Literature DB >> 31783729

Correction to: Predicting protein inter-residue contacts using composite likelihood maximization and deep learning.

Haicang Zhang1,2, Qi Zhang1,2, Fusong Ju1,2, Jianwei Zhu1,2, Yujuan Gao3, Ziwei Xie4, Minghua Deng3, Shiwei Sun5, Wei-Mou Zheng6, Dongbo Bu7,8.   

Abstract

Following publication of the original article [1], the author explained that there are several errors in the original article.

Entities:  

Year:  2019        PMID: 31783729      PMCID: PMC6884776          DOI: 10.1186/s12859-019-3198-2

Source DB:  PubMed          Journal:  BMC Bioinformatics        ISSN: 1471-2105            Impact factor:   3.169


Correction to: BMC Bioinformatics (2019) 20:537 https://doi.org/10.1186/s12859-019-3051-7 Following publication of the original article [1], the author explained that there are several errors in the original article; 1. The figures’ order in HTML and PDF does not match with each other. 2. The figures are incorrect order; the images do not match with the captions. In this correction article the figures are shown correct with the correct captions. Comparison of prediction accuracy of top L/2 contacts reported by plmDCA(y-axis) and clmDCA(x-axis) with two sequence separation threshold on the PSICOV dataset. a Sequence separation >6 AA. b Sequence separation >23 AA Predicted contacts (top L/5; sequence separation >6 AA) for protein structure with PDB ID: 1ne2A by plmDCA and clmDCA. Red (green) dots indicate correct (incorrect) prediction, while grey dots indicate all true residue-residue contacts. a The comparison between clmDCA (in upper-left triangle) and plmDCA (in lower-right triangle). b The comparison between clmDCA (in upper-left triangle) and clmDCA after refining using deep residual network (in lower-right triangle) The relationship between the prediction accuracy and quality of MSA. Here the quality of MSA is measured using Neff, i.e. the number of effective homologous sequences. Dataset: PSICOV. Sequence separation: > 6 AA Native structure and predicted structures for protein structure with PDB ID: 1vmbA. a Native structure. b Structure built using contacts predicted by plmDCA (TMscore: 0.42). c Structure built using contacts predicted by clmDCA alone (TMscore: 0.55). d Structure built using contacts predicted by clmDCA together with deep learning for refinement (TMscore: 0.72) Procedure of clmDCA to predict inter-residue contacts. a For a query protein (1wlg_A as an example), we identified its homologues by running HHblits [59] against nr90 sequence database (parameter setting: j: 3, id: 90, cov: 70) and constructed multiple sequence alignment of these proteins. b The correlation among residues in MSA was disentangled using composite likelihood maximization technique, generating prediction of inter-residue contacts. c The predicted contacts were fed into a deep neural network for refinement. d The refined prediction of inter-residue contacts
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1.  Predicting protein inter-residue contacts using composite likelihood maximization and deep learning.

Authors:  Haicang Zhang; Qi Zhang; Fusong Ju; Jianwei Zhu; Yujuan Gao; Ziwei Xie; Minghua Deng; Shiwei Sun; Wei-Mou Zheng; Dongbo Bu
Journal:  BMC Bioinformatics       Date:  2019-10-29       Impact factor: 3.169

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1.  Application of DNA-Binding Protein Prediction Based on Graph Convolutional Network and Contact Map.

Authors:  Weizhong Lu; Nan Zhou; Yijie Ding; Hongjie Wu; Yu Zhang; Qiming Fu; Haiou Li
Journal:  Biomed Res Int       Date:  2022-01-17       Impact factor: 3.411

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