Back

PPIAT:Target mass spectrometry based Protein-Protein interaction analytics tool

Kim, H.; Park, J.; Son, A.

2023-04-06 bioinformatics
10.1101/2023.04.04.535369 bioRxiv
Show abstract

MotivationThe formation of protein networking is critical for understanding the biological functions of proteins and the underlying mechanisms of disease. To gain insights into target proteins that interact with a particular disease, we need to profiling all the proteins involved in the disease beforehand. However, the profiling results may not necessarily match with an experimental target protein. Therefore, it is necessary to identify physical protein-protein interactions (PPIs) using various methods. The cross-linking mass spectrometry (XL-MS) method is a representative approach to identify physical interactions between proteins, but there are many challenges in calculating theoretical mass values for application to target mass spectrometry. ResultsThe research team developed PPIAT, which integrates information on reviewed human proteins, protein-protein interactions, cross-linkers, enzymes, and modifications. All functions are available for free on the web application. Availability and implementationThe PPIAT is available at www.ppiat.cnu.ac.kr Contactkimlab@cnu.ac.kr

Matching journals

The top 5 journals account for 50% of the predicted probability mass.

50% of probability mass above

"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.