Evidence map›Paper›PMID 30002402›Full record

ArticleScientific reports2018

IDPpi: Protein-Protein Interaction Analyses of Human Intrinsically Disordered Proteins.

Vladimir Perovic, Neven Sumonja, Lindsey A Marsh, Sandro Radovanovic, Milan Vukicevic, Stefan G E Roberts, Nevena Veljkovic

Abstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
–field-weighted citation impact
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

16 citing papers in PubMed.

  1. Article
  2. 'Intelligent' proteins.Cellular and molecular life sciences : CMLS · 2025
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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

7 authors.

Vladimir PerovicCentre for Multidisciplinary Research and Engineering, Vinca Institute of Nuclear Sciences, University of Belgrade, Belgrade, Serbia.
Neven SumonjaCentre for Multidisciplinary Research and Engineering, Vinca Institute of Nuclear Sciences, University of Belgrade, Belgrade, Serbia.
Lindsey A MarshSchool of Cellular and Molecular Medicine, University of Bristol, Bristol, UK.
Sandro RadovanovicCentre for business decision making, Faculty of organizational Sciences, University of Belgrade, Belgrade, Serbia.
Milan VukicevicCentre for business decision making, Faculty of organizational Sciences, University of Belgrade, Belgrade, Serbia.
Stefan G E RobertsSchool of Cellular and Molecular Medicine, University of Bristol, Bristol, UK.
Nevena VeljkovicCentre for Multidisciplinary Research and Engineering, Vinca Institute of Nuclear Sciences, University of Belgrade, Belgrade, Serbia. nevenav@vin.bg.ac.rs.

Funding

Biotechnology and Biological Sciences Research Council (BBSRC) BB/K000446/1European Cooperation in Science and Technology (COST) BM1405Ministarstvo Prosvete, Nauke i Tehnološkog Razvoja (Ministry of Education, Science and Technological Development of the Republic of Serbia) 173001Ministarstvo Prosvete, Nauke i Tehnološkog Razvoja (Ministry of Education, Science and Technological Development of the Republic of Serbia) III 41008Ministarstvo Prosvete, Nauke i Tehnološkog Razvoja (Ministry of Education, Science and Technological Development of the Republic of Serbia) TR 32013
6 · The paper itself

Abstract

Intrinsically disordered proteins (IDPs) are characterized by the lack of a fixed tertiary structure and are involved in the regulation of key biological processes via binding to multiple protein partners. IDPs are malleable, adapting to structurally different partners, and this flexibility stems from features encoded in the primary structure. The assumption that universal sequence information will facilitate coverage of the sparse zones of the human interactome motivated us to explore the possibility of predicting protein-protein interactions (PPIs) that involve IDPs based on sequence characteristics. We developed a method that relies on features of the interacting and non-interacting protein pairs and utilizes machine learning to classify and predict IDP PPIs. Consideration of both sequence determinants specific for conformational organizations and the multiplicity of IDP interactions in the training phase ensured a reliable approach that is superior to current state-of-the-art methods. By applying a strict evaluation procedure, we confirm that our method predicts interactions of the IDP of interest even on the proteome-scale. This service is provided as a web tool to expedite the discovery of new interactions and IDP functions with enhanced efficiency.

Indexed as

Amino Acid SequenceComputational BiologyDatasets as TopicHumansIntrinsically Disordered ProteinsMachine LearningMCF-7 CellsModels, MolecularMolecular Sequence AnnotationProtein BindingProtein Interaction MappingProtein Interaction MapsProteomeIntrinsically Disordered ProteinsProteome

Identifiers

PMID30002402
PMCPMC6043496

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Registered trials

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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.