Evidence map›Paper›PMID 35209064›Full record

ReviewMolecules (Basel, Switzerland)2022

Machine Learning Approaches for Metalloproteins.

Yue Yu, Ruobing Wang, Ruijie D Teo

Abstract readReview
In one paragraph

Review in Molecules (Basel, Switzerland), 2022. 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

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

4 citing papers in PubMed.

  1. Article
  2. Review
  3. Article
  4. 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

3 authors.

Yue YuDivision of Natural and Applied Sciences, Duke Kunshan University, Kunshan, Jiangsu 215316, China.ORCID 0000-0002-5509-2235
Ruobing WangDepartment of Chemistry, Duke University, Durham, NC 27708, USA.ORCID 0000-0002-2414-8777
Ruijie D TeoDepartment of Chemistry, Duke University, Durham, NC 27708, USA.ORCID 0000-0003-2203-9662

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Metalloproteins are a family of proteins characterized by metal ion binding, whereby the presence of these ions confers key catalytic and ligand-binding properties. Due to their ubiquity among biological systems, researchers have made immense efforts to predict the structural and functional roles of metalloproteins. Ultimately, having a comprehensive understanding of metalloproteins will lead to tangible applications, such as designing potent inhibitors in drug discovery. Recently, there has been an acceleration in the number of studies applying machine learning to predict metalloprotein properties, primarily driven by the advent of more sophisticated machine learning algorithms. This review covers how machine learning tools have consolidated and expanded our comprehension of various aspects of metalloproteins (structure, function, stability, ligand-binding interactions, and inhibitors). Future avenues of exploration are also discussed.

Indexed as

Machine LearningAmino Acid SequenceBinding SitesDrug DesignMetalloproteinsModels, MolecularProtein BindingProtein StabilityProteolysisStructure-Activity RelationshipMetalloproteinscleavage sitesdeep learninginhibitor designmachine learningmetalloenzymesmetalloproteinsprotein functionprotein stabilityprotein structure

Identifiers

PMID35209064
PMCPMC8878495

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.