4.5 Article

PSINDB: the postsynaptic protein-protein interaction database

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OXFORD UNIV PRESS
DOI: 10.1093/database/baac007

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资金

  1. European Union's Horizon 2020 research and innovation program [842490]
  2. National Research, Development and Innovation Office (NKFIH) [NN124363, TKP2020-NKA-11]
  3. Marie Curie Actions (MSCA) [842490] Funding Source: Marie Curie Actions (MSCA)

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The postsynaptic region is crucial for fundamental mechanisms such as learning and memory, and a comprehensive understanding of its protein-protein interactions (PPIs) is necessary. To address the scattered nature of PPI data, a freely available resource called the Postsynaptic Interaction Database (PSINDB) was developed. PSINDB contains detailed structural and biological information for thousands of PPIs, providing a valuable tool for molecular neurobiology research.
The postsynaptic region is the receiving part of the synapse comprising thousands of proteins forming an elaborate and dynamically changing network indispensable for the molecular mechanisms behind fundamental phenomena such as learning and memory. Despite the growing amount of information about individual protein-protein interactions (PPIs) in this network, these data are mostly scattered in the literature or stored in generic databases that are not designed to display aspects that are fundamental to the understanding of postsynaptic functions. To overcome these limitations, we collected postsynaptic PPIs complemented by a high amount of detailed structural and biological information and launched a freely available resource, the Postsynaptic Interaction Database (PSINDB), to make these data and annotations accessible. PSINDB includes tens of thousands of binding regions together with structural features, mediating and regulating the formation of PPIs, annotated with detailed experimental information about each interaction. PSINDB is expected to be useful for various aspects of molecular neurobiology research, from experimental design to network and systems biology-based modeling and analysis of changes in the protein network upon various stimuli.

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