Evidence map›Paper›PMID 12746537›Full record

ArticlePlant physiology2003

Identification of novel mitochondrial protein components of Chlamydomonas reinhardtii. A proteomic approach.

Robert van Lis, Ariane Atteia, Guillermo Mendoza-Hernández, Diego González-Halphen

Open access · bronzeAbstract read
In one paragraph

Article in Plant physiology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

30 citing papers in PubMed, 115 citations in OpenAlex.

  1. Structural dynamics of mitochondrial ATP synthase inbioRxiv : the preprint server for biology · 2025
    Article
  2. Life (Basel, Switzerland) · 2022
    Article
  3. Article
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  5. Article
  6. Review
  7. Article
  8. Article
  9. Article
  10. Establishing Chlamydomonas reinhardtii as an industrial biotechnology host.The Plant journal : for cell and molecular biology · 2015
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
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  20. Review
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.

Robert van LisDepartamento de Genética Molecular, Instituto de Fisiología Celular, Facultad de Medicina, Universidad Nacional Autónoma de México, Mexico.
Ariane Atteia
Guillermo Mendoza-Hernández
Diego González-Halphen
Instituto Nacional de Cardiología · MXUniversidad Nacional Autónoma de México · MX

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pure mitochondria of the photosynthetic alga Chlamydomonas reinhardtii were analyzed using blue native-polyacrylamide gel electrophoresis (BN-PAGE). The major oxidative phosphorylation complexes were resolved: F(1)F(0)-ATP synthase, NADH-ubiquinone oxidoreductase, ubiquinol-cytochrome c reductase, and cytochrome c oxidase. The oligomeric states of these complexes were determined. The F(1)F(0)-ATP synthase runs exclusively as a dimer, in contrast to the C. reinhardtii chloroplast enzyme, which is present as a monomer and subcomplexes. The sequence of a 60-kD protein, associated with the mitochondrial ATP synthase and with no known counterpart in any other organism, is reported. This protein may be related to the strong dimeric character of the algal F(1)F(0)-ATP synthase. The oxidative phosphorylation complexes resolved by BN-PAGE were separated into their subunits by second dimension sodium dodecyl sulfate-PAGE. A number of polypeptides were identified mainly on the basis of their N-terminal sequence. Core I and II subunits of complex III were characterized, and their proteolytic activities were predicted. Also, the heterodimeric nature of COXIIA and COXIIB subunits in cytochrome c oxidase was demonstrated. Other mitochondrial proteins like the chaperone HSP60, the alternative oxidase, the aconitase, and the ADP/ATP carrier were identified. BN-PAGE was also used to approach the analysis of the major chloroplast protein complexes of C. reinhardtii.

Indexed as

Amino Acid SequenceAnimalsChlamydomonas reinhardtiiElectron Transport Complex IElectron Transport Complex IIIElectron Transport Complex IVElectrophoresis, Gel, Two-DimensionalMitochondrial ProteinsMitochondrial Proton-Translocating ATPasesMolecular Sequence DataNADH, NADPH OxidoreductasesProteomicsSequence Homology, Amino AcidElectron Transport Complex IElectron Transport Complex IIIElectron Transport Complex IVF1F0-ATP synthaseMitochondrial ProteinsMitochondrial Proton-Translocating ATPasesNADH, NADPH Oxidoreductases

Identifiers

PMID12746537
PMCPMC166977
OpenAlexW2155273010

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.