Author

L. Deszcz

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· 3 Cell Biology· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 5 Research Focus:cell signaling & trafficking· 3 Research Focus:host-pathogen & immune response· 2 Organism:mouse· 2 Assay:proteomics· 2 Approach:biophysical modeling· 1 Research Focus:cancer & tumor microenvironment· 1 Assay:cryo-EM· 1

Frequent Co-Authors

F. Ikeda· 3 shared T. Clausen· 3 shared A. Kavirayani· 2 shared D. B. Grabarczyk· 2 shared K. Mechtler· 2 shared K. Schodl· 2 shared L. M. Fennell· 2 shared A. Bestehorn· 1 shared

Activity by Year

2019-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 25 mutual co-author links

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3 shared papersCell Biology

F. Ikeda

Mutual co-authors in cluster

Author profile →

5 papers

Recent·Most cited

Structural basis of how the BIRC6/SMAC complex regulates apoptosis and autophagy

J. F. Ehrmann, D. B. Grabarczyk, M. Heinke, L. Deszcz, R. Kurzbauer, O. Hudecz, A. Shulkina, R. Gogova, A. Meinhart, G. A. Versteeg, T. Clausen

The paper determines the cryo-EM structure of BIRC6 and its complex with HTRA2 and SMAC, revealing how SMAC inhibits BIRC6 to regulate apoptosis and autophagy.

bioRxiv · Aug 30, 2022 · PreprintBiochemistry

E3 ubiquitin ligase RNF213 employs a non-canonical zinc finger active site and is allosterically regulated by ATP

J. Ahel, A. J. Fletcher, D. B. Grabarczyk, E. Roitinger, L. Deszcz, A. Lehner, S. Virdee, T. Clausen

This study identifies a non-canonical zinc finger active site in RNF213 and shows its E3 activity depends on ATP binding and adenine nucleotide ratios.

bioRxiv · May 10, 2021Biochemistry

The ubiquitin ligase HOIL-1L regulates immune responses by interacting with linear ubiquitin chains

C. Gomez Diaz, G. Jonsson, K. Schodl, L. Deszcz, A. Bestehorn, K. Eislmayr, J. Almagro, A. Kavirayani, L. M. Fennell, A. Hagelkrueys, P. Kovarik, J. M. Penninger, F. Ikeda

This study shows that the HOIL-1L NZF domain regulates immune responses by binding linear ubiquitin chains, affecting TNF and LPS-induced inflammation in mice.

bioRxiv · Apr 13, 2021Cell Biology

The linear ubiquitin chain assembly complex generates heterotypic ubiquitin chains

A. R. Carvajal, C. G. Diaz, A. Vogel, A. Sonn-Segev, K. Schodl, L. Deszcz, Z. Orban-Nemeth, S. Sakamoto, K. Mechtler, P. Kukura, T. Clausen, D. Haselbach, F. Ikeda

This study shows LUBAC generates heterotypic ubiquitin chains with linear and oxyester-linked branches through coordinated action of HOIP and HOIL-1L.

bioRxiv · May 27, 2020Biochemistry

Site-specific ubiquitination of the E3 ligase HOIP regulates cell death and immune signaling

L. M. Fennell, L. Deszcz, A. Schleiffer, K. Mechtler, A. Kavirayani, F. Ikeda

This study identifies that site-specific ubiquitination of HOIP at K784 regulates TNF-induced inflammatory signaling and cell fate by modulating TNFR complex formation and LUBAC activity.

bioRxiv · Aug 21, 2019Cell Biology