Evidence map›Paper›PMID 23936011›Full record

ArticlePloS one2013

Glycogen phosphorylase inhibitor N-(3,5-dimethyl-Benzoyl)-N'-(β-D-glucopyranosyl)urea improves glucose tolerance under normoglycemic and diabetic conditions and rearranges hepatic metabolism.

Lilla Nagy, Tibor Docsa, Magdolna Szántó, Attila Brunyánszki, Csaba Hegedűs, Judit Márton, Bálint Kónya, László Virág, László Somsák, Pál Gergely and 1 more

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2013. 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
4.1field-weighted citation impact, top 7% 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, 45 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

11 authors at 2 institutions in 1 country.

Lilla NagyDepartment of Medical Chemistry, University of Debrecen Medical and Health Science Center, Debrecen, Hungary.
Tibor Docsa
Magdolna Szántó
Attila Brunyánszki
Csaba Hegedűs
Judit Márton
Bálint Kónya
László Virág
László Somsák
Pál Gergely
Péter Bai
University of Debrecen · HUHungarian Academy of Sciences · HU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glycogen phosphorylase (GP) catalyzes the breakdown of glycogen and largely contributes to hepatic glucose production making GP inhibition an attractive target to modulate glucose levels in diabetes. Hereby we present the metabolic effects of a novel, potent, glucose-based GP inhibitor (KB228) tested in vitro and in vivo under normoglycemic and diabetic conditions. KB228 administration enhanced glucose sensitivity in chow-fed and obese, diabetic mice that was a result of higher hepatic glucose uptake. Besides improved glucose sensitivity, we have observed further unexpected metabolic rearrangements. KB228 administration increased oxygen consumption that was probably due to the overexpression of uncoupling protein-2 (UCP2) that was observed in animal and cellular models. Furthermore, KB228 treatment induced mammalian target of rapamycin complex 2 (mTORC2) in mice. Our data demonstrate that glucose based GP inhibitors are capable of reducing glucose levels in mice under normo and hyperglycemic conditions. Moreover, these GP inhibitors induce accommodation in addition to GP inhibition--such as enhanced mitochondrial oxidation and mTORC2 signaling--to cope with the glucose influx and increased glycogen deposition in the cells, however the molecular mechanism of accommodation is unexplored.

Indexed as

AnimalsDiabetes Mellitus, ExperimentalEnzyme InhibitorsGene ExpressionGlucoseGlucose Tolerance TestGlycogen PhosphorylaseIon ChannelsLiverLiver GlycogenMaleMechanistic Target of Rapamycin Complex 2MiceMice, ObeseMitochondrial ProteinsMultiprotein ComplexesEnzyme InhibitorsGlucoseGlycogen PhosphorylaseIon ChannelsLiver GlycogenMechanistic Target of Rapamycin Complex 2Mitochondrial ProteinsMultiprotein ComplexesTOR Serine-Threonine KinasesUcp2 protein, mouseUncoupling Protein 2Urea

Identifiers

PMID23936011
PMCPMC3723905
OpenAlexW1990910948

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.