Conformational ensembles explored dynamically from disordered peptides targeting chemokine receptor CXCR4 (604 views)
Int J Mol Sc (ISSN: 1422-0067, 1661-6596, 1422-0067linking), 2015; 16(6): 12159-12173.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.257, 5-year impact factor: 3.213
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84930636141&partnerID=40&md5=3b2345c8b9e709bb01a096a4e4353606
Keywords: Chemokine, Conformational Ensemble, Intrinsically Disordered Protein (id), Intrinsically Disordered Region(idr), Chemokine Receptor Cxcr4, Antigen Binding, Article, Binding Assay, Camp Assay, Cell Migration Assay, Circular Dichroism, Controlled Study, Human, Human Cell, Hydrogen Bond, Mass Spectrometry, Molecular Dynamics, Molecular Recognition, Nuclear Magnetic Resonance Spectroscopy, Peptide Synthesis, Protein Conformation, Receptor Binding, Reversed Phase High Performance Liquid Chromatography, Simulation,
Affiliations:
*** IBB - CNR ***
Department of Pharmacy, University of Naples “Federico II” and CIRPeB, Via Mezzocannone 16, Naples, Italy
Institute of Biostructures and Bioimaging (IBB), National Research Council (CNR), Via Mezzocannone 16, Naples, Italy
Oncology Research Center of Mercogliano (CROM), Istituto Nazionale Tumori “Fondazione G. Pascale”, IRCCS, Napoli, Italy
Molecular Immunology and Immuneregulation, Istituto Nazionale Tumori “Fondazione G. Pascale”, IRCCS, Napoli, Italy
Center of Medical Informatics, AOU Second University of Naples, Napoli, Italy
UFR des Sciences Pharmaceutiques—Collège Sciences de la Santé INSERM U869, Laboratoire ARNA, Université de Bordeaux, 146 rue Léo Saignat, Bordeaux cedex, France
References:
Habchi, J., Tompa, P., Longhi, S., Uversky, V.N., Introducing protein intrinsic disorder (2014) Chem. Rev, 114, pp. 6561-658
He, B., Wang, K., Liu, Y., Xue, B., Uversky, V.N., Dunker, A.K., Predicting intrinsic disorder in proteins: An overview (2009) Cell Res, 19, pp. 929-949
Motlagh, H.N., Wrabl, J.O., Li, J., Hilsen, V.J., The ensemble nature of allostery (2014) Nature, 508, pp. 331-338
Wright, P.E., Dyson, H.J., Intrinsically unstructured proteR e:-assessing the protein structure-function paradigm (1999) J. Mol. Biol, 293, pp. 321-331
Iakoucheva, L.M., Brown, C.J., Lawson, J.D., Obradovic, Z., Dunker, A.K., Intrinsicdisorder in cell-signaling and cancer-associated proteins (2002) J. Mol. Biol, 323, pp. 573-584
Schweitzer-Stenner, R., Conformational propensities and residual structures in unfolded peptides and proteins (2012) Mol. Biosyst, 8, pp. 122-133
Uversky, V.N., Intrinsically disordered protein from A to Z.Int (2011) J. Biochem. Cell Biol, 43, pp. 1090-1103
Leone, M., Mercurio, F.A., Vincenzi, M., Accardo, A., Ringhieri, P., Tesauro, D., Carrière, F., Rossi, F., Conformational disorder in phosphopeptidSo:Lution studies by CD and NMR techniques (2014) Peptidomics, 1, pp. 14-21
Miller, M., The importance of being flexible:The case of basic region leucine zipper transcriptional regulators (2009) Curr. Protein Pept. Sci, 10, pp. 244-269
Sigalov, A.B., Uversky, V.N., Differential occurrence of protein intrinsic disord ethe in cytoplasmic signaling domains of cell receptors (2011) Self Nonself, 2, pp. 55-72
Costantini, S., Sharma, A., Raucci, R., Costantini, M., Autiero, I., Colonna, G., Genealogy of an ancient protein family: The Sirtuins, a family of disordered members.BMC Evol (2013) Biol, 13, pp. 60-80
Raucci, R., Colonna, G., Giovane, A., Castello, G., Costantini, S., N-terminal region of human chemokine receptor CXCR3: Structural analysis of CXCR3(1-48) by experimental and computational studies (2014) Biochim. Biophys. Acta, 1844, pp. 1868-1880
Mittal, J., Hyeonyoo, T., Georgiou, G., Truskett, T.T., Structural ensemble of an intrinsically disordered polypeptide (2013) J. Phys. Chem. B, 117, pp. 118-124
Chen, S., Gao, S., Cheng, D., Huang, J., The characterization and comparison of amyloidogenic segments and non-amyloidogenic segments shed light on amyloid formationB iochem (2014) Biophys. Res. Commun, 447, pp. 255-262
Costantini, S., Raucci, R., Colonna, G., Mercurio, F.A., Trotta, A.M., Ringhieri, P., Leone, M., Castello, G., . Peptides targeting chemokine receptor CXCR4: Structural behavior and biological binding studies (2014) J. Pept. Sci, 20, pp. 270-278
Palladino, P., Portella, L., Colonna, G., Raucci, R., Saviano, G., Rossi, F., Napolitano, M., Costantini, S., The N-terminal region of CXCL11 as structural templat e for CXCR3 molecular recognitionS ynthesis, conformational analysis, and binding studies (2012) Chem. Biol. Drug Des, 80, pp. 254-265
Underfriend, S., Meienhofer, J., (1985) In the Peptides, p. 7. , Hruby, V.J., Ed.
