Evidence map›Paper›PMID 30142878›Full record

ArticleInternational journal of molecular sciences2018

Investigation of α-Synuclein Amyloid Fibrils Using the Fluorescent Probe Thioflavin T.

Anna I Sulatskaya, Natalia P Rodina, Maksim I Sulatsky, Olga I Povarova, Iuliia A Antifeeva, Irina M Kuznetsova, Konstantin K Turoverov

Open access · goldAbstract read
In one paragraph

Article in International journal of molecular sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

38 citing papers in PubMed, 65 citations in OpenAlex.

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  13. Imidazo[2,1-ACS chemical neuroscience · 2024
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  17. Self-Blinking Thioflavin T for Super-resolution Imaging.The journal of physical chemistry letters · 2024
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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

7 authors at 2 institutions in 1 country.

Anna I SulatskayaLaboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology of the Russian Academy of Science, Tikhoretsky ave. 4, 194064 St. Petersburg, Russia. ansul@mail.ru.
Natalia P RodinaLaboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology of the Russian Academy of Science, Tikhoretsky ave. 4, 194064 St. Petersburg, Russia. natalia240994@gmail.com.
Maksim I SulatskyLaboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology of the Russian Academy of Science, Tikhoretsky ave. 4, 194064 St. Petersburg, Russia. m_sulatsky@mail.ru.
Olga I PovarovaLaboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology of the Russian Academy of Science, Tikhoretsky ave. 4, 194064 St. Petersburg, Russia. olp@incras.ru.
Iuliia A AntifeevaLaboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology of the Russian Academy of Science, Tikhoretsky ave. 4, 194064 St. Petersburg, Russia. julgag@yandex.ru.
Irina M KuznetsovaLaboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology of the Russian Academy of Science, Tikhoretsky ave. 4, 194064 St. Petersburg, Russia. imk@incras.ru.
Konstantin K TuroverovLaboratory of Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology of the Russian Academy of Science, Tikhoretsky ave. 4, 194064 St. Petersburg, Russia. kkt@incras.ru.ORCID 0000-0002-6977-1896
Institute of Cytology · RUPeter the Great St. Petersburg Polytechnic University · RU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In this work, α-synuclein amyloid fibrils-the formation of which is a biomarker of Parkinson's disease-were investigated using the fluorescent probe thioflavin T (ThT). The experimental conditions of protein fibrillogenesis were chosen so that a sufficient number of continuous measurements could be performed to characterize and analyze all stages of this process. The reproducibility of fibrillogenesis and the structure of the obtained aggregates (which is a critical point for further investigation) were proven using a wide range of physical-chemical methods. For the determination of ThT-α-synuclein amyloid fibril binding parameters, the sample and reference solutions were prepared using equilibrium microdialysis. By utilizing absorption spectroscopy of these solutions, the ThT-fibrils binding mode with a binding constant of about 10⁴ M

Indexed as

alpha-SynucleinAmyloidBenzothiazolesCloning, MolecularEscherichia coliFluorescent DyesGene ExpressionGenetic VectorsHumansKineticsMicrodialysisProtein BindingRecombinant ProteinsReproducibility of ResultsSolutionsSpectrometry, Fluorescencealpha-SynucleinAmyloidBenzothiazolesFluorescent DyesRecombinant ProteinsSolutionsthioflavin Tamyloid fibrilsbinding parametersequilibrium microdialysisfibrillogenesisstructural polymorphismthioflavin Tα-synuclein

Identifiers

PMID30142878
PMCPMC6163839
OpenAlexW2888254469

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.