The telomere-binding protein Rif2 and ATP-bound Rad50 have opposing roles in the activation of yeast Tel1

Autor: Roberto Galletto, John H.J. Petrini, Paolo De Bona, Peter M. J. Burgers, Sarem Hailemariam, Marcel Hohl

Publikováno v: J Biol Chem

Saccharomyces cerevisiae Tel1 is the ortholog of human ATM kinase and initiates a cell cycle checkpoint in response to dsDNA breaks (DSBs). Tel1(ATM) kinase is activated synergistically by naked dsDNA and the Mre11-Rad50-Xrs2(NBS1) complex (MRX). A m

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::090d886ed42af93d074cc9634a16d6cd
https://pubmed.ncbi.nlm.nih.gov/31640985

Ac-LPFFD-Th: A Trehalose-Conjugated Peptidomimetic as a Strong Suppressor of Amyloid- Oligomer Formation and Cytotoxicity

Autor: Filippo Caraci, Maria Laura Giuffrida, Enrico Rizzarelli, Agata Copani, Michele Saviano, Francesco Attanasio, Giuseppe Pappalardo, Marianna Flora Tomasello, Paolo De Bona, Alessandro Giuffrida, Alessandro Sinopoli, Marilisa Leone, Irina Naletova

Publikováno v: ChemBioChem
17 (2016): 1541–1549. doi:10.1002/cbic.201600243
info:cnr-pdr/source/autori:Sinopoli, Alessandro; Giuffrida, Alessandro; Tomasello, Marianna Flora; Giuffrida, Maria Laura; Leone, Marilisa; Attanasio, Francesco; Caraci, Filippo; De Bona, Paolo; Naletova, Irina; Saviano, Michele; Copani, Agata; Pappalardo, Giuseppe; Rizzarelli, Enrico/titolo:Ac-LPFFD-Th: A Trehalose-Conjugated Peptidomimetic as a Strong Suppressor of Amyloid-[beta] Oligomer Formation and Cytotoxicity/doi:10.1002%2Fcbic.201600243/rivista:ChemBioChem (Print)/anno:2016/pagina_da:1541/pagina_a:1549/intervallo_pagine:1541–1549/volume:17

The inhibition of amyloid formation is a promising therapeutic approach for the treatment of neurodegenerative diseases. Peptide-based inhibitors, which have been widely investigated, are generally derived from original amyloid sequences. Most intere

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b191264a21a81ad6a0fc8ce1429f3f39
http://hdl.handle.net/20.500.11769/47554

The Wrapping Loop and Rap1 C-terminal (RCT) Domain of Yeast Rap1 Modulate Access to Different DNA Binding Modes*

Autor: Paolo De Bona, Roberto Galletto, Erik A. Feldmann

Budding yeast Rap1 is a specific double-stranded DNA-binding protein involved in repression and activation of gene transcription and in the establishment of the nucleoprotein complex formed at telomeres. The DNA-binding domain (DBD) of Rap1 forms a h

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b496c6eea04c7c5fc73471da5cdef0e0
https://europepmc.org/articles/PMC4416850/

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

Copper(II) complexes of rat amylin fragments

Autor: Imre Sóvágó, Eugenio Garribba, Csilla Kállay, Eszter Nagy, Sarolta Timári, Giovanni Micera, Enrico Rizzarelli, Paolo De Bona, Giuseppe Pappalardo, Daniele Sanna, Ágnes Dávid

Publikováno v: Dalton transactions (2003. Print) 40 (2011): 9711–9721. doi:10.1039/c1dt10835b
info:cnr-pdr/source/autori:C. Kállay, Á. Dávid, S. Timári, E. M. Nagy, D. Sanna, E. Garribba, G. Micera, P. De Bona, G. Pappalardo, E. Rizzarelli, I. Sóvágó/titolo:Copper(II) complexes of rat amylin fragments./doi:10.1039%2Fc1dt10835b/rivista:Dalton transactions (2003. Print)/anno:2011/pagina_da:9711/pagina_a:9721/intervallo_pagine:9711–9721/volume:40

The fragments of rat amylin rIAPP(17-29) (Ac-VRSSNNLGPVLPP-NH(2)), rIAPP(17-22) (Ac-VRSSNN-NH(2)), rIAPP(19-22) (Ac-SSNN-NH(2)) and rIAPP(17-20) (Ac-VRSS-NH(2)) together with the related mutant peptides (Ac-VASS-NH(2) and Ac-VRAA-NH(2)) have been syn

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a398bbc9e0838012a627fe74ae0ccd3