Molecular-level examination of Cu2+ binding structure for amyloid fibrils of 40-residue Alzheimer's β by solid-state NMR spectroscopy (Q34779975)

4 August 2017

title

Molecular-level examination of Cu2+ binding structure for amyloid fibrils of 40-residue Alzheimer's β by solid-state NMR spectroscopy (English)

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4 August 2017

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4 August 2017

Yoshitaka Ishii

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Ruth Nussinov

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4 August 2017

Yifat Miller

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4 August 2017

Sudhakar Parthasarathy

series ordinal

object named as

Sudhakar Parthasarathy

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4 August 2017

Yiling Xiao

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4 August 2017

Dan McElheny

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4 August 2017

Fei Long

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4 August 2017

Kent Thurber

series ordinal

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4 August 2017

language of work or name

English

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publication date

22 February 2011

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Journal of the American Chemical Society

4 August 2017

published in

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4 August 2017

volume

133

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4 August 2017

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4 August 2017

page(s)

3390-3400

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Design of small molecules that target metal-A{beta} species and regulate metal-induced A{beta} aggregation and neurotoxicity.

4 August 2017

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7 July 2018

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7 July 2018

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7 July 2018

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7 July 2018

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7 July 2018

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7 July 2018

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7 July 2018

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7 July 2018

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The Aβ Peptide of Alzheimer's Disease Directly Produces Hydrogen Peroxide through Metal Ion Reduction†

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Ultrafast MAS Solid-State NMR Permits Extensive13C and1H Detection in Paramagnetic Metalloproteins

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Characterization of Copper Interactions with Alzheimer Amyloid β Peptides

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Characterization of polymorphs and solid-state reactions for paramagnetic systems by 13C solid-state NMR and ab initio calculations

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Infectious and noninfectious amyloids of the HET-s(218-289) prion have different NMR spectra

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Histidine-13 is a crucial residue in the zinc ion-induced aggregation of the A beta peptide of Alzheimer's disease

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12 December 2020

Identifiers

DOI

10.1021/JA1072178

1 reference

4 August 2017

1 reference

4 August 2017

1 reference