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Current Opinion in Structural Biology|November 30, 2019
Understanding the 26S proteasome molecular machine from a structural and conformational dynamics perspectiveEric R Greene, Ken C Dong, Andreas Martin
Annual Review of Biochemistry|April 14, 2018
Structure and Function of the 26S ProteasomeJared A M Bard, Ellen A Goodall, Eric R Greene, et al.
Molecular Cell|August 29, 2017
An AAA Motor-Driven Mechanical Switch in Rpn11 Controls Deubiquitination at the 26S ProteasomeEvan J Worden, Ken C Dong, Andreas Martin
Cell Reports|May 24, 2025
The deubiquitinase Rpn11 functions as an allosteric ubiquitin sensor to promote substrate engagement by the 26S proteasomeZaw Min Htet, Ken C Dong, Andreas Martin
Biorxiv : the Preprint Server for Biology|November 1, 2024
The deubiquitinase Rpn11 functions as an allosteric ubiquitin sensor to promote substrate engagement by the 26S proteasomeZaw Min Htet, Ken C Dong, Andreas Martin
Nature Chemical Biology|June 3, 2020
Site-specific ubiquitination affects protein energetics and proteasomal degradationEmma C Carroll, Eric R Greene, Andreas Martin, et al.
STAR Protocols|October 27, 2023
Preparation of site-specifically fluorophore-labeled polyubiquitin chains for FRET studies of Cdc48 substrate processingCameron Williams, Ken C Dong, Connor Arkinson, et al.
Molecular Cell|February 3, 2023
The Ufd1 cofactor determines the linkage specificity of polyubiquitin chain engagement by the AAA+ ATPase Cdc48Cameron Williams, Ken C Dong, Connor Arkinson, et al.
Methods in Molecular Biology (Clifton, N.J.)|November 9, 2022
High-Throughput Assay for Characterizing Rpn11 Deubiquitinase ActivityGang Xie, Ken C Dong, Evan J Worden, et al.
Biorxiv : the Preprint Server for Biology|December 25, 2025
Identification of novel ubiquitin receptors on the 26S proteasome by photo-crosslinking mass spectrometryNicole S MacRae, Ken C Dong, Hiromitsu Harimoto, et al.
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