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The Journal of Biological Chemistry|June 19, 2001
Comparison of the Pseudomonas aeruginosa and Escherichia coli PhoQ sensor domains: evidence for distinct mechanisms of signal detectionJ A Lesley, C D WaldburgerBiochemistry|October 10, 1995
Domains of Mnt repressor: roles in tetramer formation, protein stability, and operator DNA bindingC D Waldburger, R T SauerThe Journal of Biological Chemistry|October 25, 1996
Signal detection by the PhoQ sensor-transmitter. Characterization of the sensor domain and a response-impaired mutant that identifies ligand-binding determinantsC D Waldburger, R T SauerProceedings of the National Academy of Sciences of the United States of America|April 2, 1996
Barriers to protein folding: formation of buried polar interactions is a slow step in acquisition of structureC D Waldburger, T Jonsson, R T SauerBiochemistry|April 16, 1996
Nonlinear free energy relationships in Arc repressor unfolding imply the existence of unstable, native-like folding intermediatesT Jonsson, C D Waldburger, R T SauerNature Structural Biology|February 1, 1995
Are buried salt bridges important for protein stability and conformational specificity?C D Waldburger, J F Schildbach, R T SauerThe Journal of Biological Chemistry|August 9, 2001
Structural and mutational analysis of the PhoQ histidine kinase catalytic domain. Insight into the reaction mechanismA Marina, C Mott, A Auyzenberg, et al.Biochemistry|October 24, 1995
P22 Arc repressor: transition state properties inferred from mutational effects on the rates of protein unfolding and refoldingM E Milla, B M Brown, C D Waldburger, et al.FASEB Journal : Official Publication of the Federation of American Societies for Experimental Biology|January 1, 1996
Sequence determinants of folding and stability for the P22 Arc repressor dimerR T Sauer, M E Milla, C D Waldburger, et al.Pageof 1