Evidence map›Paper›PMID 29348626›Full record

ArticleScientific reports2018

Arabidopsis serine/threonine/tyrosine protein kinase phosphorylates oil body proteins that regulate oil content in the seeds.

Iyappan Ramachandiran, Anitha Vijayakumar, Visvanathan Ramya, Ram Rajasekharan

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.8field-weighted citation impact, top 18% 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

14 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Molecular Machinery of Lipid Droplet Degradation and Turnover in Plants.International journal of molecular sciences · 2023
    Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  12. Article
  13. Article
  14. 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

4 authors at 2 institutions in 1 country.

Iyappan RamachandiranDepartment of Biochemistry, Indian Institute of Science, Bangalore, 560012, India.
Anitha VijayakumarLipidomics Center, Central Food Technological Research Institute, Mysore, Karnataka, 570020, India.ORCID http://orcid.org/0000-0003-4952-8159
Visvanathan RamyaLipidomics Center, Central Food Technological Research Institute, Mysore, Karnataka, 570020, India.
Ram RajasekharanDepartment of Biochemistry, Indian Institute of Science, Bangalore, 560012, India. lipidindia@yahoo.com.
Central Food Technological Research Institute · INIndian Institute of Science Bangalore · IN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein phosphorylation is an important post-translational modification that can regulate the protein function. The current knowledge on the phosphorylation status of plant oil body (OB) proteins is inadequate. This present study identifies the distinct physiological substrates of Arabidopsis serine/threonine/tyrosine protein kinase (STYK) and its role in seed oil accumulation; the role of Arabidopsis OLE1, a major seed OB protein has also been elucidated. In vitro kinase assay followed by mass spectrometry identifies residue that are phosphorylated by STYK. Further, co-expression of OLE1 and STYK in yeast cells increases the cellular lipid levels and reduces the total lipid when OLE1 was replaced with OLE1

Indexed as

Gene Expression Regulation, PlantProtein Processing, Post-TranslationalAmino Acid SequenceArabidopsisArabidopsis ProteinsGene Expression ProfilingLipid DropletsLipid MetabolismMutationPhosphorylationProtein IsoformsProtein Serine-Threonine KinasesRecombinant ProteinsSaccharomyces cerevisiaeSeedsArabidopsis Proteinsoleosin protein, ArabidopsisProtein IsoformsProtein Serine-Threonine KinasesRecombinant Proteins

Identifiers

PMID29348626
PMCPMC5773694
OpenAlexW2783522146

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.