Author

K.-P. Knobeloch

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· 3 Immunology· 2 Biochemistry· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 6 Organism:human· 4 Assay:proteomics· 4 Research Focus:host-pathogen & immune response· 3 Organism:mouse· 3 Research Focus:cell type annotation· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:chromatin & epigenetic regulation· 1

Frequent Co-Authors

A. Beling· 2 shared A. Borg· 1 shared A. Dufner· 1 shared A. G. van der Veen· 1 shared A. Napolitano· 1 shared A. Pinto-Fernandez· 1 shared A. Sapmaz· 1 shared B. Dermaut· 1 shared

Activity by Year

2017-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 12 mutual co-author links

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2 shared papersCell Biology

A. Beling

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Author profile →

6 papers

Recent·Most cited

Rapid turnover of CTLA4 is associated with a complex architecture of reversible ubiquitylation.

P. Y. Tey, A. Dufner, K.-P. Knobeloch, J. N. Pruneda, M. J. Clague, S. Urbe

The paper investigates CTLA4 turnover, showing ubiquitylation at K203 and K213 drives lysosomal degradation, with USP8 and HD-PTP modulating this process through distinct mechanisms.

bioRxiv · Dec 31, 2023Cell Biology

USP16 is an ISG15 cross-reactive deubiquitinase targeting a subset of metabolic pathway-related proteins

J. Gan, A. Pinto-Fernandez, D. Flierman, J. J. L. L. Akkermans, D. P. O'Brien, H. Greenwood, H. C. Scott, J. Neefjes, G. Fritz, K.-P. Knobeloch, H. van Dam, B. M. Kessler, H. Ovaa, P. P. Geurink, A. Sapmaz

This study identifies USP16 as an ISG15 cross-reactive deubiquitinase that regulates metabolic pathway-related proteins during type I interferon responses.

bioRxiv · Jun 26, 2023 · PreprintBiochemistry

Ring Finger Protein 213 Assembles into a Sensor for ISGylated Proteins with Antimicrobial Activity

F. Thery, L. Martina, C. Asselman, H. Repo, Y. Zhang, K. Sedeyn, G. D. Moschonas, C. Bredow, Q. W. Teo, J. Zhang, M. Vessely, K. Leandro, D. Eggermont, D. De Sutter, K. Boucher, , F. Impens

This study identifies RNF213 as an ISG15-interacting sensor that detects ISGylated proteins and exhibits broad antimicrobial activity against multiple pathogens.

bioRxiv · Jun 3, 2021Cell Biology

SCFFbxw5 targets MCAK in G2/M to facilitate ciliogenesis in the following cell cycle

J. Schweiggert, G. Habeck, S. Hess, F. Mikes, K. Meese, S. Hata, K.-P. Knobeloch, F. Melchior

The paper identifies SCFFbxw5 as a regulator of MCAK levels during G2/M, showing that its loss impairs ciliogenesis in the subsequent G1 phase.

bioRxiv · Jan 15, 2021 · PreprintCell Biology

ISG15 drives immune pathology and respiratory failure during viral infection

N. Shaabani, J. Zak, J. L. Johnson, Z. Huang, N. Nguyen, D. C. Lazar, V. F. Vartabedian, N. Honke, M. Prinz, K.-P. Knobeloch, K.-i. Arimoto, D.-E. Zhang, S. D. Catz, J. R. Teijaro

This study shows that lack of deISGylation during viral infection leads to immune pathology and respiratory failure, with extracellular ISG15 playing a key role in inflammation and disease severity.

bioRxiv · Apr 13, 2020 · PreprintImmunology

Free ISG15 as a dimer generates IL-1β-producing CD8α+ dendritic cells at the site of infection

A. Napolitano, A. G. van der Veen, M. Bunyan, A. Borg, S. Kjaer, A. Beling, K.-P. Knobeloch, E. Frickel

The paper shows free ISG15 dimers enhance IL-1β production by CD8+ dendritic cells during Toxoplasma infection, linking ISG15 to cytokine responses.

bioRxiv · Feb 27, 2017Immunology