Author

J. R. Prabu

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· 5 Biophysics· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 6 Research Focus:protein folding & dynamics· 5 Research Focus:cell signaling & trafficking· 4 Research Focus:chromatin & epigenetic regulation· 4 Organism:human· 4 Assay:proteomics· 3 Organism:yeast· 3 Assay:cryo-EM· 2

Frequent Co-Authors

B. A. Schulman· 5 shared R. Vollrath· 3 shared D. Sherpa· 2 shared J. Chrustowicz· 2 shared L. A. Hehl· 2 shared S. S. Sidhu· 2 shared S. von Gronau· 2 shared A. F. Alpi· 1 shared

Activity by Year

2019-2023 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 23 mutual co-author links

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5 shared papersBiochemistry

B. A. Schulman

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Author profile →

6 papers

Recent·Most cited

Structural snapshots along K48-linked ubiquitin chain formation by the HECT E3 UBR5

L. A. Hehl, D. Horn-Ghetko, J. R. Prabu, R. Vollrath, D. T. Vu, D. A. Perez Berrocal, M. P. C. Mulder, G. J. van der Heden van Noort, B. A. Schulman

This study uses cryo-EM to reveal the structural mechanism of K48-linked ubiquitin chain formation by the HECT E3 ligase UBR5, showing how it orchestrates ubiquitin transfer through conformational changes.

bioRxiv · Jun 6, 2023Biochemistry

Insights into the ISG15 transfer cascade by the UBE1L activating enzyme

I. Wallace, K. Baek, J. R. Prabu, R. Vollrath, S. von Gronau, B. A. Schulman, K. N. Swatek

This study presents a cryo-EM structure of the UBE1L-UBE2L6 complex bound to ISG15, revealing mechanisms of ISG15 recognition and conjugation pathway specificity.

bioRxiv · Apr 6, 2023Biochemistry

Multifaceted N-degron recognition and ubiquitylation by GID/CTLH E3 ligases

J. Chrustowicz, D. Sherpa, J. Teyra, M. S. Loke, G. Popowicz, J. Basquin, M. Sattler, J. R. Prabu, S. S. Sidhu, B. A. Schulman

The paper identifies novel N-terminal motifs recognized by Gid4 and Gid10 E3 ligases and shows how structural flexibility and substrate context influence ubiquitylation efficiency.

bioRxiv · Sep 3, 2021Biochemistry

GID E3 ligase supramolecular chelate assembly configures multipronged ubiquitin targeting of an oligomeric metabolic enzyme

D. Sherpa, J. Chrustowicz, S. Qiao, C. R. Langlois, L. A. Hehl, K. V. Gottemukkala, F. M. Hansen, O. Karayel, S. von Gronau, J. R. Prabu, M. Mann, A. F. Alpi, B. A. Schulman

The paper reveals a supramolecular chelate assembly mechanism by which E3 ligases target oligomeric substrates, demonstrating this in yeast and human orthologs.

bioRxiv · Apr 7, 2021Biochemistry

Structural and mechanistic basis of the EMC-dependent biogenesis of distinct transmembrane clients

L. E. Miller-Vedam, B. Bräuning, K. D. Popova, N. T. Schirle Oakdale, J. L. Bonnar, J. R. Prabu, E. A. Boydston, N. Sevillano, M. J. Shurtleff, R. M. Stroud, C. S. Craik, B. Schulman, A. Frost, J. S. Weissman

The paper reveals the structural and mechanistic basis of EMC's role in biogenesis of distinct transmembrane proteins through cryo-EM structures and functional studies.

bioRxiv · Sep 2, 2020Biophysics

A Protein Engineering Approach for Uncovering Cryptic Ubiquitin-binding Sites: from a Ubiquitin-Variant Inhibitor of APC/C to K48 Chain Binding

E. R. Watson, C. R. R. Grace, W. Zhang, D. J. Miller, I. F. Davidson, J. R. Prabu, S. Yu, D. L. Bolhuis, E. T. Kulko, R. Vollrath, D. Haselbach, H. Stark, J.-M. Peters, N. G. Brown, S. S. Sidhu, B. A. Schulman

The paper identifies a cryptic ubiquitin-binding site on APC/C using ubiquitin variants, revealing its preference for K48-linked chains and demonstrating a method for uncovering such sites in large complexes.

bioRxiv · Jun 12, 2019 · PreprintBiochemistry