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Nature|October 15, 2010
The proteasome antechamber maintains substrates in an unfolded stateAmy M Ruschak, Tomasz L Religa, Sarah Breuer, et al.
Proceedings of the National Academy of Sciences of the United States of America|March 23, 2011
Malleability of folding intermediates in the homeodomain superfamilyWiktor Banachewicz, Tomasz L Religa, R D Schaeffer, et al.
The Journal of Physical Chemistry. B|December 14, 2011
Cross-validation of the structure of a transiently formed and low populated FF domain folding intermediate determined by relaxation dispersion NMR and CS-RosettaJulia Barette, Algirdas Velyvis, Tomasz L Religa, et al.
Journal of Biomolecular NMR|April 28, 2007
A single-quantum methyl 13C-relaxation dispersion experiment with improved sensitivityPatrik Lundström, Pramodh Vallurupalli, Tomasz L Religa, et al.
Science (New York, N.Y.)|September 11, 2010
A transient and low-populated protein-folding intermediate at atomic resolutionDmitry M Korzhnev, Tomasz L Religa, Wiktor Banachewicz, et al.
Journal of the American Chemical Society|August 12, 2010
13CHD2 methyl group probes of millisecond time scale exchange in proteins by 1H relaxation dispersion: an application to proteasome gating residue dynamicsAndrew J Baldwin, Tomasz L Religa, D Flemming Hansen, et al.
Structure (London, England : 1993)|September 3, 2004
Determinants of functionality in the ubiquitin conjugating enzyme familyPeter J Winn, Tomasz L Religa, James N D Battey, et al.
Proceedings of the National Academy of Sciences of the United States of America|May 23, 2007
The helix-turn-helix motif as an ultrafast independently folding domain: the pathway of folding of Engrailed homeodomainTomasz L Religa, Christopher M Johnson, Dung M Vu, et al.
Journal of the American Chemical Society|June 7, 2011
Nonnative interactions in the FF domain folding pathway from an atomic resolution structure of a sparsely populated intermediate: an NMR relaxation dispersion studyDmitry M Korzhnev, Robert M Vernon, Tomasz L Religa, et al.
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