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Chemical and biological aspects of Cu2+ interactions with peptides and aminoglycosides

Coordination chemistry reviews, 2005-11, Vol.249 (21-22), p.2323-2334

2005

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Coordination properties of Cu(II) ions towards the peptides based on the His-Xaa-His motif from Fusobacterium nucleatum P1 protein

Journal of inorganic biochemistry, 2019-12, Vol.201, p.110819-110819, Article 110819

2019

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Coordination abilities of the 1–16 and 1–28 fragments of β-amyloid peptide towards copper(II) ions: a combined potentiometric and spectroscopic study

Journal of inorganic biochemistry, 2003-07, Vol.95 (4), p.270-282

2003

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Specific structure–stability relations in metallopeptides

Coordination chemistry reviews, 1999-04, Vol.184 (1), p.319-346

1999

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Copper(II) complexes of terminally free alloferon mutants containing two histidyl binding sites inside peptide chain structure and stability

Dalton transactions : an international journal of inorganic chemistry, 2015-01, Vol.44 (47), p.20659-20674

2015

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Copper(ii) complexes of terminally free alloferon mutants containing two histidyl binding sites inside peptide chain structure and stabilityElectronic supplementary information (ESI) available. See DOI: 10.1039/c5dt01911g

2015-11

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Coordination abilities of N-terminal fragments of α-synuclein towards copper(II) ions: A combined potentiometric and spectroscopic study

Journal of inorganic biochemistry, 2005-12, Vol.99 (12), p.2282-2291

2005

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Products of Cu(II)-catalyzed oxidation in the presence of hydrogen peroxide of the 1–10, 1–16 fragments of human and mouse β-amyloid peptide

Journal of inorganic biochemistry, 2004-06, Vol.98 (6), p.940-950

2004

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Cu(II) complexes with peptides from FomA protein containing -His-Xaa-Yaa-Zaa-His and -His-His-motifs. ROS generation and DNA degradation

Journal of inorganic biochemistry, 2020-11, Vol.212, p.111250-111250, Article 111250

2020

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Copper(II) complex formation processes of alloferon I with point mutation H1K; combined spectroscopic and potentiometric studies

Journal of inorganic biochemistry, 2012-06, Vol.111, p.40-49

2012

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Copper(II) complexes of the Neb-colloostatin analogues containing histidine residue structure stability biological activity

Polyhedron, 2017-09, Vol.134, p.365-375

2017

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Stability of Cu(ii) complexes with FomA protein fragments containing two His residues in the peptide chain

Metallomics, 2019-09, Vol.11 (9), p.1518

2019

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Mono- and polynuclear copper(II) complexes with fragment of alloferons 1 and 2; combined potentiometric and spectroscopic studies

Dalton transactions : an international journal of inorganic chemistry, 2010-01, Vol.39 (17), p.4117-4125

2010

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Copper(II) complexes of alloferon 1 with point mutations (H1A) and (H9A) stability structure and biological activity

Journal of inorganic biochemistry, 2014-09, Vol.138, p.99-113

2014

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Mono- and Polynuclear Copper(II) Complexes of Alloferons 1 with Point Mutations (H6A) and (H12A): Stability Structure and Cytotoxicity

Inorganic chemistry, 2013-05, Vol.52 (10), p.5951-5961

2013

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Cu(II) interaction with N-terminal fragments of human and mouse β-amyloid peptide

Journal of inorganic biochemistry, 2001-09, Vol.86 (2), p.535-545

2001

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High stability and biological activity of the copper(II) complexes of alloferon 1 analogues containing tryptophan

Journal of inorganic biochemistry, 2016-10, Vol.163, p.147-161

2016

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Coordination of copper(ii) ions by the fragments of neuropeptide gamma containing D1, H9, H12 residues and products of copper-catalyzed oxidationElectronic supplementary information (ESI) available. See DOI: 10.1039/c1dt10592b

2012-01

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Molecular Mechanisms in Nickel Carcinogenesis: Modeling Ni(II) Binding Site in Histone H4

Environmental health perspectives, 2002-10, Vol.110 (suppl 5), p.719-723

2002

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Coordination of copper( ii ) ions by the fragments of neuropeptide gamma containing D 1 , H 9 , H 12 residues and products of copper-catalyzed oxidation

Dalton transactions : an international journal of inorganic chemistry, 2012, Vol.41 (6), p.1683-1694

