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Biochemical and Biophysical Research Communications|October 15, 1991
Chemical modification locates guanidinyl and carboxylate groups within the active site of prolidaseW L Mock, H ZhuangThe Biochemical Journal|August 15, 1994
Binding to thermolysin of phenolate-containing inhibitors necessitates a revised mechanism of catalysisW L Mock, M AksamawatiBiochemistry|November 15, 2000
Principles of hydroxamate inhibition of metalloproteases: carboxypeptidase AW L Mock, H ChengBiochemical and Biophysical Research Communications|March 27, 1999
Synergistic inhibition of carboxypeptidase A by zinc ion and imidazoleW L Mock, L WangBiochemistry|April 22, 1997
Kinetic characterization of the serralysins: a divergent catalytic mechanism pertaining to astacin-type metalloproteasesW L Mock, J YaoBioorganic & Medicinal Chemistry Letters|February 18, 1999
Catalytic activity of carboxypeptidase B and of carboxypeptidase Y with anisylazoformyl substratesW L Mock, D XuThe Journal of Biological Chemistry|August 4, 1995
Hydrolysis of picolinylprolines by prolidase. A general mechanism for the dual-metal ion containing aminopeptidasesW L Mock, Y LiuThe Journal of Biological Chemistry|April 5, 1991
Mechanistically significant diastereoselection in the sulfoximine inhibition of carboxypeptidase AW L Mock, J Z ZhangThe Journal of Biological Chemistry|June 25, 1988
pK values for active site residues of carboxypeptidase AW L Mock, J T TsayBiochemistry|June 11, 1996
Arazoformyl dipeptide substrates for thermolysin. Confirmation of a reverse protonation catalytic mechanismW L Mock, D J StanfordPageof 2