Evidence map›Paper›PMID 27228180›Full record

ArticlePloS one2016

Stoichiometry and Affinity of Thioflavin T Binding to Sup35p Amyloid Fibrils.

Anna I Sulatskaya, Irina M Kuznetsova, Mikhail V Belousov, Stanislav A Bondarev, Galina A Zhouravleva, Konstantin K Turoverov

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

13 citing papers in PubMed, 32 citations in OpenAlex.

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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

6 authors at 3 institutions in 1 country.

Anna I SulatskayaLaboratory for Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology, Russian Academy of Science, St. Petersburg, Tikhoretsky Ave. 4, 194064, Russia.
Irina M KuznetsovaLaboratory for Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology, Russian Academy of Science, St. Petersburg, Tikhoretsky Ave. 4, 194064, Russia.
Mikhail V BelousovDepartment of Genetics and Biotechnology, Saint Petersburg State University, Saint Petersburg, Universitetskaya Emb. 7-9, 199034, Russia.
Stanislav A BondarevDepartment of Genetics and Biotechnology, Saint Petersburg State University, Saint Petersburg, Universitetskaya Emb. 7-9, 199034, Russia.
Galina A ZhouravlevaDepartment of Genetics and Biotechnology, Saint Petersburg State University, Saint Petersburg, Universitetskaya Emb. 7-9, 199034, Russia.
Konstantin K TuroverovLaboratory for Structural Dynamics, Stability and Folding of Proteins, Institute of Cytology, Russian Academy of Science, St. Petersburg, Tikhoretsky Ave. 4, 194064, Russia.
St Petersburg University · RUInstitute 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 two modes of binding of the fluorescent probe thioflavin T to yeast prion protein Sup35p amyloid fibrils were revealed by absorption spectrometry of solutions prepared by equilibrium microdialysis. These binding modes exhibited significant differences in binding affinity and stoichiometry. Moreover, the absorption spectrum and the molar extinction coefficient of the dye bound in each mode were determined. The fluorescence quantum yield of the dye bound in each mode was determined via a spectrofluorimetric study of the same solutions in which the recorded fluorescence intensity was corrected for the primary inner filter effect. As previously predicted, the existence of one of the detected binding modes may be due to the incorporation of the dye into the grooves along the fiber axis perpendicular to the β-sheets of the fibrils. It was assumed that the second type of binding with higher affinity may be due to the existence of ThT binding sites that are localized to areas where amyloid fibrils are clustered.

Indexed as

AmyloidBenzothiazolesFluorescenceFluorescent DyesKineticsPeptide Termination FactorsProtein BindingSaccharomyces cerevisiae ProteinsThiazolesAmyloidBenzothiazolesFluorescent DyesPeptide Termination FactorsSaccharomyces cerevisiae ProteinsSUP35 protein, S cerevisiaeThiazolesthioflavin T

Identifiers

PMID27228180
PMCPMC4882037
OpenAlexW2400148334

What OpenQuestion holds

Textmetadata
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.