Author

S. Perati

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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Cancer Biology· 2 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:human· 3 Research Focus:cell signaling & trafficking· 2 Research Focus:cell type annotation· 2 Assay:bulk RNA-seq· 1 Research Focus:cancer & tumor microenvironment· 1 Research Focus:chromatin & epigenetic regulation· 1 Research Focus:clustering· 1

Frequent Co-Authors

A. Heslin· 2 shared A. Tulpule· 2 shared Y. P. Lin· 2 shared A. D. Ramirez· 1 shared A. M. Gacita· 1 shared A. Sweet-Cordero· 1 shared A.-F. Galic· 1 shared B. Huang· 1 shared

Activity by Year

2020-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 23 mutual co-author links

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2 shared papersCancer Biology

A. Heslin

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

FET fusion oncoproteins disrupt physiologic DNA repair and create a targetable opportunity for ATR inhibitor therapy

S. Menon, D. Gracilla, M. R. Breese, Y. P. Lin, F. S. Dela Cruz, T. Feinberg, E. De Stanchina, A.-F. Galic, H. Allegakoen, s. perati, N. Wen, A. Heslin, M. Horlbeck, J. S. Weissman, A. Sweet-Cordero, , A. Tulpule

This study shows FET fusion oncoproteins disrupt DNA repair by inhibiting ATM signaling, making ATR inhibitors a potential therapy for FET rearranged cancers.

bioRxiv · Apr 30, 2023 · PreprintCancer Biology

Nuclear damage in LMNA mutant iPSC-derived cardiomyocytes is associated with impaired lamin localization to the nuclear envelope

M. Wallace, H. Zahr, S. Perati, C. D. Morsink, L. E. Johnson, A. M. Gacita, S. Lai, L. L. Wallrath, I. J. Benjamin, E. McNally, T. J. Kirby, J. Lammerding

This study shows that LMNA mutations in iPSC-derived cardiomyocytes cause nuclear shape changes, reduced stiffness, and lamin mislocalization, linking nuclear abnormalities to LMNA-DCM pathogenesis.

bioRxiv · Oct 30, 2021 · PreprintCell Biology

Kinase-mediated RAS signaling via membraneless cytoplasmic protein granules

A. Tulpule, J. Guan, D. S. Neel, Y. P. Lin, A. Heslin, H. R. Allegakoan, S. Perati, A. D. Ramirez, X. Shi, B. Yang, S. Feng, S. Makhija, D. Brown, B. Huang, T. G. Bivona

This study identifies membraneless protein granules formed by RTK oncoproteins that activate RAS/MAPK signaling independently of lipid membranes in cancer.

bioRxiv · Apr 9, 2020Cancer Biology