Author

Y. M. Ayala

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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Biochemistry· 2 Cell Biology· 2 Pathology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Organism:human· 4 Research Focus:protein folding & dynamics· 4 Assay:proteomics· 3 Research Focus:cell signaling & trafficking· 2 Research Focus:cell type annotation· 2 Research Focus:chromatin & epigenetic regulation· 2 Assay:protein structure· 2

Frequent Co-Authors

D. D. Dhavale· 2 shared J. Mittal· 2 shared N. L. Fawzi· 2 shared P. M. dos Passos· 2 shared A. A. Hyman· 1 shared A. E. Conicella· 1 shared A. Honigmann· 1 shared A. M. D'Ordine· 1 shared

Activity by Year

2018-2024 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 17 mutual co-author links

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2 shared papersPathology

D. D. Dhavale

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Author profile →

5 papers

Recent·Most cited

Seeding competent TDP-43 persists in human patient and mouse muscle

E. M. Lynch, S. Pittman, J. Daw, C. Ikenaga, S. Chen, D. D. Dhavale, M. E. Jackrel, Y. M. Ayala, P. Kotzbauer, C. V. Ly, A. Pestronk, T. E. Lloyd, C. C. Weihl

This study shows that TDP-43 aggregate seeds persist in both mouse and human skeletal muscle even after the removal of large TDP-43 inclusions.

bioRxiv · Apr 3, 2024Pathology

Intra-condensate demixing of TDP-43 inside stress granules generates pathological aggregates

X. Yan, D. Kuster, P. Mohanty, J. Nijssen, K. Pombo-Garcia, A. Rizuan, T. M. Franzmann, A. Sergeeva, P. M. dos Passos, L. George, S.-H. Wang, J. Shenoy, H. L. Danielson, A. Honigmann, Y. M. Ayala, , A. A. Hyman

This study shows that TDP-43 aggregation in stress granules requires up-concentration and oxidative stress, leading to intra-condensate demixing and pathological aggregates.

bioRxiv · Jan 23, 2024Cell Biology

RNA-mediated ribonucleoprotein assembly controls TDP-43 nuclear retention

P. M. dos Passos, E. H. Hemamali, L. D. Mamede, L. R. Hayes, Y. M. Ayala

This study shows that RNA-mediated TDP-43 self-assembly forms macromolecular complexes that retain TDP-43 in the nucleus, preventing cytoplasmic aggregation and highlighting potential therapeutic targets.

bioRxiv · Aug 6, 2023Cell Biology

TDP-43 α-helical structure tunes liquid-liquid phase separation and function

A. E. Conicella, G. L. Dignon, G. H. Zerze, H. B. Schmidt, A. M. D'Ordine, Y. C. Kim, R. Rohatgi, Y. M. Ayala, J. Mittal, N. L. Fawzi

This study shows that mutations in TDP-43's helical region modulate its phase separation and function, with implications for ALS and synthetic biology.

bioRxiv · May 18, 2019Biochemistry

TDP-43 oligomers detected as initial intermediate species during aggregate formation

R. L. French, A. N. Reeb, H. Aligireddy, N. Kedia, D. D. Dhavale, Z. R. Grese, P. T. Kotzbauer, J. Bieschke, Y. M. Ayala

This study identifies TDP-43 oligomers as early intermediates in aggregation, showing ALS-linked mutations accelerate this process and enhance aggregate propagation.

bioRxiv · Dec 17, 2018 · PreprintBiochemistry