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The Journal of Biological Chemistry|August 22, 2001
Differential utilization of enzyme-substrate interactions for acylation but not deacylation during the catalytic cycle of Kex2 proteaseN C Rockwell, R S FullerBiochemistry|April 12, 2001
Direct measurement of acylenzyme hydrolysis demonstrates rate-limiting deacylation in cleavage of physiological sequences by the processing protease Kex2N C Rockwell, R S FullerBiochemistry|April 2, 1998
Interplay between S1 and S4 subsites in Kex2 protease: Kex2 exhibits dual specificity for the P4 side chainN C Rockwell, R S FullerAnalytical Biochemistry|May 3, 2000
Synthesis of peptidyl methylcoumarin esters as substrates and active-site titrants for the prohormone processing proteases Kex2 and PC2N C Rockwell, D J Krysan, R S FullerThe Journal of Biological Chemistry|August 7, 1999
Quantitative characterization of furin specificity. Energetics of substrate discrimination using an internally consistent set of hexapeptidyl methylcoumarinamidesD J Krysan, N C Rockwell, R S FullerBiochemistry|February 18, 1997
Internally consistent libraries of fluorogenic substrates demonstrate that Kex2 protease specificity is generated by multiple mechanismsN C Rockwell, G T Wang, G A Krafft, et al.Pageof 1