The inorganic perspective of nerve growth factor: interactions of Cu2+ and Zn2+ with the N-terminus fragment of nerve growth factor encompassing the recognition domain of the TrkA receptor (487 views)
Chemistry (ISSN: 1521-3765, 0947-6539, 1521-3765electronic), 2011 Mar 21; 17(13): 3726-3738.
Export to BibTeX Export to EndNote
Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 5.925, 5-year impact factor: 5.866
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-79952589514&partnerID=40&md5=5ded2e1a77c84995efea17aa89cccc69
Keywords: Copper, Nerve Growth Factor (ngf), Peptides, Proteins, Zinc, After-Treatment, Amino Group, Amino-Terminal Domain, Brain Areas, C Terminus, Computational Analysis, Critical Domain, Experimental Data, Metal Binding, Metal-Ion Coordination, Monomeric Units, N-Terminal Domains, Nervous System, Neuroblastoma Cell Lines, Pentacoordinate Complexes, Peptide Fragments, Physiological Ph, Proliferative Activity, Receptor Binding, Cell Culture, Complexation, Dimers, Electron Spin Resonance Spectroscopy, Protein Tyrosine Kinase A, Article, Chemical Structure, Chemistry, Human, Metabolism, Molecular Genetics, Protein Binding, Ultraviolet Spectrophotometry, Molecular Sequence Data, Molecular Structure,
Affiliations:
*** IBB - CNR ***
Dipartimento di Scienze Chimiche, Universita degli Studi di Catania, Viale Andrea Doria 6, 95125 Catania, Italy.
Istituto di Biostrutture e Bioimmagini-CNR C/o, Dipartimento di Scienze Chimiche, Viale Andrea Doria 6, 95125 Catania, Italy
References:
Levi-Montalcini, R., (1987) Science, 237, pp. 1154-116
Lad, S.P., Neet, K.E., Mufson, E.J., (2003) Curr. Drug Targets: CNS Neurol. Disord., 2, pp. 315-334
Snider, W.D., (1994) Cell, 77, pp. 627-638
Ernsberger, U., (2009) Cell Tissue Res., 336, pp. 349-384
Johnson, D., Lanahan, A., Buck, C.R., Sehgal, A., Morgan, C., Mercer, E., Bothwell, M., Chao, M., (1986) Cell, 47, pp. 545-554
Neet, K.E., Campenot, R.B., (2001) Cell. Mol. Life Sci., 58, pp. 1021-1035
Kaplan, D.R., Martin-Zanca, D., Parada, L.F., (1991) Nature, 350, pp. 158-160
Urfer, R., Tsoulfas, P., O'Connell, L., Shelton, D.L., Parada, L.F., Presta, L.G., (1995) EMBO J., 14, pp. 2795-2805
Wiesmann, C., Ultsch, M.H., Bass, S.H., De Vos, A.M., (1999) Nature, 401, pp. 184-188
Kahle, P., Burton, L.E., Schmelzer, C.H., Hertel, C., (1992) J. Biol. Chem., 267, pp. 22707-22710
Salehi, A., Delcroix, J.D., Swaab, D.F., (2004) J. Neural Transm., 111, pp. 323-345
Capsoni, S., Cattaneo, A., (2006) Cell. Mol. Neurobiol., 26, pp. 617-631
Bush, A.I., (2008) J. Alzheimer's Dis., 15, pp. 223-240
Bush, A.I., Tanzi, R.E., (2008) Neurotherapeutics, 5, pp. 421-432
Harrison, N.L., Gibbons, S.J., (1994) Neuropharmacology, 33, pp. 935-952
Ross, G.M., Shamovsky, I.L., Lawrance, G., Solc, M., Dostaler, S.M., Jimmo, S.L., Weaver, D.F., Riopelle, R.J., (1997) Nat. Med., 3, pp. 872-878
Wang, W., Post, J.I., Dow, K.E., Shin, S.H., Riopelle, R.J., Ross, G.M., (1999) Neurosci. Lett., 259, pp. 115-118
Shamovsky, I.L., Ross, G.M., Riopelle, R.J., Weaver, D.F., (1999) J. Am. Chem. Soc., 121, pp. 9797-9806
Maitra, R., Shamovsky, I.L., Wang, W., Solc, M., Lawrance, G., Dostaler, S.M., Ross, G.M., Riopelle, R.J., (2000) Neurotoxic. Res., 2, pp. 321-341
Allington, C., Shamovsky, I.L., Ross, G.M., Riopelle, R.J., (2001) Cell Death Differ., 8, pp. 451-456
