High-level secretion of human alpha 1-antitrypsin from Saccharomyces cerevisiae using inulinase signal sequence.
暂无分享,去创建一个
[1] J. Sambrook,et al. Molecular Cloning: A Laboratory Manual , 2001 .
[2] B. Chung,et al. Highly efficient secretion of heterologous proteins from Saccharomyces cerevisiae using inulinase signal peptides. , 2000, Biotechnology and bioengineering.
[3] M. Yu,et al. Refolding of alpha 1-antitrypsin expressed as inclusion bodies in Escherichia coli: characterization of aggregation. , 1995, Biochimica et biophysica acta.
[4] M. Tuite,et al. Improving secretion of recombinant proteins from yeast and mammalian cells: rational or empirical design? , 1994, Trends in biotechnology.
[5] A. McCracken,et al. Selective protein degradation in the yeast exocytic pathway. , 1993, Molecular biology of the cell.
[6] C. Scorer,et al. Foreign gene expression in yeast: a review , 1992, Yeast.
[7] J. Vandenhaute,et al. Cloning and sequencing of the inulinase gene of Kluyveromyces marxianus var. marxianus ATCC 12424 , 1991, FEBS letters.
[8] D Botstein,et al. Many random sequences functionally replace the secretion signal sequence of yeast invertase. , 1987, Science.
[9] K. Zsebo,et al. Protein secretion from Saccharomyces cerevisiae directed by the prepro-alpha-factor leader region. , 1986, The Journal of biological chemistry.
[10] A. Bollen,et al. Expression of human alpha 1-antitrypsin cDNA in the yeast Saccharomyces cerevisiae. , 1984, Proceedings of the National Academy of Sciences of the United States of America.
[11] K. Kurachi,et al. Complete sequence of the cDNA for human alpha 1-antitrypsin and the gene for the S variant. , 1984, Biochemistry.
[12] J. Thorner,et al. Isolation of the putative structural gene for the lysine-arginine-cleaving endopeptidase required for processing of yeast prepro-α-factor , 1984, Cell.
[13] K. Murata,et al. Transformation of intact yeast cells treated with alkali cations , 1983 .
[14] R. Carrell,et al. Human α1‐antitrypsin: carbohydrate attachment and sequence homology , 1981 .
[15] H. Towbin,et al. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. , 1979, Proceedings of the National Academy of Sciences of the United States of America.
[16] F. Sanger,et al. DNA sequencing with chain-terminating inhibitors. , 1977, Proceedings of the National Academy of Sciences of the United States of America.
[17] F. Maley,et al. Subunit structure of external invertase from Saccharomyces cerevisiae. , 1977, The Journal of biological chemistry.
[18] U. K. Laemmli,et al. Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.
[19] Myeong-Hee Yu,et al. Molecular properties of recombinant human alpha1-antitrypsin produced in Escherichia coli and in vitro translation system , 1993 .
[20] P. Orlean,et al. Analysis of glycoproteins from Saccharomyces cerevisiae. , 1991, Methods in enzymology.
[21] R. Crystal. The α1-antitrypsin gene and its deficiency states , 1989 .
[22] D. Moir,et al. Glycosylation and secretion of human alpha-1-antitrypsin by yeast. , 1987, Gene.
[23] G. Fink,et al. Laboratory course manual for methods in yeast genetics , 1986 .
[24] J. Travis,et al. [55] Human α1-proteinase inhibitor , 1981 .