Evidence map›Paper›PMID 25014537›Full record

ArticleThe journal of physical chemistry. B2014

ESEEM analysis of multi-histidine Cu(II)-coordination in model complexes, peptides, and amyloid-β.

K Ishara Silva, Brian C Michael, Steven J Geib, Sunil Saxena

Abstract readValidation Study
In one paragraph

Article in The journal of physical chemistry. B, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
2.1field-weighted citation impact, top 12% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

22 citing papers in PubMed, 64 citations in OpenAlex.

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  7. Endogenous Cu(II) Labeling for Distance Measurements on Proteins by EPR.Chemistry (Weinheim an der Bergstrasse, Germany) · 2024
    Article
  8. EPR spectroscopic characterisation of native CuDalton transactions (Cambridge, England : 2003) · 2024
    Article
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  13. A newJournal of magnetic resonance (San Diego, Calif. : 1997) · 2023
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  18. CuProceedings of the National Academy of Sciences of the United States of America · 2018
    Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

K Ishara SilvaDepartment of Chemistry, University of Pittsburgh , Pittsburgh, Pennsylvania 15260, United States.
Brian C Michael
Steven J Geib
Sunil Saxena
University of Pittsburgh · US

Funding

University of Pittsburgh Clinical and Translational Science InstituteUL1TR000005 · NCATS · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI REIS, STEVEN E · 2012 to 2015
$50.8M
Acquisition of a High Frequency Pulsed Electron Spin Resonance SpectrometerS10RR028701 · NCRR · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI SAXENA, SUNIL K · 2011 to 2011
$1.6M
NCATS NIH HHS UL1 TR000005NCRR NIH HHS 1S10RR028701NCRR NIH HHS S10 RR028701
6 · The paper itself

Abstract

We validate the use of ESEEM to predict the number of (14)N nuclei coupled to a Cu(II) ion by the use of model complexes and two small peptides with well-known Cu(II) coordination. We apply this method to gain new insight into less explored aspects of Cu(II) coordination in amyloid-β (Aβ). Aβ has two coordination modes of Cu(II) at physiological pH. A controversy has existed regarding the number of histidine residues coordinated to the Cu(II) ion in component II, which is dominant at high pH (∼8.7) values. Importantly, with an excess amount of Zn(II) ions, as is the case in brain tissues affected by Alzheimer's disease, component II becomes the dominant coordination mode, as Zn(II) selectively substitutes component I bound to Cu(II). We confirm that component II only contains single histidine coordination, using ESEEM and set of model complexes. The ESEEM experiments carried out on systematically (15)N-labeled peptides reveal that, in component II, His 13 and His 14 are more favored as equatorial ligands compared to His 6. Revealing molecular level details of subcomponents in metal ion coordination is critical in understanding the role of metal ions in Alzheimer's disease etiology.

Indexed as

Models, MolecularAmyloid beta-PeptidesCopperHistidineImidazolesNitrogenPeptide FragmentsPeptidesSpectrum AnalysisX-Ray DiffractionZincAmyloid beta-Peptidesamyloid beta-protein (1-16)CopperHistidineImidazolesNitrogenPeptide FragmentsPeptidesZinc

Identifiers

PMID25014537
PMCPMC4120975
OpenAlexW2323101181

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.