Thermodynamic analysis of the contributions of the copper ion and the disulfide bridge to azurin stability: Synergism among multiple depletions (312 views visite)
Arch Biochem Biophys (ISSN: 0003-9861), 2003 Jun 1; 414(1): 121-127.
Export to Esporta in BibTeX Export to Esporta in EndNote
Paper type Tipo di articolo: Journal Article,
Impact factor: 2.338, 5-year impact factor Impact factor a 5 anni: 3.252
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-0038706158&partnerID=40&md5=661f0677e3ad0293e3a54a1f582eead9
Keywords Parole chiave: Azurin, Copper, Differential Scanning Calorimetry, Disulfide Bridge, Stability, Apo Azurin, Apo Azurin C26 A, Apo Azurin C3 A, Apolipoprotein, Apolipoprotein C26 A, Apolipoprotein C3 A, Copper Ion, Copper Protein, Cysteine, Holo Azurin, Holo Azurin C26 A, Holo Azurin C3 A, Mutant Protein, Unclassified Drug, Amino Acid Substitution, Article, Comparative Study, Depletion, Parameter, Priority Journal, Protein Folding, Protein Stability, Temperature, Thermodynamics, Energy Transfer, Escherichia Coli, Models, Chemical, Mutagenesis, Site-Directed, Protein Conformation, Protein Denaturation, Protein Engineering,
Affiliations Affiliazioni:
*** IBB - CNR ***
Ist. Biostrutture e Bioimmagini-CNR, Sezione di Catania, Viale Andrea Doria 6, 95125 Catania, Italy
Dipartimento di Scienze Chimiche, Universita' di Catania, Viale Andrea Doria 6, 95125 Catania, Italy
Gorleaus Laboratories, Leiden Institute of Chemistry, Leiden University, P.O. Box 9502, 2300 RA Leiden, Netherlands
References Riferimenti:
Albert, T., (1989) Annu. Rev. Biochem., 58, pp. 765-79
Baldwin, R.L., (1986) Proc. Natl. Acad. Sci. USA, 83, pp. 8069-8072
Dill, K.A., (1990) Biochemistry, 29, pp. 7133-7155
Ackers, G.K., Smith, F.R., (1985) Annu. Rev. Biochem., 54, pp. 597-629
Carter, P.J., Winter, G., Wilkinson, A.I., Fersht, A.R., (1984) Cell, 38, pp. 835-840
Horovitz, A., Fersht, A.R., (1990) J. Mol. Biol., 214, pp. 613-617
Huzle, M.R., Fweedy, N.B., Matthews, C.R., (1986) Biochemistry, 25, pp. 6356-6360
Loskowski M., Jr., Park, S.J., Toshiro, M., Wynn, R., (1989) Protein Recognition of Immobilized Ligands: VCLA Symposia on Molecular and Cell Biology, 80, pp. 149-168. , Hutchins T.W. New York: A.R. Liss
Parry, K.M., Onuffer, I.I., Gittelmenn, M.S., Bormet, L., Matthews, C.R., (1989) Biochemistry, 28, pp. 7961-7968
Serrano, L., Horovitz, A., Auron, B., Bycroft, M., Fersht, A.R., (1990) Biochemistry, 29, pp. 9343-9352
Wells, J.A., (1990) Biochemistry, 29, pp. 8509-8517
Goldenberg, D.P., (1999) Protein Folding, pp. 353-403. , T.E. Creighton. New York: W.H. Freeman and Co
Nar, H., Messerschimdt, A., Huber, R., (1991) J. Mol. Biol., 218, pp. 427-447
Guzzi, R., Sportelli, L., La Rosa, C., Milardi, D., Grasso, D., Verbeet, M.Ph., Canters, G.W., (1999) Biophys. J., 77, pp. 1052-1063
La Rosa, C., Grasso, D., Milardi, D., Guzzi, R., Sportelli, L., (1995) J. Phys. Chem., 99, pp. 14864-14870
Canters, G.W., (1987) FEBS Lett., 212, pp. 168-172
Picard, P., Ersdal-Badju, A., Clark, S.C., (1994) Nucleic Acids Res., 22, pp. 2587-2591
Van de Kamp, M., Hali, F.C., Rosato, N., Finazzi-Agrò, A., Canters, G.W., (1990) Biochim. Biophys. Acta, pp. 283-292. , 10109
Moratal, J.M., Romeo, A., Salgano, J., Perles-Alarcon, A., Jimenez, H.R., (1995) Eur. J. Biochem., 228, pp. 653-657
Hu, C.Q., Sturtevant, J.M., Thomson, J.A., Erickson, R.E., Pace, C.N., (1992) Biochemistry, 31, pp. 4876-4882
Sanchez-Ruiz, J.M., (1992) Biophys. J., 61, pp. 921-935
Yu, Y., Makhatadze, G.I., Pace, C.N., Privalov, P.L., (1994) Biochemistry, 33, pp. 3312-3319
Privalov, P.L., (1979) Adv. Protein Chem., 33, pp. 167-239
Fukada, H., Sturtevant, J.M., Quiocho, F.A., (1983) J. Biol. Chem., 258, pp. 13193-13198
Privalov, P.L., Khechinashvili, N.N., (1974) J. Mol. Biol., 86, pp. 665-684
Milardi, D., La Rosa, C., Grasso, D., (1994) Biophys. Chem., 52, pp. 183-189
Sandberg, A., Lackner, J., Shi, Y., Schwarz, F.P., Karlsson, B.G., (2002) Biochemistry, 41, pp. 1060-1069
Sandberg, W.S., Terwilliger, D.W., (1998) Biochemistry, 27, pp. 8063-8068
Matsumura, M., Signer, G., Matthews, B.W., (1989) Nature, 342, pp. 291-292
Nicholson, H., Becktel, W.J., Matthews, B.W., (1988) Nature, 336, pp. 651-656
Shortle, D., Meeker, A.D., (1986) Proteins: Struct. Funct. Genet., 1, pp. 81-89
Hecht, M.H., Saver, R.T., (1985) J. Mol. Biol., 186, pp. 53-63
Matsumura, M., Yasumura, S., Aibe, S., (1986) Nature, 323, pp. 356-358
Shirley, B.A., Stanssen, P., Steyaert, J., Pace, C.N., (1989) J. Biol. Chem., 264, pp. 11621-11625
Pantoliano, M.W., Whitlow, M., Wood, J.F., Dodd, S.W., Hardman, K.D., Rallence, M.L., Bryan, P.N., (1989) Biochemistry, 28, pp. 7205-7213
