Evidence map›Paper›PMID 37697267›Full record

ArticleBMC bioinformatics2023

Rinmaker: a fast, versatile and reliable tool to determine residue interaction networks in proteins.

Alvise Spanò, Lorenzo Fanton, Davide Pizzolato, Jacopo Moi, Francesco Vinci, Alberto Pesce, Cedrix J Dongmo Foumthuim, Achille Giacometti, Marta Simeoni

Abstract read
In one paragraph

Article in BMC bioinformatics, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

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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

2 citing papers in PubMed.

  1. Article
  2. Review
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

9 authors.

Alvise SpanòDepartment of Environmental Science, Computer Science and Statistics, University Ca' Foscari of Venice, Via Torino 155, 30172, Venice, Italy.
Lorenzo FantonDepartment of Environmental Science, Computer Science and Statistics, University Ca' Foscari of Venice, Via Torino 155, 30172, Venice, Italy.
Davide PizzolatoDepartment of Environmental Science, Computer Science and Statistics, University Ca' Foscari of Venice, Via Torino 155, 30172, Venice, Italy.
Jacopo MoiDepartment of Molecular Science and Nanosystems, University Ca' Foscari of Venice, Via Torino 155, 30172, Venice, Italy.
Francesco VinciDepartment of Environmental Science, Computer Science and Statistics, University Ca' Foscari of Venice, Via Torino 155, 30172, Venice, Italy.
Alberto PesceDepartment of Environmental Science, Computer Science and Statistics, University Ca' Foscari of Venice, Via Torino 155, 30172, Venice, Italy.
Cedrix J Dongmo FoumthuimDepartment of Molecular Science and Nanosystems, University Ca' Foscari of Venice, Via Torino 155, 30172, Venice, Italy.
Achille GiacomettiDepartment of Molecular Science and Nanosystems, University Ca' Foscari of Venice, Via Torino 155, 30172, Venice, Italy.
Marta SimeoniDepartment of Environmental Science, Computer Science and Statistics, University Ca' Foscari of Venice, Via Torino 155, 30172, Venice, Italy. simeoni@unive.it.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundResidue Interaction Networks (RINs) map the crystallographic description of a protein into a graph, where amino acids are represented as nodes and non-covalent bonds as edges. Determination and visualization of a protein as a RIN provides insights on the topological properties (and hence their related biological functions) of large proteins without dealing with the full complexity of the three-dimensional description, and hence it represents an invaluable tool of modern bioinformatics.

resultsWe present RINmaker, a fast, flexible, and powerful tool for determining and visualizing RINs that include all standard non-covalent interactions. RINmaker is offered as a cross-platform and open source software that can be used either as a command-line tool or through a web application or a web API service. We benchmark its efficiency against the main alternatives and provide explicit tests to show its performance and its correctness.

conclusionsRINmaker is designed to be fully customizable, from a simple and handy support for experimental research to a sophisticated computational tool that can be embedded into a large computational pipeline. Hence, it paves the way to bridge the gap between data-driven/machine learning approaches and numerical simulations of simple, physically motivated, models.

Indexed as

Amino AcidsComputational BiologyMachine LearningSoftwareAmino AcidsNon-covalent bondsProtein 3D structureResidue interaction network (RIN)

Identifiers

PMID37697267
PMCPMC10496328

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LicenceCC BY
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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.