Author

A. Savastano

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

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Biophysics· 3

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:host-pathogen & immune response· 2 Assay:proteomics· 2 Organism:virus· 2 Research Focus:cell signaling & trafficking· 1 Organism:human· 1 Research Focus:protein folding & dynamics· 1 Assay:protein structure· 1

Frequent Co-Authors

M. Zweckstetter· 3 shared A. Cario· 1 shared A. G. Hendricks· 1 shared A. Ibanez de Opakua· 1 shared A. Ibanez-de-Opakua· 1 shared C. L. Berger· 1 shared M. J. Previs· 1 shared M. Rankovic· 1 shared

Activity by Year

2020-2022 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 19 mutual co-author links

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3 shared papersBiophysics

M. Zweckstetter

Mutual co-authors in cluster

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3 papers

Recent·Most cited

Contributions of the N-terminal intrinsically disordered region of the SARS-CoV-2 nucleocapsid protein to RNA-induced phase separation

M. Zachrdla, A. Savastano, A. Ibanez de Opakua, M.-S. Cima-Omori, M. Zweckstetter

This study investigates how the N-terminal intrinsically disordered region of SARS-CoV-2 nucleocapsid protein influences RNA-induced phase separation and its implications for viral replication.

bioRxiv · Mar 30, 2022 · PreprintBiophysics

The Pathogenic R5L Mutation Disrupts Formation of Tau Complexes on the Microtubule by Altering Local N-Terminal Structure

A. Cario, A. Savastano, N. B. Wood, Z. Liu, M. J. Previs, A. G. Hendricks, M. Zweckstetter, C. L. Berger

This paper investigates the R5L mutation in Tau, showing it does not reduce microtubule-binding affinity but alters N-terminal structure, impairing Tau complex formation on microtubules.

bioRxiv · Oct 15, 2021Biophysics

Nucleocapsid protein of SARS-CoV-2 phase separates into RNA-rich polymerase-containing condensates

A. Savastano, A. Ibanez-de-Opakua, M. Rankovic, M. Zweckstetter

This study shows that SARS-CoV-2 nucleocapsid protein forms RNA-rich condensates via phase separation, which recruit the viral RNA polymerase to enhance transcription.

bioRxiv · Jun 18, 2020Biophysics