Evidence map›Paper›PMID 35762726›Full record

ReviewProtein science : a publication of the Protein Society2022

Capturing the geometry, function, and evolution of enzymes with 3D templates.

Ioannis G Riziotis, Janet M Thornton

Abstract readReview
In one paragraph

Review in Protein science : a publication of the Protein Society, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing 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

9 citing papers in PubMed.

  1. Investigating enzyme function by geometric matching of catalytic motifs.Protein science : a publication of the Protein Society · 2026
    Article
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  4. Review
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  9. Capturing the geometry, function, and evolution of enzymes with 3D templates.Protein science : a publication of the Protein Society · 2022
    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

2 authors.

Ioannis G RiziotisEuropean Bioinformatics Institute (EMBL-EBI), Cambridge.ORCID 0000-0002-4035-1839
Janet M ThorntonEuropean Bioinformatics Institute (EMBL-EBI), Cambridge.ORCID 0000-0003-0824-4096

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Structural templates are 3D signatures representing protein functional sites, such as ligand binding cavities, metal coordination motifs, or catalytic sites. Here we explore methods to generate template libraries and algorithms to query structures for conserved 3D motifs. Applications of templates are discussed, as well as some exemplar cases for examining evolutionary links in enzymes. We also introduce the concept of using more than one template per structure to represent flexible sites, as an approach to better understand catalysis through snapshots captured in enzyme structures. Functional annotation from structure is an important topic that has recently resurfaced due to the new more accurate methods of protein structure prediction. Therefore, we anticipate that template-based functional site detection will be a powerful tool in the task of characterizing a vast number of new protein models.

Indexed as

AlgorithmsProteinsCatalytic DomainProtein ConformationProteinsactive sitecatalysisenzymestructuretemplate

Identifiers

PMID35762726
PMCPMC9207746

What OpenQuestion holds

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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.