Evidence map›Paper›PMID 33065111›Full record

ArticleJournal of molecular biology2020

Enzymatic Hydroxylation and Excision of Extended 5-Methylcytosine Analogues.

Miglė Tomkuvienė, Diana Ikasalaitė, Anton Slyvka, Audronė Rukšėnaitė, Mirunalini Ravichandran, Tomasz P Jurkowski, Matthias Bochtler, Saulius Klimašauskas

Open access · hybridAbstract read
In one paragraph

Article in Journal of molecular biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.5field-weighted citation impact, top 37% 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

5 citing papers in PubMed, 7 citations in OpenAlex.

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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

8 authors at 5 institutions in 4 countries.

Miglė TomkuvienėInstitute of Biotechnology, Life Sciences Center, Vilnius University, Vilnius LT-10257, Lithuania.
Diana IkasalaitėInstitute of Biotechnology, Life Sciences Center, Vilnius University, Vilnius LT-10257, Lithuania.
Anton SlyvkaInternational Institute of Molecular and Cell Biology, 02-109 Warsaw, Poland.
Audronė RukšėnaitėInstitute of Biotechnology, Life Sciences Center, Vilnius University, Vilnius LT-10257, Lithuania.
Mirunalini RavichandranSchool of Medicine, University of California, San Francisco, CA 94143, USA.
Tomasz P JurkowskiSchool of Biosciences, Cardiff University, CF10 3AX Cardiff, Wales, UK.
Matthias BochtlerInternational Institute of Molecular and Cell Biology, 02-109 Warsaw, Poland; Polish Academy of Sciences, Institute of Biochemistry and Biophysics, 02-106 Warsaw, Poland.
Saulius KlimašauskasInstitute of Biotechnology, Life Sciences Center, Vilnius University, Vilnius LT-10257, Lithuania. Electronic address: saulius.klimasauskas@bti.vu.lt.
Vilnius University · LTCardiff University · GBInstitute of Biochemistry and Biophysics, Polish Academy of Sciences · PLInternational Institute of Molecular and Cell Biology · PLUniversity of California, San Francisco · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Methylation of cytosine to 5-methylcytosine (mC) is a prevalent reversible epigenetic mark in vertebrates established by DNA methyltransferases (MTases); the methylation mark can be actively erased via a multi-step demethylation mechanism involving oxidation by Ten-eleven translocation (TET) enzyme family dioxygenases, excision of the latter oxidation products by thymine DNA (TDG) or Nei-like 1 (NEIL1) glycosylases followed by base excision repair to restore the unmodified state. Here we probed the activity of the mouse TET1 (mTET1) and Naegleria gruberi TET (nTET) oxygenases with DNA substrates containing extended derivatives of the 5-methylcytosine carrying linear carbon chains and adjacent unsaturated CC bonds. We found that the nTET and mTET1 enzymes were active on modified mC residues in single-stranded and double-stranded DNA in vitro, while the extent of the reactions diminished with the size of the extended group. Iterative rounds of nTET hydroxylations of ssDNA proceeded with high stereo specificity and included not only the natural alpha position but also the adjoining carbon atom in the extended side chain. The regioselectivity of hydroxylation was broken when the reactive carbon was adjoined with an sp

Indexed as

5-MethylcytosineAnimalsCytosineDNADNA-Binding ProteinsDNA GlycosylasesDNA MethylationDNA RepairHumansHydroxylationMiceNaegleriaOxidation-ReductionProto-Oncogene Proteins5-MethylcytosineCytosineDNADNA-Binding ProteinsDNA GlycosylasesNeil1 protein, mouseProto-Oncogene ProteinsTET1 protein, mouseDNA cytosine-5 methylationDNA glycosylaseepigenetic regulationradical intermediateTET dioxygenase

Identifiers

PMID33065111
PMCPMC7763475
OpenAlexW3092801113

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.