The effect of point mutations on copper(II) complexes with peptide fragments encompassing the 106-114 region of human prion protein (503 views)
Monatshefte Fur Chemie (ISSN: 0026-9247), 2011 Apr; 142(4): 411-419.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 1.532, 5-year impact factor: 1.543
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-79955842018&partnerID=40&md5=20c7d7c595df14b2a5dd0a029fc3ee76
Keywords: Bioinorganic Chemistry, Metal Complexes, Peptides, Prion Proteins,
Affiliations:
*** IBB - CNR ***
Department of Inorganic and Analytical Chemistry, University of Debrecen, Debrecen 4010, Hungary
Department of Colloid Chemistry, University of Debrecen, Debrecen 4010, Hungary
CNR Institute of Biomolecular Chemistry, Traversa La Crucca 3, Baldinca-Li Punti (Sassari) 07040, Italy
Department of Chemical Sciences, University of Catania, V.le A. Doria 6, Catania 95125, Italy
References:
Sigel, H., Martin, R.B., (1982) Chem Rev, 82, p. 385. , 10.1021/cr00050a003 1:CAS:528:DyaL38XlvVars78%3
Sóvágó, I., (1990) Biocoordination Chemistry, Metal Complexes of Peptides and Derivatives, p. 135. , K. Burger (eds). Ellis Horwood Chichester
Kozlowski, H., Bal, W., Dyba, M., Kowalik-Jankowska, T., (1999) Coord Chem Rev, 184, p. 319. , 10.1016/S0010-8545(98)00261-6 1:CAS:528:DyaK1MXis1Kitrw%3D
Sóvágó, I., Osz, K., (2006) Dalton Trans, p. 3841
Brown, D.R., Kozlowski, H., (2004) Dalton Trans, p. 1907
Millhauser, G.L., (2004) Acc Chem Res, 37, p. 79. , 10.1021/ar0301678 1:CAS:528:DC%2BD2cXls1Sksw%3D%3D
Joszai, V., Nagy, Z., Osz, K., Sanna, D., Di Natale, G., La Mendola, D., Pappalardo, G., Sovago, I., Transition metal complexes of terminally protected peptides containing histidyl residues (2006) Journal of Inorganic Biochemistry, 100 (8), pp. 1399-1409. , DOI 10.1016/j.jinorgbio.2006.04.003, PII S0162013406001309
Di Natale, G., Grasso, G., Impellizzeri, G., La Mendola, D., Micera, G., Mihala, N., Nagy, Z., Sovago, I., Copper(II) interaction with unstructured prion domain outside the octarepeat region: Speciation, stability, and binding details of copper(II) complexes with PrP106-126 peptides (2005) Inorganic Chemistry, 44 (20), pp. 7214-7225. , DOI 10.1021/ic050754k
Grasso, D., Grasso, G., Guantieri, V., Impellizzeri, G., Rosa, C.L., Milardi, D., Micera, G., Sovago, I., Environmental effects on a prion's helix II domain: Copper(II) and membrane interactions with PrP180-193 and its analogues (2006) Chemistry - A European Journal, 12 (2), pp. 537-547. , DOI 10.1002/chem.200500534
Osz, K., Nagy, Z., Pappalardo, G., Di Natale, G., Sanna, D., Micera, G., Rizzarelli, E., Sovago, I., Copper(II) interaction with prion peptide fragments encompassing histidine residues within and outside the octarepeat domain: Speciation, stability constants and binding details (2007) Chemistry - A European Journal, 13 (25), pp. 7129-7143. , DOI 10.1002/chem.200601568
