Evidence map›Paper›PMID 21510664›Full record

ArticleBiochemistry2011

Histone demethylase LSD1 is a folate-binding protein.

Zigmund Luka, Frank Moss, Lioudmila V Loukachevitch, Darryl J Bornhop, Conrad Wagner

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2011. 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
1.5field-weighted citation impact, top 20% 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.

  1. Review
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  5. Subcellular one carbon metabolism in cancer, aging and epigenetics.Frontiers in epigenetics and epigenomics · 2024
    Article
  6. Formaldehyde regulatesScience (New York, N.Y.) · 2023
    Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Distinct RNAProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  14. Review
  15. 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

5 authors at 1 institution in 1 country.

Zigmund LukaDepartment of Biochemistry, Vanderbilt University Medical Center, Nashville, TN 37232, USA.
Frank Moss
Lioudmila V Loukachevitch
Darryl J Bornhop
Conrad Wagner
Vanderbilt University Medical Center · US

Funding

TISSUE STORES OF FOLATE: DIETARY CONTROL AND ASSAYR01DK015289 · NIDDK · VANDERBILT UNIVERSITY · PI WAGNER, CONRAD · 1987 to 2013
$3.1M
Folate and S-adenosyimethionine in Methyl Group and One-carbon MetabolismR01DK080010 · NIDDK · VANDERBILT UNIVERSITY · PI WAGNER, CONRAD · 2009 to 2012
$1.4M
TISSUE STORES OF FOLATE: DIETARY CONTROL AND ASSAYR37DK015289 · NIDDK · VANDERBILT UNIVERSITY · PI WAGNER, CONRAD · 1995 to 2002
$620k
NIDDK NIH HHS DK080010NIDDK NIH HHS DK15289NIDDK NIH HHS R01 DK015289NIDDK NIH HHS R01 DK080010NIDDK NIH HHS R37 DK015289
6 · The paper itself

Abstract

Methylation of lysine residues in histones has been known to serve a regulatory role in gene expression. Although enzymatic removal of the methyl groups was discovered as early as 1973, the enzymes responsible for their removal were isolated and their mechanism of action was described only recently. The first enzyme to show such activity was LSD1, a flavin-containing enzyme that removes the methyl groups from lysines 4 and 9 of histone 3 with the generation of formaldehyde from the methyl group. This reaction is similar to the previously described demethylation reactions conducted by the enzymes dimethylglycine dehydrogenase and sarcosine dehydrogenase, in which protein-bound tetrahydrofolate serves as an accepter of the formaldehyde that is generated. We now show that nuclear extracts of HeLa cells contain LSD1 that is associated with folate. Using the method of back-scattering interferometry, we have measured the binding of various forms of folate to both full-length LSD1 and a truncated form of LSD1 in free solution. The 6R,S form of the natural pentaglutamate form of tetrahydrofolate bound with the highest affinity (K(d) = 2.8 μM) to full-length LSD1. The fact that folate participates in the enzymatic demethylation of histones provides an opportunity for this micronutrient to play a role in the epigenetic control of gene expression.

Indexed as

Chromatography, GelFolic AcidHeLa CellsHistone DemethylasesHumansFolic AcidHistone DemethylasesKDM1A protein, human

Identifiers

PMID21510664
PMCPMC3111596
OpenAlexW1968878794

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.