Birkaya, B., Aletta, J.M., (2005) J. Neurobiol., 63, pp. 49-61
Hwang, J.J., Park, M.H., Choi, S.Y., Koh, J.Y., (2005) J. Biol. Chem., 280, pp. 11995-12001
Shih, A., Laramee, G.R., Schmelzer, C.H., Burton, L.E., Winslow, J.W., (1994) J. Biol. Chem., 269, pp. 27679-27686
Woo, S.B., Neet, K.E., (1996) J. Biol. Chem., 271, pp. 24433-24441
Wishart, D.S., Sykes, B.D., Richards, F.M., (1992) Biochemistry, 31, pp. 1647-1651
La Mendola, D., Bonomo, R.P., Impellizzeri, G., MacCarrone, G., Pappalardo, G., Pietropaolo, A., Rizzarelli, E., Zito, V., (2005) J. Biol. Inorg. Chem., 10, pp. 463-475
Timári, S., Kállay, C., Osz, K., Sõvágõ, I., Várnagy, K., (2009) Dalton Trans., pp. 1962-1971
Kállay, C., Várnagy, K., Micera, G., Sanna, D., Sõvágõ, I., (2005) J. Inorg. Biochem., 99, pp. 1514-1525
Damante, C.A., Osz, K., Nagy, Z., Pappalardo, G., Grasso, G., Impellizzeri, G., Rizzarelli, E., Sovago, I., (2009) Inorg. Chem., 48, pp. 10405-10415
Galanis, A.S., Spyroulias, G.A., Pierattelli, R., Tzakos, A., Troganis, A., Gerothanassis, I.P., Pairas, G., Cordopatis, P., (2003) Biopolymers, 69, pp. 244-252
Gaggelli, E., Janicka-Klos, A., Jankowska, E., Kozlowski, H., Migliorini, C., Molteni, E., Valensin, D., Wieczerzak, E., (2008) J. Phys. Chem. B, 112, pp. 100-109
Camponeschi, E., Gaggelli, E., Kozłowski, H., Valensin, D., Valensin, G., (2009) Dalton Trans., pp. 4643-4645
Karavelas, T., Mylonas, M., Mlandrinos, G., Plakatouras, J.C., Hadjiliadis, N., Mlynarz, P., Kozlowski, H., (2005) J. Inorg. Biochem., 99, pp. 606-615
La Mendola, D., Magrì, A., Hansson, Ö., Bonomo, R.P., Rizzarelli, E., (2009) J. Inorg. Biochem., 103, pp. 758-765
Várnagy, K., Szabo, J., Sovago, I., Malndrinos, G., Hadjliadis, N., Sanna, D., Micera, G., (2000) J. Chem. Soc. Dalton Trans., pp. 467-472
Dorlet, P., Gambarelli, S., Faller, P., Hureau, C., (2009) Angew. Chem., 121, pp. 9437-9440
(2009) Angew. Chem. Int. Ed., 48, pp. 9273-9276
Rozga, M., Bal, W., (2010) Chem. Res. Toxicol., 23, pp. 298-308
Chao, M.V., Rajagopal, R., Lee, F.S., (2006) Clin. Sci., 110, pp. 167-173
Moscatelli, I., Pierantozzi, E., Camaioni, A., Siracusa, G., Campagnolo, L., (2009) Exp. Cell Res., 315, pp. 3220-3232
Bassili, M., Birman, E., Schor, N.F., Sargovi, H.U., (2010) Cancer Chemother. Pharmacol., 65, pp. 1047-1056
Cattaneo, A., Capsoni, S., Paoletti, F., (2008) J. Alzheimer's Dis., 15, pp. 255-283
Peleshok, J., Saragovi, H.U., (2006) Biochem. Soc. Trans., 34, pp. 612-617
Longo, F.M., Vu, T.K., Mobley, W.C., (1990) Curr. Top. Cell. Regul., 1, pp. 189-195
Colangelo, A.M., Bianco, M.R., Vitagliano, L., Cavaliere, C., Cirillo, G., Degioia, L., Diana, D., Martegani, E., (2008) J. Neurosci., 28, pp. 2698-2709
Gans, P., Sabatini, A., Vacca, A., (1996) Talanta, 43, pp. 1739-1753
Alderighi, L., Gans, P., Ienco, A., Peters, D., Sabatini, A., Vacca, A., (1999) Coord. Chem. Rev., 184, pp. 311-318
Cavanagh, J., Fairbrother, W., Iii, A.G.P., Skelton, N.J., (1996) Protein NMR Spectroscopy: Principles and Practice, , Academic Press, San Diego
Hwang, T.L., Shaka, A.J., (1995) J. Magn. Reson. Ser. A, 112, pp. 275-279
Bartels, C., Xia, T., Billeter, M., Guntert, P., Wüthrich, K., (1995) J. Biomol. NMR, 6, pp. 1-10
Stejskal, E.O., Tanner, J.E., (1965) J. Chem. Phys., 42, pp. 288-292
