Evidence map›Paper›PMID 30542593›Full record

ArticleChemical science2018

Insight into wild-type and T1372E TET2-mediated 5hmC oxidation using

Hedieh Torabifard, G Andrés Cisneros

Abstract read
In one paragraph

Article in Chemical science, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing 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

28 citing papers in PubMed.

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  15. ALKBH5-mediated mClinical and translational medicine · 2023
    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

2 authors.

Hedieh TorabifardDepartment of Chemistry , Wayne State University , Detroit , MI 48202 , USA.ORCID 0000-0003-0687-6858
G Andrés CisnerosDepartment of Chemistry , University of North Texas , Denton , TX 76203 , USA . Email: andres@unt.edu.ORCID 0000-0001-6629-3430

Funding

Theory and Simulation of DNA Repair Enzymes; Mechanism, Structure and FunctionR01GM108583 · NIGMS · WAYNE STATE UNIVERSITY · PI CISNEROS, GERARDO ANDRES · 2014 to 2022
$2.9M
The mechanism and modulation of 5-methylcytosine oxidation by TET family enzymesR01GM118501 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI KOHLI, RAHUL MANU · 2017 to 2020
$1.2M
NIGMS NIH HHS R01 GM108583NIGMS NIH HHS R01 GM118501
6 · The paper itself

Abstract

Ten-eleven translocation 2 (TET2) is an Fe/α-ketoglutarate (α-KG) dependent enzyme that dealkylates 5-methylcytosine (5mC). The reaction mechanism involves a series of three sequential oxidations that convert 5mC to 5-hydroxy-methylcytosine (5hmC), 5-formylcytosine (5fC) and 5-carboxylcytosine (5caC). Our previous biochemical and computational studies uncovered an active site scaffold that is required for wild-type (WT) stepwise oxidation (

Identifiers

PMID30542593
PMCPMC6244454

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.