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Construction of co-complex score matrix for protein complex prediction from AP-MS data

Motivation: Protein complexes are of great importance for unraveling the secrets of cellular organization and function. The AP-MS technique has provided an effective high-throughput screening to directly measure the co-complex relationship among multiple proteins, but its performance suffers from bo...

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Autores principales: Xie, Zhipeng, Kwoh, Chee Keong, Li, Xiao-Li, Wu, Min
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3117344/
https://www.ncbi.nlm.nih.gov/pubmed/21685066
http://dx.doi.org/10.1093/bioinformatics/btr212
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author Xie, Zhipeng
Kwoh, Chee Keong
Li, Xiao-Li
Wu, Min
author_facet Xie, Zhipeng
Kwoh, Chee Keong
Li, Xiao-Li
Wu, Min
author_sort Xie, Zhipeng
collection PubMed
description Motivation: Protein complexes are of great importance for unraveling the secrets of cellular organization and function. The AP-MS technique has provided an effective high-throughput screening to directly measure the co-complex relationship among multiple proteins, but its performance suffers from both false positives and false negatives. To computationally predict complexes from AP-MS data, most existing approaches either required the additional knowledge from known complexes (supervised learning), or had numerous parameters to tune. Method: In this article, we propose a novel unsupervised approach, without relying on the knowledge of existing complexes. Our method probabilistically calculates the affinity between two proteins, where the affinity score is evaluated by a co-complexed score or C2S in brief. In particular, our method measures the log-likelihood ratio of two proteins being co-complexed to being drawn randomly, and we then predict protein complexes by applying hierarchical clustering algorithm on the C2S score matrix. Results: Compared with existing approaches, our approach is computationally efficient and easy to implement. It has just one parameter to set and its value has little effect on the results. It can be applied to different species as long as the AP-MS data are available. Despite its simplicity, it is competitive or superior in performance over many aspects when compared with the state-of-the-art predictions performed by supervised or unsupervised approaches. Availability: The predicted complex sets in this article are available in the Supplementary information or by sending email to asckkwoh@ntu.edu.sg Contact: xlli@i2r.a-star.edu.sg Supplementary information: Supplementary data are available at Bioinformatics online.
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spelling pubmed-31173442011-06-17 Construction of co-complex score matrix for protein complex prediction from AP-MS data Xie, Zhipeng Kwoh, Chee Keong Li, Xiao-Li Wu, Min Bioinformatics Ismb/Eccb 2011 Proceedings Papers Committee July 17 to July 19, 2011, Vienna, Austria Motivation: Protein complexes are of great importance for unraveling the secrets of cellular organization and function. The AP-MS technique has provided an effective high-throughput screening to directly measure the co-complex relationship among multiple proteins, but its performance suffers from both false positives and false negatives. To computationally predict complexes from AP-MS data, most existing approaches either required the additional knowledge from known complexes (supervised learning), or had numerous parameters to tune. Method: In this article, we propose a novel unsupervised approach, without relying on the knowledge of existing complexes. Our method probabilistically calculates the affinity between two proteins, where the affinity score is evaluated by a co-complexed score or C2S in brief. In particular, our method measures the log-likelihood ratio of two proteins being co-complexed to being drawn randomly, and we then predict protein complexes by applying hierarchical clustering algorithm on the C2S score matrix. Results: Compared with existing approaches, our approach is computationally efficient and easy to implement. It has just one parameter to set and its value has little effect on the results. It can be applied to different species as long as the AP-MS data are available. Despite its simplicity, it is competitive or superior in performance over many aspects when compared with the state-of-the-art predictions performed by supervised or unsupervised approaches. Availability: The predicted complex sets in this article are available in the Supplementary information or by sending email to asckkwoh@ntu.edu.sg Contact: xlli@i2r.a-star.edu.sg Supplementary information: Supplementary data are available at Bioinformatics online. Oxford University Press 2011-07-01 2011-06-14 /pmc/articles/PMC3117344/ /pubmed/21685066 http://dx.doi.org/10.1093/bioinformatics/btr212 Text en © The Author(s) 2011. Published by Oxford University Press. http://creativecommons.org/licenses/by-nc/2.5 This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.5), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Ismb/Eccb 2011 Proceedings Papers Committee July 17 to July 19, 2011, Vienna, Austria
Xie, Zhipeng
Kwoh, Chee Keong
Li, Xiao-Li
Wu, Min
Construction of co-complex score matrix for protein complex prediction from AP-MS data
title Construction of co-complex score matrix for protein complex prediction from AP-MS data
title_full Construction of co-complex score matrix for protein complex prediction from AP-MS data
title_fullStr Construction of co-complex score matrix for protein complex prediction from AP-MS data
title_full_unstemmed Construction of co-complex score matrix for protein complex prediction from AP-MS data
title_short Construction of co-complex score matrix for protein complex prediction from AP-MS data
title_sort construction of co-complex score matrix for protein complex prediction from ap-ms data
topic Ismb/Eccb 2011 Proceedings Papers Committee July 17 to July 19, 2011, Vienna, Austria
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3117344/
https://www.ncbi.nlm.nih.gov/pubmed/21685066
http://dx.doi.org/10.1093/bioinformatics/btr212
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