Vello Tougu

Summary

Affiliation: Tallinn University of Technology
Country: Estonia

Publications

  1. ncbi Binding of zinc(II) and copper(II) to the full-length Alzheimer's amyloid-beta peptide
    Vello Tougu
    Department of Gene Technology, Tallinn University of Technology, Akadeemia tee, Tallinn, Estonia
    J Neurochem 104:1249-59. 2008
  2. ncbi Zn(II)- and Cu(II)-induced non-fibrillar aggregates of amyloid-beta (1-42) peptide are transformed to amyloid fibrils, both spontaneously and under the influence of metal chelators
    Vello Tougu
    Department of Gene Technology, Tallinn University of Technology, Tallinn, Estonia
    J Neurochem 110:1784-95. 2009
  3. ncbi Interactions of Zn(II) and Cu(II) ions with Alzheimer's amyloid-beta peptide. Metal ion binding, contribution to fibrillization and toxicity
    Vello Tougu
    Department of Gene Technology, Tallinn University of Technology, Akadeemia tee 15, Tallinn 12618, Estonia
    Metallomics 3:250-61. 2011
  4. ncbi Interference of low-molecular substances with the thioflavin-T fluorescence assay of amyloid fibrils
    Andra Noormägi
    Department of Gene Technology, Tallinn University of Technology, Akadeemia 15, 12618, Tallinn, Estonia
    J Pept Sci 18:59-64. 2012
  5. ncbi Label-free high-throughput screening assay for inhibitors of Alzheimer's amyloid-? peptide aggregation based on MALDI MS
    Kairit Zovo
    Department of Gene Technology, Tallinn University of Technology, Akadeemia tee 15, Tallinn 12618, Estonia
    Anal Chem 82:8558-65. 2010
  6. ncbi Zn(II) ions co-secreted with insulin suppress inherent amyloidogenic properties of monomeric insulin
    Andra Noormägi
    Department of Gene Technology, Tallinn University of Technology, Estonia
    Biochem J 430:511-8. 2010

Collaborators

Detail Information

Publications6

  1. ncbi Binding of zinc(II) and copper(II) to the full-length Alzheimer's amyloid-beta peptide
    Vello Tougu
    Department of Gene Technology, Tallinn University of Technology, Akadeemia tee, Tallinn, Estonia
    J Neurochem 104:1249-59. 2008
    ..Interaction of both Zn2+ and Cu2+ ions with Abeta peptides may occur in brain areas affected by Alzheimer's disease and Zn2+-induced transition in the peptide structure might contribute to amyloid plaque formation...
  2. ncbi Zn(II)- and Cu(II)-induced non-fibrillar aggregates of amyloid-beta (1-42) peptide are transformed to amyloid fibrils, both spontaneously and under the influence of metal chelators
    Vello Tougu
    Department of Gene Technology, Tallinn University of Technology, Tallinn, Estonia
    J Neurochem 110:1784-95. 2009
    ..The molecular background underlying metal-chelating therapies for Alzheimer's disease is discussed in this light...
  3. ncbi Interactions of Zn(II) and Cu(II) ions with Alzheimer's amyloid-beta peptide. Metal ion binding, contribution to fibrillization and toxicity
    Vello Tougu
    Department of Gene Technology, Tallinn University of Technology, Akadeemia tee 15, Tallinn 12618, Estonia
    Metallomics 3:250-61. 2011
    ..This might provide a key for understanding the putative role of copper in A? toxicity and AD pathology...
  4. ncbi Interference of low-molecular substances with the thioflavin-T fluorescence assay of amyloid fibrils
    Andra Noormägi
    Department of Gene Technology, Tallinn University of Technology, Akadeemia 15, 12618, Tallinn, Estonia
    J Pept Sci 18:59-64. 2012
    ..Our results show that interference with ThT test is a general phenomenon and more attention has to be paid to interpretation of kinetic results of protein fibrillization obtained by using fluorescent dyes...
  5. ncbi Label-free high-throughput screening assay for inhibitors of Alzheimer's amyloid-? peptide aggregation based on MALDI MS
    Kairit Zovo
    Department of Gene Technology, Tallinn University of Technology, Akadeemia tee 15, Tallinn 12618, Estonia
    Anal Chem 82:8558-65. 2010
    ..The MALDI MS-based method can significantly speed up in vitro screening of compound libraries for inhibitors of A??? fibrillization...
  6. ncbi Zn(II) ions co-secreted with insulin suppress inherent amyloidogenic properties of monomeric insulin
    Andra Noormägi
    Department of Gene Technology, Tallinn University of Technology, Estonia
    Biochem J 430:511-8. 2010
    ....