Structural features of the Cu(II) complex with the rat Abeta(1-28) fragment. (Q44760061)

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title

Structural features of the Cu(II) complex with the rat Abeta(1-28) fragment (English)

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5 January 2020

Elena Gaggelli

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Zbigniew Grzonka

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Caterina Migliorini

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Daniela Valensin

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5 January 2020

Gianni Valensin

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language of work or name

English

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publication date

1 January 2008

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published in

Chemical Communications

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issue

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page(s)

341-343

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The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor

5 January 2020

cites work

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Alzheimer's disease amyloid-beta binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits

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Methylation of the imidazole side chains of the Alzheimer disease amyloid-beta peptide results in abolition of superoxide dismutase-like structures and inhibition of neurotoxicity

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Metal binding in amyloid beta-peptides shows intra- and inter-peptide coordination modes

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Copper binding to the amyloid-beta (Abeta) peptide associated with Alzheimer's disease: folding, coordination geometry, pH dependence, stoichiometry, and affinity of Abeta-(1-28): insights from a range of complementary spectroscopic techniques

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Solution structure of amyloid beta-peptide(1-40) in a water-micelle environment. Is the membrane-spanning domain where we think it is?

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

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Relaxation Processes in a System of Two Spins

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Interaction of the human prion PrP(106-126) sequence with copper(II), manganese(II), and zinc(II): NMR and EPR studies

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Identifiers

DOI

10.1039/B713453C

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5 January 2020

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