Anderson, D.E., Becktel, W.J., Dahlgvist, F.W., (1990) Biochemistry, 29, pp. 2403-2408
Sun, D.P., Alber, T., Baase, W.A., Wozniack, J.A., Matthews, B.W., (1991) J. Mol. Biol., 221, pp. 647-667
Baldwin, R. L., (1986) Proc. Natl. Acad. Sci. USA, 83, pp. 8069-8072
Dill, K. A., (1990) Biochemistry, 29, pp. 7133-7155
Ackers, G. K., Smith, F. R., (1985) Annu. Rev. Biochem., 54, pp. 597-629
Carter, P. J., Winter, G., Wilkinson, A. I., Fersht, A. R., (1984) Cell, 38, pp. 835-840
Huzle, M. R., Fweedy, N. B., Matthews, C. R., (1986) Biochemistry, 25, pp. 6356-6360
Parry, K. M., Onuffer, I. I., Gittelmenn, M. S., Bormet, L., Matthews, C. R., (1989) Biochemistry, 28, pp. 7961-7968
Wells, J. A., (1990) Biochemistry, 29, pp. 8509-8517
Goldenberg, D. P., (1999) Protein Folding, pp. 353-403. , T. E. Creighton. New York: W. H. Freeman and Co
Canters, G. W., (1987) FEBS Lett., 212, pp. 168-172
Moratal, J. M., Romeo, A., Salgano, J., Perles-Alarcon, A., Jimenez, H. R., (1995) Eur. J. Biochem., 228, pp. 653-657
Hu, C. Q., Sturtevant, J. M., Thomson, J. A., Erickson, R. E., Pace, C. N., (1992) Biochemistry, 31, pp. 4876-4882
Sanchez-Ruiz, J. M., (1992) Biophys. J., 61, pp. 921-935
Privalov, P. L., Khechinashvili, N. N., (1974) J. Mol. Biol., 86, pp. 665-684
Sandberg, W. S., Terwilliger, D. W., (1998) Biochemistry, 27, pp. 8063-8068
Hecht, M. H., Saver, R. T., (1985) J. Mol. Biol., 186, pp. 53-63
Shirley, B. A., Stanssen, P., Steyaert, J., Pace, C. N., (1989) J. Biol. Chem., 264, pp. 11621-11625
Pantoliano, M. W., Whitlow, M., Wood, J. F., Dodd, S. W., Hardman, K. D., Rallence, M. L., Bryan, P. N., (1989) Biochemistry, 28, pp. 7205-7213
Anderson, D. E., Becktel, W. J., Dahlgvist, F. W., (1990) Biochemistry, 29, pp. 2403-2408
Sun, D. P., Alber, T., Baase, W. A., Wozniack, J. A., Matthews, B. W., (1991) J. Mol. Biol., 221, pp. 647-667
Arch Biochem Biophys (ISSN: 0003-9861), 2003 Jun 1; 414(1): 121-127.
Export to Esporta in BibTeX Export to Esporta in EndNote
Paper type Tipo di articolo: Journal Article,
Impact factor: 2.338, 5-year impact factor Impact factor a 5 anni: 3.252
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-0038706158&partnerID=40&md5=661f0677e3ad0293e3a54a1f582eead9
Keywords Parole chiave: Azurin, Copper, Differential Scanning Calorimetry, Disulfide Bridge, Stability, Apo Azurin, Apo Azurin C26 A, Apo Azurin C3 A, Apolipoprotein, Apolipoprotein C26 A, Apolipoprotein C3 A, Copper Ion, Copper Protein, Cysteine, Holo Azurin, Holo Azurin C26 A, Holo Azurin C3 A, Mutant Protein, Unclassified Drug, Amino Acid Substitution, Article, Comparative Study, Depletion, Parameter, Priority Journal, Protein Folding, Protein Stability, Temperature, Thermodynamics, Energy Transfer, Escherichia Coli, Models, Chemical, Mutagenesis, Site-Directed, Protein Conformation, Protein Denaturation, Protein Engineering,
Affiliations Affiliazioni:
*** IBB - CNR ***
Ist. Biostrutture e Bioimmagini-CNR, Sezione di Catania, Viale Andrea Doria 6, 95125 Catania, Italy
Dipartimento di Scienze Chimiche, Universita' di Catania, Viale Andrea Doria 6, 95125 Catania, Italy
Gorleaus Laboratories, Leiden Institute of Chemistry, Leiden University, P.O. Box 9502, 2300 RA Leiden, Netherlands
References Riferimenti:
Albert, T., (1989) Annu. Rev. Biochem., 58, pp. 765-79
Baldwin, R.L., (1986) Proc. Natl. Acad. Sci. USA, 83, pp. 8069-8072
Dill, K.A., (1990) Biochemistry, 29, pp. 7133-7155
Ackers, G.K., Smith, F.R., (1985) Annu. Rev. Biochem., 54, pp. 597-629
Carter, P.J., Winter, G., Wilkinson, A.I., Fersht, A.R., (1984) Cell, 38, pp. 835-840
Horovitz, A., Fersht, A.R., (1990) J. Mol. Biol., 214, pp. 613-617
Huzle, M.R., Fweedy, N.B., Matthews, C.R., (1986) Biochemistry, 25, pp. 6356-6360
Loskowski M., Jr., Park, S.J., Toshiro, M., Wynn, R., (1989) Protein Recognition of Immobilized Ligands: VCLA Symposia on Molecular and Cell Biology, 80, pp. 149-168. , Hutchins T.W. New York: A.R. Liss
Parry, K.M., Onuffer, I.I., Gittelmenn, M.S., Bormet, L., Matthews, C.R., (1989) Biochemistry, 28, pp. 7961-7968
Serrano, L., Horovitz, A., Auron, B., Bycroft, M., Fersht, A.R., (1990) Biochemistry, 29, pp. 9343-9352
Wells, J.A., (1990) Biochemistry, 29, pp. 8509-8517
Goldenberg, D.P., (1999) Protein Folding, pp. 353-403. , T.E. Creighton. New York: W.H. Freeman and Co
Nar, H., Messerschimdt, A., Huber, R., (1991) J. Mol. Biol., 218, pp. 427-447
Guzzi, R., Sportelli, L., La Rosa, C., Milardi, D., Grasso, D., Verbeet, M.Ph., Canters, G.W., (1999) Biophys. J., 77, pp. 1052-1063
La Rosa, C., Grasso, D., Milardi, D., Guzzi, R., Sportelli, L., (1995) J. Phys. Chem., 99, pp. 14864-14870
Canters, G.W., (1987) FEBS Lett., 212, pp. 168-172
