Evidence map›Paper›PMID 23154507›Full record

ReviewPlant signaling & behavior2013

Sequence diversity and conservation in factors influencing succinate dehydrogenase flavinylation.

Shaobai Huang, A Harvey Millar

Open access · bronzeAbstract readReview
In one paragraph

Review in Plant signaling & behavior, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.4field-weighted citation impact, top 35% 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

3 citing papers in PubMed, 8 citations in OpenAlex.

  1. The assembly of succinate dehydrogenase: a key enzyme in bioenergetics.Cellular and molecular life sciences : CMLS · 2019
    Review
  2. Article
  3. 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

2 authors at 2 institutions in 1 country.

Shaobai HuangARC Centre of Excellence in Plant Energy Biology and Centre for Comparative Analysis of Biomolecular Networks (CABiN); The University of Western Australia; Crawley, WA Australia.
A Harvey MillarARC Centre of Excellence in Plant Energy Biology and Centre for Comparative Analysis of Biomolecular Networks (CABiN); The University of Western Australia; Crawley, WA Australia.
ARC Centre of Excellence in Plant Energy Biology · AUWestern Australian Marine Science Institution · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The mitochondrial enzyme succinate dehydrogenase (SDH) consists of four subunits, a flavoprotein (SDH1), an iron-sulfur (Fe-S) protein (SDH2) and two integral membrane subunits (SDH3/SDH4). In mammals and yeast, an assembly factor termed SDHAF2/SDH5 is required for accumulation of flavinylated SDH1. In Arabidopsis, we have recently reported the characterization of an unknown function protein with low sequence similarity to SDHAF2 that is needed for assembly and activity of SDH and also for normal root elongation. (1) In this short communication, we have reviewed the sequence diversity and conservation of SDHAF2 across kingdoms based on phylogenetic analysis. Given that flavinylation of SDH is dependent on the SDH1:SDHAF2 interaction, we have also discussed the conservation of the C-terminal tail of SDH1, which is required for this interaction process. In combination, we provide comparative evidence for a conserved role of SDHAF2 as an assembly factor from animals to plants.

Indexed as

MitochondriaPlant ProteinsProtein BindingSuccinate DehydrogenasePlant ProteinsSuccinate Dehydrogenaseflavinylationplant mitochondriasuccinate dehydrogenase

Identifiers

PMID23154507
PMCPMC3656984
OpenAlexW2002495364

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.