A
Antonella Piccini
Researcher at Cold Spring Harbor Laboratory
Publications - 8
Citations - 1818
Antonella Piccini is an academic researcher from Cold Spring Harbor Laboratory. The author has contributed to research in topics: Replication protein A & Origin recognition complex. The author has an hindex of 8, co-authored 8 publications receiving 1753 citations. Previous affiliations of Antonella Piccini include International Centre for Genetic Engineering and Biotechnology.
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Journal ArticleDOI
Driving AMPA Receptors into Synapses by LTP and CaMKII: Requirement for GluR1 and PDZ Domain Interaction
Yasunori Hayashi,Song-Hai Shi,José A. Esteban,Antonella Piccini,Jean Christophe Poncer,Roberto Malinow +5 more
TL;DR: Results show that LTP and CaMKII activity drive AMPA-Rs to synapses by a mechanism that requires the association between GluR1 and a PDZ domain protein.
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Functional analysis of the protein phosphatase activity of PTEN.
Xiaoqun Catherine Zhang,Antonella Piccini,Michael P. Myers,Linda Van Aelst,Nicholas K. Tonks +4 more
TL;DR: A new aspect of the function of this important tumour suppressor is revealed and it is suggested that, in addition to dephosphorylating the 3 position in phosphatidylinositol phospholipids, the critical protein substrate of PTEN may be PTEN itself.
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Critical postsynaptic density 95/disc large/zonula occludens-1 interactions by glutamate receptor 1 (GluR1) and GluR2 required at different subcellular sites.
TL;DR: Dual-channel, two-photon laser scanning microscopy was used to provide high-resolution visualization and quantification of green fluorescent protein-tagged AMPA receptors in different subcellular compartments and showed that mutations on GluR1 or GluGluR2 AMPA subunit that perturb interactions with PDZ domain proteins lead to the accumulation of these receptors at different sub cellular sites.
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Mutations in the human papillomavirus type 16 E2 protein identify a region of the protein involved in binding to E1 protein
TL;DR: This study has analysed in detail the association between human papillomavirus type 16 (HPV-16) E1 and E2 proteins and found a conservation of E2 function and a common mechanism of interaction between these virally encoded proteins.
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Regulation of human papillomavirus type 16 DNA replication by E2, glucocorticoid hormone and epidermal growth factor.
TL;DR: The results have important implications for the pathogenesis of HPV infection and suggest that the relative levels of E2, glucocorticoid hormone and EGF may significantly affect the outcome of an HPV infection.