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Thomas E. Wales

Researcher at Northeastern University

Publications -  83
Citations -  4318

Thomas E. Wales is an academic researcher from Northeastern University. The author has contributed to research in topics: SH3 domain & Mass spectrometry. The author has an hindex of 28, co-authored 74 publications receiving 3318 citations. Previous affiliations of Thomas E. Wales include Duke University & University of New Mexico.

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Hydrogen exchange mass spectrometry for the analysis of protein dynamics.

TL;DR: The general principles of the hydrogen exchange coupled to mass spectrometry method are summarized, the latest variations on the experimental protocol that probe different types of protein movements are discussed, and other recent work and improvements in the field are reviewed.
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Recommendations for performing, interpreting and reporting hydrogen deuterium exchange mass spectrometry (HDX-MS) experiments.

TL;DR: Recommendations arising from community discussions emerging out of the first International Conference on Hydrogen-Exchange Mass Spectrometry (IC-HDX; 2017) are provided, meant to represent both a consensus viewpoint and an opportunity to stimulate further additions and refinements as the field advances.
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High-speed and high-resolution UPLC separation at zero degrees Celsius.

TL;DR: Construction and validation of a custom UPLC system for HXMS based on the Waters nanoACQUITY platform and contains a Peltier-cooled module that houses the injection and switching valves, online pepsin digestion column, and C-18 analytical separation column are presented.
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Identification and characterization of EX1 kinetics in H/D exchange mass spectrometry by peak width analysis.

TL;DR: A data interpretation method involving peak width analysis that makes characterization of EX1 kinetics simple and rapid is described and is robust, capable of automation, and provides quick interpretation of the key information contained in EX1 kinetic events.
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Substrate processing by the Cdc48 ATPase complex is initiated by ubiquitin unfolding

TL;DR: Cryo-EM structures of the Cdc48 ATPase in complex with Ufd1/Npl4 and poly-ubiquitinated substrate show that the CDC48 complex initiates substrate processing by unfolding a ubiquitin molecule.