Author

N. A. Ramella

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 Organism:human· 2 Assay:proteomics· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:host-pathogen & immune response· 1

Frequent Co-Authors

M. A. Tricerri· 3 shared R. A. Gisonno· 3 shared I. Diaz Ludovico· 2 shared E. D. Prieto· 1 shared E. E. Elias· 1 shared G. M. Gaddi· 1 shared G. R. Schinella· 1 shared G. S. Finarelli· 1 shared

Activity by Year

2019-2021 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 33 mutual co-author links

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3 shared papersBiophysics

M. A. Tricerri

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3 papers

Recent·Most cited

Understanding the role of apolipoprotein A-I in atherosclerosis. Post-translational modifications synergize dysfunction?

I. Diaz Ludovico, R. A. Gisonno, N. A. Ramella, M. A. Tricerri, M. A. Tricerri, M. A. Tricerri

This study investigates how post-translational modifications affect apoA-I structure and function in atherosclerosis, finding that oxidation and crosslinking impair its flexibility and lead to dysfunction.

Biochimica et Biophysica Acta (BBA) - General Subjects · Jan 1, 2021Peer-reviewedBiophysics

Dataset of the construction and characterization of stable biological nanoparticles

R. A. Gisonno, M. A. Tricerri, M. C. Gonzalez, H. A. Garda, N. A. Ramella, I. Diaz Ludovico

The paper describes the construction and characterization of stable biological nanoparticles through intra-chain crosslinking, demonstrating their utility as molecular carriers.

bioRxiv · Aug 23, 2020Biophysics

N-terminal mutants of human apolipoprotein A-I: structural perturbations associated to protein misfolding

G. M. Gaddi, R. A. Gisonno, S. A. Rosu, L. M. Curto, E. E. Elias, E. D. Prieto, G. R. Schinella, G. S. Finarelli, M. F. Cortez, N. A. Ramella, M. A. Tricerri

This study investigates how the L60R mutation in apolipoprotein A-I causes structural instability and misfolding, leading to protein aggregation and inflammatory responses.

bioRxiv · Jan 14, 2019 · PreprintBiophysics