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Proceedings of the National Academy of Sciences of the United States of America|September 15, 1993
Enzyme crystal structure in a neat organic solventP A Fitzpatrick, A C Steinmetz, D Ringe, et al.Biochemical and Biophysical Research Communications|January 28, 1994
X-ray crystal structure of cross-linked subtilisin Carlsberg in water vs. acetonitrileP A Fitzpatrick, D Ringe, A M KlibanovBiotechnology and Bioengineering|September 1, 1992
Computer-assisted modeling of subtilisin enantioselectivity in organic solventsP A Fitzpatrick, D Ringe, A M KlibanovBiochemistry|August 30, 1994
Inactivation of subtilisin Carlsberg by N-((tert-butoxycarbonyl)alanylprolylphenylalanyl)-O-benzoylhydroxyl- amine: formation of a covalent enzyme-inhibitor linkage in the form of a carbamate derivativeA C Steinmetz, H U Demuth, D RingeBiochemistry|June 13, 1995
Nature of the inactivation of elastase by N-peptidyl-O-aroyl hydroxylamine as a function of pHX Ding, B F Rasmussen, H U Demuth, et al.Biochemistry|November 22, 1994
Three-dimensional structure of chymotrypsin inactivated with (2S)-N-acetyl-L-alanyl-L-phenylalanyl alpha-chloroethane: implications for the mechanism of inactivation of serine proteases by chloroketonesK Kreutter, A C Steinmetz, T C Liang, et al.Trends in Biotechnology|March 1, 1997
Why are enzymes less active in organic solvents than in water?A M KlibanovScience (New York, N.Y.)|February 11, 1983
Immobilized enzymes and cells as practical catalystsA M KlibanovTrends in Biochemical Sciences|April 1, 1989
Enzymatic catalysis in anhydrous organic solventsA M KlibanovPageof 37