Academic Press: New York, NY, USA
Wiedemann, C.I., Bellstedt, P., Görlach, M., CAPITO-a web server-based analysis and plotting tool for circular dichroism data (2013) Bioinformatics, 29, pp. 1750-1757
Sreerama, N., Woody, R.W., Poly(Pro)II helices in globular proteins:Identification and circular dichroic analysis (1994) Biochemistry, 33, pp. 10022-10025
Bhatnagar, R.S., Gough, C.A., (1996) Circular Dichroism and the Conformational Analysis of Biomolecule, , Plenum Press: New York, NY, USA
Kumar, A., Ernst, R.R., Wuthrich, K.A., Two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete protonproton cross-relaxation networks in biological macromolecules. Biochem. Biophys. Res (1980) Commun, 95, pp. 1-6
Griesinger, C., Otting, G., Wüthrich, K., Ernst, R.R., Clean, T., For proton spin system identification in macromolecules (1988) J. Am. Chem. Soc, 110, pp. 7870-7872
Bax, A., Davis, D.G., Practical aspects of -d mensional transverse NOE spectroscop y (1985) J. Magn. Reson, 63, pp. 207-213
Wishart, D.S., Sykes, B.D., Richards, F.M., Relationship between nuclear magnetic resonance chemical shift and protein secondary structure (1991) J. Mol. Biol, 222, pp. 311-333
Wüthrich, K., (1986) NMR of Proteins and Nucleic Acids, , John Wiley & Sons: New York, NY, USA
Das, R.K., Pappu, R.V., Conformations of Intrinsically disordered Proteins Areinfluenced by Linear Sequence Distributions of Oppositely Charged Residue (2013) Natl. Acad. Sci. USA, 110, pp. 13392-13397
Vila, J.A., Baldoni, H.A., Ripoll, D.R., Ghosh, A., Scheraga, H., Helix conformation in a proline-rich environment (2004) A Theoretical Study. Biophys. J, 86, pp. 731-742
Tarek, M., Tobias, D.J., Role of protein-water hydrogen bond dynamics in the protein dynamical transition (2002) Phys. Rev. Lett, 88, p. 138101
De Clercq, E., AMD3100 story:The path to the discovery of a stem cell mobilizer (Mozobil). Biochem (2009) Pharmacol, 77, pp. 1655-1664
Portella, L., Vitale, R., De Luca, S., D’Alterio, C., Ieranò, C., Napolitano, M., Riccio, A., Barbieri, A., Preclinical development of a novel class of CXCR4 antagonist impairing solid tumors growth and metastases (2013) Plos ONE, 8, p. 74548
Teicher, B.A., Fricker, S.P., CXCL12 (SDF1)/CXCR4 pathway in cancer.Clin (2010) Cancer Res, 16, pp. 2927-2931
Piantini, U., Sorensen, O.W., Ernst, R.R., Multiple quantum filters for elucidating NMR coupling networks (1982) J. Am. Chem. Soc, 104, pp. 6800-6801
Dalvit, C., Efficient multip-solvent suppression for the study of the interactions of organic solvents with biomolecules (1998) J. Biomol. NMR, 11, pp. 437-444
Bartels, X.T., Billeter, M., Guntert, P., Wuthrich, K., The program XEASY for computer-supported NMR spectral analysis of biological macromolecules (1995) J. Biomol. NMR, 6, pp. 1-10
Van Der Spoel, D., Lindahl, E., Hess, B., Groenhof, G., Mark, A.E., Berendsen, H.J., GROMACS: Fast, flexible, and free (2005) J. Comput. Chem, 26, pp. 1701-1718
Guariniello, S., Colonna, G., Raucci, R., Costantini, M., Di Bernardo, G., Bergantino, F., Castello, G., Costantini, S., Structure-function relationship and evolutionary history of the human selenoprotein M (SelM) found over-expressed in hepatocellular carcinoma (2014) Biochim. Biophys. Acta, 1844, pp. 447-456
McDonald, I.K., Thornton, J.M., Satisfying hydrogen bonding potential in proteins (1994) J. Mol. Biol, 238, pp. 777-793
Crump, M.P., Gong, J.H., Loetscher, P., Rajarathnam, K., Amara, A., Arenzana-Seisdedos, F., Virelizier, J.L., Clark-Lewis, I., Solution structure and basis for functional activity of stromal cell derived fac1
