Author

T. Ilani

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· 1

Signature Assays, Organisms & Methods

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

Frequent Co-Authors

D. Fass· 2 shared G. Javitt· 2 shared N. Reznik· 2 shared A. D. Gallo· 1 shared A. M. Jaramillo· 1 shared A. S. Wentink· 1 shared B. Bukau· 1 shared C. M. Evans· 1 shared

Activity by Year

2022-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 20 mutual co-author links

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2 shared papersCell Biology

D. Fass

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

A unique chaperoning mechanism in Class A JDPs recognizes and stabilizes mutant p53.

G. Zoltsman, T. L. Dang, M. Kuchersky, O. Faust, M. S. Silva, T. Ilani, A. S. Wentink, B. Bukau, R. Rosenzweig

This study identifies a unique chaperoning mechanism in class-A JDPs that recognizes and stabilizes mutant p53, promoting cancer progression by preventing its degradation.

bioRxiv · Nov 28, 2023Biochemistry

The Colon Mucosal Sialylglycome Is Redox-Regulated by the Golgi Enzyme QSOX1

T. Ilani, N. Reznik, N. Yeshaya, T. Feldman, P. Vilela, Z. Lansky, G. Javitt, M. Shemesh, O. Brenner, Y. Elkis, N. Varsano, N. Murray, P. Azadi, A. M. Jaramillo, C. M. Evans, D. Fass

This study shows that QSOX1 regulates sialylation of the colon glycome by forming disulfides in Golgi glycosyltransferases, not by catalyzing mucin crosslinking.

bioRxiv · May 3, 2022 · PreprintCell Biology

Intestinal Mucin Is a Chaperone of Multivalent Copper

N. Reznik, A. D. Gallo, K. W. Rush, G. Javitt, Y. Fridmann-Sirkis, T. Ilani, N. A. Nairner, K. Chacon, K. J. Franz, D. Fass

The paper identifies intestinal mucin MUC2 as a copper chaperone that binds and protects against copper toxicity while enabling copper uptake.

bioRxiv · Jan 2, 2022Biochemistry