Di Natale, G., Osz, K., Nagy, Z., Sanna, D., Micera, G., Pappalardo, G., Sóvágó, I., Rizzerelli, E., (2009) Inorg Chem, 48, p. 4239. , 10.1021/ic802190v 1:CAS:528:DC%2BD1MXktVOlur4%3D
Hahn, M., Wolters, D., Sheldrick, W.S., Hulsbergen, F.B., Reedijk, J., [Pt(dien)]2+ migrates intramolecularly from methionine S to imidazole N(ε2) in the peptides H-His-Gly-Met-OH and Ac-His-Ala-Ala-Ala- Met-NHPh (1999) Journal of Biological Inorganic Chemistry, 4 (4), pp. 412-420. , DOI 10.1007/s007750050327
Boka, B., Nagy, Z., Varnagy, K., Sovago, I., Solution equilibria and structural characterisation of the palladium(II) and mixed metal complexes of peptides containing methionyl residues (2001) Journal of Inorganic Biochemistry, 83 (2-3), pp. 77-89. , DOI 10.1016/S0162-0134(00)00196-3, PII S0162013400001963
Várnagy, K., Bóka, B., Sóvágó, I., Sanna, D., Marras, P., Micera, G., (1998) Inorg Chim Acta, 275-276, p. 440. , 10.1016/S0020-1693(98)00079-6
Pettit, L.D., Robbins, R.A., (1995) Metal-peptide Complex Formation, in Handbook of Metal-ligand Interactions in Biological Fluids, 1, p. 636. , G. Berthon (eds). Marcel Dekker New York
Gergely, A., Farkas, E., (1982) J Chem Soc Dalton Trans, p. 381
Buhl, M., Density-functional study of vanadate-glycylserine isomers (2000) Journal of Inorganic Biochemistry, 80 (1-2), pp. 137-139. , DOI 10.1016/S0162-0134(00)00020-9, PII S0162013400000209
Farkas, E., Kiss, T., (1989) Polyhedron, 8, p. 2463. , 10.1016/S0277-5387(89)80011-7 1:CAS:528:DyaK3cXhtVKitrg%3D
Szabo-Planka, T., Arkosi, Z., Rockenbauer, A., Korecz, L., An ESR study of the copper(II)-glycyl-L-serine and copper(II)-L-seryl- glycine systems by the simultaneous analysis of multi-component isotropic spectra. Formation constants and coordination modes (2001) Polyhedron, 20 (9-10), pp. 995-1003. , DOI 10.1016/S0277-5387(01)00758-6, PII S0277538701007586
Mlynarz, P., Gaggelli, N., Panek, J., Stasiak, M., Valensin, G., Kowalik-Jankowska, T., Leplawy, M.L., Kozlowski, H., (2000) J Chem Soc Dalton Trans, p. 1033
Mlynarz, P., Kowalik-Jankowska, T., Stasiak, M., Leplawy, M.L., Kozlowski, H., (1999) J Chem Soc Dalton Trans, p. 3673
Mlynarz, P., Bal, W., Kowalik-Jankowska, T., Stasiak, M., Leplawy, M.L., Kozlowski, H., (1999) J Chem Soc Dalton Trans, p. 109
Kállay, C., Várnagy, K., Malandrinos, G., Hadjiliadis, N., Sanna, D., Sóvágó, I., (2006) Dalton Trans, p. 4545
Nishida, Y., Hayashida, K., Kida, S., (1980) J Coord Chem, 10, p. 101. , 10.1080/00958978008079856 1:CAS:528:DyaL3cXktFKgsrY%3D
Irving, H., Miles, G., Pettit, L.D., (1967) Anal Chim Acta, 38, p. 475. , 10.1016/S0003-2670(01)80616-4 1:CAS:528:DyaF2sXktlKrt78%3D
Zékány, L., Nagypál, I., (1985) Computational Methods for the Determination of Formation Constants, p. 291. , Leggett D (ed) Plenum, New York
Gans, P., Sabatini, A., Vacca, A., (1985) J Chem Soc Dalton Trans, p. 1195
Monatshefte Fur Chemie (ISSN: 0026-9247), 2011 Apr; 142(4): 411-419.
