L., Pedone, E.M., Pellecchia, M., Leone, M., (2012) Biochemistry, 51, p. 2136
Pandey, A., Blagoev, B., Kratchmarova, I., Fernandez, M., Nielsen, M., Kristiansen, T.Z., Ohara, O., Mann, M., (2002) Oncogene, 21, p. 8029
Kim, J., Lee, H., Kim, Y., Yoo, S., Park, E., Park, S., (2010) Mol. Cell. Biol., 30, p. 1582
Pasquale, E.B., (2010) Nat. Rev. Cancer, 10, p. 165
Zhuang, G., Brantley-Sieders, D.M., Vaught, D., Yu, J., Xie, L., Wells, S., Jackson, D., Chen, J., (2010) Cancer Res., 70, p. 299
Luo, P., Baldwin, R.L., (1997) Biochemistry, 36, p. 8413
Vuilleumier, S., Mutter, M., (1993) Biopolymers, 33, p. 389
Ha, S.-W., Asakura, T., Kishore, R., (2006) Biomacromolecules, 7, p. 18
Bax, A., Davis, D.G., (1985) J. Magn. Reson., 63, p. 207
Kjaergaard, M., Brander, S., Poulsen, F.M., (2011) J. Biomol. NMR, 49, p. 139
Pimenta, J., Viegas, A., Sardinha, J., Martins, I.C., Cabrita, E.J., Fontes, C.M.G.A., Prates, J.A., Pereira, R.M., (2013) Peptides, 49, p. 32
Kumar, A., Ernst, R.R., Wüthrich, K., (1980) Biochem. Biophys. Res. Commun., 95, p. 1
Wüthrich, K., (1986) NMR of Proteins and Nucleic Acids, , Wiley, New York
Griesinger, C., Otting, G., Wüthrich, K., Ernst, R.R., (1988) J. Am. Chem. Soc., 110, p. 7870
Piantini, U., Sorensen, O.W., Ernst, R.R., (1982) J. Am. Chem. Soc., 104, p. 6800
Merutka, G., Dyson, H.J., Wright, P.E., (1995) J. Biomol. NMR, 5, p. 14
Herrmann, T., Güntert, P., Wüthrich, K., (2002) J. Mol. Biol., 319, p. 209
Baxter, N.J., Williamson, M.P., (1997) J. Biomol. NMR, 9, p. 359
Rothemund, S., Weißhoff, H., Beyermann, M., Krause, E., Bienert, M., Mügge, C., Sykes, B.D., Sönnichsen, F.D., (1996) J. Biomol. NMR, 8, p. 93
Contreras, M.A., Haack, T., Royo, M., Giralt, E., Pons, M., (1997) Lett. Pept. Sci., 4, p. 29
Koradi, R., Billeter, M., Wüthrich, K., (1996) J. Mol. Graph., 14, p. 51
Sancho, J., Neira, J.L., Fersht, A.R., (1992) J. Mol. Biol., 224, p. 749
Sonnichsen, F.D., Van Eyk, J.E., Hodges, R.S., Sykes, B.D., (1992) Biochemistry, 31, p. 8790
Reymond, M.T., Merutka, G., Dyson, H.J., Wright, P.E., (1997) Protein Sci., 6, p. 706
Dyson, H.J., Rance, M., Houghten, R.A., Wright, P.E., Lerner, R.A., (1988) J. Mol. Biol., 201, p. 201
Mercurio, F.A., Scognamiglio, P.L., Di Natale, C., Marasco, D., Pellecchia, M., Leone, M., (2014) Biopolymers, 101, p. 1088
Neira, J.L., (2014) Arch. Biochem. Biophys., 558, p. 133
Villegas, V., Viguera, A.R., Avilés, F.X., Serrano, L., (1996) Fold Des., 1, p. 29
Buck, M., (1998) Q. Rev. Biophys., 31, p. 297
Buck, M., Schwalbe, H., Dobson, C.M., (1995) Biochemistry, 34, p. 13219
Lehrman, S.R., Tuls, J.L., Lund, M., (1990) Biochemistry, 29, p. 5590
Buck, M., Boyd, J., Redfield, C., Mackenzie, D.A., Jeenes, D.J., Archer, D.B., Dobson, C.M., (1995) Biochemistry, 34, p. 4041
Borthakur, S., Lee, H., Kim, S., Wang, B.-C., Buck, M., (2014) J. Biol. Chem., 289, p. 19694
Lee, H.J., Hota, P.K., Chugha, P., Guo, H., Miao, H., Zhang, L., Kim, S.-J., Buck, M., (2012) Structure, 20, p. 41
Leettola, C.N., Knight, M.J., Cascio, D., Hoffman, S., Bowie, J.U., (2014) BMC Struct. Biol., 14, p. 17
Thanos, C.D., Goodwill, K.E., Bowie, J.U., (1999) Science, 283, p. 833
Zhang, L., Buck, M., (2013) Biophys. J., 105, p. 2412
Hwang, T.L., Shaka, A.J., (1995) J. Magn. Reson. A, 112, p. 275
Bartels, C., Xia, T.H., Billeter, M., Güntert, P., Wüthrich, K., (1995) J. Biomol. NMR, 6, p. 1
Doreleijers, J.F., Sousa Da Silva, A.W., Krieger, E., Nabuurs, S.B., Spronk, C.A.E.M., Stevens, T.J., Vranken, W.F., Vuister, G.W., (2012) J. Biomol. NMR, 54, p. 267