Picard, P., Ersdal-Badju, A., Clark, S.C., (1994) Nucleic Acids Res., 22, pp. 2587-2591
Van de Kamp, M., Hali, F.C., Rosato, N., Finazzi-Agrò, A., Canters, G.W., (1990) Biochim. Biophys. Acta, pp. 283-292. , 10109
Moratal, J.M., Romeo, A., Salgano, J., Perles-Alarcon, A., Jimenez, H.R., (1995) Eur. J. Biochem., 228, pp. 653-657
Hu, C.Q., Sturtevant, J.M., Thomson, J.A., Erickson, R.E., Pace, C.N., (1992) Biochemistry, 31, pp. 4876-4882
Sanchez-Ruiz, J.M., (1992) Biophys. J., 61, pp. 921-935
Yu, Y., Makhatadze, G.I., Pace, C.N., Privalov, P.L., (1994) Biochemistry, 33, pp. 3312-3319
Privalov, P.L., (1979) Adv. Protein Chem., 33, pp. 167-239
Fukada, H., Sturtevant, J.M., Quiocho, F.A., (1983) J. Biol. Chem., 258, pp. 13193-13198
Privalov, P.L., Khechinashvili, N.N., (1974) J. Mol. Biol., 86, pp. 665-684
Milardi, D., La Rosa, C., Grasso, D., (1994) Biophys. Chem., 52, pp. 183-189
Sandberg, A., Lackner, J., Shi, Y., Schwarz, F.P., Karlsson, B.G., (2002) Biochemistry, 41, pp. 1060-1069
Sandberg, W.S., Terwilliger, D.W., (1998) Biochemistry, 27, pp. 8063-8068
Matsumura, M., Signer, G., Matthews, B.W., (1989) Nature, 342, pp. 291-292
Nicholson, H., Becktel, W.J., Matthews, B.W., (1988) Nature, 336, pp. 651-656
Shortle, D., Meeker, A.D., (1986) Proteins: Struct. Funct. Genet., 1, pp. 81-89
Hecht, M.H., Saver, R.T., (1985) J. Mol. Biol., 186, pp. 53-63
Matsumura, M., Yasumura, S., Aibe, S., (1986) Nature, 323, pp. 356-358
Shirley, B.A., Stanssen, P., Steyaert, J., Pace, C.N., (1989) J. Biol. Chem., 264, pp. 11621-11625
Pantoliano, M.W., Whitlow, M., Wood, J.F., Dodd, S.W., Hardman, K.D., Rallence, M.L., Bryan, P.N., (1989) Biochemistry, 28, pp. 7205-7213
Anderson, D.E., Becktel, W.J., Dahlgvist, F.W., (1990) Biochemistry, 29, pp. 2403-2408
Sun, D.P., Alber, T., Baase, W.A., Wozniack, J.A., Matthews, B.W., (1991) J. Mol. Biol., 221, pp. 647-667
Baldwin, R. L., (1986) Proc. Natl. Acad. Sci. USA, 83, pp. 8069-8072
Dill, K. A., (1990) Biochemistry, 29, pp. 7133-7155
Ackers, G. K., Smith, F. R., (1985) Annu. Rev. Biochem., 54, pp. 597-629
Carter, P. J., Winter, G., Wilkinson, A. I., Fersht, A. R., (1984) Cell, 38, pp. 835-840
Huzle, M. R., Fweedy, N. B., Matthews, C. R., (1986) Biochemistry, 25, pp. 6356-6360
Parry, K. M., Onuffer, I. I., Gittelmenn, M. S., Bormet, L., Matthews, C. R., (1989) Biochemistry, 28, pp. 7961-7968
Wells, J. A., (1990) Biochemistry, 29, pp. 8509-8517
Goldenberg, D. P., (1999) Protein Folding, pp. 353-403. , T. E. Creighton. New York: W. H. Freeman and Co
Canters, G. W., (1987) FEBS Lett., 212, pp. 168-172
Moratal, J. M., Romeo, A., Salgano, J., Perles-Alarcon, A., Jimenez, H. R., (1995) Eur. J. Biochem., 228, pp. 653-657
Hu, C. Q., Sturtevant, J. M., Thomson, J. A., Erickson, R. E., Pace, C. N., (1992) Biochemistry, 31, pp. 4876-4882
Sanchez-Ruiz, J. M., (1992) Biophys. J., 61, pp. 921-935
Privalov, P. L., Khechinashvili, N. N., (1974) J. Mol. Biol., 86, pp. 665-684
Sandberg, W. S., Terwilliger, D. W., (1998) Biochemistry, 27, pp. 8063-8068
Hecht, M. H., Saver, R. T., (1985) J. Mol. Biol., 186, pp. 53-63
Shirley, B. A., Stanssen, P., Steyaert, J., Pace, C. N., (1989) J. Biol. Chem., 264, pp. 11621-11625
Pantoliano, M. W., Whitlow, M., Wood, J. F., Dodd, S. W., Hardman, K. D., Rallence, M. L., Bryan, P. N., (1989) Biochemistry, 28, pp. 7205-7213
Anderson, D. E., Becktel, W. J., Dahlgvist, F. W., (1990) Biochemistry, 29, pp. 2403-2408
Sun, D. P., Alber, T., Baase, W. A., Wozniack, J. A., Matthews, B. W., (1991) J. Mol. Biol., 221, pp. 647-667
Thermodynamic analysis of the contributions of the copper ion and the disulfide bridge to azurin stability: Synergism among multiple depletions
The stabilizing potential of the copper ion and the disulfide bridge in azurin has been explored with the aim of inspecting the ways in which these two factors influence one another. Specifically, whether copper and disulfide contributions to protein stability are additive has been examined. To this aim, the thermal unfolding of a copper-depleted mutant lacking the disulfide bridge between Cys3 and Cys26 (apo C3A/C26A azurin) was studied by differential scanning calorimetry. A comparison of the unfolding parameters of holo and apo C3A/C26A azurin with the apo C3A/C26A protein has shown that the effects of simultaneous copper and disulfide depletion are additive only at two temperatures: T=15°C and T=67°C. Within this range the presence of the copper ion and the disulfide bridge has a positive synergistic effect on azurin stability. These findings might have implications for the rational use of the stabilizing potential of copper and disulfides in copper protein engineering. © 2003 Elsevier Science (USA). All rights reserved.
