- 2014. The N-terminal sequence of tyrosine hydroxylase is a conformationally versatile motif that binds 14-3-3 proteins and membranes. Journal of Molecular Biology. 426: 150-168. doi: 10.1016/j.jmb.2013.09.012
- 2013. Vitellogenin recognizes cell damage through membrane binding and shields living cells from reactive oxygen species. Journal of Biological Chemistry. 288: 28369-28381. doi: 10.1074/jbc.M113.465021
- 2012. HAMLET forms annular oligomers when deposited with phoshpolipid monolayers. Journal of Molecular Biology. 418: 90-102. doi: 10.1016/j.jmb.2012.02.006
- 2012. The peripheral binding of 14-3-3gamma to membranes involves isoform-specific histidine residues. PLoS ONE. 7. doi: 10.1371/journal.pone.0049671
- 2011. Treatment of Solid Cancers Using a New Cationic Cytolytic Peptide. European Journal of Cancer. 47: S148-S148.
- 2010. HAMLET interacts with lipid membranes and perturbs their structure and integrity. PLoS ONE. 5. 10 pages. doi: 10.1371/journal.pone.0009384
- 2013. The Peripheral Binding of Proteins to Phospholipid Membranes, with Focus on α-Lactalbumin and Tyrosine Hydroxylase. University of Bergen.
More information in national current research information system (CRIStin)
2014
Skjevik, Å. A., Mileni, M., Baumann, A., Halskau, Ø., Teigen, K., Stevens, R. C., and Martinez, A.
The N-terminal sequence of tyrosine hydroxylase is a conformationally versatile motif that binds 14-3-3 proteins and membranes. Journal of molecular biology (2014), 426, 150-168
2013
Havukainen, H., Münch, D., Baumann, A., Zhong, S., Halskau, Ø., Krogsgaard, M., and Amdam, G. V.
Vitellogenin recognizes cell damage through membrane binding and shields living cells from reactive oxygen species. J. Biol. Chem. (2013), 288, 28369-28381
2012
Bustad, H. J., Skjærven, L., Ying, M., Halskau jr, Ø., Baumann, A., Rodriguez-Larrea, D., Costas, M., Underhaug, J., Sanchez-Ruiz, J. M. and Martinez, A.
The Peripheral Binding of 14-3-3gamma to Membranes Involves Isoform-Specific Histidine Residues. PLoS ONE (2012), 7(11): e49671.
Baumann, A., Gjerde, A. U., Ying, M., Svanborg, C., Holmsen, H., Glomm, W., Martinez, A. and Halskau jr, Ø.
HAMLET forms annular oligomers when deposited with phoshpolipid monolayers. Journal of Molecular Biology (2012), 18(1-2) p. 90-102.
2011
Szczepanski, C., Bjerkvig, R., Tenstad, O., Thorsen, F. A., Wendelbo, I. H., Martinez, A., Baumann, A. and Prestegarden, L.
Treatment of Solid Cancers Using a New Cationic Cytolytic Peptide. European Journal of Cancer (2011), 47, 148.
2010
Mossberg, A-K., Puchades, M., Halskau, Ø., Baumann, A., Lanekoff, I., Chao, Y., Martinez, A., Svanborg, C. and Karlsson, R.
HAMLET interacts with lipid membranes and perturbs their structure and integrity. PLoS ONE (2010), 5(2): e9384.
2009
Halskau, Ø., Ying, M., Baumann, A., Kleppe, R., Rodriguez-Larrea, D., Almås, B., Haavik, J. and Martinez, A.
Three-way interaction between 14-3-3 proteins, the N-terminal region of tyrosine hydroxylase and negatively charged membranes. J. Biol. Chem. (2009), 284, 32758–32769.
Research groups
Membrane localization of tyrosine hydroxylase and 14-3-3 proteins – Implications for neurodegeneration
The project deals with structural and mechanistic investigation of protein-membrane interactions. Specifically, we aim to obtain insights on the structural determinants of complex formation and how the interactions are affected by mutations and other processes leading to misfolding. We focus in particular on tyrosine hydroxylase (TH), the rate limiting enzyme in the synthesis of catecholamines, interacting with membranes. As a biological membrane model we are using large unilamellar vesicles (liposomes) of defined phospholipid composition, mainly equimolar mixtures of phosphatidylcholine and porcine brain phosphatidylserine. The protein-membrane interactions are investigated by a battery of biophysical methods such as surface plasmon resonance (SPR), circular dichroism (CD), dynamic light scattering (DLS), leakage of liposome content by fluorescence, and atomic force microscopy (AFM).