r-dissociation of CXCR4 activation from binding and inhibition of HIV-1 (1997) EMBO J, 16, pp. 6996-7007
Int J Mol Sc (ISSN: 1422-0067, 1661-6596, 1422-0067linking), 2015; 16(6): 12159-12173.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 3.257, 5-year impact factor: 3.213
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-84930636141&partnerID=40&md5=3b2345c8b9e709bb01a096a4e4353606
Keywords: Chemokine, Conformational Ensemble, Intrinsically Disordered Protein (id), Intrinsically Disordered Region(idr), Chemokine Receptor Cxcr4, Antigen Binding, Article, Binding Assay, Camp Assay, Cell Migration Assay, Circular Dichroism, Controlled Study, Human, Human Cell, Hydrogen Bond, Mass Spectrometry, Molecular Dynamics, Molecular Recognition, Nuclear Magnetic Resonance Spectroscopy, Peptide Synthesis, Protein Conformation, Receptor Binding, Reversed Phase High Performance Liquid Chromatography, Simulation,
Affiliations:
*** IBB - CNR ***
Department of Pharmacy, University of Naples “Federico II” and CIRPeB, Via Mezzocannone 16, Naples, Italy
Institute of Biostructures and Bioimaging (IBB), National Research Council (CNR), Via Mezzocannone 16, Naples, Italy
Oncology Research Center of Mercogliano (CROM), Istituto Nazionale Tumori “Fondazione G. Pascale”, IRCCS, Napoli, Italy
Molecular Immunology and Immuneregulation, Istituto Nazionale Tumori “Fondazione G. Pascale”, IRCCS, Napoli, Italy
Center of Medical Informatics, AOU Second University of Naples, Napoli, Italy
UFR des Sciences Pharmaceutiques—Collège Sciences de la Santé INSERM U869, Laboratoire ARNA, Université de Bordeaux, 146 rue Léo Saignat, Bordeaux cedex, France
References:
Habchi, J., Tompa, P., Longhi, S., Uversky, V.N., Introducing protein intrinsic disorder (2014) Chem. Rev, 114, pp. 6561-658
He, B., Wang, K., Liu, Y., Xue, B., Uversky, V.N., Dunker, A.K., Predicting intrinsic disorder in proteins: An overview (2009) Cell Res, 19, pp. 929-949
Motlagh, H.N., Wrabl, J.O., Li, J., Hilsen, V.J., The ensemble nature of allostery (2014) Nature, 508, pp. 331-338
Wright, P.E., Dyson, H.J., Intrinsically unstructured proteR e:-assessing the protein structure-function paradigm (1999) J. Mol. Biol, 293, pp. 321-331
Iakoucheva, L.M., Brown, C.J., Lawson, J.D., Obradovic, Z., Dunker, A.K., Intrinsicdisorder in cell-signaling and cancer-associated proteins (2002) J. Mol. Biol, 323, pp. 573-584
Schweitzer-Stenner, R., Conformational propensities and residual structures in unfolded peptides and proteins (2012) Mol. Biosyst, 8, pp. 122-133
Uversky, V.N., Intrinsically disordered protein from A to Z.Int (2011) J. Biochem. Cell Biol, 43, pp. 1090-1103
Leone, M., Mercurio, F.A., Vincenzi, M., Accardo, A., Ringhieri, P., Tesauro, D., Carrière, F., Rossi, F., Conformational disorder in phosphopeptidSo:Lution studies by CD and NMR techniques (2014) Peptidomics, 1, pp. 14-21
Miller, M., The importance of being flexible:The case of basic region leucine zipper transcriptional regulators (2009) Curr. Protein Pept. Sci, 10, pp. 244-269
Sigalov, A.B., Uversky, V.N., Differential occurrence of protein intrinsic disord ethe in cytoplasmic signaling domains of cell receptors (2011) Self Nonself, 2, pp. 55-72
Costantini, S., Sharma, A., Raucci, R., Costantini, M., Autiero, I., Colonna, G., Genealogy of an ancient protein family: The Sirtuins, a family of disordered members.BMC Evol (2013) Biol, 13, pp. 60-80
