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

BiophysicsBiochimica et Biophysica Acta (BBA) - General SubjectsPeer-reviewedJan 1, 2021

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

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.

DOI 10.1016/j.bbagen.2020.129732

humanproteomics

𝕏 PostBluesky

BiophysicsbioRxivAug 23, 2020

Dataset of the construction and characterization of stable biological nanoparticles

R. A. Gisonno, M. A. Tricerri, M. C. Gonzalez…·I. Diaz Ludovico

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

DOI 10.1016/j.dib.2020.106536

experimental assay

𝕏 PostBluesky

BiophysicsbioRxivPreprintJan 14, 2019

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

G. M. Gaddi, R. A. Gisonno, S. A. Rosu…·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.

DOI 10.1101/520171

humanproteomics

𝕏 PostBluesky