Author

E. W. Debler

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· 2

Signature Assays, Organisms & Methods

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Approach:experimental assay· 3 Organism:human· 2 Research Focus:protein folding & dynamics· 2 Assay:structural biology· 2 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1 Assay:protein structure· 1 Research Focus:protein structure prediction· 1

Frequent Co-Authors

H. Cui· 2 shared H. Hashimoto· 2 shared S. R. Solmaz· 2 shared A. Raczkowski· 1 shared B. B. Russ· 1 shared B. PALANCADE· 1 shared C. R. Noell· 1 shared C. Wang· 1 shared

Activity by Year

2019-2022 · peak 2/yr

Co-Author Collaboration Network

10 top collaborators · 15 mutual co-author links

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2 shared papersBiophysics

H. Cui

Mutual co-authors in cluster

Author profile →

4 papers

Recent·Most cited

Structure of the pre-mRNA leakage 39-kDa proteinreveals a single domain of integrated zf-C3HC and Rsm1 modules

H. Hashimoto, D. H. Ramirez, O. Lautier, N. Pawlak, G. Blobel, B. PALANCADE, E. W. Debler

The paper determines the crystal structure of ScPml39, revealing integrated zf-C3HC and Rsm1 modules and identifies structural orthologs in S. pombe and humans.

bioRxiv · Aug 11, 2022Biochemistry

Coil-to-Helix Transition at the Nup358-BicD2 Interface Activates BicD2 for Dynein Recruitment

J. M. Gibson, H. Cui, M. Y. Ali, X. Zhao, E. W. Debler, J. Zhao, K. M. Trybus, S. R. Solmaz, C. Wang

The paper identifies a Nup358 helix that transitions to an α-helix upon BicD2 binding, facilitating dynein recruitment and processive motility.

bioRxiv · May 6, 2021Biophysics

Structural Basis of Protein Arginine Methyltransferase Activation by a Catalytically Dead Homolog (Prozyme)

H. Hashimoto, L. Kafkova, A. Raczkowski, K. D. Jordan, L. K. Read, E. W. Debler

This paper reports the crystal structure of a Trypanosoma brucei PRMT1 enzyme-prozyme heterotetramer, revealing how the prozyme stabilizes the enzyme and enables catalysis through structural and functional interactions.

bioRxiv · Sep 19, 2019Biochemistry

Role of coiled-coil registry shifts in activation of human Bicaudal D2 for dynein recruitment upon cargo-binding

C. R. Noell, J. Y. Loh, E. W. Debler, K. M. Loftus, H. Cui, B. B. Russ, P. Goyal, S. R. Solmaz

This paper investigates how coiled-coil registry shifts in BicD2 activate dynein recruitment upon cargo-binding, linking structural changes to disease mechanisms.

bioRxiv · May 15, 2019Biophysics