Evidence map›Paper›PMID 33013970›Full record

ArticleFrontiers in plant science2020

A Synthetic Biology Workflow Reveals Variation in Processing and Solubility of Nitrogenase Proteins Targeted to Plant Mitochondria, and Differing Tolerance of Targeting Sequences in a Bacterial Nitrogenase Assay.

Shoko Okada, Christina M Gregg, Robert Silas Allen, Amratha Menon, Dawar Hussain, Vanessa Gillespie, Ema Johnston, Keren Byrne, Michelle Lisa Colgrave, Craig C Wood

Open access · goldAbstract read
In one paragraph

Article in Frontiers in plant science, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
0.7field-weighted citation impact, top 34% 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

13 citing papers in PubMed, 15 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. On the Shoulders of Giants-Reaching for Nitrogenase.Molecules (Basel, Switzerland) · 2023
    Review
  5. Article
  6. Review
  7. Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. The Chloroplast ofInternational journal of molecular sciences · 2021
    Review
  13. 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

10 authors at 3 institutions in 1 country.

Shoko OkadaLand and Water, Commonwealth Scientific and Industrial Research Organisation, Acton, ACT, Australia.
Christina M GreggAgriculture and Food, Commonwealth Scientific and Industrial Research Organisation, Acton, ACT, Australia.
Robert Silas AllenAgriculture and Food, Commonwealth Scientific and Industrial Research Organisation, Acton, ACT, Australia.
Amratha MenonAgriculture and Food, Commonwealth Scientific and Industrial Research Organisation, Acton, ACT, Australia.
Dawar HussainAgriculture and Food, Commonwealth Scientific and Industrial Research Organisation, Acton, ACT, Australia.
Vanessa GillespieAgriculture and Food, Commonwealth Scientific and Industrial Research Organisation, Acton, ACT, Australia.
Ema JohnstonAgriculture and Food, Commonwealth Scientific and Industrial Research Organisation, Acton, ACT, Australia.
Keren ByrneAgriculture and Food, Commonwealth Scientific and Industrial Research Organisation, St. Lucia, QLD, Australia.
Michelle Lisa ColgraveAgriculture and Food, Commonwealth Scientific and Industrial Research Organisation, St. Lucia, QLD, Australia.
Craig C WoodAgriculture and Food, Commonwealth Scientific and Industrial Research Organisation, Acton, ACT, Australia.
Commonwealth Scientific and Industrial Research Organisation · AUAgriculture and Food · AUCSIRO Land and Water · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

While industrial nitrogen fertilizer is intrinsic to modern agriculture, it is expensive and environmentally harmful. One approach to reduce fertilizer usage is to engineer the bacterial nitrogenase enzyme complex within plant mitochondria, a location that may support enzyme function. Our current strategy involves fusing a mitochondrial targeting peptide (MTP) to nitrogenase (Nif) proteins, enabling their import to the mitochondrial matrix. However, the process of import modifies the N-terminus of each Nif protein and may impact nitrogenase assembly and function. Here we present our workflow assessing the mitochondrial processing, solubility and relative abundance of 16

Indexed as

Klebsiellamitochondrial processing peptidasemitochondrial targetingnitrogenaseplant mitochondriaprotein solubility

Identifiers

PMID33013970
PMCPMC7511584
OpenAlexW3084211132

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.