Zobrazeno 1 - 10
of 74
pro vyhledávání: '"Angelo, Toto"'
Autor:
Noah Giacon, Ettore Lo Cascio, Valeria Pennacchietti, Flavio De Maio, Giulia Santarelli, Diego Sibilia, Federica Tiberio, Maurizio Sanguinetti, Wanda Lattanzi, Angelo Toto, Alessandro Arcovito
Publikováno v:
Scientific Reports, Vol 14, Iss 1, Pp 1-11 (2024)
Abstract The COVID-19 pandemic caused by SARS-CoV-2 has highlighted the urgent need for innovative antiviral strategies to fight viral infections. Although a substantial part of the overall effort has been directed at the Spike protein to create an e
Externí odkaz:
https://doaj.org/article/1ddadc7741ce42c7a61846415285a350
Publikováno v:
Biochemistry and Biophysics Reports, Vol 39, Iss , Pp 101803- (2024)
GRB2, or Growth Factor Receptor-Bound Protein 2, is a pivotal adaptor protein in intracellular signal transduction pathways, particularly within receptor tyrosine kinase (RTK) signaling cascades. Its crystal structure reveals a modular architecture c
Externí odkaz:
https://doaj.org/article/4d1e56f4755e4ccd9e4ff1db49f9c690
Autor:
Valeria Pennacchietti, Angelo Toto
Publikováno v:
Scientific Reports, Vol 13, Iss 1, Pp 1-8 (2023)
Abstract The Envelope protein (E) is a structural protein encoded by the genome of SARS-CoV, SARS-CoV-2 and MERS-CoV Coronaviruses. It is poorly present in the virus but highly expressed in the host cell, with prominent role in virus assembly and vir
Externí odkaz:
https://doaj.org/article/449106499cd94389871dc703cddc2c65
Autor:
Noah Giacon, Ettore Lo Cascio, Darcy S. Davidson, Marcelo D. Polêto, Justin A. Lemkul, Valeria Pennacchietti, Livia Pagano, Carlotta Zamparelli, Angelo Toto, Alessandro Arcovito
Publikováno v:
Computational and Structural Biotechnology Journal, Vol 21, Iss , Pp 3259-3271 (2023)
The Envelope (E) protein of SARS-CoV-2 plays a key role in virus maturation, assembly, and virulence mechanisms. The E protein is characterized by the presence of a PDZ-binding motif (PBM) at its C-terminus that allows it to interact with several PDZ
Externí odkaz:
https://doaj.org/article/5f87ea47f88e4bfda42747021ccdc226
Autor:
Caterina Nardella, Lorenzo Visconti, Francesca Malagrinò, Livia Pagano, Marianna Bufano, Marianna Nalli, Antonio Coluccia, Giuseppe La Regina, Romano Silvestri, Stefano Gianni, Angelo Toto
Publikováno v:
Biology Direct, Vol 16, Iss 1, Pp 1-21 (2021)
Abstract The interaction between proteins is a fundamental event for cellular life that is generally mediated by specialized protein domains or modules. PDZ domains are the largest class of protein–protein interaction modules, involved in several c
Externí odkaz:
https://doaj.org/article/79a77de6d4184643b76da2ee34efbff5
Publikováno v:
Frontiers in Molecular Biosciences, Vol 9 (2022)
Externí odkaz:
https://doaj.org/article/a821306fec904a68817a6650e8ed57be
Autor:
Ettore Lo Cascio, Angelo Toto, Gabriele Babini, Flavio De Maio, Maurizio Sanguinetti, Alvaro Mordente, Stefano Della Longa, Alessandro Arcovito
Publikováno v:
Computational and Structural Biotechnology Journal, Vol 19, Iss , Pp 1838-1847 (2021)
Short Linear Motifs (SLiMs) are functional protein microdomains that typically mediate interactions between a short linear region in one protein and a globular domain in another. Surface Plasmon Resonance assays have been performed to determine the b
Externí odkaz:
https://doaj.org/article/bf96ef5a1f9242f290b6fa6905ec77aa
Autor:
Caterina Nardella, Angelo Toto, Daniele Santorelli, Livia Pagano, Awa Diop, Valeria Pennacchietti, Paola Pietrangeli, Lucia Marcocci, Francesca Malagrinò, Stefano Gianni
Publikováno v:
Biomolecules, Vol 12, Iss 8, p 1014 (2022)
SH2 domains are structural modules specialized in the recognition and binding of target sequences containing a phosphorylated tyrosine residue. They are mostly incorporated in the 3D structure of scaffolding proteins that represent fundamental regula
Externí odkaz:
https://doaj.org/article/efc0c37e52894b3385d9b1f44d7759fa
Autor:
Lorenzo Visconti, Angelo Toto, James A. Jarvis, Francesca Troilo, Francesca Malagrinò, Alfonso De Simone, Stefano Gianni
Publikováno v:
Frontiers in Molecular Biosciences, Vol 7 (2020)
SH2 domains are common protein interaction domains able to recognize short aminoacidic sequences presenting a phosphorylated tyrosine (pY). In spite of their fundamental importance for cell physiology there is a lack of information about the mechanis
Externí odkaz:
https://doaj.org/article/5a4ca9ab384b47d3b4a7921b00dbfbb7
Autor:
Francesca Malagrinò, Valeria Pennacchietti, Daniele Santorelli, Livia Pagano, Caterina Nardella, Awa Diop, Angelo Toto, Stefano Gianni
Publikováno v:
Biomolecules, Vol 12, Iss 2, p 209 (2022)
The vast majority of our current knowledge about the biochemical and biophysical properties of proteins derives from in vitro studies conducted on isolated globular domains. However, a very large fraction of the proteins expressed in the eukaryotic c
Externí odkaz:
https://doaj.org/article/00911d04a51e40aea23db07d50244f97