Evidence map›Paper›PMID 36555597›Full record

ArticleInternational journal of molecular sciences2022

Specific S100 Proteins Bind Tumor Necrosis Factor and Inhibit Its Activity.

Alexey S Kazakov, Marina Y Zemskova, Gleb K Rystsov, Alisa A Vologzhannikova, Evgenia I Deryusheva, Victoria A Rastrygina, Andrey S Sokolov, Maria E Permyakova, Ekaterina A Litus, Vladimir N Uversky and 2 more

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.9field-weighted citation impact, top 28% 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

4 citing papers in PubMed, 11 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

12 authors at 3 institutions in 2 countries.

Alexey S KazakovInstitute for Biological Instrumentation, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, 142290 Pushchino, Russia.
Marina Y ZemskovaInstitute for Biological Instrumentation, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, 142290 Pushchino, Russia.
Gleb K RystsovG.K. Skryabin Institute of Biochemistry and Physiology of Microorganisms, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, 142290 Pushchino, Russia.
Alisa A VologzhannikovaInstitute for Biological Instrumentation, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, 142290 Pushchino, Russia.ORCID 0000-0001-5550-2129
Evgenia I DeryushevaInstitute for Biological Instrumentation, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, 142290 Pushchino, Russia.
Victoria A RastryginaInstitute for Biological Instrumentation, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, 142290 Pushchino, Russia.ORCID 0000-0001-8801-3786
Andrey S SokolovInstitute for Biological Instrumentation, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, 142290 Pushchino, Russia.
Maria E PermyakovaInstitute for Biological Instrumentation, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, 142290 Pushchino, Russia.
Ekaterina A LitusInstitute for Biological Instrumentation, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, 142290 Pushchino, Russia.ORCID 0000-0002-7459-6295
Vladimir N UverskyDepartment of Molecular Medicine and USF Health Byrd Alzheimer's Research Institute, Morsani College of Medicine, University of South Florida, Tampa, FL 33612, USA.ORCID 0000-0002-4037-5857
Eugene A PermyakovInstitute for Biological Instrumentation, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, 142290 Pushchino, Russia.
Sergei E PermyakovInstitute for Biological Instrumentation, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, 142290 Pushchino, Russia.ORCID 0000-0003-4086-3137
Institute for Biological Instrumentation · RUG. K. Skryabin Institute of Biochemistry and Physiology of Microorganisms · RUUniversity of South Florida · US

Funding

Russian Science Foundation №19-14-00289
6 · The paper itself

Abstract

Tumor necrosis factor (TNF) inhibitors (anti-TNFs) represent a cornerstone of the treatment of various immune-mediated inflammatory diseases and are among the most commercially successful therapeutic agents. Knowledge of TNF binding partners is critical for identification of the factors able to affect clinical efficacy of the anti-TNFs. Here, we report that among eighteen representatives of the multifunctional S100 protein family, only S100A11, S100A12 and S100A13 interact with the soluble form of TNF (sTNF) in vitro. The lowest equilibrium dissociation constants (

Indexed as

Receptors, Tumor Necrosis FactorS100 ProteinsS100A12 ProteinTumor Necrosis Factor-alphaTumor Necrosis Factor InhibitorsReceptors, Tumor Necrosis FactorS100A12 ProteinS100 ProteinsTumor Necrosis Factor-alphaTumor Necrosis Factor Inhibitorscytokineinflammatory diseasesprotein–protein interactionS100 proteintumor necrosis factor

Identifiers

PMID36555597
PMCPMC9783754
OpenAlexW4311788100

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.