The stabilizing potential of the copper ion and the disulfide bridge in azurin has been explored with the aim of inspecting the ways in which these two factors influence one another. Specifically, whether copper and disulfide contributions to protein stability are additive has been examined. To this aim, the thermal unfolding of a copper-depleted mutant lacking the disulfide bridge between Cys3 and Cys26 (apo C3A/C26A azurin) was studied by differential scanning calorimetry. A comparison of the unfolding parameters of holo and apo C3A/C26A azurin with the apo C3A/C26A protein has shown that the effects of simultaneous copper and disulfide depletion are additive only at two temperatures: T=15°C and T=67°C. Within this range the presence of the copper ion and the disulfide bridge has a positive synergistic effect on azurin stability. These findings might have implications for the rational use of the stabilizing potential of copper and disulfides in copper protein engineering. © 2003 Elsevier Science (USA). All rights reserved.
Thermodynamic analysis of the contributions of the copper ion and the disulfide bridge to azurin stability: Synergism among multiple depletions
No results. Nessun risultato. |
Thermodynamic analysis of the contributions of the copper ion and the disulfide bridge to azurin stability: Synergism among multiple depletions
Iaccarino E, Sandomenico A, Corvino G, Foca G, Severino V, Russo R, Caporale A, Raimondo D, D'Abramo M, Alba J, Chambery A, Ruvo M
* Investigating the oxidative refolding mechanism of Cripto-1 CFC domain (275 visite)
Int J Biol Macromol (ISSN: 0141-8130linking, 1879-0003electronic), 2019 Sep 15; 137: 1179-1189.
Impact Factor: 4.784
Dettagli Esporta in BibTeX Esporta in EndNote
Smaldone G, Balasco N, Vigorita M, Ruggiero A, Cozzolino S, Berisio R, Del Vecchio P, Graziano G, Vitagliano L
* Domain communication in Thermotoga maritima Arginine Binding Protein unraveled through protein dissection (191 visite)
Int J Biol Macromol (ISSN: 0141-8130linking, 1879-0003electronic), 2018 Nov; 119: 758-769.
Impact Factor: 3.909
Dettagli Esporta in BibTeX Esporta in EndNote
Smaldone G, Vigorita M, Ruggiero A, Balasco N, Dattelbaum JD, D'Auria S, Del Vecchio P, Graziano G, Vitagliano L
* Proline 235 plays a key role in the regulation of the oligomeric states of Thermotoga maritima Arginine Binding Protein (275 visite)
Bba-Gen Subjects (ISSN: 0005-2728, 0006-3002print, 1570-9639print), 2016 Jul; 1864(7): 814-824.
Impact Factor: 4.932
Dettagli Esporta in BibTeX Esporta in EndNote
Nicastro MC, Spigolon D, Librizzi F, Moran O, Ortore MG, Bulone D, Biagio PLS, Carrotta R
* Amyloid β-peptide insertion in liposomes containing GM1-cholesterol domains (317 visite)
Biophys Chem (ISSN: 0301-4622, 0301-4622linking), 2016; 208: 9-16.
Impact Factor: 2.402
Dettagli Esporta in BibTeX Esporta in EndNote
Berisio R, Squeglia F, Ruggiero A, Petraccone L, Stellato MI, Del Vecchio P
* Differential thermodynamic behaviours of the extra-cellular regions of two Ser/Thr PrkC kinases revealed by calorimetric studies (311 visite)
Bba-Gen Subjects (ISSN: 0925-4439, 0006-3002, 1570-9639), 2015 Feb 8; 1854(5): 402-409.
Impact Factor: 5.158
Dettagli Esporta in BibTeX Esporta in EndNote
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 (532 visite)
Amino Acids (ISSN: 0939-4451, 1438-2199, 1438-2199electronic), 2015; 47(8): 1507-1515.
Impact Factor: 3.196
Dettagli Esporta in BibTeX Esporta in EndNote
Romanucci V, Milardi D, Campagna T, Gaglione M, Messere A, D'Urso A, Crisafi E, La Rosa C, Zarrelli A, Balzarini J, Di Fabio G
* Synthesis, biophysical characterization and anti-HIV activity of d(TG(3)AG) Quadruplexes bearing hydrophobic tails at the 5 '-end (335 visite)
Bioorg Med Chem (ISSN: 0968-0896, 1464-3391), 2014 Feb 1; 22(3): 960-966.
Impact Factor: 2.793
Dettagli Esporta in BibTeX Esporta in EndNote
Caterino M, Merlino A, Balsamo A, Russo Krauss I, Parisi S, Vergara A
* Reaction of Hg2+ Insertion into Cysteine Pairs Within Bovine Insulin Crystals Followed via Raman Spectroscopy (273 visite)
J Solution Chem (ISSN: 0095-9782), 2014 Feb; 43(1): 135-143.
Impact Factor: 1.177
Dettagli Esporta in BibTeX Esporta in EndNote
Palmieri M, Malgieri G, Russo L, Baglivo I, Esposito S, Netti F, Del Gatto A, De Paola I, Zaccaro L, Pedone PV, Isernia C, Milardi D, Fattorusso R
* Structural Zn(II) Implies a Switch from Fully Cooperative to Partly Downhill Folding in Highly Homologous Proteins (372 visite)
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2013 Apr 2; 135(13): 5220-5228.
Impact Factor: 11.444
Dettagli Esporta in BibTeX Esporta in EndNote
Arena G, Fattorusso R, Grasso G, Grasso GI, Isernia C, Malgieri G, Milardi D, Rizzarelli E
* Zinc(II) complexes of ubiquitin: speciation, affinity and binding features (527 visite)
Chemistry (ISSN: 1521-3765, 0947-6539, 1521-3765electronic), 2011 Oct 4; 17(41): 11596-11603.
Impact Factor: 5.925
Dettagli Esporta in BibTeX Esporta in EndNote
Monfregola L, Bugatti V, Amodeo P, De Luca S, Vittoria V
* Physical and Water Sorption Properties of Chemically Modified Pectin with an Environmentally Friendly Process (260 visite)
Biomacromolecules (ISSN: 1525-7797), 2011 Jun; 12(6): 2311-2318.
Impact Factor: 5.479
Dettagli Esporta in BibTeX Esporta in EndNote
Milardi D, Sciacca MFM, Pappalardo M, Grasso DM, La Rosa C
* The Role Of Aromatic Side-Chains In Amyloid Growth And Membrane Interaction Of The Islet Amyloid Polypeptide Fragment Lanflvh (403 visite)
Eur Biophys J, 2011 Jan; 40(1): 1-12.
Impact Factor: 3.832
Dettagli Esporta in BibTeX Esporta in EndNote
Di Natale G, Pappalardo G, Milardi D, Sciacca MF, Attanasio F, La Mendola D, Rizzarelli E
* Membrane interactions and conformational preferences of human and avian prion N-terminal tandem repeats: The role of copper(II) ions, pH, and membrane mimicking environments (451 visite)
J Phys Chem B (ISSN: 1520-6106, 1520-5207, 1520-5207electronic), 2010 Nov 4; 114(43): 13830-13838.
