Evidence map›Paper›PMID 31647140›Full record

ArticleChemistry (Weinheim an der Bergstrasse, Germany)2020

The Route from the Folded to the Amyloid State: Exploring the Potential Energy Surface of a Drug-Like Miniprotein.

Nóra Taricska, Dániel Horváth, Dóra K Menyhárd, Hanna Ákontz-Kiss, Masahiro Noji, Masatomo So, Yuji Goto, Toshimichi Fujiwara, András Perczel

Abstract read
In one paragraph

Article in Chemistry (Weinheim an der Bergstrasse, Germany), 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
–field-weighted citation impact
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

14 citing papers in PubMed.

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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

9 authors.

Nóra TaricskaLaboratory of Structural Chemistry and Biology &, MTA-ELTE Protein Modeling Research Group, Eötvös Loránd University, Pázmány Péter sétány 1A, 1117, Budapest, Hungary.
Dániel HorváthLaboratory of Structural Chemistry and Biology &, MTA-ELTE Protein Modeling Research Group, Eötvös Loránd University, Pázmány Péter sétány 1A, 1117, Budapest, Hungary.
Dóra K MenyhárdLaboratory of Structural Chemistry and Biology &, MTA-ELTE Protein Modeling Research Group, Eötvös Loránd University, Pázmány Péter sétány 1A, 1117, Budapest, Hungary.
Hanna Ákontz-KissLaboratory of Structural Chemistry and Biology &, MTA-ELTE Protein Modeling Research Group, Eötvös Loránd University, Pázmány Péter sétány 1A, 1117, Budapest, Hungary.
Masahiro NojiInstitute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka, 565-0871, Japan.
Masatomo SoInstitute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka, 565-0871, Japan.
Yuji GotoInstitute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka, 565-0871, Japan.
Toshimichi FujiwaraInstitute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka, 565-0871, Japan.
András PerczelLaboratory of Structural Chemistry and Biology &, MTA-ELTE Protein Modeling Research Group, Eötvös Loránd University, Pázmány Péter sétány 1A, 1117, Budapest, Hungary.ORCID http://orcid.org/0000-0003-1252-6416

Funding

Magyar Tudományos Akadémia K116305 OTKAthe European Union and the State of Hungary and co-financed by the European Regional Development Fund VEKOP-2.3.2-16-2017-00014
6 · The paper itself

Abstract

The amyloid formation of the folded segment of a variant of Exenatide (a marketed drug for type-2 diabetes mellitus) was studied by electronic circular dichroism (ECD) and NMR spectroscopy. We found that the optimum temperature for E5 protein amyloidosis coincides with body temperature and requires well below physiological salt concentration. Decomposition of the ECD spectra and its barycentric representation on the folded-unfolded-amyloid potential energy surface allowed us to monitor the full range of molecular transformation of amyloidogenesis. We identified points of no return (e.g.; T=37 °C, pH 4.1, c

Indexed as

Amino Acid SequenceAmyloidCircular DichroismHydrogen-Ion ConcentrationMolecular Dynamics SimulationNuclear Magnetic Resonance, BiomolecularPeptidesProtein ConformationProtein FoldingTemperatureAmyloidPeptidesaggregationamyloid beta-peptidesprotein foldingprotein modeling

Identifiers

PMID31647140
PMCPMC7028080

What OpenQuestion holds

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LicenceCC BY
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.