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Molecular and Cellular Biochemistry|August 11, 1981
gamma-Glutamylamine cyclotransferase. An enzyme involved in the catabolism of epsilon-(gamma-glutamyl)lysine and other gamma-glutamylaminesM L Fink, J E FolkProceedings of the National Academy of Sciences of the United States of America|August 1, 1980
gamma-Glutamylamine cyclotransferase: specificity toward epsilon-(L-gamma-glutamyl)-L-lysine and related compoundsM L Fink, S I Chung, J E FolkThe Journal of Biological Chemistry|July 25, 1978
Transglutaminase-catalyzed cross-linking through diamines and polyaminesJ Schrode, J E FolkThe Journal of Biological Chemistry|October 25, 1980
Half-of-the-sites and all-of-the-sites reactivity in human plasma blood coagulation factor XIIIaG F Seelig, J E FolkBioorganic & Medicinal Chemistry|May 6, 1998
Branched-chain and unsaturated 1,7-diaminoheptane derivatives as deoxyhypusine synthase inhibitorsY B Lee, J E FolkThe Journal of Biological Chemistry|October 25, 1986
Biosynthetic labeling of hypusine in mammalian cells. Carbon-hydrogen bond fissions revealed by dual labelingM H Park, J E FolkThe Journal of Biological Chemistry|March 25, 1981
Structural features of glutamine substrates for transglutaminases. Specificities of human plasma factor XIIIa and the guinea pig liver enzyme toward synthetic peptidesJ J Gorman, J E FolkThe Journal of Biological Chemistry|September 25, 1980
Noncatalytic subunits of human blood plasma coagulation factor XIII. Preparation and partial characterization of modified formsG F Seelig, J E FolkThe Journal of Biological Chemistry|February 10, 1980
Transglutaminase amine substrates for photochemical labeling and cleavable cross-linking of proteinsJ J Gorman, J E FolkThe Journal of Biological Chemistry|January 25, 1980
Structural features of glutamine substrates for human plasma factor XIIIa (activated blood coagulation factor XIII)J J Gorman, J E FolkPageof 7