Evidence map›Paper›PMID 33327463›Full record

ArticleBiomolecules2020

Structural Insight into the Contributions of the N-Terminus and Key Active-Site Residues to the Catalytic Efficiency of Glutamine Synthetase 2.

Wen-Ting Chen, Hsin-Yu Yang, Chih-Yu Lin, Yi-Zong Lee, Szu-Chin Ma, Wei-Cheng Chen, Hsien-Sheng Yin

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

Article in Biomolecules, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.2field-weighted citation impact, top 53% 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

2 citing papers in PubMed, 3 citations in OpenAlex.

  1. Glutamine metabolic enzymes: to filament or not to filament?Biochemical Society transactions · 2026
    Review
  2. 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

7 authors at 1 institution in 1 country.

Wen-Ting ChenInstitute of Bioinformatics and Structural Biology, and College of Life Sciences, National Tsing Hua University, No. 101, Section 2, Kuang-Fu Road, Hsinchu 30013, Taiwan.ORCID 0000-0003-2312-6100
Hsin-Yu YangInstitute of Bioinformatics and Structural Biology, and College of Life Sciences, National Tsing Hua University, No. 101, Section 2, Kuang-Fu Road, Hsinchu 30013, Taiwan.
Chih-Yu LinInstitute of Bioinformatics and Structural Biology, and College of Life Sciences, National Tsing Hua University, No. 101, Section 2, Kuang-Fu Road, Hsinchu 30013, Taiwan.
Yi-Zong LeeInstitute of Bioinformatics and Structural Biology, and College of Life Sciences, National Tsing Hua University, No. 101, Section 2, Kuang-Fu Road, Hsinchu 30013, Taiwan.
Szu-Chin MaInstitute of Bioinformatics and Structural Biology, and College of Life Sciences, National Tsing Hua University, No. 101, Section 2, Kuang-Fu Road, Hsinchu 30013, Taiwan.
Wei-Cheng ChenInstitute of Bioinformatics and Structural Biology, and College of Life Sciences, National Tsing Hua University, No. 101, Section 2, Kuang-Fu Road, Hsinchu 30013, Taiwan.
Hsien-Sheng YinInstitute of Bioinformatics and Structural Biology, and College of Life Sciences, National Tsing Hua University, No. 101, Section 2, Kuang-Fu Road, Hsinchu 30013, Taiwan.
National Tsing Hua University · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Glutamine synthetase (GS) catalyzes the condensation of ammonia and glutamate, along with ATP, to form glutamine. Despite extensive studies on GSs from eukaryotes and prokaryotes, the roles of the N-terminus and other structural features in catalysis remain unclear. Here we report the decameric structure of

Indexed as

BiocatalysisAmino Acid SequenceAnimalsBiophysical PhenomenaCatalytic DomainDrosophila melanogasterGlutamate-Ammonia LigaseHumansKineticsModels, MolecularMutant ProteinsProtein Structure, QuaternaryProtein Structure, SecondaryProtein SubunitsRecombinant ProteinsStructural Homology, ProteinGlutamate-Ammonia Ligaseglutamine synthetase 2Mutant ProteinsProtein SubunitsRecombinant Proteinscircular dichroismcrystal structureDrosophila melanogasterenzyme kineticsglutamine synthetase

Identifiers

PMID33327463
PMCPMC7764910
OpenAlexW3111761839

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.