Evidence map›Paper›PMID 24755625›Full record

ArticlePloS one2014

Secondary structure changes in ApoA-I Milano (R173C) are not accompanied by a decrease in protein stability or solubility.

Jitka Petrlova, Jonathan Dalla-Riva, Matthias Mörgelin, Maria Lindahl, Ewa Krupinska, Karin G Stenkula, John C Voss, Jens O Lagerstedt

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2014. 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
1.7field-weighted citation impact, top 15% 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, 24 citations in OpenAlex.

  1. Article
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  7. High-efficient bacterial production of human ApoA-I amyloidogenic variants.Protein science : a publication of the Protein Society · 2018
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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

8 authors at 2 institutions in 2 countries.

Jitka PetrlovaDepartment of Experimental Medical Science, Lund University, Lund, Sweden.
Jonathan Dalla-RivaDepartment of Experimental Medical Science, Lund University, Lund, Sweden.
Matthias MörgelinDepartment of Infection Medicine, Lund University, Lund, Sweden.
Maria LindahlDepartment of Experimental Medical Science, Lund University, Lund, Sweden.
Ewa KrupinskaDepartment of Experimental Medical Science, Lund University, Lund, Sweden.
Karin G StenkulaDepartment of Experimental Medical Science, Lund University, Lund, Sweden.
John C VossSchool of Medicine, University of California Davis, Davis, California, United States of America.
Jens O LagerstedtDepartment of Experimental Medical Science, Lund University, Lund, Sweden.
Lund University · SEUniversity of California, Davis · US

Funding

Structure of apolipoprotein A-I on defined states of HDLR01HL077268 · NHLBI · CHILDREN'S HOSPITAL &RES CTR AT OAKLAND · PI ODA, MICHAEL NOBUAKI · 2004 to 2010
$2.0M
NHLBI NIH HHS HL77268NHLBI NIH HHS R01 HL077268
6 · The paper itself

Abstract

Apolipoprotein A-I (apoA-I) is the main protein of high-density lipoprotein (HDL) and a principal mediator of the reverse cholesterol transfer pathway. Variants of apoA-I have been shown to be associated with hereditary amyloidosis. We previously characterized the G26R and L178H variants that both possess decreased stability and increased fibril formation propensity. Here we investigate the Milano variant of apoAI (R173C; apoAI-M), which despite association with low plasma levels of HDL leads to low prevalence of cardiovascular disease in carriers of this mutation. The R173C substitution is located to a region (residues 170 to 178) that contains several fibrillogenic apoA-I variants, including the L178H variant, and therefore we investigated a potential fibrillogenic property of the apoAI-M protein. Despite the fact that apoAI-M shared several features with the L178H variant regarding increased helical content and low degree of ThT binding during prolonged incubation in physiological buffer, our electron microscopy analysis revealed no formation of fibrils. These results suggest that mutations inducing secondary structural changes may be beneficial in cases where fibril formation does not occur.

Indexed as

AmyloidAnimalsApolipoprotein A-IBenzothiazolesHumansMaleMice, Inbred C57BLMutation, MissenseProtein AggregatesProtein BindingProtein StabilityProtein Structure, SecondarySolubilityThiazolesAmyloidApolipoprotein A-Iapolipoprotein A-I MilanoBenzothiazolesProtein AggregatesThiazolesthioflavin T

Identifiers

PMID24755625
PMCPMC3995965
OpenAlexW2088473473

What OpenQuestion holds

Textmetadata
LicenceCC BY
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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.