Author

S. Bhogaraju

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

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Research Focus:protein folding & dynamics· 3 Research Focus:cell signaling & trafficking· 2 Organism:human· 2 Research Focus:cell type annotation· 1 Research Focus:chromatin & epigenetic regulation· 1 Approach:deep learning· 1 Research Focus:development & morphogenesis· 1

Frequent Co-Authors

M. Adams· 2 shared S. Gharbi· 2 shared U. Mukhopadhyay· 2 shared C. Behrends· 1 shared F. Stein· 1 shared F. Weis· 1 shared I. Matic· 1 shared J. Hennig· 1 shared

Activity by Year

2021-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 23 mutual co-author links

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2 shared papersBiochemistry

M. Adams

Mutual co-authors in cluster

Author profile →

3 papers

Recent·Most cited

Structural Insights into The Role of MAGEA4 in RAD18 Regulation: Implications for Ubiquitin Ligase-Binding across the MAGE Protein Family

S. Griffith-Jones, L. Alvarez, U. Mukhopadhyay, S. Gharbi, M. Rettel, M. Adams, J. Hennig, S. Bhogaraju

This study identifies the interaction between MAGEA4 and RAD18 using NMR and AlphaFold2, revealing structural insights into how MAGEA4 regulates RAD18's ubiquitination activity and its implications for cancer.

bioRxiv · Dec 8, 2023 · PreprintBiochemistry

A ubiquitin-specific, proximity-based labeling approach for the identification of ubiquitin ligase substrates

U. Mukhopadhyay, S. Levantovsky, S. Gharbi, F. Stein, C. Behrends, S. Bhogaraju

The paper introduces a proximity-based labeling method to identify ubiquitin ligase substrates and validates it using RAD18, TRAF6, and CHIP.

bioRxiv · Sep 4, 2023 · PreprintBiochemistry

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