Evidence map›Paper›PMID 24980953›Full record

ArticleJournal of inorganic biochemistry2014

Metal-binding and redox properties of substituted linear and cyclic ATCUN motifs.

Kosh P Neupane, Amanda R Aldous, Joshua A Kritzer

Open access · greenAbstract read
In one paragraph

Article in Journal of inorganic biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.6field-weighted citation impact, top 15% 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

18 citing papers in PubMed, 43 citations in OpenAlex.

  1. Impact of the spatial distribution of positive charges on the catalytic activity of NiSOD bioinspired complexes.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2026
    Article
  2. DNA Scission by Non-Histidine Amino-Terminal Cu(II) and Ni(II) Binding-Like Peptides.Chembiochem : a European journal of chemical biology · 2026
    Article
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  10. Review
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  13. The effect of an engineered ATCUN motif on the structure and biophysical properties of the SH3 domain of c-Src tyrosine kinase.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2020
    Article
  14. Article
  15. Review
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  17. Copper trafficking to the secretory pathway.Metallomics : integrated biometal science · 2016
    Review
  18. Article
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

3 authors at 1 institution in 1 country.

Kosh P NeupaneDepartment of Chemistry, Tufts University, 62 Talbot Avenue, Medford, MA 02155, USA.
Amanda R AldousDepartment of Chemistry, Tufts University, 62 Talbot Avenue, Medford, MA 02155, USA.
Joshua A KritzerDepartment of Chemistry, Tufts University, 62 Talbot Avenue, Medford, MA 02155, USA. Electronic address: joshua.kritzer@tufts.edu.
Tufts University · US

Funding

Rapid Generation of Isoform-Selective Histone Deacetylase InhibitorsR21AG038776 · NIA · TUFTS UNIVERSITY MEDFORD · PI KRITZER, JOSHUA A · 2011 to 2012
$349k
NIA NIH HHS R21 AG038776NIA NIH HHS R21AG038776
6 · The paper itself

Abstract

The amino-terminal copper and nickel binding (ATCUN) motif is a short peptide sequence found in human serum albumin and other proteins. Synthetic ATCUN-metal complexes have been used to oxidatively cleave proteins and DNA, cross-link proteins, and damage cancer cells. The ATCUN motif consists of a tripeptide that coordinates Cu(II) and Ni(II) ions in a square planar geometry, anchored by chelation sites at the N-terminal amine, histidine imidazole and two backbone amides. Many studies have shown that the histidine is required for tight binding and square planar geometry. Previously, we showed that macrocyclization of the ATCUN motif can lead to high-affinity binding with altered metal ion selectivity and enhanced Cu(II)/Cu(III) redox cycling (Inorg. Chem. 2013, 52, 2729-2735). In this work, we synthesize and characterize several linear and cyclic ATCUN variants to explore how substitutions at the histidine alter the metal-binding and catalytic properties. UV-visible spectroscopy, EPR spectroscopy and mass spectrometry indicate that cyclization can promote the formation of ATCUN-like complexes even in the absence of imidazole. We also report several novel ATCUN-like complexes and quantify their redox properties. These findings further demonstrate the effects of conformational constraints on short, metal-binding peptides, and also provide novel redox-active metallopeptides suitable for testing as catalysts for stereoselective or regioselective oxidation reactions.

Indexed as

AlbuminsAmino Acid MotifsCatalysisCopperHydrogen-Ion ConcentrationHydroxyl RadicalNickelOxidation-ReductionPeptide FragmentsPeptides, CyclicProtein BindingAlbuminsCopperHydroxyl RadicalNickelPeptide FragmentsPeptides, CyclicATCUNCatalysisCopperCyclic peptidesMetallopeptidesNickel

Identifiers

PMID24980953
PMCPMC4119837
OpenAlexW2082884547

What OpenQuestion holds

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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.