Folding and Binding Mechanisms of the SH2 Domain from Crkl

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

Structural Characterization of the Xi Class Glutathione Transferase From the Haloalkaliphilic Archaeon Natrialba magadii

Autor: Adele Di Matteo, Luca Federici, Michele Masulli, Erminia Carletti, Daniele Santorelli, Jennifer Cassidy, Francesca Paradisi, Carmine Di Ilio, Nerino Allocati

Publikováno v: Frontiers in Microbiology, Vol 10 (2019)

Xi class glutathione transferases (GSTs) are a recently identified group, within this large superfamily of enzymes, specifically endowed with glutathione-dependent reductase activity on glutathionyl-hydroquinone. Enzymes belonging to this group are w

Externí odkaz: https://doaj.org/article/8ac5458c827a4879b10ed0ba1c62d82e

SH2 Domains: Folding, Binding and Therapeutical Approaches

Autor: Awa Diop, Daniele Santorelli, Francesca Malagrinò, Caterina Nardella, Valeria Pennacchietti, Livia Pagano, Lucia Marcocci, Paola Pietrangeli, Stefano Gianni, Angelo Toto

Publikováno v: International Journal of Molecular Sciences

SH2 (Src Homology 2) domains are among the best characterized and most studied protein-protein interaction (PPIs) modules able to bind and recognize sequences presenting a phosphorylated tyrosine. This post-translational modification is a key regulat

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::c9440ed12f9551eda6cd0ac8e46176e9
https://doi.org/10.3390/ijms232415944

Characterization of early and late transition states of the folding pathway of a SH2 domain

Autor: Angelo Toto, Francesca Malagrinò, Caterina Nardella, Valeria Pennacchietti, Livia Pagano, Daniele Santorelli, Awa Diop, Stefano Gianni

Albeit SH2 domains are abundant protein-protein interaction modules with fundamental roles in the regulation of several physiological and molecular pathways in the cell, the available information about the determinants of their thermodynamic stabilit

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f998595ae478f2cb54d3cf6d2f84f52e
http://hdl.handle.net/11588/889767

Structural and functional investigation of the Small Ribosomal Subunit Biogenesis GTP ase A (RsgA) from Pseudomonas aeruginosa

Autor: Francesco Malatesta, Daniele Santorelli, Adele Di Matteo, S. Rocchio, Carlo Travaglini-Allocatelli, Mimma Franceschini, Serena Rinaldo, Francesco Imperi, Luca Federici

Publikováno v: The FEBS journal
286 (2019): 4245–4260. doi:10.1111/febs.14959
info:cnr-pdr/source/autori:Rocchio, Serena; Santorelli, Daniele; Rinaldo, Serena; Franceschini, Mimma; Malatesta, Francesco; Imperi, Francesco; Federici, Luca; Travaglini-Allocatelli, Carlo; Di Matteo, Adele/titolo:Structural and functional investigation of the Small Ribosomal Subunit Biogenesis GTPase A (RsgA) from Pseudomonas aeruginosa/doi:10.1111%2Ffebs.14959/rivista:The FEBS journal (Print)/anno:2019/pagina_da:4245/pagina_a:4260/intervallo_pagine:4245–4260/volume:286

The Small Ribosomal Subunit Biogenesis GTPase A (RsgA) is a bacterial assembly factor involved in the late stages of the 30S subunit maturation. It is a multidomain GTPase in which the central circularly permutated GTPase domain is flanked by an OB d

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dfa2432c3bd8ce3a1598850620115d4b
https://doi.org/10.1111/febs.14959