Evidence map›Paper›PMID 26321891›Full record

ArticleClinical proteomics2015

Proteomic profiling identifies specific histone species associated with leukemic and cancer cells.

Rajbir Singh, Sean W Harshman, Amy S Ruppert, Amir Mortazavi, David M Lucas, Jennifer M Thomas-Ahner, Steven K Clinton, John C Byrd, Michael A Freitas, Mark R Parthun

Open access · goldAbstract read
In one paragraph

Article in Clinical proteomics, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

12 citing papers in PubMed, 22 citations in OpenAlex.

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  10. An inhibitor screen identifies histone-modifying enzymes as mediators of polymer-mediated transgene expression from plasmid DNA.Journal of controlled release : official journal of the Controlled Release Society · 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

10 authors at 1 institution in 1 country.

Rajbir SinghDepartment of Biological Chemistry and Pharmacology, The Ohio State University, Columbus, OH 43210 USA.
Sean W HarshmanDepartment of Molecular Virology, Immunology and Medical Genetics, The Ohio State University, Columbus, OH 43210 USA.
Amy S RuppertDepartment of Internal Medicine, The Ohio State University, Columbus, OH 43210 USA.
Amir MortazaviDepartment of Internal Medicine, The Ohio State University, Columbus, OH 43210 USA.
David M LucasDepartment of Internal Medicine, The Ohio State University, Columbus, OH 43210 USA ; Division of Medicinal Chemistry in the College of Pharmacy, The Ohio State University, Columbus, OH 43210 USA.
Jennifer M Thomas-AhnerDepartment of Internal Medicine, The Ohio State University, Columbus, OH 43210 USA.
Steven K ClintonDepartment of Internal Medicine, The Ohio State University, Columbus, OH 43210 USA.
John C ByrdDepartment of Internal Medicine, The Ohio State University, Columbus, OH 43210 USA.
Michael A FreitasDepartment of Molecular Virology, Immunology and Medical Genetics, The Ohio State University, Columbus, OH 43210 USA.
Mark R ParthunDepartment of Biological Chemistry and Pharmacology, The Ohio State University, Columbus, OH 43210 USA.
The Ohio State University · US

Funding

PathologyP01CA101956 · NCI · OHIO STATE UNIVERSITY · PI BYRD, JOHN C. · 2006 to 2010
$11.4M
Type B Histone Acetyltransferases and the Assembly of Chromatin StructureR01GM062970 · NIGMS · OHIO STATE UNIVERSITY · PI PARTHUN, MARK R · 2001 to 2018
$5.1M
Assays for Screening Histone Modifications in CancerR01CA107106 · NCI · OHIO STATE UNIVERSITY · PI FREITAS, MICHAEL A. · 2004 to 2013
$1.8M
Assays for Screening Histone Modificaitons in CancerR56CA107106 · NCI · OHIO STATE UNIVERSITY · PI FREITAS, MICHAEL A. · 2009 to 2009
$231k
NCI NIH HHS P01 CA101956NCI NIH HHS R01 CA107106NCI NIH HHS R56 CA107106NIGMS NIH HHS R01 GM062970
6 · The paper itself

Abstract

backgroundChromatin is an extraordinarily complex structure. Much of this complexity results from the presence of numerous histone post-translational modifications and histone variants. Alterations in the patterns of histone post-translational modifications are emerging as a feature of many types of cancer and have been shown to have prognostic value.

resultsWe have applied a liquid chromatography/mass spectrometry-based approach to comprehensively characterize the histone proteome in primary samples from chronic lymphocytic leukemia (CLL) patients, as well as bladder and breast cancer cell culture models. When compared to non-malignant CD19+ B cells from healthy donors, the CLL histone proteome showed a distinct signature of differentially expressed species, spanning all the histones studied and including both post-translationally modified species and unmodified, non-allelic replication-dependent histone isoforms. However, the large changes in histone H3 and H4 that are characteristic of many cancer types were not observed. One of species of H2A (mass = 14,063 Da) was the most strongly associated with time to treatment in CLL patients. CLL patient samples also demonstrated histone profiles that were distinct from those of the bladder and breast cancer cells.

conclusionsSignatures of histone profiles are complex and can distinguish between healthy individuals and CLL patients and may provide prognostic markers. In addition, histone profiles may define tissue specific malignancies.

Indexed as

ChromatinChronic lymphocytic leukemiaHistonePost-translational modification

Identifiers

PMID26321891
PMCPMC4551702
OpenAlexW1945214118

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.