Evidence map›Paper›PMID 22440515›Full record

ArticlePlant physiology2012

Phosphoproteomic analysis of seed maturation in Arabidopsis, rapeseed, and soybean.

Louis J Meyer, Jianjiong Gao, Dong Xu, Jay J Thelen

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
6.4field-weighted citation impact, top 2% 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

47 citing papers in PubMed, 96 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Dynamics of Protein Phosphorylation duringInternational journal of molecular sciences · 2022
    Article
  6. Article
  7. Article
  8. Article
  9. Phosphorylation Site Motifs in Plant Protein Kinases and Their Substrates.Methods in molecular biology (Clifton, N.J.) · 2021
    Review
  10. Article
  11. Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. Review
  20. Bioinformatic andFrontiers in plant science · 2018
    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 1 institution in 1 country.

Louis J MeyerDepartment of Biochemistry, Christopher S. Bond Life Sciences Center, Interdisciplinary Plant Group, University of Missouri, Columbia, Missouri 65211, USA.
Jianjiong Gao
Dong Xu
Jay J Thelen
University of Missouri · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

To characterize protein phosphorylation in developing seed, a large-scale, mass spectrometry-based phosphoproteomic study was performed on whole seeds at five sequential stages of development in soybean (Glycine max), rapeseed (Brassica napus), and Arabidopsis (Arabidopsis thaliana). Phosphopeptides were enriched from 0.5 mg of total peptides using a combined strategy of immobilized metal affinity and metal oxide affinity chromatography. Enriched phosphopeptides were analyzed by Orbitrap tandem mass spectrometry and mass spectra mined against cognate genome or cDNA databases in both forward and randomized orientations, the latter to calculate false discovery rate. We identified a total of 2,001 phosphopeptides containing 1,026 unambiguous phosphorylation sites from 956 proteins, with an average false discovery rate of 0.78% for the entire study. The entire data set was uploaded into the Plant Protein Phosphorylation Database (www.p3db.org), including all meta-data and annotated spectra. The Plant Protein Phosphorylation Database is a portal for all plant phosphorylation data and allows for homology-based querying of experimentally determined phosphosites. Comparisons with other large-scale phosphoproteomic studies determined that 652 of the phosphoproteins are novel to this study. The unique proteins fall into several Gene Ontology categories, some of which are overrepresented in our study as well as other large-scale phosphoproteomic studies, including metabolic process and RNA binding; other categories are only overrepresented in our study, like embryonic development. This investigation shows the importance of analyzing multiple plants and plant organs to comprehensively map the complete plant phosphoproteome.

Indexed as

Amino Acid MotifsAmino Acid SequenceArabidopsisBinding SitesBrassica rapaConserved SequenceDatabases, GeneticDNA, ComplementaryGlycine maxMolecular Sequence DataPhosphoproteinsPhosphorylationProteomeSeedsSeed Storage ProteinsTandem Mass SpectrometryDNA, ComplementaryPhosphoproteinsProteomeSeed Storage Proteins

Identifiers

PMID22440515
PMCPMC3375983
OpenAlexW2152287977

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.