Evidence map›Paper›PMID 42422879›Full record

ArticleFrontiers in molecular biosciences2026

Investigating the effect of progressive truncations at the ALS-linked protein TDP-43 RRM2 on its aggregation mechanism.

Greta Grassmann, Matteo Amadei, Arianna Lardieri, Linda Celeste Montemiglio, Alessandra Anna Passeri, Maurizio Mattarelli, Lorenzo Di Rienzo, Mattia Miotto, Giancarlo Ruocco, Edoardo Milanetti

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Article in Frontiers in molecular biosciences, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

10 authors.

Greta GrassmannCenter for Life Nano and Neuro Science, Italian Institute of Technology, Rome, Italy.
Matteo AmadeiInstitute of Molecular Biology and Pathology c/o Department of Biochemical Sciences "Alessandro Rossi Fanelli", Sapienza, University of Rome, National Research Council, Rome, Italy.
Arianna LardieriDepartment of Biochemical Sciences "Alessandro Rossi Fanelli", Sapienza, University of Rome, Rome, Italy.
Linda Celeste MontemiglioInstitute of Molecular Biology and Pathology c/o Department of Biochemical Sciences "Alessandro Rossi Fanelli", Sapienza, University of Rome, National Research Council, Rome, Italy.
Alessandra Anna PasseriDepartment of Physics and Geology, University of Perugia, Perugia, Italy.
Maurizio MattarelliDepartment of Physics and Geology, University of Perugia, Perugia, Italy.
Lorenzo Di RienzoCenter for Life Nano and Neuro Science, Italian Institute of Technology, Rome, Italy.
Mattia MiottoCenter for Life Nano and Neuro Science, Italian Institute of Technology, Rome, Italy.
Giancarlo RuoccoCenter for Life Nano and Neuro Science, Italian Institute of Technology, Rome, Italy.
Edoardo MilanettiCenter for Life Nano and Neuro Science, Italian Institute of Technology, Rome, Italy.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Amyotrophic lateral sclerosis is a neurodegenerative disease characterized by inclusions of TDP-43 protein. C-terminal fragments (CTFs) of TDP-43, generated by cleavage within its second RNA recognition motif (RRM2), have been found forming aggregates in patients. Aggregation has often been attributed to the C-terminal domain, but increasing evidence indicates that RRM2 fragments contribute to pathological inclusions. We performed extensive molecular dynamics simulations to investigate the changes resulting from the truncation that could lead to aggregation. We analyzed the full RRM2 domain (fRRM2, residues 192-261) and two fragments commonly observed in CTFs (tRRM2A, residues 220-261, and tRRM2B, residues 209-261). We found that truncation results in distinct aggregation-prone states. tRRM2B appears to rely on

Indexed as

aggregation modelALS (Amyotrophic lateral sclerosis)molecular dynamics simulationprotein aggragationprotein structure and functionTDP43

Identifiers

PMID42422879
PMCPMC13341550

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