Modulation of bacterial multicellularity via spatio-specific polysaccharide secretion.

Autor: Salim T Islam, Israel Vergara Alvarez, Fares Saïdi, Annick Guiseppi, Evgeny Vinogradov, Gaurav Sharma, Leon Espinosa, Castrese Morrone, Gael Brasseur, Jean-François Guillemot, Anaïs Benarouche, Jean-Luc Bridot, Gokulakrishnan Ravicoularamin, Alain Cagna, Charles Gauthier, Mitchell Singer, Henri-Pierre Fierobe, Tâm Mignot, Emilia M F Mauriello

Publikováno v: PLoS Biology, Vol 18, Iss 6, p e3000728 (2020)

The development of multicellularity is a key evolutionary transition allowing for differentiation of physiological functions across a cell population that confers survival benefits; among unicellular bacteria, this can lead to complex developmental b

Externí odkaz: https://doaj.org/article/1c485093bfaf4b719b33284bbf6aaf58

Non-SUMOylated alternative spliced isoforms of alpha-synuclein are more aggregation-prone and toxic

Autor: Kambiz Hassanzadeh, Castrese Morrone, Keivan Akhtari, Ellen Gerhardt, Ludovica Zaccagnini, Tiago Fleming Outeiro, Marco Feligioni

Publikováno v: Mechanisms of ageing and development 209, 111759 (2023). doi:10.1016/j.mad.2022.111759

The exon skipping of α-Synuclein (α-Syn), the main constituent of the abnormal protein aggregation in Lewy bodies of Parkinson's disease (PD), forms four isoforms. In contrast to the full length α-Syn (α-Syn 140), little is known about the splice

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c6ca16c86426562edccb2cadf5a7c7f2
https://pub.dzne.de/record/169127

The SNAP-tag technology revised: an effective chemo-enzymatic approach by using a universal azide-based substrate

Autor: Rosa Merlo (a), Diego Caprioglio (b), Michele Cillo (c), Anna Valentia (a), Rosanna Mattossovich (a), Castrese Morrone (b), Alberto Massarotti (b, Franca Rossi (b), Riccardo Miggiano (b, Antonio Leonardi (c), Alberto Minassi (b), Giuseppe Perugino (a)

Publikováno v: Journal of enzyme inhibition and medicinal chemistry
36 (2020): 85–97. doi:10.1080/14756366.2020.1841182
info:cnr-pdr/source/autori:Rosa Merlo (a), Diego Caprioglio (b), Michele Cillo (c), Anna Valentia (a), Rosanna Mattossovich (a), Castrese Morrone (b), Alberto Massarotti (b,d), Franca Rossi (b), Riccardo Miggiano (b,d), Antonio Leonardi (c), Alberto Minassi (b) and Giuseppe Perugino (a)/titolo:The SNAP-tag technology revised: an effective chemo-enzymatic approach by using a universal azide-based substrate/doi:10.1080%2F14756366.2020.1841182/rivista:Journal of enzyme inhibition and medicinal chemistry (Print)/anno:2020/pagina_da:85/pagina_a:97/intervallo_pagine:85–97/volume:36
Journal of Enzyme Inhibition and Medicinal Chemistry
article-version (VoR) Version of Record
Journal of Enzyme Inhibition and Medicinal Chemistry, Vol 36, Iss 1, Pp 85-97 (2021)

SNAP-tag® is a powerful technology for the labelling of protein/enzymes by using benzyl-guanine (BG) derivatives as substrates. Although commercially available or ad hoc produced, their synthesis and purification are necessary, increasing time and c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::16aa3a3483349c1859748a52a632fc6c
http://www.cnr.it/prodotto/i/435070

Targeting Genome Integrity in Mycobacterium Tuberculosis: From Nucleotide Synthesis to DNA Replication and Repair

Autor: Menico Rizzi, Riccardo Miggiano, Castrese Morrone, Franca Rossi

Publikováno v: Molecules, Vol 25, Iss 5, p 1205 (2020)
Molecules

Mycobacterium tuberculosis (MTB) is the causative agent of tuberculosis (TB), an ancient disease which still today causes 1.4 million deaths worldwide per year. Long-term, multi-agent anti-tubercular regimens can lead to the anticipated non-complianc

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c1071c9c929e03c532c4c8e6c6e921cc
https://doi.org/10.3390/molecules25051205

Crystal structure of a thermophilic O6-alkylguanine-DNA alkyltransferase-derived self-labeling protein-tag in covalent complex with a fluorescent probe

Autor: Castrese Morrone, Franca Rossi, Davide M. Ferraris, Anna Valenti, Giuseppe Perugino, Alberto Massarotti, Riccardo Miggiano

Publikováno v: Biochemical and biophysical research communications
500 (2018): 698–703. doi:10.1016/j.bbrc.2018.04.139
info:cnr-pdr/source/autori:Rossi, Franca; Morrone, Castrese; Massarotti, Alberto; Ferraris, Davide Maria; Valenti, Anna; Perugino, Giuseppe; Miggiano, Riccardo/titolo:Crystal structure of a thermophilic O-6-alkylguanine-DNA alkyltransferase-derived self-labeling protein-tag in covalent complex with a fluorescent probe/doi:10.1016%2Fj.bbrc.2018.04.139/rivista:Biochemical and biophysical research communications (Print)/anno:2018/pagina_da:698/pagina_a:703/intervallo_pagine:698–703/volume:500

The self-labeling protein tags are robust and versatile tools for studying different molecular aspects of cell biology. In order to be suitable for a wide spectrum of experimental conditions, it is mandatory that these systems are stable after the fl

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98b743beafd7bccac7cb7748219c6000
http://hdl.handle.net/11588/893317