Evidence map›Paper›PMID 26199864›Full record

ArticleFEBS open bio2015

Histone H3 Ser57 and Thr58 phosphorylation in the brain of 5XFAD mice.

Kyle W Anderson, Natalia Mast, Irina A Pikuleva, Illarion V Turko

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in FEBS open bio, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

14 citing papers in PubMed, 22 citations in OpenAlex.

  1. Review
  2. Review
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  5. Review
  6. Review
  7. Article
  8. Article
  9. Review
  10. Alcohol Extracts FromFrontiers in pharmacology · 2019
    Article
  11. Article
  12. Article
  13. Article
  14. Epigenetic Alterations in Alzheimer's Disease.Frontiers in behavioral neuroscience · 2015
    Review
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 3 institutions in 1 country.

Kyle W AndersonInstitute for Bioscience and Biotechnology Research, Rockville, MD 20850, USA ; Biomolecular Measurement Division, National Institute of Standards and Technology, Gaithersburg, MD 20899, USA ; Department of Chemistry and Biochemistry, University of Maryland, College Park, MD 20742, USA.
Natalia MastDepartment of Ophthalmology and Visual Sciences, Case Western Reserve University, Cleveland, OH 44106, USA.
Irina A PikulevaDepartment of Ophthalmology and Visual Sciences, Case Western Reserve University, Cleveland, OH 44106, USA.
Illarion V TurkoInstitute for Bioscience and Biotechnology Research, Rockville, MD 20850, USA ; Biomolecular Measurement Division, National Institute of Standards and Technology, Gaithersburg, MD 20899, USA.
Case Western Reserve University · USNational Institute of Standards and Technology · USUniversity of Maryland, College Park · US

Funding

TISSUE CULTURE AND HYBRIDOMA MODULEP30EY011373 · NEI · CASE WESTERN RESERVE UNIVERSITY · PI Irina A Pikuleva · 1997 to 2026
$17.7M
Structure and function of cholesterol metabolizing P450sR01GM062882 · NIGMS · UNIVERSITY OF TEXAS MEDICAL BR GALVESTON · PI PIKULEVA, IRINA A · 2001 to 2019
$5.5M
NEI NIH HHS P30 EY011373NIGMS NIH HHS R01 GM062882
6 · The paper itself

Abstract

Alzheimer's disease has been shown to have a global reduction in gene expression, called an epigenetic blockade, which may be regulated by histone post-translational modifications. Histone H3 has been shown to be highly regulated by phosphorylation. We, therefore, chose H3 for investigation of phosphorylation of the core sites serine-57 (S57) and threonine-58 (T58). Hemispheres of brains from a mouse model of rapid amyloid deposition (5XFAD) were used for measurement of S57 and T58 phosphorylation. Multiple reaction monitoring (MRM) was used to measure the level of phosphorylation, which was normalized to a non-modified "housekeeping" peptide of H3. S57 phosphorylation was decreased by 40%, T58 phosphorylation was decreased by 45%, and doubly phosphorylated S57pT58p was decreased by 30% in 5XFAD brain in comparison to C57BL/6J age- and sex-matched wild type controls. Amyloid-β (Aβ) and amyloid precursor protein were also measured to confirm that 5XFAD mice produced high levels of Aβ. Decreased phosphorylation of these sites in close proximity to DNA may lead to stabilization of DNA-histone interactions and a condensed chromatin state, consistent with the epigenetic blockade associated with AD. Our findings of H3 sites S57 and T58 exhibiting lower levels of phosphorylation in 5XFAD model compared to wild type control implicate these sites in the epigenetic blockade in neurodegeneration pathology.

Indexed as

5XFADAlzheimer’s diseaseAPP, amyloid precursor proteinAβ, amyloid-βHistoneMRM, multiple reaction monitoringMultiple reaction monitoringPhosphorylationPTM, post-translational modificationS57, serine-57T58, threonine-58

Identifiers

PMID26199864
PMCPMC4506931
OpenAlexW800443036

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.