Mixed metal copper(II)-nickel(II) and copper(II)-zinc(II) complexes of multihistidine peptide fragments of human prion protein

Autor: Giuseppe Di Natale, Giuseppe Pappalardo, Imre Sóvágó, Enrico Rizzarelli, Ildikó Turi, Viktória Jószai, Csilla Kállay

Publikováno v: Journal of Inorganic Biochemistry. 112:17-24

Mixed metal copper(II)-nickel(II) and copper(II)-zinc(II) complexes of four peptide fragments of human prion protein have been studied by potentiometric, UV–vis and circular dichroism spectroscopic techniques. One peptide contained three histidyl r

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b2a64c7e5626a9db61d380a611a080e1
https://doi.org/10.1016/j.jinorgbio.2012.02.014

Cross talk between the octarepeats domain and the prion's fifth binding site driven by copper (II) interaction with the protein N-terminus

Autor: Giuseppe Di Natale, [a] Ildikó Turi, [b] Giuseppe Pappalardo, [a] Imre Sóvágó, [b] Enrico Rizzarelli

Publikováno v: Chemistry-A European Journal (2015). doi:10.1002/chem.201405502
info:cnr-pdr/source/autori:Giuseppe Di Natale,[a] Ildikó Turi,[b] Giuseppe Pappalardo,[a] Imre Sóvágó,[b] Enrico Rizzarelli*/titolo:Cross talk between the octarepeats domain and the prion's fifth binding site driven by copper (II) interaction with the protein N-terminus/doi:10.1002%2Fchem.201405502/rivista:Chemistry-A European Journal/anno:2015/pagina_da:/pagina_a:/intervallo_pagine:/volume

Prion diseases are a group of neurodegenerative diseases based on the conformational conversion of the normal form of protein (PrPC) to the disease-related scrapie isoform (PrPSc). Copper(II) coordination to the prion protein (PrPC) has attracted con

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=cnr_________::c02d0bebcf75b065f7ad667ec7b60d59
https://publications.cnr.it/doc/304914

The effect of non-coordinating side chains on the metal binding affinities of peptides of histidine

Autor: Imre Sóvágó, Ildikó Turi, Daniele Sanna, Giuseppe Pappalardo, Eugenio Garribba

Publikováno v: Polyhedron 62 (2013): 7–17. doi:10.1016/j.poly.2013.06.014
info:cnr-pdr/source/autori:I. Turi, D. Sanna, E. Garribba, G. Pappalardo, I. Sóvágó/titolo:The effect of non-coordinating side chains on the metal binding affinities of peptides of histidine/doi:10.1016%2Fj.poly.2013.06.014/rivista:Polyhedron/anno:2013/pagina_da:7/pagina_a:17/intervallo_pagine:7–17/volume:62

Copper(II), nickel(II) and zinc(II) complexes of both N-terminally acetylated and free tetrapeptides modeling the sequences at H96 (GTHS) and H111 (MKHM) sites of prion protein have been studied by potentiometric and various spectroscopic (UV-Vis, CD

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bf8e1a958a2f256ac9584350789bc0cb

The effect of point mutations on copper(II) complexes with peptide fragments encompassing the 106-114 region of human prion protein

Autor: Csilla Kállay, Ildikó Turi, Sarolta Timári, Zoltán Nagy, Daniele Sanna, Giuseppe Pappalardo, Paolo de Bona, Enrico Rizzarelli, Imre Sóvágó

Publikováno v: Metal Ions in Neurological Systems, edited by Wolfgang Linert, Henryk Kozlowski, pp. 189–197. WIEN: SPRINGER-VERLAG, 2012
info:cnr-pdr/source/autori:C. Kállay, I. Turi, S. Timári, Z. Nagy, D. Sanna, G. Pappalardo, P. de Bona, E. Rizzarelli, I. Sóvágó/titolo:The effect of point mutations on copper(II) complexes with peptide fragments encompassing the 106-114 region of human prion protein./titolo_volume:Metal Ions in Neurological Systems/curatori_volume:Wolfgang Linert, Henryk Kozlowski/editore: /anno:2012
Metal Ions in Neurological Systems ISBN: 9783709110003

The tetrapeptides Ac-SKHM-NH2, Ac-TKHM-NH2, Ac-MKHS-NH2, Ac-S(OMe)KHM-NH2, and Ac-MKHS(OMe)-NH2 and the nonapeptides Ac-KTNSKHMAG-NH2 and Ac-KTNMKHSAG-NH2 were synthesized and their copper(II) complexes were studied by potentiometric, UV-Vis, circula

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::bdd299c7cf0db5a8c31a7852be1c4a01

Nickel(II) complexes of the multihistidine peptide fragments of human prion protein

Autor: Csilla Kállay, Dorina Szikszai, Ildikó Turi, Imre Sóvágó, Giuseppe Pappalardo, Paolo De Bona, Giuseppe Di Natale, Enrico Rizzarelli

Publikováno v: Journal of inorganic biochemistry 104 (2010): 885–891. doi:10.1016/j.jinorgbio.2010.04.008
info:cnr-pdr/source/autori:I. Turi1; C. Kállay1; D. Szikszai1; G. Pappalardo2; G. Di Natale3; P. De Bona3; E. Rizzarelli3; I. Sóvágó1./titolo:Nickel(II) complexes of the multihistidine peptide fragments of human prion protein/doi:10.1016%2Fj.jinorgbio.2010.04.008/rivista:Journal of inorganic biochemistry/anno:2010/pagina_da:885/pagina_a:891/intervallo_pagine:885–891/volume:104

Nickel(II) complexes of the peptide fragments of human prion protein containing histidyl residues both inside and outside the octarepeat domain have been studied by the combined application of potentiometric, UV-visible and circular dichroism spectro

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c4548f676fd30a979d97751ed95c24c8
https://publications.cnr.it/doc/14234