Evidence map›Paper›PMID 30644848›Full record

ArticleActa crystallographica. Section D, Structural biology2019

The crystal structure of the N-acetylglucosamine 2-epimerase from Nostoc sp. KVJ10 reveals the true dimer.

Marie Josée Haglund Halsør, Ulli Rothweiler, Bjørn Altermark, Inger Lin Uttakleiv Raeder

Open access · hybridAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Acta crystallographica. Section D, Structural biology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing papers in PubMed
0.5field-weighted citation impact, top 44% 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

1 citing paper in PubMed, 8 citations in OpenAlex.

  1. Article
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 1 institution in 1 country.

Marie Josée Haglund HalsørThe Norwegian Structural Biology Centre (NorStruct), Department of Chemistry, UiT - The Arctic University of Norway, 9037 Tromsø, Norway.
Ulli RothweilerThe Norwegian Structural Biology Centre (NorStruct), Department of Chemistry, UiT - The Arctic University of Norway, 9037 Tromsø, Norway.ORCID 0000-0003-2802-7558
Bjørn AltermarkThe Norwegian Structural Biology Centre (NorStruct), Department of Chemistry, UiT - The Arctic University of Norway, 9037 Tromsø, Norway.
Inger Lin Uttakleiv RaederThe Norwegian Structural Biology Centre (NorStruct), Department of Chemistry, UiT - The Arctic University of Norway, 9037 Tromsø, Norway.
NORCE Research AS · NO

Funding

Norges Forskningsråd 221568
6 · The paper itself

Abstract

N-Acetylglucosamine 2-epimerases (AGEs) catalyze the interconversion of N-acetylglucosamine and N-acetylmannosamine. They can be used to perform the first step in the synthesis of sialic acid from N-acetylglucosamine, which makes the need for efficient AGEs a priority. This study presents the structure of the AGE from Nostoc sp. KVJ10 collected in northern Norway, referred to as nAGE10. It is the third AGE structure to be published to date, and the first one in space group P4

Indexed as

Protein MultimerizationAcetylglucosamineCatalytic DomainChloridesCrystallography, X-RayHexosaminesNostocProtein ConformationRacemases and EpimerasesAcetylglucosamineChloridesHexosaminesN-acetylmannosamineRacemases and EpimerasesAGEcrystal packingGlcNAcManNAcN-acetylglucosamine 2-epimeraseN-acetylmannosamineNostoc sp. KVJ10sialic acid

Identifiers

PMID30644848
PMCPMC6333288
OpenAlexW2909652306

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.