Evidence map›Paper›PMID 12209014›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2002

Dual localization of human DNA topoisomerase IIIalpha to mitochondria and nucleus.

Yong Wang, Yi Lisa Lyu, James C Wang

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

52 citing papers in PubMed, 111 citations in OpenAlex.

  1. Article
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  8. Article
  9. Identification ofComputational and structural biotechnology journal · 2023
    Article
  10. Article
  11. Article
  12. Article
  13. NovelNeurology. Genetics · 2022
    Article
  14. Mitochondrial DNA Instability in Mammalian Cells.Antioxidants & redox signaling · 2022
    Review
  15. Review
  16. The many lives of type IA topoisomerases.The Journal of biological chemistry · 2020
    Review
  17. Article
  18. Review
  19. Twist and Turn-Topoisomerase Functions in Mitochondrial DNA Maintenance.International journal of molecular sciences · 2019
    Review
  20. 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

3 authors at 1 institution in 1 country.

Yong WangDepartment of Molecular and Cellular Biology, Harvard University, 7 Divinity Avenue, Cambridge, MA 02138, USA.
Yi Lisa Lyu
James C Wang
Harvard University · US

Funding

DNA TOPOISOMERASES--BIOLOGICAL FUNCTIONS &MECHANISMSR01GM024544 · NIGMS · HARVARD UNIVERSITY · PI WANG, JAMES C · 1985 to 2003
$2.2M
CELL-KILLING BY TOPOISOMERASE-ACTIVE ANTICANCER DRUGSR01CA047958 · NCI · HARVARD UNIVERSITY · PI WANG, JAMES C · 1988 to 2000
$430k
DNA TOPOISOMERASES: BIOLOGICAL FUNCTIONS AND MECHANISMSR37GM024544 · NIGMS · HARVARD UNIVERSITY · PI WANG, JAMES C · 1990 to 1999
–
NCI NIH HHS CA47958NIGMS NIH HHS GM24544NIGMS NIH HHS R01 GM024544NIGMS NIH HHS R37 GM024544
6 · The paper itself

Abstract

The human TOP3alpha gene encoding DNA topoisomerase IIIalpha (hTop3alpha) has two potential start codons for the synthesis of proteins 1,001 and 976 aa residues in length. The sequence of the N-terminal region of the 1,001-residue form resembles signal peptide sequences for mitochondrial import, and fluorescence microscopy shows that the addition of as few as the first 34 aa of the 1,001-residue form of hTop3alpha to a green fluorescent protein can direct the chimeric protein to mitochondria. Biochemical analyses of subcellular fractions of HeLa cells further demonstrate that a distinctive fraction of hTop3alpha is present inside mitochondria, as evidenced by its resistance to proteinase K. This fraction constitutes several percent of the enzyme in the nuclear fraction, suggesting that the distribution of the mitochondrial and nuclear forms of hTop3alpha is roughly in proportion to the DNA contents of these cellular compartments. The presence of a type IA DNA topoisomerase in the mitochondria of other eukaryotes is supported by an examination of the amino acid sequences of mouse and Drosophila DNA topoisomerase IIIalpha and Schizosaccharomyces pombe DNA topoisomerase III. Given the presence of at least one type IA DNA topoisomerase in all forms of life examined to date, the finding of a type IA enzyme in mitochondria further supports the notion of a key role of such enzymes in DNA transactions.

Indexed as

Amino Acid SequenceAnimalsCell NucleusDNA Topoisomerases, Type IEndopeptidase KGreen Fluorescent ProteinsHeLa CellsHumansLuminescent ProteinsMiceMitochondriaMolecular Sequence DataPeptide FragmentsProtein Sorting SignalsRecombinant Fusion ProteinsDNA Topoisomerases, Type IEndopeptidase KGreen Fluorescent ProteinsLuminescent ProteinsPeptide FragmentsProtein Sorting SignalsRecombinant Fusion Proteins

Identifiers

PMID12209014
PMCPMC129407
OpenAlexW1996126491

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.