Evidence map›Paper›PMID 30701627›Full record

ArticleProtein science : a publication of the Protein Society2019

Protein oligomerization as a metabolic control mechanism: Application to apoE.

Carl Frieden

Open access · bronzeAbstract read
In one paragraph

Article in Protein science : a publication of the Protein Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.5field-weighted citation impact, top 36% 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

11 citing papers in PubMed, 26 citations in OpenAlex.

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  8. Salmonella YqiC exerts its function through an oligomeric state.Protein science : a publication of the Protein Society · 2023
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  9. Review
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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

1 author at 1 institution in 1 country.

Carl FriedenDepartment of Biochemistry and Molecular Biophysics, Washington University School of Medicine, St. Louis, Missouri.
Washington University in St. Louis · US

Funding

ALZHEIMER'S DISEASE: DEFINING THE APOE-AMYLOID-BETA INTERACTIONRF1AG044331 · NIA · WASHINGTON UNIVERSITY · PI FRIEDEN, CARL · 2014 to 2014
$1.6M
NIA NIH HHS RF1 AG0044331NIA NIH HHS RF1 AG044331
6 · The paper itself

Abstract

It has been estimated that 30%-50% of proteins self-assemble to form complexes consisting of multiple copies of themselves. If there is a functional difference between different molecular weight forms and if these forms interconvert on a reasonable time scale then oligomerization could be an important metabolic control mechanism. The example given here is of apoE for which the oligomerization process is measured in minutes to hours and the monomer binds lipids while the tetramer does not. Examination of the literature reveals few reports on the rate constants that control the interconversion of different molecular weight forms. Perhaps it is time to collect such data.

Indexed as

AnimalsApolipoproteins EHumansKineticsLipid MetabolismProtein BindingProtein ConformationProtein IsoformsProtein MultimerizationApolipoproteins EProtein Isoformskineticslipid bindingmetabolism

Identifiers

PMID30701627
PMCPMC6423707
OpenAlexW2911541778

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.