Evidence map›Paper›PMID 31663691›Full record

ArticleMolecular informatics2020

ALADDIN: Docking Approach Augmented by Machine Learning for Protein Structure Selection Yields Superior Virtual Screening Performance.

Ningning Fan, Christoph A Bauer, Conrad Stork, Christina de Bruyn Kops, Johannes Kirchmair

Abstract read
In one paragraph

Article in Molecular informatics, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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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3 · Its place in the literature

Who cites it

4 citing papers in PubMed.

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4 · The record

Corrections and comments

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5 · Who and what money

Authors and funding

5 authors.

Ningning FanUniversität Hamburg, Faculty of Mathematics, Informatics and Natural Sciences, Department of Informatics, Center for Bioinformatics, 20146, Hamburg, Germany.ORCID 0000-0001-5588-9634
Christoph A BauerUniversity of Bergen, Department of Chemistry, N-5020, Bergen, Norway.ORCID 0000-0002-6035-6944
Conrad StorkUniversität Hamburg, Faculty of Mathematics, Informatics and Natural Sciences, Department of Informatics, Center for Bioinformatics, 20146, Hamburg, Germany.ORCID 0000-0002-5499-742X
Christina de Bruyn KopsUniversität Hamburg, Faculty of Mathematics, Informatics and Natural Sciences, Department of Informatics, Center for Bioinformatics, 20146, Hamburg, Germany.ORCID 0000-0001-8890-2137
Johannes KirchmairUniversität Hamburg, Faculty of Mathematics, Informatics and Natural Sciences, Department of Informatics, Center for Bioinformatics, 20146, Hamburg, Germany.ORCID 0000-0003-2667-5877

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein flexibility and solvation pose major challenges to docking algorithms and scoring functions. One established strategy for addressing these challenges is to use multiple protein conformations for docking (all-against-all ensemble docking). Recent studies have shown that the performance of ensemble docking can be improved by selecting the most relevant protein structures for docking. In search for a robust approach to protein structure selection, we have come up with an integrated mAchine Learning AnD DockINg approach (ALADDIN). ALADDIN employs a battery of random forest classifiers to select, individually for each compound of interest, from an ensemble of protein structures, the single most suitable protein structure for docking. ALADDIN outperformed the best single-structure docking runs, ensemble docking and a similarity-based docking approach on three out of four investigated targets, with up to 0.15, 0.11 and 0.16 higher area under the receiver operating characteristic curve (AUC) values, respectively. Only in the case of cytochrome P450 3A4, ALADDIN, like any of the other tested approaches, failed to obtain decent performance. ALADDIN can be particularly useful for structure-based virtual screening of malleable proteins, including kinases, some viral enzymes and anti-targets.

Indexed as

Machine LearningMolecular Docking SimulationAlgorithmsProtein ConformationProteinsProteinsensemble dockingmachine learningsimilarity-based dockingstructure selectionvirtual screening

Identifiers

PMID31663691
PMCPMC7187304

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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.