Impact Factor: 3.603
Dettagli Esporta in BibTeX Esporta in EndNote
Sciacca MFM, Pappalardo M, Attanasio F, Milardi D, La Rosa C, Grasso DM
* Are fibril growth and membrane damage linked processes? An experimental and computational study of IAPP(12-18) and IAPP(21-27) peptides (382 visite)
New J Chem (ISSN: 1144-0546), 2010; 34(2): 200-207.
Impact Factor: 2.631
Dettagli Esporta in BibTeX Esporta in EndNote
Sciacca MFM, Carbone V, Pappalardo M, Milardi D, La Rosa C, Grasso DM
* Interaction of human amylin with phosphatidylcholine and phosphatidylserine membranes (276 visite)
Mol Cryst Liq Cryst (ISSN: 1542-1406), 2009; 500: 73-81.
Impact Factor: 0.451
Dettagli Esporta in BibTeX Esporta in EndNote
Loguercio S, Dian C, Flagiello A, Scannella A, Pucci P, Terradot L, Zagari A
* In HspA from Helicobacter pylori vicinal disulfide bridges are a key determinant of domain B structure (240 visite)
Febs Lett (ISSN: 0014-5793, 0014-5793print, 1873-3468electronic), 2008 Oct 15; 582(23-24): 3537-3541.
Impact Factor: 3.264
Dettagli Esporta in BibTeX Esporta in EndNote
Hilvo M, Baranauskiene L, Salzano AM, Scaloni A, Matulis D, Innocenti A, Scozzafava A, Monti SM, Di Fiore A, De Simone G, Lindfors M, Janis J, Valjakka J, Pastorekova S, Pastorek J, Kulomaa MS, Nordlund HR, Supuran CT, Parkkila S
* Biochemical characterization of CA IX, one of the most active carbonic anhydrase isozymes (398 visite)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2008 Oct 10; 283(41): 27799-27809.
Impact Factor: 5.52
Dettagli Esporta in BibTeX Esporta in EndNote
Milardi D, Pappalardo M, Pannuzzo M, Grasso DM, Rosa CL
* The role of the Cys2-Cys7 disulfide bridge in the early steps of Islet amyloid polypeptide aggregation: A molecular dynamics study (423 visite)
Chem Phys Lett (ISSN: 0009-2614), 2008 Oct 1; 463(4-6): 396-399.
Impact Factor: 2.169
Dettagli Esporta in BibTeX Esporta in EndNote
Sciacca MFM, Pappalardo M, Milardi D, Grasso DM, La Rosa C
* Calcium-Activated Membrane Interaction Of The Islet Amyloid Polypeptide: Implications In The Pathogenesis Of Type Ii Diabetes Mellitus (694 visite)
Arch Biochem Biophys, 2008 Sep 15; 65(1-2): 291-298.
Impact Factor: 3.043
Dettagli Esporta in BibTeX Esporta in EndNote
Pappalardo M, Sciacca MFM, Milardi D, Grasso DM, La Rosa C
* Thermodynamics Of Azurin Folding: The Role Of The Copper Ion (286 visite)
Journal Of Thermal Analysis And Calorimetry (ISSN: 1388-6150), 2008 Sep; 93(2): 575-581.
Impact Factor: 1.63
Dettagli Esporta in BibTeX Esporta in EndNote
Dalla Serra M, Cirioni O, Vitale RM, Renzone G, Coraiola M, Giacometti A, Potrich C, Baroni E, Guella G, Sanseverino M, De Luca S, Scalise G, Amodeo P, Scaloni A
* Structural features of distinctin affecting peptide biological and biochemical properties (408 visite)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2008 Jul 29; 47(30): 7888-7899.
Impact Factor: 3.379
Dettagli Esporta in BibTeX Esporta in EndNote
De Pinto V, Tomasello F, Messina A, Guarino F, Benz R, La Mendola D, Magrì A, Milardi D, Pappalardo G
* Determination of the conformation of the human VDAC1 N-terminal peptide, a protein moiety essential for the functional properties of the pore (408 visite)
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-7633electronic), 2007 May 7; 8(7): 744-756.
Impact Factor: 3.446
Dettagli Esporta in BibTeX Esporta in EndNote
Pappalardo G, Milardi D, Magrì A, Attanasio F, Impellizzeri G, La Rosa C, Grasso D, Rizzarelli E
* Environmental factors differently affect human and rat IAPP: Conformational preferences and membrane interactions of IAPP17-29 peptide derivatives (552 visite)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2007; 13(36): 10204-10215.
Impact Factor: 5.33
Dettagli Esporta in BibTeX Esporta in EndNote
Milardi D, Arnesano F, Grasso G, Magrì A, Tabbì G, Scintilla S, Natile G, Rizzarelli E
* Ubiquitin stability and the Lys63-linked polyubiquitination site are compromised on copper binding (293 visite)
Angew Chem Int Ed (ISSN: 1433-7851, 1521-3773electronic), 2007; 46(42): 7993-7995.
Impact Factor: 10.031
Dettagli Esporta in BibTeX Esporta in EndNote
De Simone A, Berisio R, Zagari A, Vitagliano L
* Limited Tendency Of Alpha-Helical Residues To Form Disulfide Bridges: A Structural Explanation (439 visite)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2006 Dec; 12(12): 740-747.
Impact Factor: 1.801
Dettagli Esporta in BibTeX Esporta in EndNote
Sciacca MFM, Milardi D, Pappalardo M, La Rosa C, Grasso DM
* Role of electrostatics in the thermal stability of ubiquitin: A combined DSC and MM study (212 visite)
Journal Of Thermal Analysis And Calorimetry (ISSN: 1388-6150), 2006 Nov; 86(2): 311-314.
Impact Factor: 1.438
Dettagli Esporta in BibTeX Esporta in EndNote
Bucci E, Vitagliano L, Barone R, Sorrentino S, D'Alessio G, Graziano G
* On the thermal stability of the two dimeric forms of ribonuclease (370 visite)
Biophys Chem (ISSN: 0301-4622, 0301-4622linking), 2005 Jul 1; 116(2): 89-95.
Impact Factor: 1.925
Dettagli Esporta in BibTeX Esporta in EndNote
Pappalardo M, Milardi D, Grasso D, La Rosa C
* Phase behaviour of polymer-grafted DPPC membranes for drug delivery systems design (292 visite)
Journal Of Thermal Analysis And Calorimetry (ISSN: 1388-6150), 2005 May; 80(2): 413-418.
