Expression and secretion of biologically active echistatin in Saccharomyces cerevisiae
References (17)
- et al.
Expression, purification and characterization of recombinant human insulin-like growth factor I in yeast
Gene
(1988) - et al.
Codon selection in yeast
J. Biol. Chem.
(1982) Construction of high copy yeast vectors using 2 μM circle sequences
Methods Enzymol.
(1983)- et al.
Echistatin, a potent platelet aggregation inhibitor from the venom of the viper, Echis carinatus
J. Biol. Chem.
(1988) - et al.
Structure of a yeast pheromone gene (MFα): a putative α-factor precursor contains four tandem copies of mature α-factor
Cell
(1982) - et al.
Secretion of mature mouse interleukin-2 by Saccharomyces cerevisiae: use of a general secretion vector containing promoter and leader sequences of the mating pheromone α-factor
Gene
(1985) - et al.
Regulated overproduction of the GAL4 gene product greatly increases expression from galactose-inducible promoters on multi-copy expression vectors in yeast
Gene
(1987) - et al.
Expression and secretion of biologically active human atrial natriuretic peptide in Saccharomyces cerevisiae
J. Biol. Chem.
(1986)
Cited by (28)
Expression in Pichia pastoris and characterization of echistatin, an RGD-containing short disintegrin
2012, ToxiconCitation Excerpt :Site-directed mutagenesis and deletion studies on Ech are useful tools for identifying its interactions with integrins. However, it is essential to produce Ech and its mutants with the correct fold and high yields (Jacobson et al., 1989; Hofmann and Schultz, 1991; Garsky et al., 1989; Chuang et al., 1996). Ech and its mutants have been chemically synthesized and are shown to be functional (Garsky et al., 1989; Chuang et al., 1996).
Snake venom metalloproteases - Structure and function of catalytic and disintegrin domains
2006, Comparative Biochemistry and Physiology - C Toxicology and PharmacologyCitation Excerpt :A search of the Entrez protein database (www.ncbi.nlm.nih.gov/entrez), accessed in October, 2005, using the terms “disintegrin” and “Xenophidia” (super family of serpents) retrieved 195 hits. Besides protein isolation from snake venoms, several disintegrin domains have been cloned and expressed including bothrostatin (Fernandez et al., 2005), kistrin (Dennis et al., 1993), rhodostomin (Guo et al., 2001), contortrostatin (Zhou et al., 2000), bothropasin (Assakura et al., 2003), salmosin (Park et al., 1998), acugrin (Fan et al., 1999), elegantin (Rahman et al., 1998) Gan et al., 1989; Jacobson et al., 1989), adinbitor (Wang et al., 2004), jerdostatin (Sanz et al., in press), bitistatin (Knight and Romano, 2005) and jararhagin (Moura-da-Silva et al., 1999). Moreover, Garsky et al. (1989) have showed that it was possible to chemically synthesize a short disintegrin, echistatin.
Snake venoms and the hemostatic system
1998, ToxiconChromatographic separation of low-molecular-mass recombinant proteins and peptides on Superdex 30 prep grade
1994, Journal of Chromatography B: Biomedical Sciences and ApplicationsExpression, purification and characterization of multigram amounts of a recombinant hybrid hv1-hv2 hirudin variant expressed in saccharomyces cerevisiae
1993, Protein Expression and PurificationThe expression and performance of cloned genes in yeasts
1993, Mycological Research