Chatterjee, C., Majumder, B., Mukhopadhyay, C., (2004) J. Phys. Chem. B, 108, pp. 7430-7436
Chemistry (ISSN: 1521-3765, 0947-6539, 1521-3765electronic), 2011 Mar 21; 17(13): 3726-3738.
Export to BibTeX Export to EndNote
Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 5.925, 5-year impact factor: 5.866
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-79952589514&partnerID=40&md5=5ded2e1a77c84995efea17aa89cccc69
Keywords: Copper, Nerve Growth Factor (ngf), Peptides, Proteins, Zinc, After-Treatment, Amino Group, Amino-Terminal Domain, Brain Areas, C Terminus, Computational Analysis, Critical Domain, Experimental Data, Metal Binding, Metal-Ion Coordination, Monomeric Units, N-Terminal Domains, Nervous System, Neuroblastoma Cell Lines, Pentacoordinate Complexes, Peptide Fragments, Physiological Ph, Proliferative Activity, Receptor Binding, Cell Culture, Complexation, Dimers, Electron Spin Resonance Spectroscopy, Protein Tyrosine Kinase A, Article, Chemical Structure, Chemistry, Human, Metabolism, Molecular Genetics, Protein Binding, Ultraviolet Spectrophotometry, Molecular Sequence Data, Molecular Structure,
Affiliations:
*** IBB - CNR ***
Dipartimento di Scienze Chimiche, Universita degli Studi di Catania, Viale Andrea Doria 6, 95125 Catania, Italy.
Istituto di Biostrutture e Bioimmagini-CNR C/o, Dipartimento di Scienze Chimiche, Viale Andrea Doria 6, 95125 Catania, Italy
References:
Levi-Montalcini, R., (1987) Science, 237, pp. 1154-116
Lad, S.P., Neet, K.E., Mufson, E.J., (2003) Curr. Drug Targets: CNS Neurol. Disord., 2, pp. 315-334
Snider, W.D., (1994) Cell, 77, pp. 627-638
Ernsberger, U., (2009) Cell Tissue Res., 336, pp. 349-384
Johnson, D., Lanahan, A., Buck, C.R., Sehgal, A., Morgan, C., Mercer, E., Bothwell, M., Chao, M., (1986) Cell, 47, pp. 545-554
Neet, K.E., Campenot, R.B., (2001) Cell. Mol. Life Sci., 58, pp. 1021-1035
Kaplan, D.R., Martin-Zanca, D., Parada, L.F., (1991) Nature, 350, pp. 158-160
Urfer, R., Tsoulfas, P., O'Connell, L., Shelton, D.L., Parada, L.F., Presta, L.G., (1995) EMBO J., 14, pp. 2795-2805
Wiesmann, C., Ultsch, M.H., Bass, S.H., De Vos, A.M., (1999) Nature, 401, pp. 184-188
Kahle, P., Burton, L.E., Schmelzer, C.H., Hertel, C., (1992) J. Biol. Chem., 267, pp. 22707-22710
Salehi, A., Delcroix, J.D., Swaab, D.F., (2004) J. Neural Transm., 111, pp. 323-345
Capsoni, S., Cattaneo, A., (2006) Cell. Mol. Neurobiol., 26, pp. 617-631
Bush, A.I., (2008) J. Alzheimer's Dis., 15, pp. 223-240
Bush, A.I., Tanzi, R.E., (2008) Neurotherapeutics, 5, pp. 421-432
Harrison, N.L., Gibbons, S.J., (1994) Neuropharmacology, 33, pp. 935-952
Ross, G.M., Shamovsky, I.L., Lawrance, G., Solc, M., Dostaler, S.M., Jimmo, S.L., Weaver, D.F., Riopelle, R.J., (1997) Nat. Med., 3, pp. 872-878
Wang, W., Post, J.I., Dow, K.E., Shin, S.H., Riopelle, R.J., Ross, G.M., (1999) Neurosci. Lett., 259, pp. 115-118
Shamovsky, I.L., Ross, G.M., Riopelle, R.J., Weaver, D.F., (1999) J. Am. Chem. Soc., 121, pp. 9797-9806
Maitra, R., Shamovsky, I.L., Wang, W., Solc, M., Lawrance, G., Dostaler, S.M., Ross, G.M., Riopelle, R.J., (2000) Neurotoxic. Res., 2, pp. 321-341
Allington, C., Shamovsky, I.L., Ross, G.M., Riopelle, R.J., (2001) Cell Death Differ., 8, pp. 451-456
Birkaya, B., Aletta, J.M., (2005) J. Neurobiol., 63, pp. 49-61