Pettersen, E.F., Goddard, T.D., Huang, C.C., Couch, G.S., Greenblatt, D.M., Meng, E.C., Ferrin, T.E., (2004) J. Comput. Chem., 25, p. 1605
Peptide Fragments of Odin-Sam1: Conformational Analysis and Interaction Studies with EphA2-Sam
Odin is a protein belonging to the ANKS family, and has two tandem Sam domains. The first, Odin-Sam1, binds to the Sam domain of the EphA2 receptor (EphA2-Sam); this interaction could be crucial for the regulation of receptor endocytosis and might have an impact on cancer. Odin-Sam1 associates with EphA2-Sam by adopting a "mid-loop/end-helix" model. In this study three peptide sequences, encompassing the mid-loop interacting portion of Odin-Sam1 and its C-terminal α5 helix, were designed. Their conformational properties were analyzed by CD and NMR. In addition, their abilities to interact with EphA2-Sam were investigated by SPR studies. The peptides adopt a predominantly disordered state in aqueous buffer, but a higher helical content is evident in the presence of the cosolvent trifluoroethanol. Dissociation constants towards EphA2-Sam were in the high micromolar range. The structural findings suggest further routes for the design of potential anti-cancer therapeutics as inhibitors of EphA2-Sam heterotypic interactions. © 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Odin is a protein belonging to the ANKS family, and has two tandem Sam domains. The first, Odin-Sam1, binds to the Sam domain of the EphA2 receptor (EphA2-Sam); this interaction could be crucial for the regulation of receptor endocytosis and might have an impact on cancer. Odin-Sam1 associates with EphA2-Sam by adopting a "mid-loop/end-helix" model. In this study three peptide sequences, encompassing the mid-loop interacting portion of Odin-Sam1 and its C-terminal α5 helix, were designed. Their conformational properties were analyzed by CD and NMR. In addition, their abilities to interact with EphA2-Sam were investigated by SPR studies. The peptides adopt a predominantly disordered state in aqueous buffer, but a higher helical content is evident in the presence of the cosolvent trifluoroethanol. Dissociation constants towards EphA2-Sam were in the high micromolar range. The structural findings suggest further routes for the design of potential anti-cancer therapeutics as inhibitors of EphA2-Sam heterotypic interactions. © 2015 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
Peptide Fragments of Odin-Sam1: Conformational Analysis and Interaction Studies with EphA2-Sam
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Peptide Fragments of Odin-Sam1: Conformational Analysis and Interaction Studies with EphA2-Sam
Mercurio FA, Di Natale C, Pirone L, Vincenzi M, Marasco D, De Luca S, Pedone EM, Leone M
* Exploring the ability of cyclic peptides to target SAM domains: a computational and experimental study (172 visite)
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Impact Factor: 2.641
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Mercurio FA, Di Natale C, Pirone L, Marasco D, Calce E, Vincenzi M, Pedone EM, De Luca S, Leone M
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Mercurio FA, Pirone L, Di Natale C, Marasco D, Pedone EM, Leone M
* Sam domain-based stapled peptides: Structural analysis and interaction studies with the Sam domains from the EphA2 receptor and the lipid phosphatase Ship2 (224 visite)
Bioorg Chem (ISSN: 0045-2068linking, 1090-2120electronic), 2018 Oct; 80: 602-610.
