Author

E. Buratti

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· 2 Biochemistry· 1 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Organism:human· 3 Assay:proteomics· 3 Research Focus:cell signaling & trafficking· 2 Research Focus:cell type annotation· 2 Research Focus:protein folding & dynamics· 2 Approach:biophysical modeling· 1 Assay:cryo-EM· 1

Frequent Co-Authors

C. Stuani· 2 shared M. Mompean· 2 shared A. A. Skodras· 1 shared A. E. McDermott· 1 shared C. Beaumont· 1 shared C. J. Gloeckner· 1 shared D. Laurents· 1 shared D. Pantoja-Uceda· 1 shared

Activity by Year

2019-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 15 mutual co-author links

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2 shared papersBiochemistry

C. Stuani

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

hnRNP A1 induces aberrant CFTR exon 9 splicing via a newly discovered Exonic Splicing Silencer element.

C. Beaumont, M.-Y. Chou, C. Stuani, E. Buratti, P. J. Lukavsky

This study identifies an exonic splicing silencer element in CFTR exon 9 that is bound by hnRNP A1, leading to exon skipping and non-functional CFTR protein.

bioRxiv · Aug 24, 2023 · PreprintBiochemistry

Sirtuin-1 Sensitive Lysine-136 Acetylation Drives Phase Separation and Pathological Aggregation of TDP-43

J. Garcia Morato, F. Hans, F. von Zweydorf, R. Feederle, S. J. Elsaesser, A. A. Skodras, C. J. Gloeckner, E. Buratti, M. Neumann, P. J. Kahle

This study identifies K136 acetylation as a key modifier of TDP-43's RNA binding and phase separation, leading to pathological aggregation, and shows SIRT1's role in deacetylating and reducing this aggregation.

bioRxiv · May 26, 2020 · PreprintCell Biology

Phe-Gly Motifs Drive Fibrillization of TDP-43's Prion-Like Domain Droplets

D. Pantoja-Uceda, C. Stuani, D. V. Laurents, A. E. McDermott, E. Buratti, M. Mompean

The paper shows Phe-Gly motifs drive fibrillization from TDP-43 droplets, revealing structural differences between droplets and fibrils.

bioRxiv · Feb 20, 2020Biophysics

Deciphering the Amyloid Foldome of TDP-43

M. Mompean, E. Buratti, D. Laurents

The paper discusses the amyloid structures of TDP-43's C-terminal region revealed by cryo-EM, highlighting the need to consider the Q/N-rich segments in understanding TDP-43 aggregation.

bioRxiv · Aug 4, 2019 · PreprintBiophysics