Hwang, J.J., Park, M.H., Choi, S.Y., Koh, J.Y., (2005) J. Biol. Chem., 280, pp. 11995-12001
Shih, A., Laramee, G.R., Schmelzer, C.H., Burton, L.E., Winslow, J.W., (1994) J. Biol. Chem., 269, pp. 27679-27686
Woo, S.B., Neet, K.E., (1996) J. Biol. Chem., 271, pp. 24433-24441
Wishart, D.S., Sykes, B.D., Richards, F.M., (1992) Biochemistry, 31, pp. 1647-1651
La Mendola, D., Bonomo, R.P., Impellizzeri, G., MacCarrone, G., Pappalardo, G., Pietropaolo, A., Rizzarelli, E., Zito, V., (2005) J. Biol. Inorg. Chem., 10, pp. 463-475
Timári, S., Kállay, C., Osz, K., Sõvágõ, I., Várnagy, K., (2009) Dalton Trans., pp. 1962-1971
Kállay, C., Várnagy, K., Micera, G., Sanna, D., Sõvágõ, I., (2005) J. Inorg. Biochem., 99, pp. 1514-1525
Damante, C.A., Osz, K., Nagy, Z., Pappalardo, G., Grasso, G., Impellizzeri, G., Rizzarelli, E., Sovago, I., (2009) Inorg. Chem., 48, pp. 10405-10415
Galanis, A.S., Spyroulias, G.A., Pierattelli, R., Tzakos, A., Troganis, A., Gerothanassis, I.P., Pairas, G., Cordopatis, P., (2003) Biopolymers, 69, pp. 244-252
Gaggelli, E., Janicka-Klos, A., Jankowska, E., Kozlowski, H., Migliorini, C., Molteni, E., Valensin, D., Wieczerzak, E., (2008) J. Phys. Chem. B, 112, pp. 100-109
Camponeschi, E., Gaggelli, E., Kozłowski, H., Valensin, D., Valensin, G., (2009) Dalton Trans., pp. 4643-4645
Karavelas, T., Mylonas, M., Mlandrinos, G., Plakatouras, J.C., Hadjiliadis, N., Mlynarz, P., Kozlowski, H., (2005) J. Inorg. Biochem., 99, pp. 606-615
La Mendola, D., Magrì, A., Hansson, Ö., Bonomo, R.P., Rizzarelli, E., (2009) J. Inorg. Biochem., 103, pp. 758-765
Várnagy, K., Szabo, J., Sovago, I., Malndrinos, G., Hadjliadis, N., Sanna, D., Micera, G., (2000) J. Chem. Soc. Dalton Trans., pp. 467-472
Dorlet, P., Gambarelli, S., Faller, P., Hureau, C., (2009) Angew. Chem., 121, pp. 9437-9440
(2009) Angew. Chem. Int. Ed., 48, pp. 9273-9276
Rozga, M., Bal, W., (2010) Chem. Res. Toxicol., 23, pp. 298-308
Chao, M.V., Rajagopal, R., Lee, F.S., (2006) Clin. Sci., 110, pp. 167-173
Moscatelli, I., Pierantozzi, E., Camaioni, A., Siracusa, G., Campagnolo, L., (2009) Exp. Cell Res., 315, pp. 3220-3232
Bassili, M., Birman, E., Schor, N.F., Sargovi, H.U., (2010) Cancer Chemother. Pharmacol., 65, pp. 1047-1056
Cattaneo, A., Capsoni, S., Paoletti, F., (2008) J. Alzheimer's Dis., 15, pp. 255-283
Peleshok, J., Saragovi, H.U., (2006) Biochem. Soc. Trans., 34, pp. 612-617
Longo, F.M., Vu, T.K., Mobley, W.C., (1990) Curr. Top. Cell. Regul., 1, pp. 189-195
Colangelo, A.M., Bianco, M.R., Vitagliano, L., Cavaliere, C., Cirillo, G., Degioia, L., Diana, D., Martegani, E., (2008) J. Neurosci., 28, pp. 2698-2709
Gans, P., Sabatini, A., Vacca, A., (1996) Talanta, 43, pp. 1739-1753
Alderighi, L., Gans, P., Ienco, A., Peters, D., Sabatini, A., Vacca, A., (1999) Coord. Chem. Rev., 184, pp. 311-318
Cavanagh, J., Fairbrother, W., Iii, A.G.P., Skelton, N.J., (1996) Protein NMR Spectroscopy: Principles and Practice, , Academic Press, San Diego
Hwang, T.L., Shaka, A.J., (1995) J. Magn. Reson. Ser. A, 112, pp. 275-279
Bartels, C., Xia, T., Billeter, M., Guntert, P., Wüthrich, K., (1995) J. Biomol. NMR, 6, pp. 1-10
Stejskal, E.O., Tanner, J.E., (1965) J. Chem. Phys., 42, pp. 288-292
Chatterjee, C., Majumder, B., Mukhopadhyay, C., (2004) J. Phys. Chem. B, 108, pp. 7430-7436
