Evidence map›Paper›PMID 29216272›Full record

ArticlePloS one2017

A thermal after-effect of UV irradiation of muscle glycogen phosphorylase b.

Valeriya V Mikhaylova, Tatiana B Eronina, Natalia A Chebotareva, Sergey Yu Kleymenov, Vladimir V Shubin, Boris I Kurganov

Abstract read
In one paragraph

Article in PloS one, 2017. 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
–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

3 citing papers in PubMed.

  1. Refolding Increases the Chaperone-like Activity of αInternational journal of molecular sciences · 2023
    Article
  2. Article
  3. Article
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.

Valeriya V MikhaylovaDepartment of Structural Biochemistry of Proteins, Bach Institute of Biochemistry, Federal State Institution "Federal Research Centre "Fundamentals of Biotechnology" of the Russian Academy of Sciences", Moscow, Russia.ORCID http://orcid.org/0000-0002-2148-1697
Tatiana B EroninaDepartment of Structural Biochemistry of Proteins, Bach Institute of Biochemistry, Federal State Institution "Federal Research Centre "Fundamentals of Biotechnology" of the Russian Academy of Sciences", Moscow, Russia.
Natalia A ChebotarevaDepartment of Structural Biochemistry of Proteins, Bach Institute of Biochemistry, Federal State Institution "Federal Research Centre "Fundamentals of Biotechnology" of the Russian Academy of Sciences", Moscow, Russia.
Sergey Yu KleymenovDepartment of Structural Biochemistry of Proteins, Bach Institute of Biochemistry, Federal State Institution "Federal Research Centre "Fundamentals of Biotechnology" of the Russian Academy of Sciences", Moscow, Russia.
Vladimir V ShubinDepartment of Structural Biochemistry of Proteins, Bach Institute of Biochemistry, Federal State Institution "Federal Research Centre "Fundamentals of Biotechnology" of the Russian Academy of Sciences", Moscow, Russia.
Boris I KurganovDepartment of Structural Biochemistry of Proteins, Bach Institute of Biochemistry, Federal State Institution "Federal Research Centre "Fundamentals of Biotechnology" of the Russian Academy of Sciences", Moscow, Russia.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Different test systems are used to characterize the anti-aggregation efficiency of molecular chaperone proteins and of low-molecular-weight chemical chaperones. Test systems based on aggregation of UV-irradiated protein are of special interest because they allow studying the protective action of different agents at physiological temperatures. The kinetics of UV-irradiated glycogen phosphorylase b (UV-Phb) from rabbit skeletal muscle was studied at 37°C using dynamic light scattering in a wide range of protein concentrations. It has been shown that the order of aggregation with respect to the protein is equal to unity. A conclusion has been made that the rate-limiting stage of the overall process of aggregation is heat-induced structural reorganization of a UV-Phb molecule, which contains concealed damage.

Indexed as

Ultraviolet RaysCircular DichroismGlycogen PhosphorylaseKineticsMuscle, SkeletalProtein DenaturationGlycogen Phosphorylase

Identifiers

PMID29216272
PMCPMC5720721

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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.