Evidence map›Paper›PMID 35423687›Full record

ArticleRSC advances2020

Time-resolved detection of SDS-induced conformational changes in α-synuclein by a micro-stopped-flow system.

Shunki Takaramoto, Yusuke Nakasone, Kei Sadakane, Shinsaku Maruta, Masahide Terazima

Open access · goldAbstract read
In one paragraph

Article in RSC advances, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
0.9field-weighted citation impact, top 32% 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

3 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. Magnetic resonance letters · 2025
    Article
  3. 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

5 authors at 2 institutions in 2 countries.

Shunki TakaramotoDepartment of Chemistry, Graduate School of Science, Kyoto University Kyoto 606-8502 Japan mterazima@kuchem.kyoto-u.ac.jp.ORCID https://orcid.org/0000-0002-8195-3115
Yusuke NakasoneDepartment of Chemistry, Graduate School of Science, Kyoto University Kyoto 606-8502 Japan mterazima@kuchem.kyoto-u.ac.jp.
Kei SadakaneDepartment of Bioinformatics, Graduate School of Engineering, Soka University Hachioji Tokyo 192-8577 Japan.
Shinsaku MarutaDepartment of Bioinformatics, Graduate School of Engineering, Soka University Hachioji Tokyo 192-8577 Japan.
Masahide TerazimaDepartment of Chemistry, Graduate School of Science, Kyoto University Kyoto 606-8502 Japan mterazima@kuchem.kyoto-u.ac.jp.ORCID https://orcid.org/0000-0001-6828-479X
Kyoto University · JPSoka University · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

An intrinsically disordered protein, α-synuclein (αSyn), binds to negatively charged phospholipid membranes and adopts an α-helical structure. This conformational change is also induced by interaction with sodium dodecyl sulfate (SDS), which is an anionic surfactant used in previous studies to mimic membrane binding. However, while the structure of the αSyn and SDS complex has been studied widely by various static measurements, the process of structural change from the denatured state to the folded state remains unclear. In this study, the interaction dynamics between αSyn and SDS micelles was investigated using time-resolved measurements with a micro-stopped-flow system, which has been recently developed. In particular, the time-resolved diffusion based on the transient grating technique in combination with a micro-stopped-flow system revealed the gradual change in diffusion triggered by the presence of SDS micelles. This change is induced not only by binding to SDS micelles, but also by an intramolecular conformational change. It was interesting to find that the diffusion coefficient decreased in an intermediate state and then increased to the final state in the binding reaction. We also carried out stopped-flow-kinetic measurements of circular dichroism and intramolecular fluorescence resonance energy transfer, and the

Identifiers

PMID35423687
PMCPMC8693425
OpenAlexW3118811522

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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.