Export to BibTeX Export to EndNote
Paper type: Journal Article,
Impact factor: 1.532, 5-year impact factor: 1.543
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-79955842018&partnerID=40&md5=20c7d7c595df14b2a5dd0a029fc3ee76
Keywords: Bioinorganic Chemistry, Metal Complexes, Peptides, Prion Proteins,
Affiliations:
*** IBB - CNR ***
Department of Inorganic and Analytical Chemistry, University of Debrecen, Debrecen 4010, Hungary
Department of Colloid Chemistry, University of Debrecen, Debrecen 4010, Hungary
CNR Institute of Biomolecular Chemistry, Traversa La Crucca 3, Baldinca-Li Punti (Sassari) 07040, Italy
Department of Chemical Sciences, University of Catania, V.le A. Doria 6, Catania 95125, Italy
References:
Sigel, H., Martin, R.B., (1982) Chem Rev, 82, p. 385. , 10.1021/cr00050a003 1:CAS:528:DyaL38XlvVars78%3
Sóvágó, I., (1990) Biocoordination Chemistry, Metal Complexes of Peptides and Derivatives, p. 135. , K. Burger (eds). Ellis Horwood Chichester
Kozlowski, H., Bal, W., Dyba, M., Kowalik-Jankowska, T., (1999) Coord Chem Rev, 184, p. 319. , 10.1016/S0010-8545(98)00261-6 1:CAS:528:DyaK1MXis1Kitrw%3D
Sóvágó, I., Osz, K., (2006) Dalton Trans, p. 3841
Brown, D.R., Kozlowski, H., (2004) Dalton Trans, p. 1907
Millhauser, G.L., (2004) Acc Chem Res, 37, p. 79. , 10.1021/ar0301678 1:CAS:528:DC%2BD2cXls1Sksw%3D%3D
Joszai, V., Nagy, Z., Osz, K., Sanna, D., Di Natale, G., La Mendola, D., Pappalardo, G., Sovago, I., Transition metal complexes of terminally protected peptides containing histidyl residues (2006) Journal of Inorganic Biochemistry, 100 (8), pp. 1399-1409. , DOI 10.1016/j.jinorgbio.2006.04.003, PII S0162013406001309
Di Natale, G., Grasso, G., Impellizzeri, G., La Mendola, D., Micera, G., Mihala, N., Nagy, Z., Sovago, I., Copper(II) interaction with unstructured prion domain outside the octarepeat region: Speciation, stability, and binding details of copper(II) complexes with PrP106-126 peptides (2005) Inorganic Chemistry, 44 (20), pp. 7214-7225. , DOI 10.1021/ic050754k
Grasso, D., Grasso, G., Guantieri, V., Impellizzeri, G., Rosa, C.L., Milardi, D., Micera, G., Sovago, I., Environmental effects on a prion's helix II domain: Copper(II) and membrane interactions with PrP180-193 and its analogues (2006) Chemistry - A European Journal, 12 (2), pp. 537-547. , DOI 10.1002/chem.200500534
Osz, K., Nagy, Z., Pappalardo, G., Di Natale, G., Sanna, D., Micera, G., Rizzarelli, E., Sovago, I., Copper(II) interaction with prion peptide fragments encompassing histidine residues within and outside the octarepeat domain: Speciation, stability constants and binding details (2007) Chemistry - A European Journal, 13 (25), pp. 7129-7143. , DOI 10.1002/chem.200601568
Di Natale, G., Osz, K., Nagy, Z., Sanna, D., Micera, G., Pappalardo, G., Sóvágó, I., Rizzerelli, E., (2009) Inorg Chem, 48, p. 4239. , 10.1021/ic802190v 1:CAS:528:DC%2BD1MXktVOlur4%3D
Hahn, M., Wolters, D., Sheldrick, W.S., Hulsbergen, F.B., Reedijk, J., [Pt(dien)]2+ migrates intramolecularly from methionine S to imidazole N(ε2) in the peptides H-His-Gly-Met-OH and Ac-His-Ala-Ala-Ala- Met-NHPh (1999) Journal of Biological Inorganic Chemistry, 4 (4), pp. 412-420. , DOI 10.1007/s007750050327
