Structure-Function Insights into the Dual Role in Nucleobase and Nicotinamide Metabolism and a Possible Use in Cancer Gene Therapy of the URH1p Riboside Hydrolase

Autor: Alejandra Angela Carriles, Laura Muzzolini, Claudia Minici, Paola Tornaghi, Marco Patrone, Massimo Degano

Publikováno v: International Journal of Molecular Sciences, Vol 25, Iss 13, p 7032 (2024)

The URH1p enzyme from the yeast Saccharomyces cerevisiae has gained significant interest due to its role in nitrogenous base metabolism, particularly involving uracil and nicotinamide salvage. Indeed, URH1p was initially classified as a nucleoside hy

Externí odkaz: https://doaj.org/article/ccc489dde5e243b08e16e335fb570d50

Combinatorial allosteric modulation of agonist response in a self-interacting G-protein coupled receptor

Autor: Valeria Berno, Marco Patrone, Eugenia Cammarota, Massimo Degano, Paola Tornaghi, Davide Mazza

Publikováno v: Communications Biology, Vol 3, Iss 1, Pp 1-12 (2020)
Communications Biology

The structural plasticity of G-protein coupled receptors (GPCRs) enables the long-range transmission of conformational changes induced by specific orthosteric site ligands and other pleiotropic factors. Here, we demonstrate that the ligand binding ca

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5bb93e92ecbdf27921224a4ceec5245f

The structure of N184K amyloidogenic variant of gelsolin highlights the role of the H-bond network for protein stability and aggregation properties

Autor: Francesco Bonì, Marco Patrone, Emanuele Scalone, Eloise Mastrangelo, Alberto Barbiroli, Toni Giorgino, Davide Mattioni, Matteo de Rosa, Maria A. Vanoni, Mario Milani, Michela Bollati

Publikováno v: European biophysics journal 49 (2020): 11–19. doi:10.1007/s00249-019-01409-9
info:cnr-pdr/source/autori:de Rosa, Matteo; Barbiroli, Alberto; Bonì, Francesco; Scalone, Emanuele; Mattioni, Davide; Vanoni, Maria A.; Patrone, Marco; Bollati, Michela; Mastrangelo, Eloise; Giorgino, Toni; Milani, Mario/titolo:The structure of N184K amyloidogenic variant of gelsolin highlights the role of the H-bond network for protein stability and aggregation properties/doi:10.1007%2Fs00249-019-01409-9/rivista:European biophysics journal/anno:2020/pagina_da:11/pagina_a:19/intervallo_pagine:11–19/volume:49

Mutations in the gelsolin protein are responsible for a rare conformational disease known as AGel amyloidosis. Four of these mutations are hosted by the second domain of the protein (G2): D187N/Y, G167R and N184K. The impact of the latter has been so

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b2d618c098a8d6f14eac9625c7a346e8

IL-27, but not IL-35, inhibits neuroinflammation through modulating GM-CSF expression

Autor: Francesca Ruffini, Annamaria Finardi, Roberto Furlan, Marco Patrone, Massimo Degano, Giacomo Casella, Hélène Descamps, Luca Muzio, Federico Colombo, Chiara Maiorino, Burkhard Becher, Gianvito Martino

Publikováno v: Scientific Reports, Vol 7, Iss 1, Pp 1-11 (2017)
Scientific Reports

IL-27 and IL-35 are heterodimeric cytokines, members of the IL-12 family and considered to have immunomodulatory properties. Their role during neuroinflammation had been investigated using mutant mice devoid of either one of their subunits or lacking

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::3e3337e1787a6dcbbd2e92e9996c205b
https://www.zora.uzh.ch/id/eprint/143524/

Protein pUL128 of Human Cytomegalovirus Is Necessary for Monocyte Infection and Blocking of Migration

Autor: Thomas Mertens, Sarah Straschewski, Paul Walther, Giada Frascaroli, Andrea Gallina, Marco Patrone

Publikováno v: Journal of Virology. 85:5150-5158

We have previously shown that only endotheliotropic strains of human cytomegalovirus (HCMV), such as TB40E, infect monocytes and impair their chemokine-driven migration. The proteins encoded by the UL128-131A region (UL128, UL130, and UL131A) of the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5d00e4b469607fc63a7ac7162e3fd203
https://doi.org/10.1128/jvi.02100-10