Author

T. Colby

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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Cell Biology· 2 Biochemistry· 1 Plant Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 4 Research Focus:host-pathogen & immune response· 2 Assay:proteomics· 2 Organism:Arabidopsis· 1 Research Focus:cell type annotation· 1 Research Focus:differential expression· 1 Organism:human· 1 Organism:plant (other)· 1

Frequent Co-Authors

I. Matic· 4 shared I. Dikic· 2 shared R. Mukherjee· 2 shared A. Bhattacharya· 1 shared A. Gonzalez· 1 shared C. Proksch· 1 shared D. Shin· 1 shared D. Thieme· 1 shared

Activity by Year

2020-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 22 mutual co-author links

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4 shared papersCell Biology

I. Matic

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Untargeted proteomics identifies plant substrates of the bacterial-derived ADP-ribosyltransferase AvrRpm1

S. Kaur, T. Colby, D. Thieme, C. Proksch, S. Matschi, I. Matic, L. Wirthmueller

The paper identifies plant substrates of the bacterial ADP-ribosyltransferase AvrRpm1 using untargeted proteomics, revealing ADP-ribosylation sites on RIN4 in legumes and Arabidopsis.

bioRxiv · Sep 25, 2023Plant Biology

Serine ubiquitination of p62 regulates Nrf2 dependent redox homeostasis

R. Mukherjee, M. Hoffmann, A. Gonzalez, A. Bhattacharya, S. K. Kuncha, R. Rathore, D. Shin, T. Colby, I. Matic, M. Misra, I. Dikic

This study shows that serine ubiquitination of p62 by Legionella pneumophila SidE effectors inhibits Nrf2 signaling, altering redox homeostasis and host metabolism during infection.

bioRxiv · Jun 17, 2023 · PreprintCell Biology

Structural basis for protein glutamylation by the Legionella pseudokinase SidJ

M. Adams, R. Sharma, T. Colby, F. Weis, I. Matic, S. Bhogaraju

This study determines the cryo-EM structure of SidJ in complex with SdeA, revealing its mechanism of glutamylation and substrate recognition.

bioRxiv · Jul 16, 2021Biochemistry

Serine-ubiquitination regulates Golgi morphology and the secretory pathway upon Legionella infection

Y. Liu, R. Mukherjee, F. Bonn, T. Colby, I. Matic, M. Glogger, M. Heilemann, I. Dikic

This study shows that Legionella's SdeA effector causes Golgi disruption via serine ubiquitination of GRASP55 and GRASP65, affecting the secretory pathway and cytokine release.

bioRxiv · Jul 27, 2020Cell Biology