Raucci, R., Colonna, G., Giovane, A., Castello, G., Costantini, S., N-terminal region of human chemokine receptor CXCR3: Structural analysis of CXCR3(1-48) by experimental and computational studies (2014) Biochim. Biophys. Acta, 1844, pp. 1868-1880
Mittal, J., Hyeonyoo, T., Georgiou, G., Truskett, T.T., Structural ensemble of an intrinsically disordered polypeptide (2013) J. Phys. Chem. B, 117, pp. 118-124
Chen, S., Gao, S., Cheng, D., Huang, J., The characterization and comparison of amyloidogenic segments and non-amyloidogenic segments shed light on amyloid formationB iochem (2014) Biophys. Res. Commun, 447, pp. 255-262
Costantini, S., Raucci, R., Colonna, G., Mercurio, F.A., Trotta, A.M., Ringhieri, P., Leone, M., Castello, G., . Peptides targeting chemokine receptor CXCR4: Structural behavior and biological binding studies (2014) J. Pept. Sci, 20, pp. 270-278
Palladino, P., Portella, L., Colonna, G., Raucci, R., Saviano, G., Rossi, F., Napolitano, M., Costantini, S., The N-terminal region of CXCL11 as structural templat e for CXCR3 molecular recognitionS ynthesis, conformational analysis, and binding studies (2012) Chem. Biol. Drug Des, 80, pp. 254-265
Underfriend, S., Meienhofer, J., (1985) In the Peptides, p. 7. , Hruby, V.J., Ed.
Academic Press: New York, NY, USA
Wiedemann, C.I., Bellstedt, P., Görlach, M., CAPITO-a web server-based analysis and plotting tool for circular dichroism data (2013) Bioinformatics, 29, pp. 1750-1757
Sreerama, N., Woody, R.W., Poly(Pro)II helices in globular proteins:Identification and circular dichroic analysis (1994) Biochemistry, 33, pp. 10022-10025
Bhatnagar, R.S., Gough, C.A., (1996) Circular Dichroism and the Conformational Analysis of Biomolecule, , Plenum Press: New York, NY, USA
Kumar, A., Ernst, R.R., Wuthrich, K.A., Two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete protonproton cross-relaxation networks in biological macromolecules. Biochem. Biophys. Res (1980) Commun, 95, pp. 1-6
Griesinger, C., Otting, G., Wüthrich, K., Ernst, R.R., Clean, T., For proton spin system identification in macromolecules (1988) J. Am. Chem. Soc, 110, pp. 7870-7872
Bax, A., Davis, D.G., Practical aspects of -d mensional transverse NOE spectroscop y (1985) J. Magn. Reson, 63, pp. 207-213
Wishart, D.S., Sykes, B.D., Richards, F.M., Relationship between nuclear magnetic resonance chemical shift and protein secondary structure (1991) J. Mol. Biol, 222, pp. 311-333
Wüthrich, K., (1986) NMR of Proteins and Nucleic Acids, , John Wiley & Sons: New York, NY, USA
Das, R.K., Pappu, R.V., Conformations of Intrinsically disordered Proteins Areinfluenced by Linear Sequence Distributions of Oppositely Charged Residue (2013) Natl. Acad. Sci. USA, 110, pp. 13392-13397
Vila, J.A., Baldoni, H.A., Ripoll, D.R., Ghosh, A., Scheraga, H., Helix conformation in a proline-rich environment (2004) A Theoretical Study. Biophys. J, 86, pp. 731-742
Tarek, M., Tobias, D.J., Role of protein-water hydrogen bond dynamics in the protein dynamical transition (2002) Phys. Rev. Lett, 88, p. 138101
De Clercq, E., AMD3100 story:The path to the discovery of a stem cell mobilizer (Mozobil). Biochem (2009) Pharmacol, 77, pp. 1655-1664
Portella, L., Vitale, R., De Luca, S., D’Alterio, C., Ieranò, C., Napolitano, M., Riccio, A., Barbieri, A., Preclinical development of a novel class of CXCR4 antagonist impairing solid tumors growth and metastases (2013) Plos ONE, 8, p. 74548
Teicher, B.A., Fricker, S.P., CXCL12 (SDF1)/CXCR4 pathway in cancer.Clin (2010) Cancer Res, 16, pp. 2927-2931
Piantini, U., Sorensen, O.W., Ernst, R.R., Multiple quantum filters for elucidating NMR coupling networks (1982) J. Am. Chem. Soc, 104, pp. 6800-6801
