Evidence map›Paper›PMID 25435987›Full record

ArticleOncology letters2015

Alternative splicing isoform in succinate dehydrogenase complex, subunit C causes downregulation of succinate-coenzyme Q oxidoreductase activity in mitochondria.

Nana Satoh, Chikako Yokoyama, Noriaki Itamura, Yoshiharu Miyajima-Nakano, Hisashi Hisatomi

Open access · diamondAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Oncology letters, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
0.2field-weighted citation impact, top 41% 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

10 citing papers in PubMed, 14 citations in OpenAlex.

  1. Review
  2. Succinate dehydrogenase complex subunit C: Role in cellular physiology and disease.Experimental biology and medicine (Maywood, N.J.) · 2023
    Review
  3. Article
  4. Review
  5. Exploring the Leukemogenic Potential of GATA-1Antioxidants (Basel, Switzerland) · 2021
    Article
  6. Article
  7. Review
  8. Article
  9. Alternative splicing isoforms in health and disease.Pflugers Archiv : European journal of physiology · 2018
    Review
  10. 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

5 authors at 1 institution in 1 country.

Nana SatohLaboratory of Cellular and Molecular Biochemistry, Department of Materials and Life Science, Seikei Universty, Musashino, Tokyo 180-8633, Japan.
Chikako YokoyamaLaboratory of Cellular and Molecular Biochemistry, Department of Materials and Life Science, Seikei Universty, Musashino, Tokyo 180-8633, Japan.
Noriaki ItamuraLaboratory of Cellular and Molecular Biochemistry, Department of Materials and Life Science, Seikei Universty, Musashino, Tokyo 180-8633, Japan.
Yoshiharu Miyajima-NakanoLaboratory of Cellular and Molecular Biochemistry, Department of Materials and Life Science, Seikei Universty, Musashino, Tokyo 180-8633, Japan.
Hisashi HisatomiLaboratory of Cellular and Molecular Biochemistry, Department of Materials and Life Science, Seikei Universty, Musashino, Tokyo 180-8633, Japan.
Seikei University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mitochondrial succinate dehydrogenase (SDH) is localized to the inner mitochondrial membrane and is responsible for the redox of succinic acid. SDH is a tetrameric iron-sulfur flavoprotein of the tricarboxylic acid cycle and respiratory chain. The SDH complex, subunit C (

Indexed as

alternative splicingdominant-negative inhibitorsubunit Csuccinate dehydrogenase complex

Identifiers

PMID25435987
PMCPMC4246615
OpenAlexW2148286560

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.