About
10
Publications
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72
Citations
Introduction
Current institution
Additional affiliations
March 2014 - February 2021
Position
- PhD Student
Description
- Mechanisms, regulation, and applications of oxidative protein folding and disulfide bond formation.
February 2013 - February 2014
Paras Biopharmaceuticals Finland Oy
Position
- Researcher
Description
- Development of expression and purification methods for E. coli production of biopharmaceutical proteins.
January 2012 - June 2012
Position
- Master's Student
Description
- Six months in the lab for structural and kinetic studies of human Ero1beta.
Education
March 2014 - March 2021
University of Oulu
Field of study
- Biochemistry and molecular medicine (thesis: Novel regulatory mechanisms and structural aspects of oxidative protein folding)
September 2011 - April 2013
September 2009 - September 2011
Publications
Publications (10)
In the methylotrophic yeast Komagataella phaffii, we identified an ER-resident protein disulfide isomerase (PDI) family member, Erp41, with a peculiar combination of active site motifs. Like fungal ERp38, it has two thioredoxin-like domains which contain active site motifs (a and a’), followed by an alpha-helical ERp29c C-terminal domain (c domain)...
Oxidative protein folding in the endoplasmic reticulum (ER) is driven mainly by protein disulfide isomerase PDI and oxidoreductin Ero1. Their activity is tightly regulated and interconnected with the unfolded protein response (UPR). The mechanisms of disulfide bond formation have mainly been studied in human or in the yeast Saccharomyces cerevisiae...
Academic dissertation that was presented in a public defence on 15 February 2021.
In this study, comprehensive kinetic measurements for the Ero1-PDI pathway are reported that reveal novel regulatory mechanisms for oxidative protein folding (OPF). These include a mechanism consisting of high affinity and apparent cooperativity for substrate oxygen...
The folding of disulfide bond containing proteins in the endoplasmic reticulum (ER) is a complex process that requires protein folding factors, some of which are protein-specific. The ER resident saposin-like protein pERp1 (MZB1, CNPY5) is crucial for the correct folding of IgA, IgM and integrins. pERp1 also plays a role in ER calcium homeostasis a...
The major cat allergen Fel d 1 is one of the most common and potent causes of animal related allergy. Medical treatment of cat allergy has relied on immunotherapy carried out with cat dander extract. This approach has been problematic, mainly due to inconsistent levels of the major allergen in the produced extracts. Recombinant DNA technology has b...
Protein maturation in the endoplasmic reticulum (ER) depends on a fine balance between oxidative protein folding and quality control mechanisms, which together ensure high-capacity export of properly folded proteins from the ER. Oxidative protein folding needs to be regulated to avoid hyperoxidation. The folding capacity of the ER is regulated by t...
Candida antarctica lipase B (CalB) is a very efficient catalyst and is used in a wide range of industries from food flavour to pharmaceutical, and biodiesel manufacturing. It has a high degree of enantioselective and regioselective substrate specificity and is stable over a wide range of biophysical conditions including pH, temperature and solvent...
Oxidative protein folding in the ER is driven mainly by oxidases of the endoplasmic reticulum oxidoreductin 1 (Ero1) family. Their action is regulated to avoid cell stress, including hyperoxidation. Previously published regulatory mechanisms are based on the rearrangement of active site and regulatory disulfides. In this study, we identify two nove...
