Evidence map›Paper›PMID 29228193›Full record

ArticleBioinformatics (Oxford, England)2018

DeepSF: deep convolutional neural network for mapping protein sequences to folds.

Jie Hou, Badri Adhikari, Jianlin Cheng

Abstract read
In one paragraph

Article in Bioinformatics (Oxford, England), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
65citing 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

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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

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

  1. Pooled it
  2. Article
  3. Article
  4. Review
  5. Protein Structure Prediction Methods.Advances in experimental medicine and biology · 2026
    Review
  6. Article
  7. Endowing protein language models with structural knowledge.Bioinformatics (Oxford, England) · 2025
    Article
  8. SLAE: Strictly Local All-atom Environment for Protein Representation.bioRxiv : the preprint server for biology · 2025
    Article
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5 more citing papers are in PubMed but not listed here.

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.

Jie HouDepartment of Electrical Engineering and Computer Science, University of Missouri, Columbia, MO 65211, USA.
Badri AdhikariDepartment of Mathematics and Computer Science, University of Missouri-St. Louis, St. Louis, MO 63121, USA.
Jianlin ChengDepartment of Electrical Engineering and Computer Science, University of Missouri, Columbia, MO 65211, USA.

Funding

Integrated Prediction of Protein Struture at 1D, 2D and 3D LevelsR01GM093123 · NIGMS · UNIVERSITY OF MISSOURI-COLUMBIA · PI CHENG, JIANLIN · 2010 to 2023
$3.8M
NIGMS NIH HHS R01 GM093123
6 · The paper itself

Abstract

Motivation: Protein fold recognition is an important problem in structural bioinformatics. Almost all traditional fold recognition methods use sequence (homology) comparison to indirectly predict the fold of a target protein based on the fold of a template protein with known structure, which cannot explain the relationship between sequence and fold. Only a few methods had been developed to classify protein sequences into a small number of folds due to methodological limitations, which are not generally useful in practice. Results: We develop a deep 1D-convolution neural network (DeepSF) to directly classify any protein sequence into one of 1195 known folds, which is useful for both fold recognition and the study of sequence-structure relationship. Different from traditional sequence alignment (comparison) based methods, our method automatically extracts fold-related features from a protein sequence of any length and maps it to the fold space. We train and test our method on the datasets curated from SCOP1.75, yielding an average classification accuracy of 75.3%. On the independent testing dataset curated from SCOP2.06, the classification accuracy is 73.0%. We compare our method with a top profile-profile alignment method-HHSearch on hard template-based and template-free modeling targets of CASP9-12 in terms of fold recognition accuracy. The accuracy of our method is 12.63-26.32% higher than HHSearch on template-free modeling targets and 3.39-17.09% higher on hard template-based modeling targets for top 1, 5 and 10 predicted folds. The hidden features extracted from sequence by our method is robust against sequence mutation, insertion, deletion and truncation, and can be used for other protein pattern recognition problems such as protein clustering, comparison and ranking. Availability and implementation: The DeepSF server is publicly available at: http://iris.rnet.missouri.edu/DeepSF/. Contact: chengji@missouri.edu. Supplementary information: Supplementary data are available at Bioinformatics online.

Indexed as

Neural Networks, ComputerProtein FoldingSoftwareAnimalsComputational BiologyHumansModels, MolecularSequence AlignmentSequence Analysis, Protein

Identifiers

PMID29228193
PMCPMC5905591

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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.