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Brigitte Gasser

Researcher at University of Natural Resources and Life Sciences, Vienna

Publications -  107
Citations -  6945

Brigitte Gasser is an academic researcher from University of Natural Resources and Life Sciences, Vienna. The author has contributed to research in topics: Pichia pastoris & Saccharomyces cerevisiae. The author has an hindex of 44, co-authored 104 publications receiving 5920 citations. Previous affiliations of Brigitte Gasser include Laos Ministry of Agriculture and Forestry & Boehringer Ingelheim.

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Book ChapterDOI

Recombinant Protein Production in Yeasts

TL;DR: Advantages and limitations of the main and most promising yeast hosts, including Saccharomyces cerevisiae, Pichia pastoris, and Hansenula polymorpha as those presently used in large scale production of heterologous proteins are summarized.
Journal ArticleDOI

Protein folding and conformational stress in microbial cells producing recombinant proteins: a host comparative overview

TL;DR: In this article, the main cellular players of this complex process are described for the most important cell factories used for biotechnological purposes, and the characterization of such adverse conditions and the elicited cell responses have permitted to better understand the physiology and molecular biology of conformational stress.
Journal ArticleDOI

Effects of gene dosage, promoters, and substrates on unfolded protein stress of recombinant Pichia pastoris.

TL;DR: An increase of BiP was observed upon induction of expression, indicating that the intracellular product fraction exerts an unfolded protein response in the host cells.
Journal ArticleDOI

Stress in recombinant protein producing yeasts.

TL;DR: Apart from discussing well-documented stress reactions of yeasts in the context of heterologous protein production, some more speculative topics like quorum sensing and apoptosis are addressed.
Journal ArticleDOI

Engineering of Pichia pastoris for improved production of antibody fragments.

TL;DR: It is concluded that protein folding and heterodimer assembly in the ER are rate limiting steps in Fab secretion, and the formation of interchain disulfide bonds can be seen as a major rate limiting factor to Fab assembly and subsequent secretion.