Boka, B., Nagy, Z., Varnagy, K., Sovago, I., Solution equilibria and structural characterisation of the palladium(II) and mixed metal complexes of peptides containing methionyl residues (2001) Journal of Inorganic Biochemistry, 83 (2-3), pp. 77-89. , DOI 10.1016/S0162-0134(00)00196-3, PII S0162013400001963
Várnagy, K., Bóka, B., Sóvágó, I., Sanna, D., Marras, P., Micera, G., (1998) Inorg Chim Acta, 275-276, p. 440. , 10.1016/S0020-1693(98)00079-6
Pettit, L.D., Robbins, R.A., (1995) Metal-peptide Complex Formation, in Handbook of Metal-ligand Interactions in Biological Fluids, 1, p. 636. , G. Berthon (eds). Marcel Dekker New York
Gergely, A., Farkas, E., (1982) J Chem Soc Dalton Trans, p. 381
Buhl, M., Density-functional study of vanadate-glycylserine isomers (2000) Journal of Inorganic Biochemistry, 80 (1-2), pp. 137-139. , DOI 10.1016/S0162-0134(00)00020-9, PII S0162013400000209
Farkas, E., Kiss, T., (1989) Polyhedron, 8, p. 2463. , 10.1016/S0277-5387(89)80011-7 1:CAS:528:DyaK3cXhtVKitrg%3D
Szabo-Planka, T., Arkosi, Z., Rockenbauer, A., Korecz, L., An ESR study of the copper(II)-glycyl-L-serine and copper(II)-L-seryl- glycine systems by the simultaneous analysis of multi-component isotropic spectra. Formation constants and coordination modes (2001) Polyhedron, 20 (9-10), pp. 995-1003. , DOI 10.1016/S0277-5387(01)00758-6, PII S0277538701007586
Mlynarz, P., Gaggelli, N., Panek, J., Stasiak, M., Valensin, G., Kowalik-Jankowska, T., Leplawy, M.L., Kozlowski, H., (2000) J Chem Soc Dalton Trans, p. 1033
Mlynarz, P., Kowalik-Jankowska, T., Stasiak, M., Leplawy, M.L., Kozlowski, H., (1999) J Chem Soc Dalton Trans, p. 3673
Mlynarz, P., Bal, W., Kowalik-Jankowska, T., Stasiak, M., Leplawy, M.L., Kozlowski, H., (1999) J Chem Soc Dalton Trans, p. 109
Kállay, C., Várnagy, K., Malandrinos, G., Hadjiliadis, N., Sanna, D., Sóvágó, I., (2006) Dalton Trans, p. 4545
Nishida, Y., Hayashida, K., Kida, S., (1980) J Coord Chem, 10, p. 101. , 10.1080/00958978008079856 1:CAS:528:DyaL3cXktFKgsrY%3D
Irving, H., Miles, G., Pettit, L.D., (1967) Anal Chim Acta, 38, p. 475. , 10.1016/S0003-2670(01)80616-4 1:CAS:528:DyaF2sXktlKrt78%3D
Zékány, L., Nagypál, I., (1985) Computational Methods for the Determination of Formation Constants, p. 291. , Leggett D (ed) Plenum, New York
Gans, P., Sabatini, A., Vacca, A., (1985) J Chem Soc Dalton Trans, p. 1195
The effect of point mutations on copper(II) complexes with peptide fragments encompassing the 106-114 region of human prion protein
The tetrapeptides Ac-SKHM-NH(2), Ac-TKHM-NH(2), Ac-MKHS-NH(2), Ac-S(OMe)KHM-NH(2), and Ac-MKHS(OMe)-NH(2) and the nonapeptides Ac-KTNSKHMAG-NH(2) and Ac-KTNMKHSAG-NH(2) were synthesized and their copper(II) complexes were studied by potentiometric, UV-Vis, circular dichroism (CD), and electron paramagnetic resonance (EPR) spectroscopic methods. These peptides mimic the 109-112 and 106-114 residues of the sequence of human prion protein. The imidazole-N donor atoms of histidyl residues were found to be the primary metal binding sites of all peptide fragments. This binding mode provides a good possibility for the cooperative