Zobrazeno 1 - 10
of 48
pro vyhledávání: '"Francesca Malagrinò"'
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:
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
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
Autor:
Francesca Malagrinò, Antonio Coluccia, Marianna Bufano, Giuseppe La Regina, Michela Puxeddu, Angelo Toto, Lorenzo Visconti, Alessio Paone, Maria Chiara Magnifico, Francesca Troilo, Francesca Cutruzzolà, Romano Silvestri, Stefano Gianni
Publikováno v:
Cells, Vol 9, Iss 11, p 2435 (2020)
Gab2 is a scaffolding protein, overexpressed in many types of cancers, that plays a key role in the formation of signaling complexes involved in cellular proliferation, migration, and differentiation. The interaction between Gab2 and the C-terminal S
Externí odkaz:
https://doaj.org/article/3646716e8dc34cf583d1b85c7e400090
Publikováno v:
Life, Vol 10, Iss 6, p 85 (2020)
Gab2 is a scaffold protein with a crucial role in colocalizing signaling proteins and it is involved in the regulation of several important molecular pathways. SHP2 is a protein phosphatase that binds, through its two SH2 domains, specific consensus
Externí odkaz:
https://doaj.org/article/c8eef5a84be24dd5906d153097af50b2
Autor:
Karim Zuhra, Catarina S. Tomé, Letizia Masi, Giorgio Giardina, Giulia Paulini, Francesca Malagrinò, Elena Forte, João B. Vicente, Alessandro Giuffrè
Publikováno v:
Cells, Vol 8, Iss 8, p 828 (2019)
Hydrogen sulfide (H2S) is an endogenously produced signaling molecule. The enzymes 3-mercaptopyruvate sulfurtransferase (MST), partly localized in mitochondria, and the inner mitochondrial membrane-associated sulfide:quinone oxidoreductase (SQR), bes
Externí odkaz:
https://doaj.org/article/1f05ae45fda74332904ade2530a68b1d
Autor:
Francesca Malagrinò, Serena Rinaldo, Angelo Toto, Stefano Gianni, Caterina Nardella, Livia Pagano
Publikováno v:
Protein Science : A Publication of the Protein Society
SH2 domains are a class of protein–protein interaction modules with the function to recognize and bind sequences characterized by the presence of a phosphorylated tyrosine. SHP2 is a protein phosphatase involved in the Ras‐ERK1/2 signaling pathwa
Autor:
Francesca Malagrinò, Giuliana Fusco, Valeria Pennacchietti, Angelo Toto, Caterina Nardella, Livia Pagano, Alfonso de Simone, Stefano Gianni
Publikováno v:
Protein science : a publication of the Protein Society. 31(9)
PDZ domains are the most diffused protein-protein interaction modules of the human proteome and are often present in tandem repeats. An example is PDZD2, a protein characterized by the presence of six PDZ domains that undergoes a proteolytic cleavage