Dalvit, C., Efficient multip-solvent suppression for the study of the interactions of organic solvents with biomolecules (1998) J. Biomol. NMR, 11, pp. 437-444
Bartels, X.T., Billeter, M., Guntert, P., Wuthrich, K., The program XEASY for computer-supported NMR spectral analysis of biological macromolecules (1995) J. Biomol. NMR, 6, pp. 1-10
Van Der Spoel, D., Lindahl, E., Hess, B., Groenhof, G., Mark, A.E., Berendsen, H.J., GROMACS: Fast, flexible, and free (2005) J. Comput. Chem, 26, pp. 1701-1718
Guariniello, S., Colonna, G., Raucci, R., Costantini, M., Di Bernardo, G., Bergantino, F., Castello, G., Costantini, S., Structure-function relationship and evolutionary history of the human selenoprotein M (SelM) found over-expressed in hepatocellular carcinoma (2014) Biochim. Biophys. Acta, 1844, pp. 447-456
McDonald, I.K., Thornton, J.M., Satisfying hydrogen bonding potential in proteins (1994) J. Mol. Biol, 238, pp. 777-793
Crump, M.P., Gong, J.H., Loetscher, P., Rajarathnam, K., Amara, A., Arenzana-Seisdedos, F., Virelizier, J.L., Clark-Lewis, I., Solution structure and basis for functional activity of stromal cell derived fac1
r-dissociation of CXCR4 activation from binding and inhibition of HIV-1 (1997) EMBO J, 16, pp. 6996-7007
Conformational ensembles explored dynamically from disordered peptides targeting chemokine receptor CXCR4
This work reports on the design andthe synthesis of two short linear peptides both containing a few amino acids with disorder propensity and an allylic ester group at the C-terminal end. Their structural properties were firstly analyzed by means of experimental techniques in solution such as CD and NMR methodsthat highlighted peptide flexibility. These results were further confirmed by MD simulationsthat demonstrated the ability of the peptides to assume conformational ensembles. Theyrevealed a network of transient and dynamic -bonds and interactions with water molecules. Binding assays with a well-known drug-target, i.e., the CXCR4 receptor, were also carried out in an attempt to verify their biological function and the possibility to use the assays to develop new specific targets for CXCR4. Moreover, our data indicate that these peptides represent useful tools for molecular recognition processes in which a flexible conformation is required in order to obtain an interaction with a specific target. © 2015 by the authors; licensee MDPI, Basel, Switzerland.
This work reports on the design andthe synthesis of two short linear peptides both containing a few amino acids with disorder propensity and an allylic ester group at the C-terminal end. Their structural properties were firstly analyzed by means of experimental techniques in solution such as CD and NMR methodsthat highlighted peptide flexibility. These results were further confirmed by MD simulationsthat demonstrated the ability of the peptides to assume conformational ensembles. Theyrevealed a network of transient and dynamic -bonds and interactions with water molecules. Binding assays with a well-known drug-target, i.e., the CXCR4 receptor, were also carried out in an attempt to verify their biological function and the possibility to use the assays to develop new specific targets for CXCR4. Moreover, our data indicate that these peptides represent useful tools for molecular recognition processes in which a flexible conformation is required in order to obtain an interaction with a specific target. © 2015 by the authors; licensee MDPI, Basel, Switzerland.
