Illuminating the dark protein-protein interactome.
Full text not available from this repository.Item Type: | Article |
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Status: | Published |
Official URL: | https://doi.org/10.1016/j.crmeth.2022.100275 |
Journal or Publication Title: | Cell Reports Methods |
Volume: | 2 |
Number: | 8 |
Page Range: | p. 100275 |
Date: | 22 August 2022 |
Divisions: | Gene and Stem Cell Therapy |
Depositing User: | General Admin |
Identification Number: | 10.1016/j.crmeth.2022.100275 |
ISSN: | 26672375 |
Date Deposited: | 15 Mar 2023 04:32 |
Abstract: | In living systems, a complex network of protein-protein interactions (PPIs) underlies most biochemical events. The human protein-protein interactome has been surveyed using yeast two-hybrid (Y2H)- and mass spectrometry (MS)-based approaches such as affinity purification coupled to MS (AP-MS). Despite decades of systematic investigations and collaborative multi-disciplinary efforts, there is no "gold standard" for documenting PPIs. A surprisingly large fraction of the human interactome remains uncharted, which we refer to as the "dark interactome." In this review, we highlight the complexity of the human interactome and discuss the current status of the human reference interactome maps. We discuss why a large proportion of the human interactome has remained refractory to traditional approaches. We propose an experimental model that can enable the identification of the dark interactome in a cell-type-specific manner. We also propose a framework to implement when embarking on studies designed to rigorously identify and characterize protein interactions. |
Creators: | Creators Email Sharifi Tabar, Mehdi UNSPECIFIED Parsania, Chirag UNSPECIFIED Chen, Hong UNSPECIFIED Su, Xiao-Dong UNSPECIFIED Bailey, Charles G. UNSPECIFIED Rasko, John E.J. UNSPECIFIED |
Last Modified: | 15 Mar 2023 04:32 |
URI: | https://eprints.centenary.org.au/id/eprint/1430 |
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