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Elisabetta Boeri Erba
Researcher at University of Grenoble
Publications - 43
Citations - 2019
Elisabetta Boeri Erba is an academic researcher from University of Grenoble. The author has contributed to research in topics: Mass spectrometry & Gene. The author has an hindex of 20, co-authored 36 publications receiving 1811 citations. Previous affiliations of Elisabetta Boeri Erba include University of Turin & University of Michigan.
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Assembly reflects evolution of protein complexes
TL;DR: An analysis of over 5,000 unique atomic structures shows that the quaternary structure of homomers is conserved in over 70% of protein pairs sharing as little as 30% sequence identity, and allows reliable prediction of evolution and assembly of a complex solely from its crystal structure.
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Integrin-induced Epidermal Growth Factor (EGF) Receptor Activation Requires c-Src and p130Cas and Leads to Phosphorylation of Specific EGF Receptor Tyrosines
Laura Moro,Laura Dolce,Sara Cabodi,Elena Bergatto,Elisabetta Boeri Erba,Monica Smeriglio,Emilia Turco,Saverio Francesco Retta,Maria Gabriella Giuffrida,Mascia Venturino,Jasminka Godovac-Zimmermann,Amedeo Conti,Erik Schaefer,Laura Beguinot,Carlo Tacchetti,Paolo Gaggini,Lorenzo Silengo,Guido Tarone,Paola Defilippi +18 more
TL;DR: Data indicate that integrin-mediated adhesion induces assembly of a macromolecular complex containing c-Src and p130Cas and leads to phosphorylation of specific EGF receptor tyrosine residues.
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Symmetrical modularity of the COP9 signalosome complex suggests its multifunctionality.
TL;DR: This work applies an emerging mass spectrometry approach to gain insight into the structure of the CSN complex and indicates that the catalytically active human complex, reconstituted in vitro, is composed of a single copy of each of the eight subunits.
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The emerging role of native mass spectrometry in characterizing the structure and dynamics of macromolecular complexes
Elisabetta Boeri Erba,Elisabetta Boeri Erba,Elisabetta Boeri Erba,Carlo Petosa,Carlo Petosa,Carlo Petosa +5 more
TL;DR: The application of native MS to the study of protein−ligand interactions and its emerging role in elucidating the structure of macromolecular assemblies, including soluble and membrane protein complexes are reviewed.
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The tyrosine phosphatase Shp2 interacts with NPM-ALK and regulates anaplastic lymphoma cell growth and migration.
Claudia Voena,Chiara Conte,Chiara Ambrogio,Elisabetta Boeri Erba,Francesco Boccalatte,Shabaz Mohammed,Ole N. Jensen,Giorgio Palestro,Giorgio Inghirami,Roberto Chiarle +9 more
TL;DR: Findings show a direct involvement of Shp2 in NPM-ALK lymphomagenesis, highlighting its critical role in lymphoma cell proliferation and migration.