Evidence map›Paper›PMID 28177315›Full record

ArticleActa crystallographica. Section F, Structural biology communications2017

Crystal structure of the N-terminal anticodon-binding domain of the nondiscriminating aspartyl-tRNA synthetase from Helicobacter pylori.

Chomphunuch Songsiriritthigul, Suwimon Suebka, Chun Jung Chen, Pitchayada Fuengfuloy, Pitak Chuawong

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

5 authors.

Chomphunuch SongsiriritthigulSynchrotron Light Research Institute (Public Organization), 111 University Avenue, Nakhon Ratchasima 30000, Thailand.
Suwimon SuebkaDepartment of Chemistry and Center of Excellence for Innovation in Chemistry, Faculty of Science, and Special Research Unit for Advanced Magnetic Resonance, Kasetsart University, 50 Ngamwongwan Road, Chatuchak, Bangkok 10900, Thailand.
Chun Jung ChenLife Science Group, Scientific Research Division, National Synchrotron Radiation Research Center, Hsinchu 30076, Taiwan.
Pitchayada FuengfuloyDepartment of Chemistry and Center of Excellence for Innovation in Chemistry, Faculty of Science, and Special Research Unit for Advanced Magnetic Resonance, Kasetsart University, 50 Ngamwongwan Road, Chatuchak, Bangkok 10900, Thailand.
Pitak ChuawongDepartment of Chemistry and Center of Excellence for Innovation in Chemistry, Faculty of Science, and Special Research Unit for Advanced Magnetic Resonance, Kasetsart University, 50 Ngamwongwan Road, Chatuchak, Bangkok 10900, Thailand.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The N-terminal anticodon-binding domain of the nondiscriminating aspartyl-tRNA synthetase (ND-AspRS) plays a crucial role in the recognition of both tRNA

Indexed as

Amino Acid SequenceAnticodonApoproteinsAspartate-tRNA LigaseBacterial ProteinsBinding SitesCloning, MolecularCrystallography, X-RayEscherichia coliGene ExpressionHelicobacter pyloriModels, MolecularPlasmidsProtein BindingProtein Conformation, alpha-HelicalProtein Conformation, beta-StrandAnticodonApoproteinsAspartate-tRNA LigaseBacterial ProteinsRecombinant ProteinsRNA, Transfer, AsnRNA, Transfer, Aspanticodon-binding domaincrystal structureHelicobacter pylorinondiscriminating aspartyl-tRNA synthetase

Identifiers

PMID28177315
PMCPMC5297925

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.