Author

D. Eletto

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· 1 Cancer Biology· 1 Immunology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:cancer & tumor microenvironment· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:drug response / drug discovery· 1 Research Focus:gene regulatory network inference· 1 Approach:genetic perturbation / CRISPR· 1 Research Focus:host-pathogen & immune response· 1 Organism:human· 1

Frequent Co-Authors

A. E. Moor· 1 shared A. Lafzi· 1 shared A. W. Paton· 1 shared B. G. Hale· 1 shared C. Borrelli· 1 shared C.-C. A. Hu· 1 shared C.-H. A. Tang· 1 shared D. Blumenthal· 1 shared

Activity by Year

2020-2023 · peak 1/yr

Co-Author Collaboration Network

10 top collaborators · 16 mutual co-author links

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1 shared paperCancer Biology

A. E. Moor

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

In vivo screening of tumor-hepatocyte interactions identifies Plexin B2 as a gatekeeper of liver metastasis

C. Borrelli, M. Roberts, D. Eletto, A. Lafzi, J. A. Kretz, H. Fazilaty, M.-D. Hussherr, E. Guido Vinzoni, K. Handler, J. Michler, S. Adivarahan, S. Piscuoglio, X. Ficht, A. E. Moor

The paper identifies Plexin B2 in hepatocytes as a critical regulator of liver metastasis by promoting epithelial traits in tumor cells through Rac1 signaling.

bioRxiv · May 15, 2023 · PreprintCancer Biology

Genome-Wide CRISPR Screening Identifies BRD9 as a Druggable Component of Interferon-Stimulated Gene Expression and Antiviral Activity

J. Börold, D. Eletto, I. Busnadiego, N. K. Mair, E. Moritz, S. Schiefer, N. Schmidt, P. P. Petric, W. W.-L. Wong, M. Schwemmle, B. G. Hale

This study identifies BRD9 as a critical component of IFN signaling and antiviral activity through CRISPR screening, showing its druggability for targeting constitutive ISG expression.

bioRxiv · Feb 4, 2021Immunology

The interdomain helix between the kinase and RNase domains of IRE1α transmits the conformational change that underlies ER stress-induced activation.

D. Ricci, S. Tutton, I. Marrocco, M. Ying, D. Blumenthal, D. Eletto, J. Vargas, S. Boyle, H. Fazelinia, J. C. Paton, A. W. Paton, C.-H. A. Tang, C.-C. A. Hu, T. Gidalevitz, Y. Argon

This study identifies the interdomain helix between IRE1α kinase and RNase domains as critical for transmitting conformational changes during ER stress, revealing its role in regulating oligomerization, RNase activity, and kinase function.

bioRxiv · Jan 14, 2020 · PreprintBiochemistry