Evidence map›Paper›PMID 34554340›Full record

ArticleJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry2021

Dual roles of tau R peptides on Cu(II)/(I)-mediated reactive oxygen species formation.

Camilla Golec, Shaelyn Mortensen, Saba Anwar, Sanela Martic-Milne

Abstract read
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In one paragraph

Article in Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.5field-weighted citation impact, top 37% 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

2 citing papers in PubMed, 5 citations in OpenAlex.

  1. Review
  2. Role of the Cysteine in R3 Tau Peptide in Copper Binding and Reactivity.International journal of molecular sciences · 2022
    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

4 authors at 2 institutions in 2 countries.

Camilla GolecDepartment of Forensic Science, Environmental and Life Science Program, Trent University, Peterborough, ON, Canada.
Shaelyn MortensenDepartment of Forensic Science, Environmental and Life Science Program, Trent University, Peterborough, ON, Canada.
Saba AnwarDepartment of Chemistry, Oakland University, Rochester, MI, USA.
Sanela Martic-MilneDepartment of Forensic Science, Environmental and Life Science Program, Trent University, Peterborough, ON, Canada. sanelamartic@trentu.ca.ORCID 0000-0001-6642-2298
Trent University · CAOakland University · US

Funding

NIGMS NIH HHS R15GM11905301
6 · The paper itself

Abstract

Metal dyshomeostasis plays a critical role in the reactive oxygen species (ROS) formation and protein misfolding and aggregation; hence, contributing to neurodegeneration. Tau protein plays a key role in normal cellular function by maintaining microtubule formation in brain. The role of metal ions on tau protein biochemistry has not been systematically evaluated, but earlier reports indicated that metal ions modulate the complex biochemistry of this protein and its peptides. Herein, we evaluated interactions of biologically-relevant Cu(II) ions with the four repeat peptides of tau protein (R1 through R4) and their role on the formation of ROS, Cu(II) to Cu(I) reduction, and ultimately, peptide aggregation. The role of R peptides on ROS formation was characterized in the absence and presence of biological reducing agent, ascorbate by using UV-Vis and fluorescence spectroscopy. In the presence of the reducing agent, all Cu(II)-peptide complexes reduced hydroxyl radical (OH·), while only Cu(II)-R3 complex depleted the hydrogen peroxide (H

Indexed as

Hydrogen Peroxidetau ProteinsAmyloid beta-PeptidesCopperPeptidesReactive Oxygen SpeciesAmyloid beta-PeptidesCopperHydrogen PeroxidePeptidesReactive Oxygen Speciestau ProteinsAggregationMetal ionsNeurodegenerationReactive oxygen speciesTau peptide

Identifiers

PMID34554340
OpenAlexW3200252567

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.