The inorganic perspective of nerve growth factor: interactions of Cu2+ and Zn2+ with the N-terminus fragment of nerve growth factor encompassing the recognition domain of the TrkA receptor
There is a significant overlap between brain areas with Zn(2+) and Cu(2+) pathological dys-homeostasis and those in which the nerve growth factor (NGF) performs its biological role. The protein NGF is necessary for the development and maintenance of the sympathetic and sensory nervous systems. Its flexible N-terminal region has been shown to be a critical domain for TrkA receptor binding and activation. Computational analyses show that Zn(2+) and Cu(2+) form pentacoordinate complexes involving both the His4 and His8 residues of the N-terminal domain of one monomeric unit and the His84 and Asp105 residues of the other monomeric unit of the NGF active dimer. To date, neither experimental data on the coordination features have been reported, nor has one of the hypotheses according to which Zn(2+) and Cu(2+) may have different binding environments or the Ser1 alpha-amino group could be involved in coordination been supported. The peptide fragment, encompassing the 1-14 sequence of the human NGF amino-terminal domain (NGF(1-14)), blocked at the C terminus, was synthesised and its Cu(2+) and Zn(2+) complexes characterized by means of potentiometric and spectroscopic (UV/Vis, CD, NMR, and EPR) techniques. The N-terminus-acetylated form of NGF(1-14) was also investigated to evaluate the involvement of the Ser1 alpha-amino group in metal-ion coordination. Our results demonstrate that the amino group is the first anchoring site for Cu(2+) and is involved in Zn(2+) coordination at physiological pH. Finally, a synergic proliferative activity of both NGF(1-14) and the whole protein on SHSY5Y neuroblastoma cell line was found after treatment in the presence of Cu(2+). This effect was not observed after treatment with the N-acetylated peptide fragment, demonstrating a functional involvement of the N-terminal amino group in metal binding and peptide activity. Copyright 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
There is a significant overlap between brain areas with Zn(2+) and Cu(2+) pathological dys-homeostasis and those in which the nerve growth factor (NGF) performs its biological role. The protein NGF is necessary for the development and maintenance of the sympathetic and sensory nervous systems. Its flexible N-terminal region has been shown to be a critical domain for TrkA receptor binding and activation. Computational analyses show that Zn(2+) and Cu(2+) form pentacoordinate complexes involving both the His4 and His8 residues of the N-terminal domain of one monomeric unit and the His84 and Asp105 residues of the other monomeric unit of the NGF active dimer. To date, neither experimental data on the coordination features have been reported, nor has one of the hypotheses according to which Zn(2+) and Cu(2+) may have different binding environments or the Ser1 alpha-amino group could be involved in coordination been supported. The peptide fragment, encompassing the 1-14 sequence of the human NGF amino-terminal domain (NGF(1-14)), blocked at the C terminus, was synthesised and its Cu(2+) and Zn(2+) complexes characterized by means of potentiometric and spectroscopic (UV/Vis, CD, NMR, and EPR) techniques. The