Evidence map›Paper›PMID 26267866›Full record

ArticleProtein science : a publication of the Protein Society2015

Conformational stability of the RNP domain controls fibril formation of PABPN1.

Jens Liebold, Reno Winter, Ralph Golbik, Gerd Hause, Christoph Parthier, Elisabeth Schwarz

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

Article in Protein science : a publication of the Protein Society, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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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

0 citing papers in PubMed, 0 citations in OpenAlex.

No citing paper in PubMed yet.

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

6 authors at 1 institution in 1 country.

Jens LieboldDepartment of Protein Biochemistry, Institute of Biochemistry and Biotechnology, Martin Luther University, Halle Wittenberg, 06120, Halle, Germany.
Reno WinterDepartment of Protein Biochemistry, Institute of Biochemistry and Biotechnology, Martin Luther University, Halle Wittenberg, 06120, Halle, Germany.
Ralph GolbikDepartment of Virology, Institute of Biochemistry and Biotechnology, Martin Luther University, Halle Wittenberg, 06120, Halle, Germany.
Gerd HauseBiocenter, Martin Luther University, Halle Wittenberg, 06120, Halle, Germany.
Christoph ParthierDepartment of Physical Biotechnology, Institute of Biochemistry and Biotechnology, Martin Luther University, Halle Wittenberg, 06120, Halle, Germany.
Elisabeth SchwarzDepartment of Protein Biochemistry, Institute of Biochemistry and Biotechnology, Martin Luther University, Halle Wittenberg, 06120, Halle, Germany.
Martin Luther University Halle-Wittenberg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The disease oculopharyngeal muscular dystrophy is caused by alanine codon trinucleotide expansions in the N-terminal segment of the nuclear poly(A) binding protein PABPN1. As histochemical features of the disease, intranuclear inclusions of PABPN1 have been reported. Whereas the purified N-terminal domain of PABPN1 forms fibrils in an alanine-dependent way, fibril formation of the full-length protein occurs also in the absence of alanines. Here, we addressed the question whether the stability of the RNP domain or domain swapping within the RNP domain may add to fibril formation. A variant of full-length PABPN1 with a stabilizing disulfide bond at position 185/201 in the RNP domain fibrillized in a redox-sensitive manner suggesting that the integrity of the RNP domain may contribute to fibril formation. Thermodynamic analysis of the isolated wild-type and the disulfide-linked RNP domain showed two state unfolding/refolding characteristics without detectable intermediates. Quantification of the thermodynamic stability of the mutant RNP domain pointed to an inverse correlation between fibril formation of full-length PABPN1 and the stability of the RNP domain.

Indexed as

AmyloidDisulfidesHumansKineticsPoly(A)-Binding Protein IProtein ConformationProtein Structure, TertiaryTemperatureAmyloidDisulfidesPABPN1 protein, humanPoly(A)-Binding Protein Iconformational stabilitydomain swappingfibril formationPABPN1protein misfoldingthermodynamics

Identifiers

PMID26267866
PMCPMC4622212
OpenAlexW1543024219

What OpenQuestion holds

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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.