Impact Factor: 3.9
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Mercurio FA, Costantini S, Di Natale C, Pirone L, Guariniello S, Scognamiglio PL, Marasco D, Pedone EM, Leone M
* Structural investigation of a C-terminal EphA2 receptor mutant: Does mutation affect the structure and interaction properties of the Sam domain? (229 visite)
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Impact Factor: 4.28
Dettagli Esporta in BibTeX Esporta in EndNote
Mercurio FA, Marasco D, Di Natale C, Pirone L, Costantini S, Pedone EM, Leone M
* Targeting EphA2-Sam and Its Interactome: Design and Evaluation of Helical Peptides Enriched in Charged Residues (322 visite)
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Impact Factor: 2.847
Dettagli Esporta in BibTeX Esporta in EndNote
Mercurio F, Leone M
* The Sam Domain of EphA2 receptor and its relevance to cancer: a novel challenge for drug discovery? (205 visite)
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Impact Factor: 3.249
Dettagli Esporta in BibTeX Esporta in EndNote
Mercurio FA, Scognamiglio PL, Di Natale C, Marasco D, Pellecchia M, Leone M
* Cd And Nmr Conformational Studies Of A Peptide Encompassing The Mid Loop Interface Of Ship2-Sam (244 visite)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2014 Nov; 101(11): 1088-1098.
Impact Factor: 2.385
Dettagli Esporta in BibTeX Esporta in EndNote
Mercurio FA, Marasco D, Pirone L, Scognamiglio PL, Pedone E, Pellecchia M, Leone M
* Heterotypic Sam-Sam Association Between Odin-Sam1 And Arap3-Sam: Binding Affinity And Structural Insights (237 visite)
Chembiochem (ISSN: 1439-4227, 1439-9422, 1439-7633), 2013 Jan 2; 14(1): 100-106.
Impact Factor: 2.92
Dettagli Esporta in BibTeX Esporta in EndNote
Mercurio FA, Marasco D, Pirone L, Pedone E, Pellecchia M, Leone M
* Solution Structure of the First Sam Domain of Odin and Binding Studies with the EphA2 Receptor (272 visite)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2012 Mar 13; 51(10): 2136-2145.
Impact Factor: 3.377
Dettagli Esporta in BibTeX Esporta in EndNote
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Mercurio FA, Di Natale C, Pirone L, Vincenzi M, Marasco D, De Luca S, Pedone EM, Leone M
* Exploring the ability of cyclic peptides to target SAM domains: a computational and experimental study (172 visite)
Chembiochem (ISSN: 1439-4227linking, 1439-7633), 2019 Sep 20; N/D: N/D-N/D.
Impact Factor: 2.641
Dettagli Esporta in BibTeX Esporta in EndNote
Mercurio FA, Di Natale C, Pirone L, Marasco D, Calce E, Vincenzi M, Pedone EM, De Luca S, Leone M
* Design and analysis of EphA2-SAM peptide ligands: A multi-disciplinary screening approach (128 visite)
Bioorg Chem (ISSN: 0045-2068linking, 1090-2120electronic), 2019 Mar; 84: 434-443.
