Evidence map›Paper›PMID 29694863›Full record

ArticleBiophysical journal2018

Insights into the Aggregation Mechanism of PolyQ Proteins with Different Glutamine Repeat Lengths.

Tetyana Yushchenko, Elke Deuerling, Karin Hauser

Abstract read
In one paragraph

Article in Biophysical journal, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. Development of aniScience · 2026
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  3. Review
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  11. Protein clearance strategies for disease intervention.Journal of neural transmission (Vienna, Austria : 1996) · 2022
    Review
  12. Article
  13. Article
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  15. Article
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  18. Dissecting the role of glutamine in seeding peptide aggregation.Computational and structural biotechnology journal · 2021
    Article
  19. Article
  20. Review
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

3 authors.

Tetyana YushchenkoBiophysical Chemistry, Department of Chemistry, University of Konstanz, Konstanz, Germany; Konstanz Research School Chemical Biology, University of Konstanz, Konstanz, Germany.
Elke DeuerlingMolecular Microbiology, Department of Biology, University of Konstanz, Konstanz, Germany; Konstanz Research School Chemical Biology, University of Konstanz, Konstanz, Germany.
Karin HauserBiophysical Chemistry, Department of Chemistry, University of Konstanz, Konstanz, Germany; Konstanz Research School Chemical Biology, University of Konstanz, Konstanz, Germany. Electronic address: karin.hauser@uni-konstanz.de.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Polyglutamine (polyQ) diseases, including Huntington's disease, result from the aggregation of an abnormally expanded polyQ repeat in the affected protein. The length of the polyQ repeat is essential for the disease's onset; however, the molecular mechanism of polyQ aggregation is still poorly understood. Controlled conditions and initiation of the aggregation process are prerequisites for the detection of transient intermediate states. We present an attenuated total reflection Fourier-transform infrared spectroscopic approach combined with protein immobilization to study polyQ aggregation dependent on the polyQ length. PolyQ proteins were engineered mimicking the mammalian N-terminus fragment of the Huntingtin protein and containing a polyQ sequence with the number of glutamines below (Q11), close to (Q38), and above (Q56) the disease threshold. A monolayer of the polyQ construct was chemically immobilized on the internal reflection element of the attenuated total reflection cell, and the aggregation was initiated via enzymatic cleavage. Structural changes of the polyQ sequence were monitored by time-resolved infrared difference spectroscopy. We observed faster aggregation kinetics for the longer sequences, and furthermore, we could distinguish β-structured intermediates for the different constructs, allowing us to propose aggregation mechanisms dependent on the repeat length. Q11 forms a β-structured aggregate by intermolecular interaction of stretched monomers, whereas Q38 and Q56 undergo conformational changes to various β-structured intermediates, including intramolecular β-sheets.

Indexed as

Protein AggregatesRepetitive Sequences, Amino AcidAmino Acid SequenceModels, MolecularPeptidesProtein ConformationPeptidespolyglutamineProtein Aggregates

Identifiers

PMID29694863
PMCPMC5937114

What OpenQuestion holds

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Registered trials

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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.