Authors:
ERSDALBADJU E
LU AQ
ZUO YC
PICARD V
BOCK SC
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Citation: V. Picard et al., PARTIAL GLYCOSYLATION OF ANTITHROMBIN-III ASPARAGINE-135 IS CAUSED BYA SERINE, RATHER THAN A THREONINE, IN THE 3RD POSITION OF ITS N-GLYCOSYLATION CONSENSUS SEQUENCE, AND IS RESPONSIBLE FOR THE PRODUCTION OF BETA-ATIII, Thrombosis and haemostasis, 73(6), 1995, pp. 1251-1251
Authors:
ERSDALBADJU E
LU AQ
PENG XM
PICARD V
ZENDEHROUH P
TURK B
BJORK I
OLSON ST
BOCK SC
Citation: E. Ersdalbadju et al., ELIMINATION OF GLYCOSYLATION HETEROGENEITY AFFECTING HEPARIN AFFINITYOF RECOMBINANT HUMAN ANTITHROMBIN-III BY EXPRESSION OF A BETA-LIKE VARIANT IN BACULOVIRUS-INFECTED INSECT CELLS, Biochemical journal, 310, 1995, pp. 323-330
Citation: V. Picard et al., PARTIAL GLYCOSYLATION OF ANTITHROMBIN-III ASPARAGINE-135 IS CAUSED BYTHE SERINE IN THE 3RD POSITION OF ITS N-GLYCOSYLATION CONSENSUS SEQUENCE AND IS RESPONSIBLE FOR PRODUCTION OF THE BETA-ANTITHROMBIN-III ISOFORM WITH ENHANCED HEPARIN AFFINITY, Biochemistry, 34(26), 1995, pp. 8433-8440
Citation: V. Picard et al., A RAPID AND EFFICIENT ONE-TUBE PCR-BASED MUTAGENESIS TECHNIQUE USING PFU DNA-POLYMERASE, Nucleic acids research, 22(13), 1994, pp. 2587-2591
Citation: E. Ersdalbadju et al., STRUCTURAL DISSECTION OF THE ANTITHROMBIN-III HEPARIN-BINDING SITE - K107 AND K114 ARE NOT DIRECTLY INVOLVED IN HEPARIN-BINDING, Thrombosis and haemostasis, 69(6), 1993, pp. 759-759