Peep Palumaa
Department of Gene Technology
Tallinn University of Technology
Tallinn
Estonia
Name/email consistency: high
- Modulation of redox switches of copper chaperone Cox17 by Zn(II) ions determined by new ESI MS-based approach. Zovo, K., Palumaa, P. Antioxid. Redox Signal. (2009)
- Metal binding of metallothionein-3 versus metallothionein-2: lower affinity and higher plasticity. Palumaa, P., Tammiste, I., Kruusel, K., Kangur, L., Jörnvall, H., Sillard, R. Biochim. Biophys. Acta (2005)
- Metal-binding mechanism of Cox17, a copper chaperone for cytochrome c oxidase. Palumaa, P., Kangur, L., Voronova, A., Sillard, R. Biochem. J. (2004)
- Brain-specific metallothionein-3 has higher metal-binding capacity than ubiquitous metallothioneins and binds metals noncooperatively. Palumaa, P., Eriste, E., Njunkova, O., Pokras, L., Jörnvall, H., Sillard, R. Biochemistry (2002)
- Evidence for non-isostructural replacement of Zn(2+) with Cd(2+) in the beta-domain of brain-specific metallothionein-3. Palumaa, P., Njunkova, O., Pokras, L., Eriste, E., Jörnvall, H., Sillard, R. FEBS Lett. (2002)









