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Nature|October 31, 1998
Unfolded conformations of alpha-lytic protease are more stable than its native stateJ L Sohl, S S Jaswal, D A AgardStructure (London, England : 1993)|October 15, 1994
Influenza hemagglutinin: kinetic control of protein functionD Baker, D A AgardProceedings of the National Academy of Sciences of the United States of America|September 29, 1999
Kinetic stability as a mechanism for protease longevityE L Cunningham, S S Jaswal, J L Sohl, et al.Biochemistry|April 1, 1997
Inhibition of alpha-lytic protease by pro region C-terminal steric occlusion of the active siteJ L Sohl, A K Shiau, S D Rader, et al.Current Opinion in Cell Biology|December 1, 1993
The role of pro regions in protein foldingD Baker, A K Shiau, D A AgardActa Crystallographica. Section D, Biological Crystallography|January 1, 1993
Uniqueness and the ab initio phase problem in macromolecular crystallographyD Baker, A E Krukowski, D A AgardProteins|April 1, 1992
Protease pro region required for folding is a potent inhibitor of the mature enzymeD Baker, J L Silen, D A AgardActa Crystallographica. Section D, Biological Crystallography|September 1, 1993
PRISM: application to the solution of two protein structuresC Bystroff, D Baker, R J Fletterick, et al.Pageof 187