Area of research
Molecular Biology · Cell Biology
Research interest
Research interests include Ubiquitin and proteasome pathways, Endoplasmic Reticulum Stress and Disease, Autophagy in Disease and Therapy, and RNA and protein synthesis mechanisms.
NUB1 traps unfolded FAT10 for ubiquitin-independent degradation by the 26S proteasome
The deubiquitinase Rpn11 functions as an allosteric ubiquitin sensor to promote substrate engagement by the 26S proteasome
2024 VCP International Conference: Exploring multi-disciplinary approaches from basic science of valosin containing protein, an AAA+ ATPase protein, to the therapeutic advancement for VCP-associated multisystem proteinopathy
Structural landscape of the degrading 26S proteasome reveals conformation-specific binding of TXNL1
Mechanisms and regulation of substrate degradation by the 26S proteasome
The Ufd1 cofactor determines the linkage specificity of polyubiquitin chain engagement by the AAA+ ATPase Cdc48
The N1 domain of the peroxisomal AAA-ATPase Pex6 is required for Pex15 binding and proper assembly with Pex1
Preparation of site-specifically fluorophore-labeled polyubiquitin chains for FRET studies of Cdc48 substrate processing
Ubiquitin modulates 26 <i>S</i> proteasome conformational dynamics and promotes substrate degradation
High-Throughput Assay for Characterizing Rpn11 Deubiquitinase Activity
A pentameric protein ring with novel architecture is required for herpesviral packaging
Proteasome interaction with ubiquitinated substrates: from mechanisms to therapies
Site-specific ubiquitination affects protein energetics and proteasomal degradation
The AAA+ ATPase Msp1 is a processive protein translocase with robust unfoldase activity
The 26S Proteasome Utilizes a Kinetic Gateway to Prioritize Substrate Degradation
Stairway to translocation: AAA+ motor structures reveal the mechanisms of ATP‐dependent substrate translocation
The Cdc48 unfoldase prepares well-folded protein substrates for degradation by the 26S proteasome
Multisystem Proteinopathy Mutations in VCP/p97 Increase NPLOC4·UFD1L Binding and Substrate Processing
Understanding the 26S proteasome molecular machine from a structural and conformational dynamics perspective
Specific lid-base contacts in the 26s proteasome control the conformational switching required for substrate degradation
Structure and Function of the 26S Proteasome
Substrate-engaged 26 <i>S</i> proteasome structures reveal mechanisms for ATP-hydrolysis–driven translocation
Mechanism for the Regulated Control of Bacterial Transcription Termination by a Universal Adaptor Protein
The peroxisomal AAA-ATPase Pex1/Pex6 unfolds substrates by processive threading
Recombinant Expression, Unnatural Amino Acid Incorporation, and Site-Specific Labeling of 26S Proteasomal Subcomplexes
An AAA Motor-Driven Mechanical Switch in Rpn11 Controls Deubiquitination at the 26S Proteasome
Knots can impair protein degradation by ATP-dependent proteases
Atomic structure of the 26S proteasome lid reveals the mechanism of deubiquitinase inhibition
Substrate-translocating loops regulate mechanochemical coupling and power production in AAA+ protease ClpXP
The ClpXP Protease Unfolds Substrates Using a Constant Rate of Pulling but Different Gears