Conformational ensembles explored dynamically from disordered peptides targeting chemokine receptor CXCR4
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Conformational ensembles explored dynamically from disordered peptides targeting chemokine receptor CXCR4
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Palladino P, Pedone C, Ragone R, Rossi F, Saviano M, Benedetti E
* A simplified model of the binding interaction between stromal cell-derived factor-1 chemokine and CXC chemokine receptor (351 views)
Protein Pept Lett (ISSN: 0929-8665, 1875-5305), 2003 Apr; 10(2): 133-138.
Impact Factor: 0.46
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Palladino P, De Capua A, Pedone C, Ragone R, Rossi F, Limatola C, Ragozzino D, Benedetti E
* A simplified model of the interaction between SDF-1 chemokine and the CXCR4 receptor (384 views)
Peptide Revolution, 2003 Apr; 10(2): 133-138.
Impact Factor: 4.659
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* NMR spectroscopy in the conformational analysis of peptides: an overview (91 views)
Curr Med Chem (ISSN: 0929-8673linking, 1875-533xelectronic), 2021; 28(14): 2729-2782.
Impact Factor: 4.184
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Pelagalli A, Nardelli A, Lucarelli E, Zannetti A, Brunetti A
* Autocrine signals increase Ovine Mesenchymal Stem Cells migration through Aquaporin-1 and CXCR4 overexpression (723 views)
J Cell Physiol (ISSN: 1097-4652electronic, 0021-9541linking), 2018 Jan 18; 233(8): 6241-6249.
Impact Factor: 5.546
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Brancaccio D, Diana D, Di Maro S, Di Leva FS, Tomassi S, Fattorusso R, Russo L, Scala S, Trotta AM, Portella L, Novellino E, Marinelli L, Carotenuto A
* Ligand-Based NMR Study of C-X-C Chemokine Receptor Type 4 (CXCR4)-Ligand Interactions on Living Cancer Cells (1107 views)
J Med Chem (ISSN: 0022-2623, 1520-4804, 0022-2623print), 2018; 61(7): 2910-2923.
Impact Factor: 5.207
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Fontanella R, Pelagalli A, Nardelli A, D'Alterio C, Ierano C, Cerchia L, Lucarelli E, Scala S, Zannetti A
* A novel antagonist of CXCR4 prevents bone marrow-derived mesenchymal stem cell-mediated osteosarcoma and hepatocellular carcinoma cell migration and invasion (931 views) (PDF 283 views)
Cancer Lett (ISSN: 0304-3835), 2015 Oct 27; 370(1): 100-107.
Impact Factor: 7.36
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Calce E, Monfregola L, Saviano M, De Luca S
* HER2-mediated anticancer drug delivery: strategies to prepare targeting ligands highly specific for the receptor (573 views)
Curr Med Chem (ISSN: 0929-8673, 1875-533x, 1875-533xelectronic), 2015 May 20; 22(21): 2525-2538.
Impact Factor: 3.455
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Calce E, Vitale RM, Scaloni A, Amodeo P, De Luca S
* Air oxidation method employed for the disulfide bond formation of natural and synthetic peptides (604 views)
Amino Acids (ISSN: 0939-4451, 1438-2199, 1438-2199electronic), 2015; 47(8): 1507-1515.
Impact Factor: 3.196
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Neve Polimeno M, Ierano C, D'Alterio C, Simona Losito N, Napolitano M, Portella L, Scognamiglio G, Tatangelo F, Maria Trotta A, Curley S, Costantini S, Liuzzi R, Izzo F, Scala S
* CXCR4 expression affects overall survival of HCC patients whereas CXCR7 expression does not (671 views)
Cell Mol Immunol (ISSN: 1672-7681), 2014 Nov 3; 12(4): 474-482.
Impact Factor: 4.112
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D'Alterio C, Avallone A, Tatangelo F, Delrio P, Pecori B, Cella L, Pelella A, D'Armiento FP, Carlomagno C, Bianco F, Silvestro L, Pacelli R, Napolitano M, Iaffaioli RV, Scala S
* A prognostic model comprising pT stage, N status, and the chemokine receptors CXCR4 and CXCR7 powerfully predicts outcome in neoadjuvant resistant rectal cancer patients (441 views)
Int J Cancer (ISSN: 0020-7136), 2014 Jul 15; 135(2): 379-390.
Impact Factor: 5.085
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Portella L, Vitale R, De Luca S, D'Alterio C, Ieranò C, Napolitano M, Riccio A, Polimeno MN, Monfregola L, Barbieri A, Luciano A, Ciarmiello A, Arra C, Castello G, Amodeo P, Scala S
* Preclinical Development of a Novel Class of CXCR4 Antagonist Impairing Solid Tumors Growth and Metastases (505 views)
Plosone (ISSN: 1932-6203, 1932-6203electronic, 1932-6203linking), 2013 Sep 13; 8(9): N/D-N/D.