Impact Factor: 1.425
Dettagli Esporta in BibTeX Esporta in EndNote
La Rosa C, Milardi D, Amato E, Pappalardo M, Grasso D
* Molecular mechanism of the inhibition of cytochrome c aggregation by Phe-Gly (463 visite)
Arch Biochem Biophys (ISSN: 0003-9861), 2005 Mar 1; 435(1): 182-189.
Impact Factor: 3.152
Dettagli Esporta in BibTeX Esporta in EndNote
Grasso D, Milardi D, La Rosa C, Rizzarelli E
* The different role of Cu++ and Zn++ ions in affecting the interaction of prion peptide PrP106-126 with model membranes (266 visite)
Chem Commun (ISSN: 1359-7345, 1364-548x, 1364-548xelectronic), 2004 Jan 21; 10(2): 246-247.
Impact Factor: 3.997
Dettagli Esporta in BibTeX Esporta in EndNote
Guzzi R, Milardi D, La Rosa C, Grasso D, Verbeet MP, Canters GW, Sportelli L
* The effect of copper/zinc replacement on the folding free energy of wild type and Cys3Ala/Cys26Ala azurin (292 visite)
Int J Biol Macromol (ISSN: 0141-8130, 0141-8130linking, 1879-0003electronic), 2003 Jan 15; 31(4-5): 163-170.
Impact Factor: 1.427
Dettagli Esporta in BibTeX Esporta in EndNote
Grasso D, Milardi D, Guantieri V, La Rosa C, Rizzarelli E
* Interaction of prion peptide PrP 180-193 with DPPC model membranes: A thermodynamic study (351 visite)
New J Chem (ISSN: 1144-0546), 2003; 27(2): 359-364.
Impact Factor: 2.272
Dettagli Esporta in BibTeX Esporta in EndNote
Grasso D, Milardi D, La Rosa C, Impellizzeri G, Pappalardo G
* The interaction of a peptide with a scrambled hydrophobic/hydrophilic sequence (Pro-Asp-Ala-Asp-Ala-His-Ala-His-Ala-His-Ala-Ala-Ala-His-Gly) (PADH) with DPPC model membranes: A DSC study (238 visite)
Thermochim Acta (ISSN: 0040-6031), 2002 Jul 15; 390(1-2): 73-78.
Impact Factor: 0.974
Dettagli Esporta in BibTeX Esporta in EndNote
Grasso D, Milardi D, La Rosa C, Rizzarelli E
* DSC study of the interaction of the prion peptide PrP106-126 with artificial membranes (331 visite)
New J Chem (ISSN: 1144-0546), 2001; 25(12): 1543-1548.
Impact Factor: 2.44
Dettagli Esporta in BibTeX Esporta in EndNote
Martínez JC, Viguera AR, Berisio R, Wilmanns M, Mateo PL, Filimonov VV, Serrano L
Thermodynamic analysis of α-spectrin SH3 and two of its circular permutants with different loop lengths: Discerning the reasons for rapid folding in proteins (353 visite)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 1999 Jan 12; 38(2): 549-559.
Impact Factor: 4.493
Dettagli Esporta in BibTeX Esporta in EndNote
35 Records (35 escludendo Abstract e Conferenze).
Impact factor totale: 124.872 (124.872 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 132.131 (132.131 escludendo Abstract e Conferenze).
Vai a fine pagina Versione per copia e incolla facile Esporta tutto in BibTeX Esporta tutto in EndNote
Iaccarino E, Sandomenico A, Corvino G, Foca G, Severino V, Russo R, Caporale A, Raimondo D, D'Abramo M, Alba J, Chambery A, Ruvo M
* Investigating the oxidative refolding mechanism of Cripto-1 CFC domain (275 visite)
Int J Biol Macromol (ISSN: 0141-8130linking, 1879-0003electronic), 2019 Sep 15; 137: 1179-1189.
Impact Factor: 4.784
Dettagli Esporta in BibTeX Esporta in EndNote
Smaldone G, Balasco N, Vigorita M, Ruggiero A, Cozzolino S, Berisio R, Del Vecchio P, Graziano G, Vitagliano L
* Domain communication in Thermotoga maritima Arginine Binding Protein unraveled through protein dissection (191 visite)
Int J Biol Macromol (ISSN: 0141-8130linking, 1879-0003electronic), 2018 Nov; 119: 758-769.
Impact Factor: 3.909
Dettagli Esporta in BibTeX Esporta in EndNote
Smaldone G, Vigorita M, Ruggiero A, Balasco N, Dattelbaum JD, D'Auria S, Del Vecchio P, Graziano G, Vitagliano L
* Proline 235 plays a key role in the regulation of the oligomeric states of Thermotoga maritima Arginine Binding Protein (275 visite)
Bba-Gen Subjects (ISSN: 0005-2728, 0006-3002print, 1570-9639print), 2016 Jul; 1864(7): 814-824.
Impact Factor: 4.932
Dettagli Esporta in BibTeX Esporta in EndNote
Nicastro MC, Spigolon D, Librizzi F, Moran O, Ortore MG, Bulone D, Biagio PLS, Carrotta R
* Amyloid β-peptide insertion in liposomes containing GM1-cholesterol domains (317 visite)
Biophys Chem (ISSN: 0301-4622, 0301-4622linking), 2016; 208: 9-16.
Impact Factor: 2.402
Dettagli Esporta in BibTeX Esporta in EndNote
Berisio R, Squeglia F, Ruggiero A, Petraccone L, Stellato MI, Del Vecchio P
* Differential thermodynamic behaviours of the extra-cellular regions of two Ser/Thr PrkC kinases revealed by calorimetric studies (311 visite)
Bba-Gen Subjects (ISSN: 0925-4439, 0006-3002, 1570-9639), 2015 Feb 8; 1854(5): 402-409.
Impact Factor: 5.158
Dettagli Esporta in BibTeX Esporta in EndNote
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 (532 visite)
Amino Acids (ISSN: 0939-4451, 1438-2199, 1438-2199electronic), 2015; 47(8): 1507-1515.
Impact Factor: 3.196
Dettagli Esporta in BibTeX Esporta in EndNote
Romanucci V, Milardi D, Campagna T, Gaglione M, Messere A, D'Urso A, Crisafi E, La Rosa C, Zarrelli A, Balzarini J, Di Fabio G
* Synthesis, biophysical characterization and anti-HIV activity of d(TG(3)AG) Quadruplexes bearing hydrophobic tails at the 5 '-end (335 visite)
Bioorg Med Chem (ISSN: 0968-0896, 1464-3391), 2014 Feb 1; 22(3): 960-966.