2012

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Coordination Abilities of a Fragment Containing D 1 and H 12 Residues of Neuropeptide γ and Products of Metal-Catalyzed Oxidation

Inorganic chemistry, 2010-03, Vol.49 (5), p.2182-2192

2010

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Coordination of copper(II) ions by the 11–20 and 11–28 fragments of human and mouse β-amyloid peptide

Journal of inorganic biochemistry, 2002-09, Vol.92 (1), p.1-10

2002

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Interaction of Ni(II) and Cu(II) with a metal binding sequence of histone H4: AKRHRK, a model of the H4 tail

Biochimica et biophysica acta, 2000-07, Vol.1475 (2), p.163-168

2000

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Acid–Base Properties of the (1-4,18-36) Fragments of Neuropeptide K and their Mono- and Polynuclear Copper(II) Complexes Products of Metal-Catalyzed Oxidation

Inorganic chemistry, 2013-01, Vol.52 (1), p.130-143

2013

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Copper(II) complexes of terminally free alloferon peptide mutants containing two different histidyl (H1 and H6 or H9 or H12) binding sites Structure Stability and Biological Activity

Journal of inorganic biochemistry, 2015-10, Vol.151, p.44-57

2015

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Chemical and biological aspects of Cu2+ interactions with peptides and aminoglycosides

Coordination properties of Cu(II) ions towards the peptides based on the His-Xaa-His motif from Fusobacterium nucleatum P1 protein

Coordination abilities of the 1–16 and 1–28 fragments of β-amyloid peptide towards copper(II) ions: a combined potentiometric and spectroscopic study

Specific structure–stability relations in metallopeptides

Copper(II) complexes of terminally free alloferon mutants containing two histidyl binding sites inside peptide chain structure and stability

Copper(ii) complexes of terminally free alloferon mutants containing two histidyl binding sites inside peptide chain structure and stabilityElectronic supplementary information (ESI) available. See DOI: 10.1039/c5dt01911g

Coordination abilities of N-terminal fragments of α-synuclein towards copper(II) ions: A combined potentiometric and spectroscopic study

Products of Cu(II)-catalyzed oxidation in the presence of hydrogen peroxide of the 1–10, 1–16 fragments of human and mouse β-amyloid peptide

Cu(II) complexes with peptides from FomA protein containing -His-Xaa-Yaa-Zaa-His and -His-His-motifs. ROS generation and DNA degradation

Copper(II) complex formation processes of alloferon I with point mutation H1K; combined spectroscopic and potentiometric studies

Copper(II) complexes of the Neb-colloostatin analogues containing histidine residue structure stability biological activity

Stability of Cu(ii) complexes with FomA protein fragments containing two His residues in the peptide chain

Mono- and polynuclear copper(II) complexes with fragment of alloferons 1 and 2; combined potentiometric and spectroscopic studies

Copper(II) complexes of alloferon 1 with point mutations (H1A) and (H9A) stability structure and biological activity

Mono- and Polynuclear Copper(II) Complexes of Alloferons 1 with Point Mutations (H6A) and (H12A): Stability Structure and Cytotoxicity

Cu(II) interaction with N-terminal fragments of human and mouse β-amyloid peptide

High stability and biological activity of the copper(II) complexes of alloferon 1 analogues containing tryptophan

Coordination of copper(ii) ions by the fragments of neuropeptide gamma containing D1, H9, H12 residues and products of copper-catalyzed oxidationElectronic supplementary information (ESI) available. See DOI: 10.1039/c1dt10592b

Molecular Mechanisms in Nickel Carcinogenesis: Modeling Ni(II) Binding Site in Histone H4

Coordination of copper( ii ) ions by the fragments of neuropeptide gamma containing D 1 , H 9 , H 12 residues and products of copper-catalyzed oxidation

Coordination Abilities of a Fragment Containing D 1 and H 12 Residues of Neuropeptide γ and Products of Metal-Catalyzed Oxidation

Coordination of copper(II) ions by the 11–20 and 11–28 fragments of human and mouse β-amyloid peptide

Interaction of Ni(II) and Cu(II) with a metal binding sequence of histone H4: AKRHRK, a model of the H4 tail

Acid–Base Properties of the (1-4,18-36) Fragments of Neuropeptide K and their Mono- and Polynuclear Copper(II) Complexes Products of Metal-Catalyzed Oxidation

Copper(II) complexes of terminally free alloferon peptide mutants containing two different histidyl (H1 and H6 or H9 or H12) binding sites Structure Stability and Biological Activity

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