X-ray absorption and diffraction studies of the metal binding sites in amyloid beta-peptide (Q37001423)

17 August 2017

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title

X-ray absorption and diffraction studies of the metal binding sites in amyloid beta-peptide (English)

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17 August 2017

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Victor Streltsov

1

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17 August 2017

language of work or name

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15 November 2007

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European Biophysics Journal

17 August 2017

published in

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17 August 2017

volume

37

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17 August 2017

issue

3

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17 August 2017

page(s)

257-263

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Metal switch for amyloid formation: insight into the structure of the nucleus

17 August 2017

cites work

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Metal binding modes of Alzheimer's amyloid beta-peptide in insoluble aggregates and soluble complexes.

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Structural models of amyloid-like fibrils

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Engineering metal ion coordination to regulate amyloid fibril assembly and toxicity

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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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Beta-structures in fibrous proteins.

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NMR reveals anomalous copper(II) binding to the amyloid Abeta peptide of Alzheimer's disease

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Structural and thermodynamical properties of CuII amyloid-beta16/28 complexes associated with Alzheimer's disease.

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Metal ions, pH, and cholesterol regulate the interactions of Alzheimer's disease amyloid-beta peptide with membrane lipid

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Copper-mediated amyloid-beta toxicity is associated with an intermolecular histidine bridge.

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3D structure of Alzheimer's amyloid-beta(1-42) fibrils

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Structural changes of region 1-16 of the Alzheimer disease amyloid beta-peptide upon zinc binding and in vitro aging

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Preparation of amyloid beta-protein for structural and functional studies

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Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils

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Synchrotron radiation effects on catalytic systems as probed with a combined in-situ UV-vis/XAFS spectroscopic setup

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

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Atomic structures of amyloid cross-beta spines reveal varied steric zippers

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Metals and neuroscience.

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Beta-amyloid protein oligomers induced by metal ions and acid pH are distinct from those generated by slow spontaneous ageing at neutral pH.

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Structure of amyloid beta fragments in aqueous environments

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N-Terminal deletions modify the Cu2+ binding site in amyloid-beta

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Role of aspartate-1 in Cu(II) binding to the amyloid-beta peptide of Alzheimer's disease

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Inhibitors of amyloid toxicity based on beta-sheet packing of Abeta40 and Abeta42.

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Molecular basis for passive immunotherapy of Alzheimer's disease

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Probing the influence of X-rays on aqueous copper solutions using time-resolved in situ combined video/X-ray absorption near-edge/ultraviolet-visible spectroscopy

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3D EXAFS refinement of the Cu site of azurin sheds light on the nature of structural change at the metal centre in an oxidation-reduction process: an integrated approach combining EXAFS and crystallography

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Characterization of chemical exchange between soluble and aggregated states of beta-amyloid by solution-state NMR upon variation of salt conditions

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Characterization of Copper Interactions with Alzheimer Amyloid β Peptides

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Structure of the cross-beta spine of amyloid-like fibrils

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The structural biology of protein aggregation diseases: Fundamental questions and some answers

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Structures of human insulin-degrading enzyme reveal a new substrate recognition mechanism

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In situ characterization and mapping of iron compounds in Alzheimer's disease tissue.

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Detection, identification and mapping of iron anomalies in brain tissue using X-ray absorption spectroscopy

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A structural model for Alzheimer's beta -amyloid fibrils based on experimental constraints from solid state NMR

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Characterization of copper binding to the peptide amyloid-β(1–16) associated with Alzheimer's disease

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Amyloid-beta binds Cu2+ in a mononuclear metal ion binding site

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Redox reactions of copper complexes formed with different beta-amyloid peptides and their neuropathological [correction of neuropathalogical] relevance

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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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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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Redox chemistry of copper-amyloid-beta: the generation of hydroxyl radical in the presence of ascorbate is linked to redox-potentials and aggregation state

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Abeta produced as a fusion to maltose binding protein can be readily purified and stably associates with copper and zinc.

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Recent atomic models of amyloid fibril structure

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12 December 2020

10.1007/S00249-007-0232-5

Identifiers

DOI

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17 August 2017

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