Evidence map›Paper›PMID 16618929›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2006

Mapping the Arabidopsis organelle proteome.

Tom P J Dunkley, Svenja Hester, Ian P Shadforth, John Runions, Thilo Weimar, Sally L Hanton, Julian L Griffin, Conrad Bessant, Federica Brandizzi, Chris Hawes and 3 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 212 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
212citing papers in PubMed, 1 pooled it
18.3field-weighted citation impact, top 1% 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

212 citing papers in PubMed, 1 synthesis or guideline pooled it, 524 citations in OpenAlex.

  1. Pooled it
  2. PMF proteins mediate mitochondrial fusion in Arabidopsis.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. Review
  7. Genome-Wide Identification and Functional Analysis of the GUX Gene Family inInternational journal of molecular sciences · 2024
    Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Preparation of Highly Enriched ER Membranes Using Free-Flow Electrophoresis.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  13. Characteristics analysis ofPlant signaling & behavior · 2023
    Article
  14. Article
  15. Review
  16. Article
  17. Phytochelatins: Sulfur-Containing Metal(loid)-Chelating Ligands in Plants.International journal of molecular sciences · 2023
    Review
  18. Article
  19. Article
  20. Article

152 more citing papers are in PubMed but not listed here.

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

13 authors at 4 institutions in 2 countries.

Tom P J DunkleyDepartment of Biochemistry, University of Cambridge, Downing Site, Cambridge CB2 1QW, United Kingdom.
Svenja Hester
Ian P Shadforth
John Runions
Thilo Weimar
Sally L Hanton
Julian L Griffin
Conrad Bessant
Federica Brandizzi
Chris Hawes
Rod B Watson
Paul Dupree
Kathryn S Lilley
University of Cambridge · GBCranfield University · GBOxford Brookes University · GBUniversity of Saskatchewan · CA

Funding

Biotechnology and Biological Sciences Research Council BBS/B/10684
6 · The paper itself

Abstract

A challenging task in the study of the secretory pathway is the identification and localization of new proteins to increase our understanding of the functions of different organelles. Previous proteomic studies of the endomembrane system have been hindered by contaminating proteins, making it impossible to assign proteins to organelles. Here we have used the localization of organelle proteins by the isotope tagging technique in conjunction with isotope tags for relative and absolute quantitation and 2D liquid chromatography for the simultaneous assignment of proteins to multiple subcellular compartments. With this approach, the density gradient distributions of 689 proteins from Arabidopsis thaliana were determined, enabling confident and simultaneous localization of 527 proteins to the endoplasmic reticulum, Golgi apparatus, vacuolar membrane, plasma membrane, or mitochondria and plastids. This parallel analysis of endomembrane components has enabled protein steady-state distributions to be determined. Consequently, genuine organelle residents have been distinguished from contaminating proteins and proteins in transit through the secretory pathway.

Indexed as

ArabidopsisArabidopsis ProteinsOrganellesPeptide MappingProteomeRecombinant Fusion ProteinsSubcellular FractionsArabidopsis ProteinsProteomeRecombinant Fusion Proteins

Identifiers

PMID16618929
PMCPMC1458916
OpenAlexW2097847369

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.