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Dynamics of the discovery process of protein-protein interactions from low content studies

BACKGROUND: Thousands of biological and biomedical investigators study of the functional role of single genes and their protein products in normal physiology and in disease. The findings from these studies are reported in research articles that stimulate new research. It is now established that a co...

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Autores principales: Wang, Zichen, Clark, Neil R., Ma’ayan, Avi
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BioMed Central 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4456804/
https://www.ncbi.nlm.nih.gov/pubmed/26048415
http://dx.doi.org/10.1186/s12918-015-0173-z
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author Wang, Zichen
Clark, Neil R.
Ma’ayan, Avi
author_facet Wang, Zichen
Clark, Neil R.
Ma’ayan, Avi
author_sort Wang, Zichen
collection PubMed
description BACKGROUND: Thousands of biological and biomedical investigators study of the functional role of single genes and their protein products in normal physiology and in disease. The findings from these studies are reported in research articles that stimulate new research. It is now established that a complex regulatory networks's is controlling human cellular fate, and this community of researchers are continually unraveling this network topology. Attempts to integrate results from such accumulated knowledge resulted in literature-based protein-protein interaction networks (PPINs) and pathway databases. These databases are widely used by the community to analyze new data collected from emerging genome-wide studies with the assumption that the data within these literature-based databases is the ground truth and contain no biases. While suspicion for research focus biases is growing, a concrete proof for it is still missing. It is difficult to prove because the real PPINs are mostly unknown. RESULTS: Here we analyzed the longitudinal discovery process of literature-based mammalian and yeast PPINs to observe that these networks are discovered non-uniformly. The pattern of discovery is related to a theoretical concept proposed by Kauffman called “expanding the adjacent possible”. We introduce a network discovery model which explicitly includes the space of possibilities in the form of a true underlying PPIN. CONCLUSIONS: Our model strongly suggests that research focus biases exist in the observed discovery dynamics of these networks. In summary, more care should be placed when using PPIN databases for analysis of newly acquired data, and when considering prior knowledge when designing new experiments. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12918-015-0173-z) contains supplementary material, which is available to authorized users.
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spelling pubmed-44568042015-06-06 Dynamics of the discovery process of protein-protein interactions from low content studies Wang, Zichen Clark, Neil R. Ma’ayan, Avi BMC Syst Biol Research Article BACKGROUND: Thousands of biological and biomedical investigators study of the functional role of single genes and their protein products in normal physiology and in disease. The findings from these studies are reported in research articles that stimulate new research. It is now established that a complex regulatory networks's is controlling human cellular fate, and this community of researchers are continually unraveling this network topology. Attempts to integrate results from such accumulated knowledge resulted in literature-based protein-protein interaction networks (PPINs) and pathway databases. These databases are widely used by the community to analyze new data collected from emerging genome-wide studies with the assumption that the data within these literature-based databases is the ground truth and contain no biases. While suspicion for research focus biases is growing, a concrete proof for it is still missing. It is difficult to prove because the real PPINs are mostly unknown. RESULTS: Here we analyzed the longitudinal discovery process of literature-based mammalian and yeast PPINs to observe that these networks are discovered non-uniformly. The pattern of discovery is related to a theoretical concept proposed by Kauffman called “expanding the adjacent possible”. We introduce a network discovery model which explicitly includes the space of possibilities in the form of a true underlying PPIN. CONCLUSIONS: Our model strongly suggests that research focus biases exist in the observed discovery dynamics of these networks. In summary, more care should be placed when using PPIN databases for analysis of newly acquired data, and when considering prior knowledge when designing new experiments. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (doi:10.1186/s12918-015-0173-z) contains supplementary material, which is available to authorized users. BioMed Central 2015-06-06 /pmc/articles/PMC4456804/ /pubmed/26048415 http://dx.doi.org/10.1186/s12918-015-0173-z Text en © Wang et al. 2015 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly credited. The Creative Commons Public Domain Dedication waiver (http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated.
spellingShingle Research Article
Wang, Zichen
Clark, Neil R.
Ma’ayan, Avi
Dynamics of the discovery process of protein-protein interactions from low content studies
title Dynamics of the discovery process of protein-protein interactions from low content studies
title_full Dynamics of the discovery process of protein-protein interactions from low content studies
title_fullStr Dynamics of the discovery process of protein-protein interactions from low content studies
title_full_unstemmed Dynamics of the discovery process of protein-protein interactions from low content studies
title_short Dynamics of the discovery process of protein-protein interactions from low content studies
title_sort dynamics of the discovery process of protein-protein interactions from low content studies
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4456804/
https://www.ncbi.nlm.nih.gov/pubmed/26048415
http://dx.doi.org/10.1186/s12918-015-0173-z
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