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Many proteins form complexes to carry out their functions, making protein-protein interactions (PPIs) essential for an organism's survival. Most PPIs are stabilized by numerous weak noncovalent chemical forces. The physical shape of the interfaces determines the way two proteins interact. Many globular proteins have closely-matching shapes on their surfaces, which form a large number of weak bonds. Additionally, many PPIs occur between two helices or between a surface cleft and a...
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Postsynaptic potential (PSP) refers to a change in the electrical potential of a neuron when neurotransmitters released by presynaptic neurons bind to postsynaptic receptors. This potential can either be excitatory, leading to depolarization and ultimately action potential generation, or inhibitory, leading to hyperpolarization and suppression of the postsynaptic neuron.
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Synaptic integration mainly includes the summation of graded potentials. Graded potentials, regardless of their type, cause subtle alterations in membrane voltage, resulting in either depolarization or hyperpolarization. These incremental changes, when combined or summed, can propel the neuron toward its threshold. Consider, for example, a membrane experiencing a +15 mV shift, causing it to depolarize from -70 mV to -55 mV. In this scenario, graded potentials govern the membrane's ability to...
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Identifying Protein-protein Interaction Sites Using Peptide Arrays
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PSINDB: the postsynaptic protein-protein interaction database.

Zsofia E Kalman1, Dániel Dudola1, Bálint Mészáros2

  • 1Faculty of Information Technology and Bionics, Pázmány Péter Catholic University, Práter u. 50/A, Budapest 1083, Hungary.

Database : the Journal of Biological Databases and Curation
|March 2, 2022
PubMed
Summary
This summary is machine-generated.

Scientists created the Postsynaptic Interaction Database (PSINDB) to organize protein interactions in the postsynaptic region. This resource aids research into learning, memory, and neurobiology by providing accessible structural and biological data.

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Area of Science:

  • Neurobiology
  • Molecular Biology
  • Systems Biology

Background:

  • The postsynaptic region's protein network is crucial for learning and memory.
  • Existing data on protein-protein interactions (PPIs) are fragmented and lack detailed annotations.
  • A centralized, specialized resource is needed for understanding postsynaptic functions.

Purpose of the Study:

  • To create a comprehensive, freely available database of postsynaptic protein-protein interactions (PPIs).
  • To integrate detailed structural and biological information with PPI data.
  • To facilitate research in molecular neurobiology and systems biology.

Main Methods:

  • Collected postsynaptic PPI data from scientific literature.
  • Annotated interactions with structural features, binding regions, and experimental details.
  • Developed the Postsynaptic Interaction Database (PSINDB) for data accessibility.

Main Results:

  • PSINDB provides access to tens of thousands of postsynaptic PPIs.
  • The database includes detailed information on binding regions and structural features.
  • Data is annotated with experimental context for each interaction.

Conclusions:

  • PSINDB offers a valuable resource for molecular neurobiology research.
  • The database supports experimental design and computational modeling of postsynaptic networks.
  • PSINDB enhances the study of dynamic changes in protein networks.