Structures and free energy landscapes of aqueous zinc(II)-bound amyloid-β(1-40) and zinc(II)-bound amyloid-β(1-42) with dynamics. (Q36950757)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22674434%20AND%20SRC:MED&resulttype=core&format=json

3 February 2020

title

Structures and free energy landscapes of aqueous zinc(II)-bound amyloid-β(1-40) and zinc(II)-bound amyloid-β(1-42) with dynamics (English)

1 reference

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3 February 2020

1 reference

3

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3 February 2020

Orkide Coşkuner-Weber

series ordinal

4

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3 February 2020

author name string

Olivia Wise-Scira

series ordinal

1

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3 February 2020

Liang Xu

series ordinal

2

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publication date

7 June 2012

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Journal of Biological Inorganic Chemistry

3 February 2020

published in

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volume

17

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issue

6

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3 February 2020

page(s)

927-938

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Amyloid-β peptide structure in aqueous solution varies with fragment size

3 February 2020

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4 September 2018

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4 September 2018

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4 September 2018

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Characterization of the ZnII binding to the peptide amyloid-beta1-16 linked to Alzheimer's disease.

4 September 2018

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4 September 2018

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4 September 2018

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4 September 2018

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4 September 2018

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4 September 2018

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4 September 2018

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4 September 2018

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Replica Temperatures for Uniform Exchange and Efficient Roundtrip Times in Explicit Solvent Parallel Tempering Simulations

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Examining the zinc binding site of the amyloid-beta peptide

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12 December 2020

Zinc Lowers Amyloid-β Toxicity by Selectively Precipitating Aggregation Intermediates†

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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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Identifiers

DOI

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:22674434%20AND%20SRC:MED&resulttype=core&format=json

3 February 2020

1 reference

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3 February 2020

PubMed publication ID

22674434

1 reference

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