Evidence map›Paper›PMID 36233301›Full record

ArticleInternational journal of molecular sciences2022

Calcium-Bound S100P Protein Is a Promiscuous Binding Partner of the Four-Helical Cytokines.

Alexey S Kazakov, Evgenia I Deryusheva, Maria E Permyakova, Andrey S Sokolov, Victoria A Rastrygina, Vladimir N Uversky, Eugene A Permyakov, Sergei E Permyakov

Open access · goldAbstract read
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 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.0field-weighted citation impact, top 27% 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

7 citing papers in PubMed, 12 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Review
  7. Specific S100 Proteins Bind Tumor Necrosis Factor and Inhibit Its Activity.International journal of molecular sciences · 2022
    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

8 authors at 2 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.
Evgenia I DeryushevaInstitute 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.
Andrey S SokolovInstitute 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
Vladimir N UverskyInstitute for Biological Instrumentation, Pushchino Scientific Center for Biological Research of the Russian Academy of Sciences, 142290 Pushchino, Russia.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 · RUUniversity of South Florida · US

Funding

Russian Science Foundation 19-14-00289-П
6 · The paper itself

Abstract

S100 proteins are multifunctional calcium-binding proteins of vertebrates that act intracellularly, extracellularly, or both, and are engaged in the progression of many socially significant diseases. Their extracellular action is typically mediated by the recognition of specific receptor proteins. Recent studies indicate the ability of some S100 proteins to affect cytokine signaling through direct interaction with cytokines. S100P was shown to be the S100 protein most actively involved in interactions with some four-helical cytokines. To assess the selectivity of the S100P protein binding to four-helical cytokines, we have probed the interaction of Ca

Indexed as

CalciumCalcium-Binding ProteinsCytokinesCalcium, DietaryCarrier ProteinsHumansImmunologic FactorsMolecular Docking SimulationNeoplasm ProteinsProtein BindingReceptor for Advanced Glycation End ProductsS100 ProteinsCalciumCalcium-Binding ProteinsCalcium, DietaryCarrier ProteinsCytokinesImmunologic FactorsNeoplasm ProteinsReceptor for Advanced Glycation End ProductsS100P protein, humanS100 Proteinscytokineprotein–protein interactionS100PS100 protein

Identifiers

PMID36233301
PMCPMC9569990
OpenAlexW4303946024

What OpenQuestion holds

Textmetadata
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.