Helene Bustad Johannessen
- Visitor AddressInstitutt for Biomedisin, Jonas Lies vei 91BergenRoom5A113B
- Postal AddressPostboks 78045020 Bergen
- Bustad, HJ. et al., Conformational stability and activity analysis of two hydroxymethylbilane synthase mutants, K132N and V215E, with different phenotypic association with acute intermittent porphyria. Biosci. Rep. 2013;33(4):e00056
- Bustad, HJ, Skjaerven, L. et al., The Peripheral Binding of 14-3-3γ to Membranes Involves Isoform-Specific Histidine Residues. PLoS One. 2012;7(11):e49671
- Bustad, HJ. et al., The binding of 14-3-3γ to membranes studied by intrinsic fluorescence spectroscopy. FEBS Lett, 2011. 585(8): p. 1163-1168.
- Steinkopf, S. et al., pH-dependent interaction of psychotropic drug with glycerophospholipid monolayers studied by the Langmuir technique. Biophys Chem, 2010. 152(1-3): p. 65-73.
- (2022). High-affinity anti-Arc nanobodies provide tools for structural and functional studies. PLOS ONE. 33 pages.
- (2022). Characterisation of a common hotspot variant in acute intermittent porphyria sheds light on the mechanism of hydroxymethylbilane synthase function. FEBS Open Bio. 2136-2146.
- (2021). Genetic Dominant Variants in STUB1, Segregating in Families with SCA48, Display In Vitro Functional Impairments Indistinctive from Recessive Variants Associated with SCAR16. International Journal of Molecular Sciences.
- (2021). Characterization of porphobilinogen deaminase mutants reveals that arginine-173 is crucial for polypyrrole elongation mechanism. iScience.
- (2020). Arc self‐association and formation of virus‐like capsids are mediated by an N‐terminal helical coil motif. The FEBS Journal.
- (2019). A Pharmacological Chaperone Therapy for Acute Intermittent Porphyria. Molecular Therapy.
- (2017). In vitro characterization of six STUB1 variants in spinocerebellar ataxia 16 reveals altered structural properties for the encoded CHIP proteins. Bioscience Reports. 1-12.
- (2015). Arc is a flexible modular protein capable of reversible self-oligomerization. Biochemical Journal. 145-158.
- (2013). Conformational stability and activity analysis of two hydroxymethylbilane synthase mutants, K132N and V215E, with different phenotypic association with acute intermittent porphyria. Bioscience Reports. 617-U203.
- (2012). The peripheral binding of 14-3-3gamma to membranes involves isoform-specific histidine residues. PLOS ONE.
- (2011). The binding of 14-3-3 gamma to membranes studied by intrinsic fluorescence spectroscopy. FEBS Letters. 1163-1168.
- (2020). Norsk fagspråk må styrkes. Klassekampen.
- (2017). Det er hardt å være forskar! Bioingeniøren. 28-29.
- (2013). Searching for pharmacological chaperones aiding to stabilize hydroxymethylbilane synthase. The FEBS Journal. 298-298.
- (2010). Characterization of the molecular basis of acute intermittent porphyria. The FEBS Journal. 76-76.
- (2010). CHARACTERIZATION OF THE MOLECULAR BASIS OF ACUTE INTERMITTENT PORPHYRIA. The Journal of Inherited Metabolic Disease (JIMD). S177-S177.
- (2007). pH-dependent drug interaction with glycerophospholipid monolayers studied by the Langmuir technique. Chemistry and Physics of Lipids. S31-S32.
Academic literature review
- (2021). Acute intermittent porphyria: An overview of therapy developments and future perspectives focusing on stabilisation of HMBS and proteostasis regulators. International Journal of Molecular Sciences. 25 pages.
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