BioPlex display: an interactive suite for large-scale AP–MS protein–protein interaction data

DK Schweppe, EL Huttlin, JW Harper… - Journal of proteome …, 2018 - ACS Publications
Journal of proteome research, 2018ACS Publications
The development of large-scale data sets requires a new means to display and disseminate
research studies to large audiences. Knowledge of protein–protein interaction (PPI)
networks has become a principle interest of many groups within the field of proteomics. At
the confluence of technologies, such as cross-linking mass spectrometry, yeast two-hybrid,
protein cofractionation, and affinity purification mass spectrometry (AP–MS), detection of
PPIs can uncover novel biological inferences at a high-throughput. Thus new platforms to …
The development of large-scale data sets requires a new means to display and disseminate research studies to large audiences. Knowledge of protein–protein interaction (PPI) networks has become a principle interest of many groups within the field of proteomics. At the confluence of technologies, such as cross-linking mass spectrometry, yeast two-hybrid, protein cofractionation, and affinity purification mass spectrometry (AP–MS), detection of PPIs can uncover novel biological inferences at a high-throughput. Thus new platforms to provide community access to large data sets are necessary. To this end, we have developed a web application that enables exploration and dissemination of the growing BioPlex interaction network. BioPlex is a large-scale interactome data set based on AP–MS of baits from the human ORFeome. The latest BioPlex data set release (BioPlex 2.0) contains 56 553 interactions from 5891 AP–MS experiments. To improve community access to this vast compendium of interactions, we developed BioPlex Display, which integrates individual protein querying, access to empirical data, and on-the-fly annotation of networks within an easy-to-use and mobile web application. BioPlex Display enables rapid acquisition of data from BioPlex and development of hypotheses based on protein interactions.
ACS Publications