Evidence map›Paper›PMID 10715320›Full record

ArticleThe Plant cell2000

Proteomics of the chloroplast: systematic identification and targeting analysis of lumenal and peripheral thylakoid proteins.

J B Peltier, G Friso, D E Kalume, P Roepstorff, F Nilsson, I Adamska, K J van Wijk

Abstract read
In one paragraph

Article in The Plant cell, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.

0numbers the graph read from it
0cells of the map it votes in
89citing papers in PubMed
–field-weighted citation impact
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

89 citing papers in PubMed.

  1. Article
  2. Euglena gracilis Subcellular Fractionation.Methods in molecular biology (Clifton, N.J.) · 2026
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  13. Review
  14. The Lipid Composition ofPlant physiology · 2020
    Article
  15. Review
  16. Proteomic Analysis and Functional Validation of aFrontiers in plant science · 2019
    Article
  17. Review
  18. Review
  19. Article
  20. Singlet oxygen- and EXECUTER1-mediated signaling is initiated in grana margins and depends on the protease FtsH2.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

7 authors.

J B PeltierDepartment of Biochemistry, Arrhenius Laboratories, Stockholm University, S-10691 Stockholm, Sweden.
G Friso
D E Kalume
P Roepstorff
F Nilsson
I Adamska
K J van Wijk

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The soluble and peripheral proteins in the thylakoids of pea were systematically analyzed by using two-dimensional electrophoresis, mass spectrometry, and N-terminal Edman sequencing, followed by database searching. After correcting to eliminate possible isoforms and post-translational modifications, we estimated that there are at least 200 to 230 different lumenal and peripheral proteins. Sixty-one proteins were identified; for 33 of these proteins, a clear function or functional domain could be identified, whereas for 10 proteins, no function could be assigned. For 18 proteins, no expressed sequence tag or full-length gene could be identified in the databases, despite experimental determination of a significant amount of amino acid sequence. Nine previously unidentified proteins with lumenal transit peptides are presented along with their full-length genes; seven of these proteins possess the twin arginine motif that is characteristic for substrates of the TAT pathway. Logoplots were used to provide a detailed analysis of the lumenal targeting signals, and all nuclear-encoded proteins identified on the two-dimensional gels were used to test predictions for chloroplast localization and transit peptides made by the software programs ChloroP, PSORT, and SignalP. A combination of these three programs was found to provide a useful tool for evaluating chloroplast localization and transit peptides and also could reveal possible alternative processing sites and dual targeting. The potential of proteomics for plant biology and homology-based searching with mass spectrometry data is discussed.

Indexed as

Amino Acid SequenceChloroplastsDatabases, FactualElectron TransportElectrophoresis, Gel, Two-DimensionalExpressed Sequence TagsGas Chromatography-Mass SpectrometryGene Expression Regulation, PlantImmunoblottingMolecular Sequence DataPhotosynthetic Reaction Center Complex ProteinsPisum sativumPlant ProteinsReproducibility of ResultsSequence Analysis, ProteinSoftwarePhotosynthetic Reaction Center Complex ProteinsPlant Proteins

Identifiers

PMID10715320
PMCPMC139834

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.