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Biochemistry|November 19, 1985
Comparison of the kinetics and mechanism of the papain-catalyzed hydrolysis of esters and thiono estersA C Storer, P R CareyBiochemical and Biophysical Research Communications|December 28, 1983
Comparison of the substrate conformations in the active sites of papain, chymopapain, ficin and bromelain by resonance Raman spectroscopyP R Carey, Y Ozaki, A C StorerBiochemistry|September 27, 1983
Conformational states of N-acylglycine dithioesters in solution: resonance Raman studies of isotopically substituted models for enzyme-substrate complexesH Lee, A C Storer, P R CareyBiochemistry|September 27, 1983
Relaxed and perturbed substrate conformations in enzyme active sites: evidence from multichannel resonance raman spectraA C Storer, H Lee, P R CareyBiochemistry|January 12, 1988
Comparison of the kinetics of the papain-catalyzed hydrolysis of glycine- and alanine-based esters and thiono estersA C Storer, R H Angus, P R CareyThe Journal of Biological Chemistry|May 10, 1979
The use of resonance Raman spectroscopy to monitor catalytically important bonds during enzymic catalysis. Application to the hydrolysis of methyl thionohippurate by papainA C Storer, W F Murphy, P R CareyBiochemistry|June 9, 1981
Resonance Raman and electronic absorption spectral studies of some beta-(2-furyl)acryloylglyceraldehyde-3-phosphate dehydrogenasesA C Storer, D J Phelps, P R CareyThe Journal of Biological Chemistry|July 15, 1986
Benzoylamidoacetonitrile is bound as a thioimidate in the active site of papainJ R Brisson, P R Carey, A C StorerBiochemistry|June 3, 1986
Conformational activation of acylpapains and acylcathepsin B's: resonance Raman and kinetic evidenceR H Angus, P R Carey, H Lee, et al.Biochemistry|January 12, 1988
Conformational variability in an enzyme's active site: resonance Raman evidence for different acyl group conformations in N-acylglycine and N-acylalanine dithioacyl papainsR H Angus, H Lee, A C Storer, et al.Pageof 13