Impact Factor: 3.534
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Russo L, Raiola L, Campitiello MA, Magrì A, Fattorusso R, Malgieri G, Pappalardo G, La Mendola D, Isernia C
* Probing the residual structure in avian prion hexarepeats by CD, NMR and MD techniques (419 views)
Molecules (ISSN: 1420-3049, 1420-3049electronic, 1420-3049linking), 2013 Sep; 18(9): 11467-11484.
Impact Factor: 2.095
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Sandomenico A, Monti SM, Palumbo R, Ruvo M
* A New Fc Epsilon Ri Receptor-Mimetic Peptide (pepe) That Blocks Ige Binding To Its High Affinity Receptor And Prevents Mediator Release From Rbl 2h3 Cells (666 views)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2011 Sep; 17(9): 604-609.
Impact Factor: 1.799
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Lusso P, Vangelista L, Cimbro R, Secchi M, Sironi F, Longhi R, Faiella M, Maglio O, Pavone V
* Molecular engineering of RANTES peptide mimetics with potent anti-HIV-1 activity (586 views)
Faseb J (ISSN: 0892-6638, 0892-6638linking), 2011 Apr; 25(4): 1230-1243.
Impact Factor: 5.712
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Napolitano M, Ottaiano A, Mauro F, Ieranò C, Satriano R, Pacelli R, Franco R, De Angelis V, Castello G, Scala S
* CD4(+)CD45RA(+)CXCR4(+) lymphocytes are inversely associated with progression in stages I-III melanoma patients (403 views)
Cancer Immunol Immunother (ISSN: 0340-7004, 0340-7004linking), 2010 Apr; 59(4): 511-517.
Impact Factor: 4.293
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Ierano C, Giuliano P, D'Alterio C, Cioffi M, Mettivier V, Portella L, Napolitano M, Barbieri A, Arra C, Liguori G, Franco R, Palmieri G, Rozzo C, Pacelli R, Castello G, Scala S
* A point mutation (G574A) in the chemokine receptor CXCR4 detected in human cancer cells enhances migration (394 views)
Cell Cycle (ISSN: 1538-4101), 2009 Apr 15; 8(8): 1228-1237.
Impact Factor: 4.087
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Palladino P, Tizzano B, Pedone C, Ragone R, Rossi F, Saviano G, Tancredi T, Benedetti E
* Structural determinants of unexpected agonist activity in a retro-peptide analogue of the SDF-1α N-terminus (378 views)
Febs Lett (ISSN: 0014-5793, 0014-5793print, 1873-3468electronic), 2005 Oct 10; 579(24): 5293-5298.
Impact Factor: 3.415
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Verdoliva A, Marasco D, De Capua A, Saporito A, Bellofiore P, Manfredi V, Fattorusso R, Pedone C, Ruvo M
* A new ligand for immunoglobulin G subdomains by screening of a synthetic peptide library (501 views)
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-7633electronic), 2005 Jul; 6(7): 1242-1253.
Impact Factor: 3.94
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Palladino P, Pedone C, Ragone R, Rossi F, Saviano M, Benedetti E
* A simplified model of the binding interaction between stromal cell-derived factor-1 chemokine and CXC chemokine receptor (351 views)
Protein Pept Lett (ISSN: 0929-8665, 1875-5305), 2003 Apr; 10(2): 133-138.
Impact Factor: 0.46
View Export to BibTeX Export to EndNote
Palladino P, De Capua A, Pedone C, Ragone R, Rossi F, Limatola C, Ragozzino D, Benedetti E
* A simplified model of the interaction between SDF-1 chemokine and the CXCR4 receptor (384 views)
Peptide Revolution, 2003 Apr; 10(2): 133-138.
Impact Factor: 4.659
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18 Records (17 excluding Abstracts).
Total impact factor: 72.139 (68.605 excluding Abstracts).
Total 5 year impact factor: 67.217 (63.202 excluding Abstracts).
Total impact factor: 72.139 (68.605 excluding Abstracts).
Total 5 year impact factor: 67.217 (63.202 excluding Abstracts).
604 views. Last view on Tuesday 30 May 2023, 3:12:41
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