Evidence map›Paper›PMID 29142195›Full record

ArticleNature communications2017

Structural basis for tRNA-dependent cysteine biosynthesis.

Meirong Chen, Koji Kato, Yume Kubo, Yoshikazu Tanaka, Yuchen Liu, Feng Long, William B Whitman, Pascal Lill, Christos Gatsogiannis, Stefan Raunser and 5 more

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

Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.

0numbers the graph read from it
0cells of the map it votes in
5citing papers in PubMed
0.1field-weighted citation impact, top 48% 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

5 citing papers in PubMed, 6 citations in OpenAlex.

  1. Article
  2. Article
  3. Unconventional genetic code systems in archaea.Frontiers in microbiology · 2022
    Review
  4. Article
  5. 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

15 authors at 7 institutions in 3 countries.

Meirong ChenGraduate School of Life Science, Hokkaido University, Sapporo, 060-0810, Japan.
Koji KatoGraduate School of Life Science, Hokkaido University, Sapporo, 060-0810, Japan.
Yume KuboGraduate School of Life Science, Hokkaido University, Sapporo, 060-0810, Japan.
Yoshikazu TanakaGraduate School of Life Science, Hokkaido University, Sapporo, 060-0810, Japan.
Yuchen LiuDepartment of Biological Sciences, Louisiana State University, Baton Rouge, LA, 70803, USA.
Feng LongDepartment of Microbiology, University of Georgia, Athens, GA, 30602, USA.
William B WhitmanDepartment of Microbiology, University of Georgia, Athens, GA, 30602, USA.
Pascal LillDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, 44227, Germany.
Christos GatsogiannisDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, 44227, Germany.
Stefan RaunserDepartment of Structural Biochemistry, Max Planck Institute of Molecular Physiology, Dortmund, 44227, Germany.
Nobutaka ShimizuPhoton Factory, Institute of Materials Structure Science, High Energy Accelerator Research Organization (KEK), Tsukuba, 305-0801, Japan.
Akira ShinodaFaculty of Advanced Life Science, Hokkaido University, Sapporo, 060-0810, Japan.
Akiyoshi NakamuraBioproduction Research Institute, National Institute of Advanced Industrial Science and Technology (AIST), Sapporo, 062-8517, Japan.
Isao TanakaFaculty of Advanced Life Science, Hokkaido University, Sapporo, 060-0810, Japan.
Min YaoGraduate School of Life Science, Hokkaido University, Sapporo, 060-0810, Japan. yao@castor.sci.hokudai.ac.jp.ORCID http://orcid.org/0000-0003-1687-5904
Hokkaido University · JPMax Planck Institute of Molecular Physiology · DEUniversity of Georgia · USHigh Energy Accelerator Research Organization · JPHokkaido University of Science · JPLouisiana State University · USNational Institute of Advanced Industrial Science and Technology · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cysteine can be synthesized by tRNA-dependent mechanism using a two-step indirect pathway, where O-phosphoseryl-tRNA synthetase (SepRS) catalyzes the ligation of a mismatching O-phosphoserine (Sep) to tRNA

Indexed as

Amino Acyl-tRNA SynthetasesArchaeal ProteinsCrystallography, X-RayCysteineGenetic CodeMethanocaldococcusMicroscopy, ElectronModels, MolecularMutationPhosphoserineProtein BindingProtein ConformationRNA, Transfer, CysScattering, Small AngleAmino Acyl-tRNA SynthetasesArchaeal ProteinsCysteinePhosphoserineRNA, Transfer, Cys

Identifiers

PMID29142195
PMCPMC5688128
OpenAlexW2768068608

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.