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Author
4
Bal, W.
4
Krezel, A.
1
Karavelas, T.
1
Kozlowski, H.
1
Malandrinos, G.
1
Melissas, V. S.
1
Mlynarz, P.
1
Papavasilelou, K. D.
Subject
6
oxidative damage
4
copper(ii) complexes
4
h3
4
metal-binding sequence
3
ch3co-cys-ala-ile-his-nh2
3
nickel(ii)
3
stability
3
tail
2
c-terminal tail
2
hexapeptides
.
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Item Type
7
journalArticle
Date
3
2005
2
2004
2
2002
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ΑΠΟΘΕΤΗΡΙΟ "ΟΛΥΜΠΙΑΣ"
Σχολή Θετικών Επιστημών
Τμήμα Μαθηματικών
Τμήμα Μηχανικών Επιστήμης Υλικών
Τμήμα Μηχανικών Ηλεκτρονικών Υπολογιστών και Πληροφορικής
Τμήμα Φυσικής
Τμήμα Χημείας
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Interactions of Ni(II) and Cu(II) ions with the hydrolysis products of the C-terminal -ESHH-motif of histone H2A model peptides. Association of the stability of the complexes formed with the cleavage of the -ES-bond (Journal article)
Interactions of transition metal ions with His-containing peptide models of histone H2A (Journal article)
Interactions of Zn(II) ions with three His-containing peptide models of histone H2A (Journal article)
Coordination properties of Cu(II) and Ni(II) ions towards the C-terminal peptide fragment -ELAKHA- of histone H2B (Journal article)
The binding of Ni(II) ions to terminally blocked hexapeptides derived from the metal binding -ESHH- motif of histone H2A (Journal article)
An extremely stable Ni(II) complex derived from the hydrolytic cleavage of the C-terminal tail of histone H2A (Journal article)
Potentiometric and spectroscopic studies of the interaction of Cu(II) ions with the hexapeptides AcThrAlaSeHisHisLysNH(2), AcThrGluAlaHisHisLysNH(2), AcThrGluSerAlaHisLysNH(2) and AcThrGluSerHisAlaLysNH(2), models of C-terminal tail of histone H2A (Journal article)