Evidence map›Paper›PMID 30837676›Full record

ArticleScientific reports2019

DESTINI: A deep-learning approach to contact-driven protein structure prediction.

Mu Gao, Hongyi Zhou, Jeffrey Skolnick

Abstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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.

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3 · Its place in the literature

Who cites it

26 citing papers in PubMed.

  1. Review
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  8. High-Performance Deep Learning Toolbox for Genome-Scale Prediction of Protein Structure and Function.Workshop on Machine Learning in HPC Environments. Workshop on Machine Learning in HPC Environments · 2021
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  16. Incorporating Machine Learning into Established Bioinformatics Frameworks.International journal of molecular sciences · 2021
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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.

Mu GaoCenter for the Study of Systems Biology, School of Biological Sciences, Georgia Institute of Technology, Atlanta, GA, 30332, USA.
Hongyi ZhouCenter for the Study of Systems Biology, School of Biological Sciences, Georgia Institute of Technology, Atlanta, GA, 30332, USA.
Jeffrey SkolnickCenter for the Study of Systems Biology, School of Biological Sciences, Georgia Institute of Technology, Atlanta, GA, 30332, USA. skolnick@gatech.edu.

Funding

Purchase of a GPU cluster for deep learning applications in protein-protein interaction and supercomplex prediction and biochemical literature annotation.R35GM118039 · NIGMS · GEORGIA INSTITUTE OF TECHNOLOGY · PI JEFFREY SKOLNICK · 2016 to 2026
$5.8M
NIGMS NIH HHS R35 GM118039
6 · The paper itself

Abstract

The amino acid sequence of a protein encodes the blueprint of its native structure. To predict the corresponding structural fold from the protein's sequence is one of most challenging problems in computational biology. In this work, we introduce DESTINI (deep structural inference for proteins), a novel computational approach that combines a deep-learning algorithm for protein residue/residue contact prediction with template-based structural modelling. For the first time, the significantly improved predictive ability is demonstrated in the large-scale tertiary structure prediction of over 1,200 single-domain proteins. DESTINI successfully predicts the tertiary structure of four times the number of "hard" targets (those with poor quality templates) that were previously intractable, viz, a "glass-ceiling" for previous template-based approaches, and also improves model quality for "easy" targets (those with good quality templates). The significantly better performance by DESTINI is largely due to the incorporation of better contact prediction into template modelling. To understand why deep-learning accomplishes more accurate contact prediction, systematic clustering reveals that deep-learning predicts coherent, native-like contact patterns compared to co-evolutionary analysis. Taken together, this work presents a promising strategy towards solving the protein structure prediction problem.

Indexed as

Deep LearningComputational BiologyProteinsProtein Structure, TertiaryProteins

Identifiers

PMID30837676
PMCPMC6401133

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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.