Evidence map›Paper›PMID 25713596›Full record

ArticleAlgorithms for molecular biology : AMB2015

Algorithmic approaches to protein-protein interaction site prediction.

Tristan T Aumentado-Armstrong, Bogdan Istrate, Robert A Murgita

Abstract read
In one paragraph

Article in Algorithms for molecular biology : AMB, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing 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

25 citing papers in PubMed.

  1. Review
  2. Assessing the functional impact of protein binding site definition.Protein science : a publication of the Protein Society · 2024
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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

3 authors.

Tristan T Aumentado-Armstrong *Department of Anatomy and Cell Biology, McGill University, Montreal, Canada.
Bogdan Istrate *Department of Anatomy and Cell Biology, McGill University, Montreal, Canada.
Robert A MurgitaDepartment of Microbiology and Immunology, McGill University, Montreal, Canada.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Interaction sites on protein surfaces mediate virtually all biological activities, and their identification holds promise for disease treatment and drug design. Novel algorithmic approaches for the prediction of these sites have been produced at a rapid rate, and the field has seen significant advancement over the past decade. However, the most current methods have not yet been reviewed in a systematic and comprehensive fashion. Herein, we describe the intricacies of the biological theory, datasets, and features required for modern protein-protein interaction site (PPIS) prediction, and present an integrative analysis of the state-of-the-art algorithms and their performance. First, the major sources of data used by predictors are reviewed, including training sets, evaluation sets, and methods for their procurement. Then, the features employed and their importance in the biological characterization of PPISs are explored. This is followed by a discussion of the methodologies adopted in contemporary prediction programs, as well as their relative performance on the datasets most recently used for evaluation. In addition, the potential utility that PPIS identification holds for rational drug design, hotspot prediction, and computational molecular docking is described. Finally, an analysis of the most promising areas for future development of the field is presented.

Indexed as

Biological databasesFeature selectionHomologyInterface typesMachine learningPrediction algorithmProtein-protein bindingProtein-protein interactionProtein-protein interfaceProtein structure

Identifiers

PMID25713596
PMCPMC4338852

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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.