Evidence map›Paper›PMID 22461885›Full record

ArticlePloS one2012

A unified multitask architecture for predicting local protein properties.

Yanjun Qi, Merja Oja, Jason Weston, William Stafford Noble

Abstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
18citing 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

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

  1. Pooled it
  2. Deep learning for protein secondary structure prediction: Pre and post-AlphaFold.Computational and structural biotechnology journal · 2022
    Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Opportunities and obstacles for deep learning in biology and medicine.Journal of the Royal Society, Interface · 2018
    Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Deep Learning for Population Genetic Inference.PLoS computational biology · 2016
    Article
  15. Article
  16. Review
  17. Article
  18. A Deep Learning Network Approach to ab initio Protein Secondary Structure Prediction.IEEE/ACM transactions on computational biology and bioinformatics
    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.

Yanjun QiMachine Learning Department, NEC Labs America, Princeton, New Jersey, United States of America.
Merja Oja
Jason Weston
William Stafford Noble

Funding

ZDS2P REGULATES SWE1P-DEPENDENT POLARIZED CELL GROWTH IN S CEREVISIAEP41RR011823 · NCRR · UNIVERSITY OF WASHINGTON · PI DAVIS, TRACY · 1996 to 2011
$24.7M
Recognizing protein folds with discriminative learningR01GM074257 · NIGMS · SLOAN-KETTERING INST CAN RESEARCH · PI LESLIE, CHRISTINA S · 2005 to 2009
$1.5M
NCRR NIH HHS P41 RR0011823NCRR NIH HHS P41 RR011823NIGMS NIH HHS R01 GM074257
6 · The paper itself

Abstract

A variety of functionally important protein properties, such as secondary structure, transmembrane topology and solvent accessibility, can be encoded as a labeling of amino acids. Indeed, the prediction of such properties from the primary amino acid sequence is one of the core projects of computational biology. Accordingly, a panoply of approaches have been developed for predicting such properties; however, most such approaches focus on solving a single task at a time. Motivated by recent, successful work in natural language processing, we propose to use multitask learning to train a single, joint model that exploits the dependencies among these various labeling tasks. We describe a deep neural network architecture that, given a protein sequence, outputs a host of predicted local properties, including secondary structure, solvent accessibility, transmembrane topology, signal peptides and DNA-binding residues. The network is trained jointly on all these tasks in a supervised fashion, augmented with a novel form of semi-supervised learning in which the model is trained to distinguish between local patterns from natural and synthetic protein sequences. The task-independent architecture of the network obviates the need for task-specific feature engineering. We demonstrate that, for all of the tasks that we considered, our approach leads to statistically significant improvements in performance, relative to a single task neural network approach, and that the resulting model achieves state-of-the-art performance.

Indexed as

Neural Networks, ComputerProtein Structure, SecondaryAlgorithmsBinding SitesComputational BiologyMembrane ProteinsProteinsReproducibility of ResultsMembrane ProteinsProteins

Identifiers

PMID22461885
PMCPMC3312883

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.