Evidence map›Paper›PMID 35074909›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2022

Ultrafast end-to-end protein structure prediction enables high-throughput exploration of uncharacterized proteins.

Shaun M Kandathil, Joe G Greener, Andy M Lau, David T Jones

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing 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

15 citing papers in PubMed.

  1. Article
  2. Review
  3. Bioinformatic Analysis of WNT Family Proteins.Bioinformatics and biology insights · 2025
    Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. When will RNA get its AlphaFold moment?Nucleic acids research · 2023
    Article
  9. When will RNA get its AlphaFold moment?Nucleic acids research · 2023
    Article
  10. Review
  11. Open-Source Machine Learning in Computational Chemistry.Journal of chemical information and modeling · 2023
    Review
  12. Article
  13. Article
  14. Article
  15. 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

4 authors.

Shaun M KandathilDepartment of Computer Science, University College London, London, WC1E 6BT, United Kingdom.ORCID 0000-0002-2671-2140
Joe G GreenerDepartment of Computer Science, University College London, London, WC1E 6BT, United Kingdom.
Andy M LauDepartment of Computer Science, University College London, London, WC1E 6BT, United Kingdom.ORCID 0000-0003-0572-7826
David T JonesDepartment of Computer Science, University College London, London, WC1E 6BT, United Kingdom d.t.jones@ucl.ac.uk.ORCID 0000-0001-8626-3765

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Deep learning-based prediction of protein structure usually begins by constructing a multiple sequence alignment (MSA) containing homologs of the target protein. The most successful approaches combine large feature sets derived from MSAs, and considerable computational effort is spent deriving these input features. We present a method that greatly reduces the amount of preprocessing required for a target MSA, while producing main chain coordinates as a direct output of a deep neural network. The network makes use of just three recurrent networks and a stack of residual convolutional layers, making the predictor very fast to run, and easy to install and use. Our approach constructs a directly learned representation of the sequences in an MSA, starting from a one-hot encoding of the sequences. When supplemented with an approximate precision matrix, the learned representation can be used to produce structural models of comparable or greater accuracy as compared to our original DMPfold method, while requiring less than a second to produce a typical model. This level of accuracy and speed allows very large-scale three-dimensional modeling of proteins on minimal hardware, and we demonstrate this by producing models for over 1.3 million uncharacterized regions of proteins extracted from the BFD sequence clusters. After constructing an initial set of approximate models, we select a confident subset of over 30,000 models for further refinement and analysis, revealing putative novel protein folds. We also provide updated models for over 5,000 Pfam families studied in the original DMPfold paper.

Indexed as

Models, MolecularProtein ConformationSoftwareAlgorithmsCaspasesComputational BiologyDatabases, ProteinDeep LearningHigh-Throughput Screening AssaysProteinsCaspasesProteinsbioinformaticsmachine learningprotein structure prediction

Identifiers

PMID35074909
PMCPMC8795500

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.