Evidence map›Paper›PMID 36139085›Full record

ReviewBiomolecules2022

Protein Function Analysis through Machine Learning.

Chris Avery, John Patterson, Tyler Grear, Theodore Frater, Donald J Jacobs

Abstract readReview
In one paragraph

Review in Biomolecules, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed, 1 pooled it
–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

13 citing papers in PubMed, 1 synthesis or guideline pooled it.

  1. Pooled it
  2. Article
  3. Article
  4. Review
  5. ESM-scan-A tool to guide amino acid substitutions.Protein science : a publication of the Protein Society · 2024
    Article
  6. Protein subcellular localization prediction tools.Computational and structural biotechnology journal · 2024
    Review
  7. Review
  8. Review
  9. Article
  10. Article
  11. Review
  12. Review
  13. 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.

Chris AveryDepartment of Bioinformatics and Genomics, University of North Carolina at Charlotte, Charlotte, NC 28223, USA.
John PattersonDepartment of Bioinformatics and Genomics, University of North Carolina at Charlotte, Charlotte, NC 28223, USA.
Tyler GrearDepartment of Bioinformatics and Genomics, University of North Carolina at Charlotte, Charlotte, NC 28223, USA.ORCID 0000-0002-8319-8432
Theodore FraterDepartment of Bioinformatics and Genomics, University of North Carolina at Charlotte, Charlotte, NC 28223, USA.
Donald J JacobsDepartment of Physics and Optical Science, University of North Carolina at Charlotte, Charlotte, NC 28223, USA.ORCID 0000-0001-7711-1639

Funding

Supplement: Student support for computationally designing peptides to interfere with p53-MDM2 and p53-sirtuin interactionR15GM146200 · NIGMS · UNIVERSITY OF NORTH CAROLINA CHARLOTTE · PI JACOBS, DONALD · 2022 to 2023
$611k
NIGMS NIH HHS R15 GM146200NIH HHS R15GM146200
6 · The paper itself

Abstract

Machine learning (ML) has been an important arsenal in computational biology used to elucidate protein function for decades. With the recent burgeoning of novel ML methods and applications, new ML approaches have been incorporated into many areas of computational biology dealing with protein function. We examine how ML has been integrated into a wide range of computational models to improve prediction accuracy and gain a better understanding of protein function. The applications discussed are protein structure prediction, protein engineering using sequence modifications to achieve stability and druggability characteristics, molecular docking in terms of protein-ligand binding, including allosteric effects, protein-protein interactions and protein-centric drug discovery. To quantify the mechanisms underlying protein function, a holistic approach that takes structure, flexibility, stability, and dynamics into account is required, as these aspects become inseparable through their interdependence. Another key component of protein function is conformational dynamics, which often manifest as protein kinetics. Computational methods that use ML to generate representative conformational ensembles and quantify differences in conformational ensembles important for function are included in this review. Future opportunities are highlighted for each of these topics.

Indexed as

Computational BiologyProteinsLigandsMachine LearningMolecular Docking SimulationMolecular Dynamics SimulationProtein ConformationLigandsProteinsallosteryconformational samplingforce fieldsmachine learningmolecular dockingprotein dynamicsprotein functionprotein–protein interactionsprotein structure prediction

Identifiers

PMID36139085
PMCPMC9496392

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.