Impact Factor: 3.929
Dettagli Esporta in BibTeX Esporta in EndNote
Vincenzi M, Mercurio FA, Leone M
* Sam domains in multiple diseases (144 visite)
Curr Med Chem (ISSN: 0929-8673linking, 1875-533xelectronic), 2018 Oct 9; N/D: N/D-N/D.
Impact Factor: 3.469
Dettagli Esporta in BibTeX Esporta in EndNote
Mercurio FA, Pirone L, Di Natale C, Marasco D, Pedone EM, Leone M
* Sam domain-based stapled peptides: Structural analysis and interaction studies with the Sam domains from the EphA2 receptor and the lipid phosphatase Ship2 (224 visite)
Bioorg Chem (ISSN: 0045-2068linking, 1090-2120electronic), 2018 Oct; 80: 602-610.
Impact Factor: 3.9
Dettagli Esporta in BibTeX Esporta in EndNote
Mercurio FA, Costantini S, Di Natale C, Pirone L, Guariniello S, Scognamiglio PL, Marasco D, Pedone EM, Leone M
* Structural investigation of a C-terminal EphA2 receptor mutant: Does mutation affect the structure and interaction properties of the Sam domain? (229 visite)
Bba-Gen Subjects (ISSN: 0005-2728, 0006-3002print, 1570-9639linking), 2017 Jun 06; 1865(9): 1095-1104.
Impact Factor: 4.28
Dettagli Esporta in BibTeX Esporta in EndNote
Mercurio FA, Marasco D, Di Natale C, Pirone L, Costantini S, Pedone EM, Leone M
* Targeting EphA2-Sam and Its Interactome: Design and Evaluation of Helical Peptides Enriched in Charged Residues (322 visite)
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-4227linking), 2016 Nov 17; 17(22): 2179-2188.
Impact Factor: 2.847
Dettagli Esporta in BibTeX Esporta in EndNote
Mercurio F, Leone M
* The Sam Domain of EphA2 receptor and its relevance to cancer: a novel challenge for drug discovery? (205 visite)
Curr Med Chem (ISSN: 0929-8673, 1875-533x, 1875-533xelectronic), 2016 Nov 01; N/D: N/D-N/D.
Impact Factor: 3.249
Dettagli Esporta in BibTeX Esporta in EndNote
Mercurio FA, Scognamiglio PL, Di Natale C, Marasco D, Pellecchia M, Leone M
* Cd And Nmr Conformational Studies Of A Peptide Encompassing The Mid Loop Interface Of Ship2-Sam (244 visite)
Biopolymers (ISSN: 0006-3525, 0006-6352, 0006-3525print), 2014 Nov; 101(11): 1088-1098.
Impact Factor: 2.385
Dettagli Esporta in BibTeX Esporta in EndNote
Mercurio FA, Marasco D, Pirone L, Scognamiglio PL, Pedone E, Pellecchia M, Leone M
* Heterotypic Sam-Sam Association Between Odin-Sam1 And Arap3-Sam: Binding Affinity And Structural Insights (237 visite)
Chembiochem (ISSN: 1439-4227, 1439-9422, 1439-7633), 2013 Jan 2; 14(1): 100-106.
Impact Factor: 2.92
Dettagli Esporta in BibTeX Esporta in EndNote
Mercurio FA, Marasco D, Pirone L, Pedone E, Pellecchia M, Leone M
* Solution Structure of the First Sam Domain of Odin and Binding Studies with the EphA2 Receptor (272 visite)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2012 Mar 13; 51(10): 2136-2145.
Impact Factor: 3.377
Dettagli Esporta in BibTeX Esporta in EndNote
10 Records (10 escludendo Abstract e Conferenze).
Impact factor totale: 32.997 (32.997 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 35.926 (35.926 escludendo Abstract e Conferenze).
Impact factor totale: 32.997 (32.997 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 35.926 (35.926 escludendo Abstract e Conferenze).
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