Evidence map›Paper›PMID 12972648›Full record

ArticlePlant physiology2003

Fatty acid biosynthesis in mitochondria of grasses: malonyl-coenzyme A is generated by a mitochondrial-localized acetyl-coenzyme A carboxylase.

Manfred Focke, Ellen Gieringer, Sabine Schwan, Lothar Jänsch, Stefan Binder, Hans-Peter Braun

Open access · bronzeAbstract readComparative Study
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 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

16 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. Article
  3. Identification and Phenotypic Characterization ofFrontiers in plant science · 2018
    Article
  4. Acyl-lipid metabolism.The arabidopsis book · 2013
    Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Acyl-lipid metabolism.The arabidopsis book · 2010
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Complex nested promoters control tissue-specific expression of acetyl-CoA carboxylase genes in wheat.Proceedings of the National Academy of Sciences of the United States of America · 2004
    Article
  16. 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

6 authors at 2 institutions in 1 country.

Manfred FockeBotanik II, Universität Karlsruhe, 76128 Karlsruhe, Germany.
Ellen Gieringer
Sabine Schwan
Lothar Jänsch
Stefan Binder
Hans-Peter Braun
Universität Ulm · DELeibniz University Hannover · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We present biochemical evidence for the occurrence of a 250-kD multifunctional acetyl-coenzyme A carboxylase in barley (Hordeum vulgare) mitochondria. Organelles from 6-d-old barley seedlings were purified by differential centrifugation and Percoll density gradient centrifugation. Upon analysis by two-dimensional Blue-native (BN)/SDS-PAGE, an abundant 250-kD protein can be visualized, which runs at 500 kD on the native gel dimension. A similar 500-kD complex is present in etioplasts from barley. The mitochondrial 250-kD protein is biotinylated as indicated by specific reaction with an antibody directed against biotin. Peptide sequence analysis by electrospray ionization tandem mass spectrometry of the 250-kD proteins from both organellar fractions revealed amino acid sequences that are 100% identical to plastidic acetyl-coenzyme A carboxylase from wheat (Triticum aestivum). The 500-kD complex was also detected in wheat mitochondria, but is absent in mitochondrial fractions from Arabidopsis. Specific acetyl-coenzyme A carboxylation activity in barley mitochondria is higher than in etioplasts, suggesting an important role of mitochondria in fatty acid biosynthesis. Functional implications are discussed.

Indexed as

Acetyl-CoA CarboxylaseAmino Acid SequenceFatty AcidsHordeumMalonyl Coenzyme AMitochondriaMolecular Sequence DataPeptide FragmentsPoaceaeSequence AlignmentSequence Homology, Amino AcidThermolysinTriticumAcetyl-CoA CarboxylaseFatty AcidsMalonyl Coenzyme APeptide FragmentsThermolysin

Identifiers

PMID12972648
PMCPMC219060
OpenAlexW2063947430

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.