Author

I. A. Rota

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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Immunology· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:cell type annotation· 2 Research Focus:host-pathogen & immune response· 2 Organism:human· 2 Organism:mouse· 2 Assay:proteomics· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:chromatin & epigenetic regulation· 1

Frequent Co-Authors

G. A. Hollander· 3 shared A. E. Handel· 2 shared E. Sezgin· 2 shared J. A. Newman· 2 shared M. E. Deadman· 2 shared N. Prevot· 2 shared O. GileadiiD· 2 shared S. Maio· 2 shared

Activity by Year

2018-2021 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 37 mutual co-author links

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3 shared papersImmunology

G. A. Hollander

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Author profile →

3 papers

Recent·Most cited

A FOXN1 mutation competitively displaces wild-type FOXN1 from higher order nuclear condensates to cause immunodeficiency

I. A. Rota, A. E. Handel, F. Klein, S. Maio, F. Dhalla, M. E. Deadman, S. Cheuk, J. A. Newman, Y. S. Michaels, S. Zuklys, N. Prevot, P. Hublitz, P. D. Charles, A. S. Gkazi, E. Adamopoulou, , G. A. Hollander

This paper identifies a FOXN1 mutation that displaces wild-type FOXN1 from nuclear condensates, leading to immunodeficiency and athymia in heterozygotes.

bioRxiv · Mar 28, 2021 · PreprintImmunology

The chaperonin CCT8 controls proteostasis essential for T cell maturation, selection, and function

B. E. Oftedal, S. Maio, A. Handel, M. P. White, D. Howie, S. Davis, N. Prevot, I. A. Rota, M. E. Deadman, B. M. Kessler, R. Fisher, N. S. Trede, E. Sezgin, R. M. Maizels, G. A. Hollander

This study shows that the chaperonin CCT8 is essential for T cell maturation, selection, and function by maintaining proteostasis, and its absence impairs immune protection against helminths.

bioRxiv · Aug 11, 2020Immunology

The structural basis for forkhead box family specificity revealed by the crystal structure of human FOXN1 in complex with DNA

J. A. Newman, H. Aitkenhead, A. Gavard, I. A. Rota, A. E. Handel, G. A. Hollander, O. Gileadi

This paper presents the crystal structure of human FOXN1 bound to DNA, revealing structural basis for its specificity and reduced affinity for methylated DNA.

bioRxiv · Sep 26, 2018Biochemistry