RETENTION OF AMYLASE IN THE SECRETORY GRANULES OF PAROTID GLAND AFTER EXTENSIVE RELEASE OF CA⁺⁺ BY IONOPHORE A-23187.FLASHNER Y; SCHRAMM M.1977; J. CELL BIOL.; U.S.A.; DA. 1977; VOL. 74; NO 3; PP. 789-793; BIBL. 17 REF.Article

NEW ANTIBIOTIC SUBSTANCE PRODUCED BY SALMONELLA TYPHIMURIUM LT2 = NOUVELLE SUBSTANCE ANTIBIOTIQUE PRODUITE PAR SALMONELLA TYPHIMURIUM LT2BEN GURION R; FLASHNER Y.1982; J. BACTERIOL.; ISSN 0021-9193; USA; DA. 1982; VOL. 152; NO 1; PP. 542-544; BIBL. 17 REF.Article

COL E1 DNA SEQUENCES INTERACTING IN CIS, ESSENTIAL FOR MITOMYCIN-C INDUCED LETHALITYSHAFFERMAN A; FLASHNER Y; COHEN S et al.1979; MOLEC. GEN. GENT.; DEU; DA. 1979; VOL. 176; NO 1; PP. 139-146; BIBL. 35 REF.Article

A DNA SEGMENT WITHIN THE COLICIN E1 STRUCTURAL GENE ON COLE1 AFFECTING IMMUNITY TO COLICINSHAFFERMAN A; COHEN S; FLASHNER Y et al.1978; MOLEC. GEN. GENET.; DEU; DA. 1978; VOL. 164; NO 3; PP. 259-264; BIBL. 20 REF.Article

Dual mechanism of repression at a distance in the lac operonFLASHNER, Y; GRALLA, J. D.Proceedings of the National Academy of Sciences of the United States of America. 1988, Vol 85, Num 23, pp 8968-8972, issn 0027-8424Article

DNA Dynamic flexibility and protein recognition: differential stimulation by bacterial histone-like protein HUFLASHNER, Y; GRALLA, J. D.Cell (Cambridge). 1988, Vol 54, Num 5, pp 713-721, issn 0092-8674Article

α and β replication origins of plasmid R6K show similar distortions of the DNA helix in vivoFLASHNER, Y; SHAFFERMAN, A.Proceedings of the National Academy of Sciences of the United States of America. 1990, Vol 87, Num 23, pp 9123-9127, issn 0027-8424, 5 p.Article

Identification and characterization of the functional α origin of DNA replication of the R6K plasmid and its relatedness to the R6K β and γ originsSHAFFERMAN, A; FLASHNER, Y; HERTMAN, I et al.MGG. Molecular & general genetics. 1987, Vol 208, Num 1-2, pp 263-270, issn 0026-8925Article

Molecular aspects of genetic instability of an artificial 68 bp perfect palindrome in Escherichia coliSHAFFERMAN, A; FLASHNER, Y; HERTMAN, I et al.MGG. Molecular & general genetics. 1987, Vol 208, Num 1-2, pp 294-300, issn 0026-8925Article

N-glycosylation of human acetylcholinesterase : effects on activity, stability and biosynthesisVELAN, B; KRONMAN, C; ORDENTLICH, A et al.Biochemical journal (London. 1984). 1993, Vol 296, pp 649-656, issn 0264-6021, 3Article

Dissection of the human acetylcholinesterase active center determinants of substrate specificity : identification of residues constituting the anionic site, the hydrophobic site, and the acyl pocketORDENTLICH, A; BARAK, D; KRONMAN, C et al.The Journal of biological chemistry (Print). 1993, Vol 268, Num 23, pp 17083-17095, issn 0021-9258Article

Substrate inhibition of acetylcholinesterase : residues affecting signal transduction from the surface to the catalytic centerSHAFFERMAN, A; VELAN, B; ORDENTLICH, A et al.EMBO journal (Print). 1992, Vol 11, Num 10, pp 3561-3568, issn 0261-4189Article

The effect of elimination of intersubunit disulfide bonds on the activity, assembly, and secretion of recombinant human acetlycholinesterase : expression of acetylcholinesterase cys-580 → ala mutantVELAN, B; GROSFELD, H; KRONMAN, C et al.The Journal of biological chemistry (Print). 1991, Vol 266, Num 35, pp 23977-23984, issn 0021-9258Article

Mutagenesis of human acetylcholinesterase : identification of residues involved in catalytic activity and in polypeptide foldingSHAFFERMAN, A; KRONMAN, C; HAREL, M et al.The Journal of biological chemistry (Print). 1992, Vol 267, Num 25, pp 17640-17648, issn 0021-9258Article

Recombinant human acetylcholinesterase is secreted from transiently transfected 293 cells as a soluble globular enzymeVELAN, B; KRONMAN, C; SHAFFERMAN, A et al.Cellular and molecular neurobiology. 1991, Vol 11, Num 1, pp 143-156, issn 0272-4340Article

Production and secretion of high levels of recombinant human acetylcholinesterase in cultured cell lines : microheterogeneity of the catalytic subunitKRONMAN, C; VELAN, B; COHEN, S et al.Gene (Amsterdam). 1992, Vol 121, Num 2, pp 295-304, issn 0378-1119Article