Evidence map›Paper›PMID 33770072›Full record

ArticlePLoS computational biology2021

Deducing high-accuracy protein contact-maps from a triplet of coevolutionary matrices through deep residual convolutional networks.

Yang Li, Chengxin Zhang, Eric W Bell, Wei Zheng, Xiaogen Zhou, Dong-Jun Yu, Yang Zhang

Abstract read
In one paragraph

Article in PLoS computational biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing 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

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3 · Its place in the literature

Who cites it

36 citing papers in PubMed.

  1. Article
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  6. Recent Progress of Protein Tertiary Structure Prediction.Molecules (Basel, Switzerland) · 2024
    Review
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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

7 authors.

Yang LiSchool of Computer Science and Engineering, Nanjing University of Science and Technology, Nanjing, China.ORCID 0000-0003-2480-1972
Chengxin ZhangDepartment of Computational Medicine and Bioinformatics, University of Michigan, Ann Arbor, Michigan, United States of America.ORCID 0000-0001-7290-1324
Eric W BellDepartment of Computational Medicine and Bioinformatics, University of Michigan, Ann Arbor, Michigan, United States of America.ORCID 0000-0002-3419-4398
Wei ZhengDepartment of Computational Medicine and Bioinformatics, University of Michigan, Ann Arbor, Michigan, United States of America.ORCID 0000-0002-2984-9003
Xiaogen ZhouDepartment of Computational Medicine and Bioinformatics, University of Michigan, Ann Arbor, Michigan, United States of America.ORCID 0000-0001-6839-1923
Dong-Jun YuSchool of Computer Science and Engineering, Nanjing University of Science and Technology, Nanjing, China.ORCID 0000-0002-6786-8053
Yang ZhangDepartment of Computational Medicine and Bioinformatics, University of Michigan, Ann Arbor, Michigan, United States of America.ORCID 0000-0002-2739-1916

Funding

Structure-based functional annotation of microbial genomesR01AI134678 · NIAID · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI Lydia Petra Freddolino, SCOTT J. HULTGREN · 2018 to 2026
$6.5M
Training Program in BioinformaticsT32GM070449 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ATHEY, BRIAN DAVID, BURMEISTER, MARGIT · 2005 to 2020
$3.6M
Advanced approaches to protein structure predictionR35GM136422 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ZHANG, YANG · 2020 to 2021
$946k
High-Performance Computing Cluster for Biomedical ResearchS10OD026825 · OD · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI ATHEY, BRIAN DAVID · 2020 to 2020
$600k
NIAID NIH HHS R01 AI134678NIGMS NIH HHS R35 GM136422NIGMS NIH HHS T32 GM070449NIH HHS S10 OD026825
6 · The paper itself

Abstract

The topology of protein folds can be specified by the inter-residue contact-maps and accurate contact-map prediction can help ab initio structure folding. We developed TripletRes to deduce protein contact-maps from discretized distance profiles by end-to-end training of deep residual neural-networks. Compared to previous approaches, the major advantage of TripletRes is in its ability to learn and directly fuse a triplet of coevolutionary matrices extracted from the whole-genome and metagenome databases and therefore minimize the information loss during the course of contact model training. TripletRes was tested on a large set of 245 non-homologous proteins from CASP 11&12 and CAMEO experiments and outperformed other top methods from CASP12 by at least 58.4% for the CASP 11&12 targets and 44.4% for the CAMEO targets in the top-L long-range contact precision. On the 31 FM targets from the latest CASP13 challenge, TripletRes achieved the highest precision (71.6%) for the top-L/5 long-range contact predictions. It was also shown that a simple re-training of the TripletRes model with more proteins can lead to further improvement with precisions comparable to state-of-the-art methods developed after CASP13. These results demonstrate a novel efficient approach to extend the power of deep convolutional networks for high-accuracy medium- and long-range protein contact-map predictions starting from primary sequences, which are critical for constructing 3D structure of proteins that lack homologous templates in the PDB library.

Indexed as

Neural Networks, ComputerProteinsComputational BiologyProtein ConformationProtein FoldingReproducibility of ResultsSequence Analysis, ProteinProteins

Identifiers

PMID33770072
PMCPMC8026059

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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.