Evidence map›Paper›PMID 28155660›Full record

ArticleBMC systems biology2016

A novel index of protein-protein interface propensity improves interface residue recognition.

Wentao Dai, Aiping Wu, Liangxiao Ma, Yi-Xue Li, Taijiao Jiang, Yuan-Yuan Li

Abstract read
In one paragraph

Article in BMC systems biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

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14citing papers in PubMed
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1 · What the graph read from it

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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

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3 · Its place in the literature

Who cites it

14 citing papers in PubMed.

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  9. Mutation Edgotype Drives Fitness Effect in Human.Frontiers in bioinformatics · 2021
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4 · The record

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5 · Who and what money

Authors and funding

6 authors.

Wentao DaiShanghai Center for Bioinformation Technology, 1278 Keyuan Road, Shanghai, 2012035, People's Republic of China.
Aiping WuSuzhou Institute of Systems Medicine, Suzhou, Jiangsu, 215123, China.
Liangxiao MaShanghai Center for Bioinformation Technology, 1278 Keyuan Road, Shanghai, 2012035, People's Republic of China.
Yi-Xue LiShanghai Center for Bioinformation Technology, 1278 Keyuan Road, Shanghai, 2012035, People's Republic of China.
Taijiao JiangSuzhou Institute of Systems Medicine, Suzhou, Jiangsu, 215123, China. taijiao@ibms.pumc.edu.cn.
Yuan-Yuan LiShanghai Center for Bioinformation Technology, 1278 Keyuan Road, Shanghai, 2012035, People's Republic of China. yyli@scbit.org.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundProtein-protein interface holds important information of protein-protein interactions which play key roles in most biological processes. In the past few years, a lot of efforts have been made to improve interface residue recognition by characterizing protein-protein interfaces and extracting relevant features. However, most previous studies were carried out in a qualitative level, and there are also some inconsistencies between them.

resultsIn the present work, to improve interface residue recognition, we built a novel quantitative residue protein-protein interface propensity index (QIPI) and gained a comprehensive picture of protein-protein interface through analyzing protein-protein interfaces on our comprehensive protein-protein interfaces dataset (Astral2.05-40-4506). Furthermore, in order to assess the effect of QIPI in improving the protein-protein interface prediction, we developed an interface residue recognition method SPR (Single domain based Patch Recognition) based on the QIPI. The evaluation results proved that our novel QIPI is able to improve the interface residue recognition.

conclusionsThrough a comprehensive quantitative analysis of protein-protein interface, we constructed a novel quantitative protein-protein interface propensity index (QIPI), which could be easily applied to improve the interface residue recognition and helpful in understanding the protein-protein interface. AVAILABILITY: QIPI and SPR are available to non-commercial users at our website: http://www.scbit.org/QIPI/ .

Indexed as

Computational BiologyProtein Interaction MappingProteinsProtein Structure, SecondarySolventsProteinsSolvents

Identifiers

PMID28155660
PMCPMC5259823

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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.