Isolation of the Pichia pastoris glyceraldehyde-3-phosphate dehydrogenase gene and regulation and use of its promoter
- 1 February 1997
- Vol. 186 (1) , 37-44
- https://doi.org/10.1016/s0378-1119(96)00675-0
Abstract
No abstract availableKeywords
This publication has 22 references indexed in Scilit:
- Methylotrophic yeasts as factories for the production of foreign proteinsYeast, 1995
- Mutational analysis of the N-terminal topogenic signal of watermelon glyoxysomal malate dehydrogenase using the heterologous host Hansenula polymorpha.Proceedings of the National Academy of Sciences, 1994
- Recent Advances in the Expression of Foreign Genes in Pichia pastorisNature Biotechnology, 1993
- An efficient screen for peroxisome-deficient mutants of Pichia pastorisJournal of Bacteriology, 1992
- Development of the yeast Pichia pastoris as a model organism for a genetic and molecular analysis of peroxisome assemblyYeast, 1992
- [12] High-efficiency transformation of yeast by electroporationPublished by Elsevier ,1991
- Glyoxysomal malate dehydrogenase from watermelon is synthesized with an amino-terminal transit peptide.Proceedings of the National Academy of Sciences, 1990
- Pichia pastoris as a host system for transformations.Molecular and Cellular Biology, 1985
- Dihydroxyacetone synthase is localized in the peroxisomal matrix of methanol-grown Hansenula polymorphaArchiv für Mikrobiologie, 1985
- Transcriptional mapping of two yeast genes coding for glyceraldehyde 3-phosphate dehydrogenase isolated by sequence homology with the chicken geneGene, 1983