Evidence map›Paper›PMID 21871906›Full record

ReviewMutation research2012

Biotin requirements for DNA damage prevention.

Janos Zempleni, Daniel Camara Teixeira, Toshinobu Kuroishi, Elizabeth L Cordonier, Scott Baier

Open access · greenAbstract readReview
In one paragraph

Review in Mutation research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.4field-weighted citation impact, top 22% 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

15 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Review
  6. Article
  7. Genomic Insights intoJournal of microbiology and biotechnology · 2023
    Article
  8. Review
  9. Review
  10. Article
  11. Nutritional status of patients with phenylketonuria in Japan.Molecular genetics and metabolism reports · 2016
    Article
  12. Article
  13. Review
  14. Article
  15. 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

5 authors at 1 institution in 1 country.

Janos ZempleniDepartment of Nutrition and Health Sciences, University of Nebraska-Lincoln, 316 Ruth Leverton Hall, Lincoln, NE 68583-0806, USA. jzempleni2@unl.edu
Daniel Camara Teixeira
Toshinobu Kuroishi
Elizabeth L Cordonier
Scott Baier
University of Nebraska–Lincoln · US

Funding

Vitamin-dependent modifications of histonesR01DK063945 · NIDDK · UNIVERSITY OF NEBRASKA LINCOLN · PI ZEMPLENI, JANOS · 2004 to 2011
$2.3M
Biotin sensing and chromatin remodeling by holocarboxylase synthetaseR01DK077816 · NIDDK · UNIVERSITY OF NEBRASKA LINCOLN · PI ZEMPLENI, JANOS · 2009 to 2011
$861k
Novel histone biotinylation sites and relationships to other epigenetic marksR21DK082476 · NIDDK · UNIVERSITY OF NEBRASKA LINCOLN · PI CHANG, YIE-HWA, EISSENBERG, JOEL C · 2009 to 2010
$535k
Epigenetic effects of biotin on activation of endogenous viral sequencesR21ES015206 · NIEHS · UNIVERSITY OF NEBRASKA LINCOLN · PI ZEMPLENI, JANOS · 2006 to 2007
$396k
NIDDK NIH HHS DK063945NIDDK NIH HHS DK077816NIDDK NIH HHS DK082476NIDDK NIH HHS R01 DK063945NIDDK NIH HHS R01 DK077816NIDDK NIH HHS R21 DK082476NIEHS NIH HHS ES015206NIEHS NIH HHS R21 ES015206
6 · The paper itself

Abstract

Biotin serves as a covalently bound coenzyme in five human carboxylases; biotin is also attached to histones H2A, H3, and H4, although the abundance of biotinylated histones is low. Biotinylation of both carboxylases and histones is catalyzed by holocarboxylase synthetase. Human biotin requirements are unknown. Recommendations for adequate intake of biotin are based on the typical intake of biotin in an apparently healthy population, which is only a crude estimate of the true intake due to analytical problems. Importantly, intake recommendations do not take into account possible effects of biotin deficiency on impairing genome stability. Recent studies suggest that biotin deficiency causes de-repression of long terminal repeats, thereby causing genome instability. While it was originally proposed that these effects are caused by loss of biotinylated histones, more recent evidence suggests a more immediate role of holocarboxylase synthetase in forming multiprotein complexes in chromatin that are important for gene repression. Holocarboxylase synthetase appears to interact physically with the methyl-CpG-binding domain protein 2 and, perhaps, histone methyl transferases, thereby creating epigenetic synergies between biotinylation and methylation events. These observations might offer a mechanistic explanation for some of the birth defects seen in biotin-deficient animal models.

Indexed as

DNA DamageBiotinBiotinylationGenomic InstabilityHumansNutritional RequirementsTerminal Repeat SequencesBiotin

Identifiers

PMID21871906
PMCPMC3228911
OpenAlexW1993878784

What OpenQuestion holds

Textmetadata
LicenceTDM
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.