Impact Factor: 2.793
Dettagli Esporta in BibTeX Esporta in EndNote
Caterino M, Merlino A, Balsamo A, Russo Krauss I, Parisi S, Vergara A
* Reaction of Hg2+ Insertion into Cysteine Pairs Within Bovine Insulin Crystals Followed via Raman Spectroscopy (273 visite)
J Solution Chem (ISSN: 0095-9782), 2014 Feb; 43(1): 135-143.
Impact Factor: 1.177
Dettagli Esporta in BibTeX Esporta in EndNote
Palmieri M, Malgieri G, Russo L, Baglivo I, Esposito S, Netti F, Del Gatto A, De Paola I, Zaccaro L, Pedone PV, Isernia C, Milardi D, Fattorusso R
* Structural Zn(II) Implies a Switch from Fully Cooperative to Partly Downhill Folding in Highly Homologous Proteins (372 visite)
J Am Chem Soc (ISSN: 0002-7863, 0002-2786, 1520-5126), 2013 Apr 2; 135(13): 5220-5228.
Impact Factor: 11.444
Dettagli Esporta in BibTeX Esporta in EndNote
Arena G, Fattorusso R, Grasso G, Grasso GI, Isernia C, Malgieri G, Milardi D, Rizzarelli E
* Zinc(II) complexes of ubiquitin: speciation, affinity and binding features (527 visite)
Chemistry (ISSN: 1521-3765, 0947-6539, 1521-3765electronic), 2011 Oct 4; 17(41): 11596-11603.
Impact Factor: 5.925
Dettagli Esporta in BibTeX Esporta in EndNote
Monfregola L, Bugatti V, Amodeo P, De Luca S, Vittoria V
* Physical and Water Sorption Properties of Chemically Modified Pectin with an Environmentally Friendly Process (260 visite)
Biomacromolecules (ISSN: 1525-7797), 2011 Jun; 12(6): 2311-2318.
Impact Factor: 5.479
Dettagli Esporta in BibTeX Esporta in EndNote
Milardi D, Sciacca MFM, Pappalardo M, Grasso DM, La Rosa C
* The Role Of Aromatic Side-Chains In Amyloid Growth And Membrane Interaction Of The Islet Amyloid Polypeptide Fragment Lanflvh (403 visite)
Eur Biophys J, 2011 Jan; 40(1): 1-12.
Impact Factor: 3.832
Dettagli Esporta in BibTeX Esporta in EndNote
Di Natale G, Pappalardo G, Milardi D, Sciacca MF, Attanasio F, La Mendola D, Rizzarelli E
* Membrane interactions and conformational preferences of human and avian prion N-terminal tandem repeats: The role of copper(II) ions, pH, and membrane mimicking environments (451 visite)
J Phys Chem B (ISSN: 1520-6106, 1520-5207, 1520-5207electronic), 2010 Nov 4; 114(43): 13830-13838.
Impact Factor: 3.603
Dettagli Esporta in BibTeX Esporta in EndNote
Sciacca MFM, Pappalardo M, Attanasio F, Milardi D, La Rosa C, Grasso DM
* Are fibril growth and membrane damage linked processes? An experimental and computational study of IAPP(12-18) and IAPP(21-27) peptides (382 visite)
New J Chem (ISSN: 1144-0546), 2010; 34(2): 200-207.
Impact Factor: 2.631
Dettagli Esporta in BibTeX Esporta in EndNote
Sciacca MFM, Carbone V, Pappalardo M, Milardi D, La Rosa C, Grasso DM
* Interaction of human amylin with phosphatidylcholine and phosphatidylserine membranes (276 visite)
Mol Cryst Liq Cryst (ISSN: 1542-1406), 2009; 500: 73-81.
Impact Factor: 0.451
Dettagli Esporta in BibTeX Esporta in EndNote
Loguercio S, Dian C, Flagiello A, Scannella A, Pucci P, Terradot L, Zagari A
* In HspA from Helicobacter pylori vicinal disulfide bridges are a key determinant of domain B structure (240 visite)
Febs Lett (ISSN: 0014-5793, 0014-5793print, 1873-3468electronic), 2008 Oct 15; 582(23-24): 3537-3541.
Impact Factor: 3.264
Dettagli Esporta in BibTeX Esporta in EndNote
Hilvo M, Baranauskiene L, Salzano AM, Scaloni A, Matulis D, Innocenti A, Scozzafava A, Monti SM, Di Fiore A, De Simone G, Lindfors M, Janis J, Valjakka J, Pastorekova S, Pastorek J, Kulomaa MS, Nordlund HR, Supuran CT, Parkkila S
* Biochemical characterization of CA IX, one of the most active carbonic anhydrase isozymes (398 visite)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2008 Oct 10; 283(41): 27799-27809.
Impact Factor: 5.52
Dettagli Esporta in BibTeX Esporta in EndNote
Milardi D, Pappalardo M, Pannuzzo M, Grasso DM, Rosa CL
* The role of the Cys2-Cys7 disulfide bridge in the early steps of Islet amyloid polypeptide aggregation: A molecular dynamics study (423 visite)
Chem Phys Lett (ISSN: 0009-2614), 2008 Oct 1; 463(4-6): 396-399.
Impact Factor: 2.169
Dettagli Esporta in BibTeX Esporta in EndNote
Sciacca MFM, Pappalardo M, Milardi D, Grasso DM, La Rosa C
* Calcium-Activated Membrane Interaction Of The Islet Amyloid Polypeptide: Implications In The Pathogenesis Of Type Ii Diabetes Mellitus (694 visite)
Arch Biochem Biophys, 2008 Sep 15; 65(1-2): 291-298.
Impact Factor: 3.043
Dettagli Esporta in BibTeX Esporta in EndNote
Pappalardo M, Sciacca MFM, Milardi D, Grasso DM, La Rosa C
* Thermodynamics Of Azurin Folding: The Role Of The Copper Ion (286 visite)
Journal Of Thermal Analysis And Calorimetry (ISSN: 1388-6150), 2008 Sep; 93(2): 575-581.
Impact Factor: 1.63
Dettagli Esporta in BibTeX Esporta in EndNote
Dalla Serra M, Cirioni O, Vitale RM, Renzone G, Coraiola M, Giacometti A, Potrich C, Baroni E, Guella G, Sanseverino M, De Luca S, Scalise G, Amodeo P, Scaloni A
* Structural features of distinctin affecting peptide biological and biochemical properties (408 visite)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 2008 Jul 29; 47(30): 7888-7899.
