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Peep Palumaa

Department of Gene Technology

Tallinn University of Technology

Tallinn

Estonia

[email]@staff.ttu.ee

Name/email consistency: high

 
 
 
 
 
 
 

Affiliation

  • Department of Gene Technology, Tallinn University of Technology, Tallinn, Estonia. 2002 - 2009

References

  1. 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) [Pubmed]
  2. 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) [Pubmed]
  3. Metal-binding mechanism of Cox17, a copper chaperone for cytochrome c oxidase. Palumaa, P., Kangur, L., Voronova, A., Sillard, R. Biochem. J. (2004) [Pubmed]
  4. 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) [Pubmed]
  5. 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) [Pubmed]
 
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