Evidence map›Paper›PMID 33812316›Full record

ReviewCurrent opinion in chemical biology2021

Intrinsically disordered proteins and biomolecular condensates as drug targets.

Mateusz Biesaga, Marta Frigolé-Vivas, Xavier Salvatella

Open access · greenAbstract readReview
In one paragraph

Review in Current opinion in chemical biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
6.4field-weighted citation impact, top 2% 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

62 citing papers in PubMed, 119 citations in OpenAlex.

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  16. Ensemble Docking for Intrinsically Disordered Proteins.Journal of chemical information and modeling · 2025
    Article
  17. Article
  18. Conformational signatures induced by ubiquitin modification in the amyloid-forming tau repeat domain.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  19. Article
  20. Article

2 more citing papers are in PubMed but not listed here.

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

3 authors at 2 institutions in 1 country.

Mateusz BiesagaInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Baldiri Reixac 10, 08028, Barcelona, Spain; Joint BSC-IRB Research Programme in Computational Biology, Baldiri Reixac 10, 08028, Barcelona, Spain.
Marta Frigolé-VivasInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Baldiri Reixac 10, 08028, Barcelona, Spain; Joint BSC-IRB Research Programme in Computational Biology, Baldiri Reixac 10, 08028, Barcelona, Spain.
Xavier SalvatellaInstitute for Research in Biomedicine (IRB Barcelona), The Barcelona Institute of Science and Technology, Baldiri Reixac 10, 08028, Barcelona, Spain; Joint BSC-IRB Research Programme in Computational Biology, Baldiri Reixac 10, 08028, Barcelona, Spain; ICREA, Passeig Lluís Companys 23, 08010, Barcelona, Spain. Electronic address: xavier.salvatella@irbbarcelona.org.
Universitat Politècnica de Catalunya · ESInstitute for Research in Biomedicine · ES

Funding

European Research Council 648201
6 · The paper itself

Abstract

Intrinsically disordered domains represent attractive therapeutic targets because they play key roles in cancer, as well as in neurodegenerative and infectious diseases. They are, however, considered undruggable because they do not form stable binding pockets for small molecules and, therefore, have not been prioritized in drug discovery. Under physiological solution conditions many biomedically relevant intrinsically disordered proteins undergo phase separation processes leading to the formation of mesoscopic highly dynamic assemblies, generally known as biomolecular condensates that define environments that can be quite different from the solutions surrounding them. In what follows, we review key recent findings in this area and show how biomolecular condensation can offer opportunities for modulating the activities of intrinsically disordered targets.

Indexed as

1-(5-Isoquinolinesulfonyl)-2-MethylpiperazineDrug DiscoveryHumansIntrinsically Disordered ProteinsPharmaceutical PreparationsPhase TransitionProtein BindingProtein MultimerizationPyrimidinesStructure-Activity RelationshipThermodynamicsTransition Temperature1-(5-Isoquinolinesulfonyl)-2-MethylpiperazinefasudilIntrinsically Disordered ProteinsPharmaceutical PreparationsPyrimidinesSEN1576Biomolecular condensatesDrug discoveryFree energy landscapeIntrinsically disordered proteins

Identifiers

PMID33812316
PMCPMC7616887
OpenAlexW3149136862

What OpenQuestion holds

Textmetadata
LicenceTDM
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.