The Coordination of NiIIand CuIIIons to the Polyhistidyl Motif of Hpn Protein: Is It as Strong as We Think?

Specific poly-histidyl and poly-cysteil protein sites involved in Ni2+ homeostasis in Helicobacter pylori. Impact of Bi3+ ions on Ni2+ binding to proteins. Structural and thermodynamic aspects

(2011) Danuta Witkowska et al.   COORDINATION CHEMISTRY REVIEWS

The –Cys–Cys– motif in Helicobacter pylori's Hpn and HspA proteins is an essential anchoring site for metal ions

(2011) Magdalena Rowinska-Zyrek et al.   DALTON TRANSACTIONS

Coordination of Cu2+and Ni2+ with the histone model peptide of H2B N-terminal tail (1-31 residues): A spectroscopic study

(2010) Ana Mónica Nunes et al.   DALTON TRANSACTIONS

Cu2+ and Ni2+ interactions with N-terminal fragments of Hpn and Hpn-like proteins from Helicobacter pylori

(2010) Danuta Witkowska et al.   JOURNAL OF INORGANIC BIOCHEMISTRY

Nickel Homeostasis and Nickel Regulation: An Overview

(2009) Yanjie Li et al.   CHEMICAL REVIEWS

Copper(ii) coordination outside the tandem repeat region of an unstructured domain of chicken prion protein

(2009) Ewa Gralka et al.   Molecular BioSystems

Binding of Ni2+ and Cu2+ ions to peptides with a Cys–His motif

(2008) Kinga Kulon et al.   DALTON TRANSACTIONS

Structural Characterization of the Intra- and Inter-Repeat Copper Binding Modes within the N-Terminal Region of “Prion Related Protein” (PrP-rel-2) of Zebrafish

(2008) Elena Gaggelli et al.   JOURNAL OF PHYSICAL CHEMISTRY B

The role of the histidine residue in the coordination abilities of peptides with a multi-histidine sequence towards copper(II) ions

(2008) Agnieszka Matera et al.   POLYHEDRON