Evidence map›Paper›PMID 32453748›Full record

ArticlePLoS computational biology2020

Sequence-based prediction of protein binding mode landscapes.

Attila Horvath, Marton Miskei, Viktor Ambrus, Michele Vendruscolo, Monika Fuxreiter

Open access · goldAbstract read
In one paragraph

Article in PLoS computational biology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
3.5field-weighted citation impact, top 6% 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

37 citing papers in PubMed, 62 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Intrinsic disorder in the human vitreous proteome.International journal of biological macromolecules · 2024
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  11. Deep mutational scanning of the RNase III-like domain inFrontiers in cellular and infection microbiology · 2024
    Article
  12. CELLULAR RNA INTERACTS WITH MAVS TO PROMOTE ANTIVIRAL SIGNALING.bioRxiv : the preprint server for biology · 2023
    Article
  13. Review
  14. Article
  15. Review
  16. Antibiotics (Basel, Switzerland) · 2023
    Article
  17. Article
  18. Protein interactions: anything new?Essays in biochemistry · 2022
    Article
  19. SH2 Domains: Folding, Binding and Therapeutical Approaches.International journal of molecular sciences · 2022
    Review
  20. 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

5 authors at 3 institutions in 3 countries.

Attila HorvathMTA-DE Laboratory of Protein Dynamics, Department of Biochemistry and Molecular Biology, University of Debrecen, Debrecen, Hungary.ORCID 0000-0002-6127-8925
Marton MiskeiMTA-DE Laboratory of Protein Dynamics, Department of Biochemistry and Molecular Biology, University of Debrecen, Debrecen, Hungary.
Viktor AmbrusMTA-DE Laboratory of Protein Dynamics, Department of Biochemistry and Molecular Biology, University of Debrecen, Debrecen, Hungary.
Michele VendruscoloCentre for Misfolding Diseases, Department of Chemistry, University of Cambridge, Cambridge, United Kingdom.ORCID 0000-0002-3616-1610
Monika FuxreiterMTA-DE Laboratory of Protein Dynamics, Department of Biochemistry and Molecular Biology, University of Debrecen, Debrecen, Hungary.ORCID 0000-0002-4463-6727
University of Debrecen · HUAustralian National University · AUUniversity of Cambridge · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Interactions between disordered proteins involve a wide range of changes in the structure and dynamics of the partners involved. These changes can be classified in terms of binding modes, which include disorder-to-order (DO) transitions, when proteins fold upon binding, as well as disorder-to-disorder (DD) transitions, when the conformational heterogeneity is maintained in the bound states. Furthermore, systematic studies of these interactions are revealing that proteins may exhibit different binding modes with different partners. Proteins that exhibit this context-dependent binding can be referred to as fuzzy proteins. Here we investigate amino acid code for fuzzy binding in terms of the entropy of the probability distribution of transitions towards decreasing order. We implement these entropy calculations into the FuzPred (http://protdyn-fuzpred.org) algorithm to predict the range of context-dependent binding modes of proteins from their amino acid sequences. As we illustrate through a variety of examples, this method identifies those binding sites that are sensitive to the cellular context or post-translational modifications, and may serve as regulatory points of cellular pathways.

Indexed as

Binding SitesProtein BindingProtein Processing, Post-TranslationalAlgorithmsComputational BiologyDatabases, ProteineIF-2 KinaseEukaryotic Initiation Factor-2Fuzzy LogicHumansIntrinsically Disordered ProteinsProbabilityProtein DomainsProtein FoldingProteinsROC CurveEIF2AK2 protein, humaneIF-2 KinaseEukaryotic Initiation Factor-2Intrinsically Disordered ProteinsProteinsSaccharomyces cerevisiae ProteinsSUI2 protein, S cerevisiaeTP53 protein, humanTumor Suppressor Protein p53

Identifiers

PMID32453748
PMCPMC7304629
OpenAlexW3031661900

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.