Evidence map›Paper›PMID 21203933›Full record

ReviewProtein & cell2010

A loop matters for FTO substrate selection.

Zhifu Han, Ning Huang, Tianhui Niu, Jijie Chai

Open access · bronzeAbstract readReview
In one paragraph

Review in Protein & cell, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.1field-weighted citation impact, top 45% 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

6 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
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  4. Review
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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

4 authors at 2 institutions in 1 country.

Zhifu HanNational Institute of Biological Sciences, No. 7 Science Park Road, Beijing, 102206, China.
Ning Huang
Tianhui Niu
Jijie Chai
National Institute of Biological Sciences, Beijing · CNTsinghua University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Recent studies have unequivocally established the link between FTO and obesity. FTO was biochemically shown to belong to the AlkB-like family DNA/RNA demethylase. However, FTO differs from other AlkB members in that it has unique substrate specificity and contains an extended C-terminus with unknown functions. Insight into the substrate selection mechanism and a functional clue to the C-terminus of FTO were gained from recent structural and biochemical studies. These data would be valuable to design FTO-specific inhibitors that can be potentially translated into therapeutic agents for treatment of obesity or obesity-related diseases.

Indexed as

AlkB Homolog 1, Histone H2a DioxygenaseAlpha-Ketoglutarate-Dependent Dioxygenase FTOAmino Acid MotifsAnimalsCatalytic DomainDNADNA Repair EnzymesHumansMethylationObesityProteinsRNASubstrate SpecificityALKBH1 protein, humanAlkB Homolog 1, Histone H2a DioxygenaseAlpha-Ketoglutarate-Dependent Dioxygenase FTODNADNA Repair EnzymesFTO protein, humanProteinsRNA

Identifiers

PMID21203933
PMCPMC4875277
OpenAlexW2137662259

What OpenQuestion holds

Textmetadata
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.