Impact Factor: 3.379
Dettagli Esporta in BibTeX Esporta in EndNote
De Pinto V, Tomasello F, Messina A, Guarino F, Benz R, La Mendola D, Magrì A, Milardi D, Pappalardo G
* Determination of the conformation of the human VDAC1 N-terminal peptide, a protein moiety essential for the functional properties of the pore (408 visite)
Chembiochem (ISSN: 1439-4227, 1439-7633, 1439-7633electronic), 2007 May 7; 8(7): 744-756.
Impact Factor: 3.446
Dettagli Esporta in BibTeX Esporta in EndNote
Pappalardo G, Milardi D, Magrì A, Attanasio F, Impellizzeri G, La Rosa C, Grasso D, Rizzarelli E
* Environmental factors differently affect human and rat IAPP: Conformational preferences and membrane interactions of IAPP17-29 peptide derivatives (552 visite)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2007; 13(36): 10204-10215.
Impact Factor: 5.33
Dettagli Esporta in BibTeX Esporta in EndNote
Milardi D, Arnesano F, Grasso G, Magrì A, Tabbì G, Scintilla S, Natile G, Rizzarelli E
* Ubiquitin stability and the Lys63-linked polyubiquitination site are compromised on copper binding (293 visite)
Angew Chem Int Ed (ISSN: 1433-7851, 1521-3773electronic), 2007; 46(42): 7993-7995.
Impact Factor: 10.031
Dettagli Esporta in BibTeX Esporta in EndNote
De Simone A, Berisio R, Zagari A, Vitagliano L
* Limited Tendency Of Alpha-Helical Residues To Form Disulfide Bridges: A Structural Explanation (439 visite)
J Pept Sci (ISSN: 1075-2617, 1099-1387, 1075-2617print), 2006 Dec; 12(12): 740-747.
Impact Factor: 1.801
Dettagli Esporta in BibTeX Esporta in EndNote
Sciacca MFM, Milardi D, Pappalardo M, La Rosa C, Grasso DM
* Role of electrostatics in the thermal stability of ubiquitin: A combined DSC and MM study (212 visite)
Journal Of Thermal Analysis And Calorimetry (ISSN: 1388-6150), 2006 Nov; 86(2): 311-314.
Impact Factor: 1.438
Dettagli Esporta in BibTeX Esporta in EndNote
Bucci E, Vitagliano L, Barone R, Sorrentino S, D'Alessio G, Graziano G
* On the thermal stability of the two dimeric forms of ribonuclease (370 visite)
Biophys Chem (ISSN: 0301-4622, 0301-4622linking), 2005 Jul 1; 116(2): 89-95.
Impact Factor: 1.925
Dettagli Esporta in BibTeX Esporta in EndNote
Pappalardo M, Milardi D, Grasso D, La Rosa C
* Phase behaviour of polymer-grafted DPPC membranes for drug delivery systems design (292 visite)
Journal Of Thermal Analysis And Calorimetry (ISSN: 1388-6150), 2005 May; 80(2): 413-418.
Impact Factor: 1.425
Dettagli Esporta in BibTeX Esporta in EndNote
La Rosa C, Milardi D, Amato E, Pappalardo M, Grasso D
* Molecular mechanism of the inhibition of cytochrome c aggregation by Phe-Gly (463 visite)
Arch Biochem Biophys (ISSN: 0003-9861), 2005 Mar 1; 435(1): 182-189.
Impact Factor: 3.152
Dettagli Esporta in BibTeX Esporta in EndNote
Grasso D, Milardi D, La Rosa C, Rizzarelli E
* The different role of Cu++ and Zn++ ions in affecting the interaction of prion peptide PrP106-126 with model membranes (266 visite)
Chem Commun (ISSN: 1359-7345, 1364-548x, 1364-548xelectronic), 2004 Jan 21; 10(2): 246-247.
Impact Factor: 3.997
Dettagli Esporta in BibTeX Esporta in EndNote
Guzzi R, Milardi D, La Rosa C, Grasso D, Verbeet MP, Canters GW, Sportelli L
* The effect of copper/zinc replacement on the folding free energy of wild type and Cys3Ala/Cys26Ala azurin (292 visite)
Int J Biol Macromol (ISSN: 0141-8130, 0141-8130linking, 1879-0003electronic), 2003 Jan 15; 31(4-5): 163-170.
Impact Factor: 1.427
Dettagli Esporta in BibTeX Esporta in EndNote
Grasso D, Milardi D, Guantieri V, La Rosa C, Rizzarelli E
* Interaction of prion peptide PrP 180-193 with DPPC model membranes: A thermodynamic study (351 visite)
New J Chem (ISSN: 1144-0546), 2003; 27(2): 359-364.
Impact Factor: 2.272
Dettagli Esporta in BibTeX Esporta in EndNote
Grasso D, Milardi D, La Rosa C, Impellizzeri G, Pappalardo G
* The interaction of a peptide with a scrambled hydrophobic/hydrophilic sequence (Pro-Asp-Ala-Asp-Ala-His-Ala-His-Ala-His-Ala-Ala-Ala-His-Gly) (PADH) with DPPC model membranes: A DSC study (238 visite)
Thermochim Acta (ISSN: 0040-6031), 2002 Jul 15; 390(1-2): 73-78.
Impact Factor: 0.974
Dettagli Esporta in BibTeX Esporta in EndNote
Grasso D, Milardi D, La Rosa C, Rizzarelli E
* DSC study of the interaction of the prion peptide PrP106-126 with artificial membranes (331 visite)
New J Chem (ISSN: 1144-0546), 2001; 25(12): 1543-1548.
Impact Factor: 2.44
Dettagli Esporta in BibTeX Esporta in EndNote
Martínez JC, Viguera AR, Berisio R, Wilmanns M, Mateo PL, Filimonov VV, Serrano L
Thermodynamic analysis of α-spectrin SH3 and two of its circular permutants with different loop lengths: Discerning the reasons for rapid folding in proteins (353 visite)
Biochemistry (ISSN: 0006-2960, 1520-4995, 1520-4995electronic), 1999 Jan 12; 38(2): 549-559.
Impact Factor: 4.493
Dettagli Esporta in BibTeX Esporta in EndNote
35 Records (35 escludendo Abstract e Conferenze).
Impact factor totale: 124.872 (124.872 escludendo Abstract e Conferenze).
Impact factor a 5 anni totale: 132.131 (132.131 escludendo Abstract e Conferenze).
Last modified by Ultima modifica di Marco Comerci on in data Sunday 12 July 2020, 13:15:11
312 views visite. Last view on Ultima visita in data Sunday 29 August 2021, 16:13:19
ibb.cnr.it