Author

A. Itzen

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 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 2 Organism:human· 2 Assay:proteomics· 2 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Research Focus:differential expression· 1 Research Focus:protein folding & dynamics· 1 Approach:statistical model· 1

Frequent Co-Authors

S. Vieweg· 2 shared B. Braeuning· 1 shared C. Hedberg· 1 shared C. Pett· 1 shared D. Hoepfner· 1 shared D. Pourjafar-Dehkordi· 1 shared J. Fauser· 1 shared K. Mulholland· 1 shared

Activity by Year

2019-2020 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 17 mutual co-author links

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2 shared papersBiochemistry

S. Vieweg

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Monoclonal anti-AMP-antibodies reveal broad and diverse AMPylation patterns in cancer cells

D. Hoepfner, J. Fauser, M. S. Kaspers, C. Pett, C. Hedberg, A. Itzen

The paper develops three monoclonal anti-AMP antibodies that detect AMPylation in cancer cells, revealing diverse and broad modification patterns.

bioRxiv · Jun 23, 2020 · PreprintBiochemistry

PINK1-dependent phosphorylation of Serine111 within the SF3 motif of Rab GTPases impairs effector interactions and LRRK2 mediated phosphorylation at Threonine72

S. Vieweg, K. Mulholland, B. Braeuning, N. Kachariya, Y.-C. Lai, R. Toth, M. Sattler, M. Groll, A. Itzen, M. Muqit

This study shows that PINK1 phosphorylates Rab GTPases at Ser111, which inhibits LRRK2-mediated phosphorylation at Thr72, suggesting PINK1 activators could treat LRRK2-related Parkinson's.

bioRxiv · Sep 12, 2019Biochemistry

Phosphorylation of Ser111 in Rab8a modulates Rabin8 dependent activation by perturbation of side chain interaction networks

D. Pourjafar-Dehkordi, S. Vieweg, A. Itzen, M. Zacharias

This study shows that phosphorylation of Ser111 in Rab8a reduces its activation by Rabin8 through perturbation of side chain interactions.

bioRxiv · Jun 13, 2019Biophysics