Evidence map›Paper›PMID 28193863›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2017

Modular electron-transport chains from eukaryotic organelles function to support nitrogenase activity.

Jianguo Yang, Xiaqing Xie, Mingxuan Yang, Ray Dixon, Yi-Ping Wang

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
2.9field-weighted citation impact, top 8% 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

36 citing papers in PubMed, 75 citations in OpenAlex.

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  17. The Chloroplast ofInternational journal of molecular sciences · 2021
    Review
  18. Photovoltaic-driven microbial protein production can use land and sunlight more efficiently than conventional crops.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  19. Article
  20. Nitrogen fixation in maize: breeding opportunities.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2021
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

5 authors at 2 institutions in 2 countries.

Jianguo YangState Key Laboratory of Protein and Plant Gene Research, College of Life Sciences, Peking University, Beijing 100871, China.
Xiaqing XieState Key Laboratory of Protein and Plant Gene Research, College of Life Sciences, Peking University, Beijing 100871, China.
Mingxuan YangState Key Laboratory of Protein and Plant Gene Research, College of Life Sciences, Peking University, Beijing 100871, China.
Ray DixonDepartment of Molecular Microbiology, John Innes Centre, Norwich, NR4 7UH, United Kingdom ray.dixon@jic.ac.uk wangyp@pku.edu.cn.
Yi-Ping WangState Key Laboratory of Protein and Plant Gene Research, College of Life Sciences, Peking University, Beijing 100871, China; ray.dixon@jic.ac.uk wangyp@pku.edu.cn.
Peking University · CNJohn Innes Centre · GB

Funding

Biotechnology and Biological Sciences Research Council BB/J004553/1Biotechnology and Biological Sciences Research Council BBS/E/J/00000016
6 · The paper itself

Abstract

A large number of genes are necessary for the biosynthesis and activity of the enzyme nitrogenase to carry out the process of biological nitrogen fixation (BNF), which requires large amounts of ATP and reducing power. The multiplicity of the genes involved, the oxygen sensitivity of nitrogenase, plus the demand for energy and reducing power, are thought to be major obstacles to engineering BNF into cereal crops. Genes required for nitrogen fixation can be considered as three functional modules encoding electron-transport components (ETCs), proteins required for metal cluster biosynthesis, and the "core" nitrogenase apoenzyme, respectively. Among these modules, the ETC is important for the supply of reducing power. In this work, we have used

Indexed as

AnabaenaElectron TransportEscherichia coliEukaryotaFerredoxin-NADP ReductaseMolybdenumNitrogenaseOrganellesOxidation-ReductionFerredoxin-NADP ReductaseMolybdenumNitrogenaseelectron transportnitrogenase engineeringnitrogen fixationplant organelles

Identifiers

PMID28193863
PMCPMC5373397
OpenAlexW2588944645

What OpenQuestion holds

Textmetadata
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.