Evidence map›Paper›PMID 12686611›Full record

ArticleMolecular biology of the cell2003

Composition and dynamics of human mitochondrial nucleoids.

Nuria Garrido, Lorena Griparic, Eija Jokitalo, Jorma Wartiovaara, Alexander M van der Bliek, Johannes N Spelbrink

Open access · greenAbstract readComparative Study
In one paragraph

Article in Molecular biology of the cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 175 papers.

0numbers the graph read from it
0cells of the map it votes in
175citing papers in PubMed
8.7field-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

175 citing papers in PubMed, 365 citations in OpenAlex.

  1. Mitochondrial dysfunction in urologic disease.Prostate cancer and prostatic diseases · 2026
    Review
  2. Review
  3. Review
  4. Review
  5. Mitochondrial pearling: membrane biophysics, CaFrontiers in cell and developmental biology · 2026
    Review
  6. Review
  7. Article
  8. Cytosine methylase and hydroxymethylase activity in mammalian mitochondria.Frontiers in cell and developmental biology · 2025
    Article
  9. Article
  10. Review
  11. Article
  12. Review
  13. Review
  14. Mitochondria in disease: changes in shapes and dynamics.Trends in biochemical sciences · 2024
    Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

115 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

6 authors at 3 institutions in 2 countries.

Nuria GarridoInstitute of Medical Technology and Tampere University Hospital, Lenkkeilijänkatu 6, 33014 University of Tampere, Tampere, Finland.
Lorena Griparic
Eija Jokitalo
Jorma Wartiovaara
Alexander M van der Bliek
Johannes N Spelbrink
Tampere University Hospital · FIUniversity of California, Los Angeles · USUniversity of Helsinki · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The organization of multiple mitochondrial DNA (mtDNA) molecules in discrete protein-DNA complexes called nucleoids is well studied in Saccharomyces cerevisiae. Similar structures have recently been observed in human cells by the colocalization of a Twinkle-GFP fusion protein with mtDNA. However, nucleoids in mammalian cells are poorly characterized and are often thought of as relatively simple structures, despite the yeast paradigm. In this article we have used immunocytochemistry and biochemical isolation procedures to characterize the composition of human mitochondrial nucleoids. The results show that both the mitochondrial transcription factor TFAM and mitochondrial single-stranded DNA-binding protein colocalize with Twinkle in intramitochondrial foci defined as nucleoids by the specific incorporation of bromodeoxyuridine. Furthermore, mtDNA polymerase POLG and various other as yet unidentified proteins copurify with mtDNA nucleoids using a biochemical isolation procedure, as does TFAM. The results demonstrated that mtDNA in mammalian cells is organized in discrete protein-rich structures within the mitochondrial network. In vivo time-lapse imaging of nucleoids show they are dynamic structures able to divide and redistribute in the mitochondrial network and suggest that nucleoids are the mitochondrial units of inheritance. Nucleoids did not colocalize with dynamin-related protein 1, Drp1, a protein of the mitochondrial fission machinery.

Indexed as

Mitochondrial ProteinsBase SequenceCell LineDNA-Binding ProteinsDNA-Directed DNA PolymeraseDNA HelicasesDNA, MitochondrialDNA Polymerase gammaDNA PrimaseGreen Fluorescent ProteinsHumansLuminescent ProteinsMicroscopy, FluorescenceNuclear ProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiaeDNA-Binding ProteinsDNA-Directed DNA PolymeraseDNA HelicasesDNA, MitochondrialDNA Polymerase gammaDNA PrimaseGreen Fluorescent ProteinsLuminescent ProteinsMitochondrial Proteinsmitochondrial transcription factor ANuclear ProteinsPOLG protein, humanRecombinant Fusion ProteinsTFAM protein, humanTranscription FactorsTWNK protein, human

Identifiers

PMID12686611
PMCPMC153124
OpenAlexW2128417824

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.