Switching between the Alternative Structures and Functions of a 2-Cys Peroxiredoxin, by Site-Directed Mutagenesis

Autor: Angelucci, F., Saccoccia, F., Ardini, M., Boumis, G., Brunori, M., Di Leandro, L., Ippoliti, R., Miele, A.E., Natoli, G., Scotti, S., Bellelli, A.

Publikováno v: In Journal of Molecular Biology 15 November 2013 425(22):4556-4568

Identification of novel multi-stage histone deacetylase (HDAC) inhibitors that impair Schistosoma mansoni viability and egg production

Autor: Guidi A, Saccoccia F, Gennari N, Gimmelli R, Nizi E, Lalli C, Paonessa G, Papoff G, Bresciani A, Ruberti G*.

Publikováno v: Parasites & vectors (2018).
info:cnr-pdr/source/autori:Guidi A*, Saccoccia F*, Gennari N**, Gimmelli R*, Nizi E**, Lalli C*, Paonessa G**, Papoff G*, Bresciani A**, Ruberti G*./titolo:Identification of novel multi-stage histone deacetylase (HDAC) inhibitors that impair Schistosoma mansoni viability and egg production/doi:/rivista:Parasites & vectors/anno:2018/pagina_da:/pagina_a:/intervallo_pagine:/volume

BACKGROUND: Novel anti-schistosomal multi-stage drugs are needed because only a single drug, praziquantel, is available for the treatment of schistosomiasis and is poorly effective on larval and juvenile stages of the parasite. Schistosomes have a co

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=cnr_________::c93d097683d8430d370095b6100ecdd2
http://www.cnr.it/prodotto/i/397114

The chemical advantage of sulfur over selenium: controlling the switching-in-function of the moonlighting behaviour of Peroxiredoxin

Autor: Saccoccia, F, Angelucci, Francesco, Boumis, G, Desiato, G, Miele, Ae, Bellelli, A.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______3983::17a1d856d0d7f10bbc6c4d97a52d2285
http://hdl.handle.net/11697/16191

Peroxiredoxins for Nanotechnology: a Biochemical Approach to Produce Nanoconductors

Autor: Ardini, Matteo, Angelucci, Francesco, Di Leandro, L, Scotti, S, Bellelli, A, Saccoccia, F, Ippoliti, Rodolfo

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=od______3983::a5b70d2389364859861494c28491be9a
http://hdl.handle.net/11697/88486

Crystal structure of the PPAR-gamma ligand binding domain complexed with a novel partial agonist: a new region of the hydrophobic pocket could be exploited for drug design

Autor: Montanari R., Saccoccia F., Scotti E., Crestani M., Godio C., Gilardi F., Loiodice F., Fracchiolla G., Laghezza A., Tortorella P., Lavecchia A., Novellino E., Mazza F., Pochetti G.

Publikováno v: Journal of medicinal chemistry 51 (2008): 7768–7776. doi:10.1021/jm800733h
info:cnr-pdr/source/autori:Montanari R., Saccoccia F., Scotti E., Crestani M., Godio C., Gilardi F., Loiodice F., Fracchiolla G., Laghezza A., Tortorella P., Lavecchia A., Novellino E., Mazza F., Pochetti G./titolo:Crystal structure of the PPAR-gamma ligand binding domain complexed with a novel partial agonist: a new region of the hydrophobic pocket could be exploited for drug design/doi:10.1021%2Fjm800733h/rivista:Journal of medicinal chemistry/anno:2008/pagina_da:7768/pagina_a:7776/intervallo_pagine:7768–7776/volume:51

The peroxisome proliferator-activated receptors (PPARs) are ligand-dependent transcription factors regulating glucose and lipid metabolism. The search for new PPAR ligands with reduced adverse effects with respect to the marketed antidiabetic agents

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=cnr_________::371e412757e4af3050f54a491bc3e0c0
https://publications.cnr.it/doc/19779