Expression of heterologous proteins in Pichia pastoris: a useful experimental tool in protein engineering and production

By Rachel Daly, M. Hearn. Journal of Molecular Recognition, 2005

827 citations recorded by the source corpus.

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

Current strategies for the use of affinity tags and tag removal for the purification of recombinant proteins. (2006, background): “, Escherichia coli, Saccharomyces cerevisiae, Pichia pastoris, insect and mammalian cell lines) have been developed to express heterologous proteins [2–7].”
Daedalus: a robust, turnkey platform for rapid production of decigram quantities of active recombinant proteins in human cell lines using novel lentiviral vectors (2011, positive): “Yeast-based expression systems, particularly those employing Saccharomyces cerevisiae and Pichia pastoris, offer improvements over bacterial systems in terms of yield, the complexity of proteins successfully expressed and the ability to perform some (but not all) post-translational modifications (3,”