Evidence map›Paper›PMID 24601643›Full record

ArticleJournal of proteome research2014

Histone H1 phosphorylation in breast cancer.

Sean W Harshman, Michael E Hoover, Chengsi Huang, Owen E Branson, Sarah B Chaney, Carolyn M Cheney, Thomas J Rosol, Charles L Shapiro, Vicki H Wysocki, Kay Huebner and 1 more

Abstract read
In one paragraph

Article in Journal of proteome research, 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
1.9field-weighted citation impact, top 14% 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, 42 citations in OpenAlex.

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  11. Study on the Antibreast Cancer Mechanism and Bioactive Components ofEvidence-based complementary and alternative medicine : eCAM · 2020
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  19. Chromatographic efficiency and selectivity in top-down proteomics of histones.Journal of chromatography. B, Analytical technologies in the biomedical and life sciences · 2017
    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

11 authors at 1 institution in 1 country.

Sean W HarshmanDepartment of Molecular Virology, Immunology and Medical Genetics, ‡Comprehensive Cancer Center, §Department of Chemistry & Biochemistry, ⊥Veterinary Biosciences, College of Veterinary Medicine, and ∥Department of Internal Medicine, Division of Hematology, The Ohio State University , Columbus, Ohio 43210, United States.
Michael E Hoover
Chengsi Huang
Owen E Branson
Sarah B Chaney
Carolyn M Cheney
Thomas J Rosol
Charles L Shapiro
Vicki H Wysocki
Kay Huebner
Michael A Freitas
The Ohio State University · US

Funding

Translational Therapeutics Research Program (TT)P30CA016058 · NCI · OHIO STATE UNIVERSITY · PI Tasleem J Padamsee · 1985 to 2026
$132.3M
MicroRNA profiles of TN breast cancer to define subgroups and targets for therapyU01CA154200 · NCI · OHIO STATE UNIVERSITY · PI HUEBNER, KAY · 2010 to 2014
$2.3M
NCI NIH HHS CA154200NCI NIH HHS P30 CA016058NCI NIH HHS U01 CA154200
6 · The paper itself

Abstract

Breast cancer is the second leading cause of cancer-related deaths in women. The need for new clinical biomarkers in breast cancer is necessary to further predict prognosis and therapeutic response. In this article, the LC-MS histone H1 phosphorylation profiles were established for three distinct breast cancer cell lines. The results show that the extent of H1 phosphorylation can distinguish between the different cell lines. The histone H1 from the metastatic cell line, MDA-MB-231, was subjected to chemical derivitization and LC-MS/MS analysis. The results suggest that the phosphorylation at threonine 146 is found on both histone H1.2 and histone H1.4. Cell lines were then treated with an extracellular stimulus, estradiol or kinase inhibitor LY294002, to monitor changes in histone H1 phosphorylation. The data show that histone H1 phosphorylation can increase and decrease in response to extracellular stimuli. Finally, primary breast tissues were stained for the histone H1 phosphorylation at threonine 146. Variable staining patterns across tumor grades and subtypes were observed with pT146 labeling correlating with tumor grade. These results establish the potential for histone H1 phosphorylation at threonine 146 as a clinical biomarker in breast cancer.

Indexed as

Amino Acid SequenceBlotting, WesternBreast NeoplasmsCell LineCell Line, TumorChromatography, LiquidChromonesEnzyme InhibitorsEstradiolFemaleHistonesHumansImmunohistochemistryMass SpectrometryMCF-7 CellsMolecular Sequence Data2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-oneChromonesEnzyme InhibitorsEstradiolHistonesMorpholinesPhosphatidylinositol 3-KinasesPhosphoinositide-3 Kinase InhibitorsPhosphoproteinsProtein IsoformsThreonine

Identifiers

PMID24601643
PMCPMC4012839
OpenAlexW2314572326

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.