Author

D. L. Bolhuis

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 Cell Biology· 1

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:human· 3 Research Focus:protein structure prediction· 2 Assay:proteomics· 2 Organism:Arabidopsis· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1 Assay:cryo-EM· 1

Frequent Co-Authors

N. G. Brown· 3 shared D. Haselbach· 2 shared A. Schleiffer· 1 shared B. A. Schulman· 1 shared C. A. Mills· 1 shared C. Hsu· 1 shared C. R. R. Grace· 1 shared D. J. Miller· 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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3 shared papersBiochemistry

N. G. Brown

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Proteomic Analysis Reveals a PLK1-Dependent G2/M Degradation Program and Links PKA-AKAP2 to Cell Cycle Control

R. D. Mouery, C. Hsu, T. Bonacci, D. L. Bolhuis, X. Wang, C. A. Mills, E. D. Toomer, O. G. Canterbury, K. C. Robertson, T. B. Branigan, N. G. Brown, L. E. Herring, M. Emanuele

The paper uses proteomics and PLK1 inhibition to identify proteins degraded at G2/M, showing PLK1's role in coordinating proteolysis via SCF ligases and linking AKAP2 to cell cycle control.

bioRxiv · Oct 11, 2023 · PreprintCell Biology

Crystal structure of the Arabidopsis SPIRAL2 C-terminal domain reveals a p80-Katanin-like domain

D. L. Bolhuis, R. Dixit, K. C. Slep

The paper determines the crystal structure of the Arabidopsis SPIRAL2 C-terminal domain, revealing a p80-Katanin-like fold and highlighting evolutionary convergence with katanin complexes.

bioRxiv · Dec 28, 2022 · PreprintBiophysics

Cryo-EM structure of the chain-elongating E3 ligase UBR5

Z. Hodakova, I. Grishkovskaya, H. L. Brunner, D. L. Bolhuis, K. Belacic, A. Schleiffer, H. Kotisch, N. G. Brown, D. Haselbach

The paper presents the cryo-EM structure of UBR5, revealing its dimeric architecture and dynamic domain movements, and identifies AKIRIN2 as an interacting protein.

bioRxiv · Nov 3, 2022 · PreprintBiochemistry

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