Rita Berisio

Dr. Rita Berisio

Institute of Biostructures and Bioimaging, CNR, Via Mezzocannone 16, I-80134 Napoli, Italy
orcid

Research Focus & Metrics

Academic Career Length

29Years (1998-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

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20 May 2020 in Cells
Verified
Journal Article
Open access
PDF file
MRMaria Romano
Maria Romano
Alessia RuggieroAlessia Ruggiero
Alessia Ruggiero
FSFlavia Squeglia
Flavia Squeglia
Giovanni MagaGiovanni Maga
Giovanni Maga
Rita BerisioRita Berisio
Rita Berisio
The current coronavirus disease-2019 (COVID-19) pandemic is due to the novel coronavirus SARS-CoV-2. The scientific community has mounted a strong response by accelerating research and innovation, and has quickly set the foundation for understanding the molecular determinants of the disease for the development of targeted therapeutic interventions. The replication of the viral genome within the infected cells is a key stage of the SARS-CoV-2 life cycle. It is a complex process involving the action of several viral and host proteins in order to perform RNA polymerization, proofreading and final capping. This review provides an update of the structural and functional data on the key actors of the replicatory machinery of SARS-CoV-2, to fill the gaps in the currently available structural data, which is mainly obtained through homology modeling. Moreover, learning from similar viruses, we collect data from the literature to reconstruct the pattern of interactions among the protein actors of the SARS-CoV-2 RNA polymerase machinery. Here, an important role is played by co-factors such as Nsp8 and Nsp10, not only as allosteric activators but also as molecular connectors that hold the entire machinery together to enhance the efficiency of RNA replication.

6 January 2014 in Proceedings of the National Academy of Sciences
Verified
Journal Article
Closed access
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MHMasahiro Hayafune
Masahiro Hayafune
Rita BerisioRita Berisio
Rita Berisio
RMRoberta Marchetti
Roberta Marchetti
Alba SilipoAlba Silipo
Alba Silipo
MKMiyu Kayama
Miyu Kayama
NSNaoto Shibuya
Naoto Shibuya
Significance: Chitin perception by plant receptors triggers various defense responses important for plant immunity. We show the molecular basis of chitin recognition by the rice receptor, CEBiP (chitin-elicitor binding protein), and following receptor dimerization based on the results of biochemical studies, epitope mapping by saturation transfer difference NMR spectroscopy and molecular modeling/docking studies. These results clearly indicated that two CEBiP molecules simultaneously bind to one N -acetylchitoheptaose/octaose from the opposite side, through a binding site in the central lysin motif region, resulting in the dimerization of CEBiP. Based on these observations, we proposed a hypothetical model for the ligand-induced activation of a receptor complex, involving CEBiP and Oryza sativa chitin-elicitor receptor kinase 1 (OsCERK1).

1 February 2002 in Protein Science
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Journal Article
Closed access
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Rita BerisioRita Berisio
Rita Berisio
LVLuigi Vitagliano
Luigi Vitagliano
LMLelio Mazzarella
Lelio Mazzarella
AZAdriana Zagari
Adriana Zagari

1 January 2003 in Molecular Cell
Verified
Journal Article
Closed access
ABAnat Bashan
Anat Bashan
IAIlana Agmon
Ilana Agmon
RZRaz Zarivach
Raz Zarivach
FSFrank Schluenzen
Frank Schluenzen
JHJoerg Harms
Joerg Harms
AYAda Yonath
Ada Yonath

29 October 2014 in Chemistry – A European Journal
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Journal Article
Closed access
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Antonio MolinaroAntonio Molinaro
Antonio Molinaro
OHOtto Holst
Otto Holst
FLFlaviana Di Lorenzo
Flaviana Di Lorenzo
MCMaire Callaghan
Maire Callaghan
ANAlessandra Nurisso
Alessandra Nurisso
SMSonsoles Martin-Santamaria
Sonsoles Martin-Santamaria

20 February 2001 in Biopolymers
Verified
Journal Article
Closed access
PDF file
LVLuigi Vitagliano
Luigi Vitagliano
Rita BerisioRita Berisio
Rita Berisio
LMLelio Mazzarella
Lelio Mazzarella
AZAdriana Zagari
Adriana Zagari