deprotonation and metal ion coordination of two amide functions preceding histidine. The (N(im),N(-),N(-))-bonded species predominate in the pH range 5.5-7.0 and the free coordination sites of these species make possible the metal binding of weakly coordinating side chains. The comparison of the potentiometric and spectroscopic results revealed the stabilizing role of the oxygen donors of seryl, threonyl, or methoxyseryl residues of Ac-SKHM-NH(2), Ac-TKHM-NH(2), Ac-S(OMe)KHM-NH(2), and Ac-KTNSKHMAG-NH(2) containing the mutations in position 109. These interactions were, however, not observed in the peptides containing the specific amino acids in other locations of the peptide sequence.
The tetrapeptides Ac-SKHM-NH(2), Ac-TKHM-NH(2), Ac-MKHS-NH(2), Ac-S(OMe)KHM-NH(2), and Ac-MKHS(OMe)-NH(2) and the nonapeptides Ac-KTNSKHMAG-NH(2) and Ac-KTNMKHSAG-NH(2) were synthesized and their copper(II) complexes were studied by potentiometric, UV-Vis, circular dichroism (CD), and electron paramagnetic resonance (EPR) spectroscopic methods. These peptides mimic the 109-112 and 106-114 residues of the sequence of human prion protein. The imidazole-N donor atoms of histidyl residues were found to be the primary metal binding sites of all peptide fragments. This binding mode provides a good possibility for the cooperative deprotonation and metal ion coordination of two amide functions preceding histidine. The (N(im),N(-),N(-))-bonded species predominate in the pH range 5.5-7.0 and the free coordination sites of these species make possible the metal binding of weakly coordinating side chains. The comparison of the potentiometric and spectroscopic results revealed the stabilizing role of the oxygen donors of seryl, threonyl, or methoxyseryl residues of Ac-SKHM-NH(2), Ac-TKHM-NH(2), Ac-S(OMe)KHM-NH(2), and Ac-KTNSKHMAG-NH(2) containing the mutations in position 109. These interactions were, however, not observed in the peptides containing the specific amino acids in other locations of the peptide sequence.
The effect of point mutations on copper(II) complexes with peptide fragments encompassing the 106-114 region of human prion protein
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The effect of point mutations on copper(II) complexes with peptide fragments encompassing the 106-114 region of human prion protein
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Pietropaolo A, Magri A, Greco V, Losasso V, La Mendola D, Sciuto S, Carloni P, Rizzarelli E
* Binding of Zn(II) to Tropomyosin Receptor Kinase A in Complex with Its Cognate Nerve Growth Factor: Insights from Molecular Simulation and in Vitro Essays (233 views)
Acs Chem Neurosci (ISSN: 1948-7193electronic, 1948-7193linking), 2018 Jan 12; N/D: N/D-N/D.
Impact Factor: 4.348
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Chino M, Leone L, Maglio O, D'Alonzo D, Pirro F, Pavone V, Nastri F, Lombardi A
* A De Novo Heterodimeric Due Ferri Protein Minimizes the Release of Reactive Intermediates in Dioxygen-Dependent Oxidation (246 views) (PDF 169 views)
Angew Chem Int Ed (ISSN: 1433-7851, 1521-3773electronic, 1433-7851linking), 2017 Dec 4; 56(49): 15580-15583.
