Helene Bustad Johannessen

Guest Researcher

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.

Academic article

Show author(s) (2022). High-affinity anti-Arc nanobodies provide tools for structural and functional studies. PLOS ONE. 33 pages.
Show author(s) (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.

Show author(s) (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.
Show author(s) (2021). Characterization of porphobilinogen deaminase mutants reveals that arginine-173 is crucial for polypyrrole elongation mechanism. iScience.

Show author(s) (2020). Arc self‐association and formation of virus‐like capsids are mediated by an N‐terminal helical coil motif. The FEBS Journal.

Show author(s) (2019). A Pharmacological Chaperone Therapy for Acute Intermittent Porphyria. Molecular Therapy.

Show author(s) (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.

Show author(s) (2015). Arc is a flexible modular protein capable of reversible self-oligomerization. Biochemical Journal. 145-158.

Show author(s) (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.

Show author(s) (2012). The peripheral binding of 14-3-3gamma to membranes involves isoform-specific histidine residues. PLOS ONE.

Show author(s) (2011). The binding of 14-3-3 gamma to membranes studied by intrinsic fluorescence spectroscopy. FEBS Letters. 1163-1168.

Feature article

Abstract

Show author(s) (2013). Searching for pharmacological chaperones aiding to stabilize hydroxymethylbilane synthase. The FEBS Journal. 298-298.

Show author(s) (2010). Characterization of the molecular basis of acute intermittent porphyria. The FEBS Journal. 76-76.
Show author(s) (2010). CHARACTERIZATION OF THE MOLECULAR BASIS OF ACUTE INTERMITTENT PORPHYRIA. The Journal of Inherited Metabolic Disease (JIMD). S177-S177.

Show author(s) (2007). pH-dependent drug interaction with glycerophospholipid monolayers studied by the Langmuir technique. Chemistry and Physics of Lipids. S31-S32.

Academic literature review

Show author(s) (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.

Research groups