N-terminus-acetylated form of NGF(1-14) was also investigated to evaluate the involvement of the Ser1 alpha-amino group in metal-ion coordination. Our results demonstrate that the amino group is the first anchoring site for Cu(2+) and is involved in Zn(2+) coordination at physiological pH. Finally, a synergic proliferative activity of both NGF(1-14) and the whole protein on SHSY5Y neuroblastoma cell line was found after treatment in the presence of Cu(2+). This effect was not observed after treatment with the N-acetylated peptide fragment, demonstrating a functional involvement of the N-terminal amino group in metal binding and peptide activity. Copyright 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
The inorganic perspective of nerve growth factor: interactions of Cu2+ and Zn2+ with the N-terminus fragment of nerve growth factor encompassing the recognition domain of the TrkA receptor
| ▼ New peptide–based molecules as NGF mimetics in the therapy of neurological dysfunctions |
The inorganic perspective of nerve growth factor: interactions of Cu2+ and Zn2+ with the N-terminus fragment of nerve growth factor encompassing the recognition domain of the TrkA receptor
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Int J Radiat Oncol (ISSN: 0360-3016, 1879-355x, 1879-355xelectronic), 2012 Apr 1; 82(5): 1802-1808.
Impact Factor: 4.524
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Cirillo G, Colangelo AM, Bianco MR, Cavaliere C, Zaccaro L, Sarmientos P, Alberghina L, Papa M
* BB14, a Nerve Growth Factor (NGF)-like peptide shown to be effective in reducing reactive astrogliosis and restoring synaptic homeostasis in a rat model of peripheral nerve injury (380 views)
Biotechnology Advances (ISSN: 0734-9750), 2012 Jan; 30(1): 223-232.
Impact Factor: 9.599
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Colangelo AM, Bianco MR, Vitagliano L, Cavaliere C, Cirillo G, De Gioia L, Diana D, Colombo D, Redaelli C, Zaccaro L, Morelli G, Papa M, Sarmientos P, Alberghina L, Martegani E
* A New Nerve Growth Factor (ngf)-Mimetic Peptide Active On Neuropathic Pain In Rats (591 views)
J Neurosci (ISSN: 0270-6474, 0270-0647, 1529-2401), 2008 Mar 12; 28(11): 2698-2709.
Impact Factor: 7.452
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Arpaia P, Clemente F, Manna C
* In vivo assessment of skin impedance recovery after low-voltage pulses electroporation (5516 views)
Imeko Tc Int Symp (ISSN: 9788-8903), 2008; N/D: 934-937.
Impact Factor: 0
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Bianco MR, Cirillo G, Cavaliere C, Colangelo AM, Vitagliano L, Morelli G, Sarmientos P, Martegani E, Alberghina L, Papa M
* A new Nerve Growth Factor (NGF)-mimetic peptide reduces gliosis and is active on neuropathic pain in rats (290 views)
Neuron Glia Biology (ISSN: 1740-925x), 2007; 2: N/D-N/D.
Impact Factor: 6.636
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8 Records (7 excluding Abstracts).
Total impact factor: 41.664 (35.028 excluding Abstracts).
Total 5 year impact factor: 41.728 (37.86 excluding Abstracts).
Total impact factor: 41.664 (35.028 excluding Abstracts).
Total 5 year impact factor: 41.728 (37.86 excluding Abstracts).
487 views. Last view on Wednesday 10 August 2022, 8:32:45
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