Evidence map›Paper›PMID 27410735›Full record

ArticleBiophysical journal2016

Structure Change from β-Strand and Turn to α-Helix in Histone H2A-H2B Induced by DNA Damage Response.

Yudai Izumi, Kentaro Fujii, Frank Wien, Chantal Houée-Lévin, Sandrine Lacombe, Daniela Salado-Leza, Erika Porcel, Rawand Masoud, Satoshi Yamamoto, Matthieu Réfrégiers and 2 more

Abstract read
In one paragraph

Article in Biophysical journal, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
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

4 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. 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

12 authors.

Yudai IzumiQuantum Beam Science Center, Japan Atomic Energy Agency, Ibaraki, Japan. Electronic address: izumi-yudai@hiroshima-u.ac.jp.
Kentaro FujiiQuantum Beam Science Center, Japan Atomic Energy Agency, Ibaraki, Japan.
Frank WienSynchrotron SOLEIL, Gif-sur-Yvette, France.
Chantal Houée-LévinLaboratoire de Chimie Physique, CNRS UMR 8000, Université Paris Sud, Université Paris Saclay, Orsay, France.
Sandrine LacombeInstitut des Sciences Moléculaires d'Orsay (ISMO), CNRS UMR 8214, Université Paris Sud, Université Paris Saclay, Orsay, France.
Daniela Salado-LezaInstitut des Sciences Moléculaires d'Orsay (ISMO), CNRS UMR 8214, Université Paris Sud, Université Paris Saclay, Orsay, France.
Erika PorcelInstitut des Sciences Moléculaires d'Orsay (ISMO), CNRS UMR 8214, Université Paris Sud, Université Paris Saclay, Orsay, France.
Rawand MasoudLaboratoire de Chimie Physique, CNRS UMR 8000, Université Paris Sud, Université Paris Saclay, Orsay, France.
Satoshi YamamotoGraduate School of Science and Engineering, Ibaraki University, Ibaraki, Japan.
Matthieu RéfrégiersSynchrotron SOLEIL, Gif-sur-Yvette, France.
Marie-Anne Hervé du PenhoatInstitut de Minéralogie, de Physique des Matériaux, et de Cosmochimie, Sorbonne Universités-UPMC Univ Paris 06, UMR CNRS 7590, MNHN, IRD UMR 206, Paris, France.
Akinari YokoyaQuantum Beam Science Center, Japan Atomic Energy Agency, Ibaraki, Japan; Graduate School of Science and Engineering, Ibaraki University, Ibaraki, Japan.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Using synchrotron radiation-based circular dichroism spectroscopy, we found that the DNA damage response induces an increase of α-helix structure and a decrease of β-strand and turn structures in histone H2A-H2B extracted from x-irradiated human HeLa cells. The structural alterations correspond to the assumption that an average of eight amino acid residues form new α-helix structures at 310 K. We propose the structural transition from β-strand and turn structures to an α-helix structure in H2A-H2B as a novel, to our knowledge, process involved in the DNA damage response.

Indexed as

DNA DamageHeLa CellsHistonesHumansProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandTemperatureUbiquitinationHistones

Identifiers

PMID27410735
PMCPMC4945303

What OpenQuestion holds

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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.