Evidence map›Paper›PMID 28516021›Full record

ArticleIntrinsically disordered proteins

Multiple fuzzy interactions in the moonlighting function of thymosin-β4.

Agnes Tantos, Beata Szabo, Andras Lang, Zoltan Varga, Maksym Tsylonok, Monika Bokor, Tamas Verebelyi, Pawel Kamasa, Kalman Tompa, Andras Perczel and 5 more

Open access · bronzeAbstract read
In one paragraph

Article in Intrinsically disordered proteins. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.2field-weighted citation impact, top 46% 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

9 citing papers in PubMed, 16 citations in OpenAlex.

  1. Phosphorylation event changes the RNA binding mode of EZH2 disordered segment.Protein science : a publication of the Protein Society · 2026
    Article
  2. Article
  3. Functional Characterization of the N-Terminal Disordered Region of theInternational journal of molecular sciences · 2022
    Article
  4. Integrin-linked kinase (ILK): the known vs. the unknown and perspectives.Cellular and molecular life sciences : CMLS · 2022
    Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. 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

15 authors at 8 institutions in 4 countries.

Agnes TantosInstitute of Enzymology; Research Centre for Natural Sciences; Hungarian Academy of Sciences; Budapest, Hungary.
Beata SzaboInstitute of Enzymology; Research Centre for Natural Sciences; Hungarian Academy of Sciences; Budapest, Hungary.
Andras LangEötvös Loránd University; Institute of Chemistry; Budapest, Hungary.
Zoltan VargaInstitute of Enzymology; Research Centre for Natural Sciences; Hungarian Academy of Sciences; Budapest, Hungary.
Maksym TsylonokVIB Department of Structural Biology; Vrije Universiteit Brussel; Brussels, Belgium.
Monika BokorInstitute for Solid State Physics and Optics; Wigner Research Centre for Physics of the Hungarian Academy of Sciences; Budapest, Hungary.
Tamas VerebelyiInstitute for Solid State Physics and Optics; Wigner Research Centre for Physics of the Hungarian Academy of Sciences; Budapest, Hungary.
Pawel KamasaInstitute for Solid State Physics and Optics; Wigner Research Centre for Physics of the Hungarian Academy of Sciences; Budapest, Hungary.
Kalman TompaInstitute for Solid State Physics and Optics; Wigner Research Centre for Physics of the Hungarian Academy of Sciences; Budapest, Hungary.
Andras PerczelEötvös Loránd University; Institute of Chemistry; Budapest, Hungary.
Laszlo BudayInstitute of Enzymology; Research Centre for Natural Sciences; Hungarian Academy of Sciences; Budapest, Hungary.
Si Hyung LeeDivision of Biosystems Research; Korea Research Institute of Bioscience and Biotechnology; Daejeon, Republic of Korea.
Yejin ChooDivision of Biosystems Research; Korea Research Institute of Bioscience and Biotechnology; Daejeon, Republic of Korea.
Kyou-Hoon HanDivision of Biosystems Research; Korea Research Institute of Bioscience and Biotechnology; Daejeon, Republic of Korea.
Peter TompaInstitute of Enzymology; Research Centre for Natural Sciences; Hungarian Academy of Sciences; Budapest, Hungary.
Wigner Research Centre for Physics · HUHungarian Academy of Sciences · HUDaejeon University · KREötvös Loránd University · HUHUN-REN Research Centre for Natural Sciences · HUInstitute of Molecular Life Sciences · HUKorea Research Institute of Bioscience and Biotechnology · KRVrije Universiteit Brussel · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Thymosine β4 (Tß4) is a 43 amino acid long intrinsically disordered protein (IDP), which was initially identified as an actin-binding and sequestering molecule. Later it was described to have multiple other functions, such as regulation of endothelial cell differentiation, blood vessel formation, wound repair, cardiac cell migration, and survival.

Indexed as

fuzzy complexILKintrinsically disordered proteinmoonlightingPINCHstabilinThymosin β4uncoupled binding and foldingweak interaction

Identifiers

PMID28516021
PMCPMC5424802
OpenAlexW1997937668

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.