Evidence map›Paper›PMID 25488574›Full record

ReviewCritical reviews in biochemistry and molecular biology

Protein-mediated assembly of succinate dehydrogenase and its cofactors.

Jonathan G Van Vranken, Un Na, Dennis R Winge, Jared Rutter

Open access · greenAbstract readReview
In one paragraph

Review in Critical reviews in biochemistry and molecular biology. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.

0numbers the graph read from it
0cells of the map it votes in
70citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

70 citing papers in PubMed, 117 citations in OpenAlex.

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10 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

4 authors at 1 institution in 1 country.

Jonathan G Van VrankenDepartment of Biochemistry and.
Un Na
Dennis R Winge
Jared Rutter
University of Utah · US

Funding

Succinate Dehydrogenase: Biogenesis and Role in DiseaseR01GM110755 · NIGMS · UNIVERSITY OF UTAH · PI WINGE, DENNIS R. · 2014 to 2021
$2.3M
NIGMS NIH HHS R01 GM110755
6 · The paper itself

Abstract

Succinate dehydrogenase (or complex II; SDH) is a heterotetrameric protein complex that links the tribarboxylic acid cycle with the electron transport chain. SDH is composed of four nuclear-encoded subunits that must translocate independently to the mitochondria and assemble into a mature protein complex embedded in the inner mitochondrial membrane. Recently, it has become clear that failure to assemble functional SDH complexes can result in cancer and neurodegenerative syndromes. The effort to thoroughly elucidate the SDH assembly pathway has resulted in the discovery of four subunit-specific assembly factors that aid in the maturation of individual subunits and support the assembly of the intact complex. This review will focus on these assembly factors and assess the contribution of each factor to the assembly of SDH. Finally, we propose a model of the SDH assembly pathway that incorporates all extant data.

Indexed as

Protein ConformationCatalytic DomainCell NucleusElectron TransportHumansMitochondriaProtein SubunitsSuccinate DehydrogenaseProtein SubunitsSuccinate DehydrogenaseAssembly factorsredox-active cofactorsrespiratory chainsuccinate dehydrogenase

Identifiers

PMID25488574
PMCPMC4653115
OpenAlexW2014522149

What OpenQuestion holds

Textmetadata
LicenceTDM
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.