Evidence map›Paper›PMID 26343042›Full record

ArticleChromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology2015

Distribution of histone H4 modifications as revealed by a panel of specific monoclonal antibodies.

Yoko Hayashi-Takanaka, Kazumitsu Maehara, Akihito Harada, Takashi Umehara, Shigeyuki Yokoyama, Chikashi Obuse, Yasuyuki Ohkawa, Naohito Nozaki, Hiroshi Kimura

Open access · hybridAbstract read
In one paragraph

Article in Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

34 citing papers in PubMed, 57 citations in OpenAlex.

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  18. Live-cell epigenome manipulation by synthetic histone acetylation catalyst system.Proceedings of the National Academy of Sciences of the United States of America · 2021
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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

9 authors at 4 institutions in 1 country.

Yoko Hayashi-TakanakaGraduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama, 226-8501, Japan.
Kazumitsu MaeharaDepartment of Advanced Medical Initiatives, Faculty of Medicine, Kyushu University, Fukuoka, 812-8582, Japan.
Akihito HaradaDepartment of Advanced Medical Initiatives, Faculty of Medicine, Kyushu University, Fukuoka, 812-8582, Japan.
Takashi UmeharaRIKEN Center for Life Science Technologies, Yokohama, 230-0045, Japan.
Shigeyuki YokoyamaRIKEN Structural Biology Laboratory, Yokohama, 230-0045, Japan.
Chikashi ObuseSchool of Life Sciences, Hokkaido University, Sapporo, 001-0021, Japan.
Yasuyuki OhkawaCREST, JST, Kawaguchi, Saitama, 332-0012, Japan.
Naohito NozakiMAB Institute Inc, Sapporo, 001-0021, Japan.
Hiroshi KimuraGraduate School of Bioscience and Biotechnology, Tokyo Institute of Technology, 4259 Nagatsuta, Midori-ku, Yokohama, 226-8501, Japan. hkimura@bio.titech.ac.jp.ORCID http://orcid.org/0000-0003-0854-083X
Kyushu University · JPTokyo Institute of Technology · JPHokkaido University · JPRIKEN · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Post-translational histone modifications play a critical role in genome functions such as epigenetic gene regulation and genome maintenance. The tail of the histone H4 N-terminus contains several amino acids that can be acetylated and methylated. Some of these modifications are known to undergo drastic changes during the cell cycle. In this study, we generated a panel of mouse monoclonal antibodies against histone H4 modifications, including acetylation at K5, K8, K12, and K16, and different levels of methylation at K20. Their specificity was evaluated by ELISA and immunoblotting using synthetic peptide and recombinant proteins that harbor specific modifications or amino acid substitutions. Immunofluorescence confirmed the characteristic distributions of target modifications. An H4K5 acetylation (H4K5ac)-specific antibody CMA405 reacted with K5ac only when the neighboring K8 was unacetylated. This unique feature allowed us to detect newly assembled H4, which is diacetylated at K5 and K12, and distinguish it from hyperacetylated H4, where K5 and K8 are both acetylated. Chromatin immunoprecipiation combined with deep sequencing (ChIP-seq) revealed that acetylation of both H4K8 and H4K16 were enriched around transcription start sites. These extensively characterized and highly specific antibodies will be useful for future epigenetics and epigenome studies.

Indexed as

Antibodies, MonoclonalProtein Processing, Post-TranslationalAcetylationAnimalsBlotting, WesternCell Line, TransformedChromatinChromatin ImmunoprecipitationEpigenesis, GeneticHeLa CellsHigh-Throughput Nucleotide SequencingHistonesHumansImmunoglobulin GImmunohistochemistryMethylationAntibodies, MonoclonalChromatinHistonesImmunoglobulin GChromatinEpigeneticsHistone modificationMonoclonal antibody

Identifiers

PMID26343042
PMCPMC4666908
OpenAlexW2143756108

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.