Impact Factor: 12.102
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Magrì A, Di Natale G, Rizzarelli E
Copper-assisted interaction between amyloid-beta and prion: Ternary metal complexes with A beta N-terminus and octarepeat (277 views)
Inorg Chim Acta, 2017; N/D: N/D-N/D.
Impact Factor: 1.85
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Messori L, Merlino A
* Cisplatin binding to proteins: A structural perspective (451 views)
Coord Chem Rev (ISSN: 0010-8545), 2016; 315: 67-89.
Impact Factor: 13.324
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Trusso Sfrazzetto G, Satriano C, Tomaselli GA, Rizzarelli E
* Synthetic fluorescent probes to map metallostasis and intracellular fate of zinc and copper (330 views)
Coord Chem Rev (ISSN: 0010-8545), 2016; 311: 125-167.
Impact Factor: 13.324
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Musumeci D, Rozza L, Merlino A, Paduano L, Marzo T, Massai L, Messori L, Montesarchio D
* Interaction of anticancer Ru(III) complexes with single stranded and duplex DNA model systems (517 views)
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9226linking), 2015; 44(31): 13914-13925.
Impact Factor: 4.177
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Di Natale G, Osz K, Kállay C, Pappalardo G, Sanna D, Impellizzeri G, Sóvágó I, Rizzarelli E
* Affinity, speciation, and molecular features of copper(II) complexes with a prion tetraoctarepeat domain in aqueous solution: insights into old and new results (422 views)
Chemistry (ISSN: 1521-3765, 0947-6539, 1521-3765electronic), 2013 Mar 11; 19(11): 3751-3761.
Impact Factor: 5.696
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Faiella M, Maglio O, Nastri F, Lombardi A, Lista L, Hagen WR, Pavone V
* De Novo Design, Synthesis and Characterisation of MP3, A New Catalytic Four-Helix Bundle Hemeprotein (474 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2012 Dec 7; 18(50): 15960-15971.
Impact Factor: 5.831
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Nastri F, Lista L, Ringhieri P, Vitale R, Faiella M, Andreozzi C, Travascio P, Maglio O, Lombardi A, Pavone V
* A Heme-Peptide Metalloenzyme Mimetic with Natural Peroxidase-Like Activity (435 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2011 Apr; 17(16): 4444-4453.
Impact Factor: 5.925
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Józsa E, Osz K, Kállay C, de Bona P, Damante CA, Pappalardo G, Rizzarelli E, Sóvágó I
* Nickel(ii) and mixed metal complexes of amyloid-β N-terminus (448 views)
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2010 Sep 14; 39(30): 7046-7053.
Impact Factor: 3.647
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La Mendola D, Magrì A, Campagna T, Campitiello MA, Raiola L, Isernia C, Hansson O, Bonomo RP, Rizzarelli E
* A doppel alpha-helix peptide fragment mimics the copper(II) interactions with the whole protein (1115 views)
Chemistry (ISSN: 0947-6539, 1521-3765, 1521-3765electronic), 2010 Jun 1; 16(21): 6212-6223.
Impact Factor: 5.476
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Di Natale G, Pappalardo G, Milardi D, Sciacca MFM, Attanasio F, La Mendola D, Rizzarelli E
* Different Interactions Of Human And Avian Prion Proteins N-Terminal Tandem Repeat Peptides And Their Copper (ii) Complexes With Model Membranes (385 views)
Journal Of Chemical Physics, 2010; 114: 13830-13838.
Impact Factor: 2.028
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Jozsa E, Hosz K, Kallay C, De Bona P, Damante CA, Pappalardo G, Rizzarelli E, Sovago I
* Nickel (ii) And Mixed Metal Complexes Of Amyloid-B N-Terminus. Results Of Potentiometric And Spectroscopic Studies On The Binary Nickel (ii) And Mixed Metal Nickel (ii)-Copper (ii) And Nickel (ii)-Copper (ii)-Zinc (ii) Complexes Of Peptide Fragments (489 views)
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2010; 39(30): 7046-7053.
Impact Factor: 3.647
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Bellia F, La Mendola D, Pedone C, Rizzarelli E, Saviano M, Vecchio G
* Selectively functionalized cyclodextrins and their metal complexes (415 views)
Chem Soc Rev (ISSN: 1460-4744, 0306-0012, 1460-4744electronic), 2009 Sep; 38(9): 2756-2781.
Impact Factor: 20.086
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La Mendola D, Pietropaolo A, Pappalardo G, Zannoni C, Rizzarelli E
* Prion Proteins Leading to Neurodegeneration (vol 5, pg 579, 2008) (233 views)
Current Alzheimer Research (ISSN: 1567-2050), 2009 Jun; 6(3): N/D-N/D.
Impact Factor: 4.971
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La Mendola D, Pietropaolo A, Pappalardo G, Zannoni C, Rizzarelli E
* Prion proteins leading to neurodegeneration (420 views)
Current Alzheimer Research (ISSN: 1567-2050), 2008 Dec; 5(6): 579-590.
Impact Factor: 4.132
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Di Natale G, Damante CA, Nagy Z, Osz K, Pappalardo G, Rizzarelli E, Sóvágó I
* Copper(II) binding to two novel histidine-containing model hexapeptides: evidence for a metal ion driven turn conformation (423 views)
J Chem Res (ISSN: 1873-3344, 0162-0134, 0162-0134print), 2008 Nov; 102(11): 2012-2019.
Impact Factor: 3.133
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Joszal V, Nagy Z, Osz K, Sanna D, Di Natale G, La Mendola D, Pappalardo G, Rizzarelli E, Sovago I
* Transition metal complexes of terminally protected peptides containing histidyl residues (513 views)
J Chem Res (ISSN: 0162-0134, 1873-3344, 0162-0134print), 2006 Sep; 100(8): 1399-1409.
Impact Factor: 2.654
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Di Natale G, Impellizzeri G, Pappalardo G
* Conformational properties of peptide fragments homologous to the 106-114 and 106-126 residues of the human prion protein: a CD and NMR spectroscopic study (424 views)
Org Biomol Chem (ISSN: 1477-0520, 1477-0539, 1477-0539electronic), 2005 Feb 7; 3(3): 490-497.
Impact Factor: 2.547
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Bonomo RP, Cucinotta V, Giuffrida A, Impellizzeri G, Magrì A, Pappalardo G, Rizzarelli E, Santoro AM, Tabbì G, Vagliasindi LI
* A re-investigation of copper coordination in the octa-repeats region of the prion protein (376 views)
Dalton T (ISSN: 1477-9226, 1477-9234, 1477-9234electronic), 2005 Jan 7; (1): 150-158.
Impact Factor: 3.003
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Tizzano B, Marasco D, Benedetti E, De Capua A, Palladino P, Pedone C, Perretta G, Rossi F, Ragone R, Ruvo M
* Conformational conversion of prion proteins: Role synthetic PRP 173-195 fibrillogenic peptide (354 views)
Peptide Revolution, 2004; N/D: N/D-N/D.
Impact Factor: 4.659
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Pappalardo G, Impellizzeri G, Campagna T
* Copper(II) binding of prion protein's octarepeat model peptides (505 views)
Inorg Chim Acta (ISSN: 0020-1693), 2004; 357(1): 185-194.
Impact Factor: 1.554
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23 Records (21 excluding Abstracts).
Total impact factor: 130.686 (121.056 excluding Abstracts).
Total 5 year impact factor: 129.652 (120.185 excluding Abstracts).
Total impact factor: 130.686 (121.056 excluding Abstracts).
Total 5 year impact factor: 129.652 (120.185 excluding Abstracts).
503 views. Last view on Wednesday 08 March 2023, 10:43:42
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