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Related Concept Videos

Protein Networks02:26

Protein Networks

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An organism can have thousands of different proteins, and these proteins must cooperate to ensure the health of an organism. Proteins bind to other proteins and form complexes to carry out their functions. Many proteins interact with multiple other proteins creating a complex network of protein interactions.
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Protein-protein Interfaces02:04

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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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RNA Structure01:19

RNA Structure

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The basic structure of RNA consists of a string of ribonucleotides attached by phosphodiester bonds. Although most RNA is single-stranded, it can form complex secondary and tertiary structures. Such structures play essential roles in the regulation of transcription and translation.
Different Types of RNA Have the Same Basic Structure
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Conserved Binding Sites01:49

Conserved Binding Sites

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Many proteins’ biological role depends on their interactions with their ligands, small molecules that bind to specific locations on the protein known as ligand-binding sites. Ligand-binding sites are often conserved among homologous proteins as these sites are critical for protein function.
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Nucleic Acid Structure01:25

Nucleic Acid Structure

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The pentose sugar in DNA is deoxyribose, while in RNA the pentose sugar is ribose. The difference between the sugars is the presence of the hydroxyl group on the ribose's second carbon and a hydrogen on the deoxyribose's second carbon. The phosphate residue attaches to the hydroxyl group of the 5′ carbon of one sugar and the hydroxyl group of the 3′ carbon of the sugar of the next nucleotide, which forms  a 5′ to 3′ phosphodiester linkage.
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Protein Organization01:24

Protein Organization

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Proteins are polymers of amino acid residues. They are versatile and responsible for different cellular functions, including DNA replication, molecular transport, catalysis, and structural support. Proteins have a hierarchical structure comprising at least three levels of organization: primary, secondary, and tertiary structure. Some large proteins have a quaternary structure where individual protein subunits are linked together.
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RNA Secondary Structure Prediction Using High-throughput SHAPE
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diPaRIS: Dynamic and Interpretable Protein-RNA Interactions Prediction With U-Shaped Network and Novel Structure

Lishen Zhang1,2,3, Chengqian Lu4, Xiaoqing Peng5

  • 1School of Computer Science and Engineering, Central South University, Changsha, 410083, China.

Advanced Science (Weinheim, Baden-Wurttemberg, Germany)
|August 29, 2025
PubMed
Summary
This summary is machine-generated.

diPaRIS, a deep learning tool, accurately predicts dynamic protein-RNA interactions by integrating in vivo RNA structures. This method enhances understanding of gene-disease links and biological processes.

Keywords:
Protein‐RNA interactionsRNA structure encodingdeep learninginterpretable analysis

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Area of Science:

  • Molecular Biology
  • Computational Biology
  • Genomics

Background:

  • Protein-RNA interactions are crucial for biological processes and disease.
  • Existing computational methods struggle to capture nucleotide correlations within RNA structures.
  • Accurate prediction of these interactions is essential for understanding gene function and disease.

Purpose of the Study:

  • To develop a deep learning method, diPaRIS, for predicting dynamic protein-RNA interactions.
  • To improve the accuracy and interpretability of protein-RNA interaction predictions.
  • To integrate in vivo RNA structural information for enhanced predictive power.

Main Methods:

  • Developed diPaRIS, a deep learning model utilizing a U-shaped network architecture.
  • Introduced a novel encoding scheme for SHAPE-seq data to capture nucleotide correlations.
  • Integrated in vivo RNA structures for a comprehensive representation.

Main Results:

  • diPaRIS demonstrated superior performance across 44 datasets, achieving high accuracy, AUC, AUPR, and F1-scores.
  • The model excelled in cross-cell line predictions, outperforming existing methods.
  • Generated interpretable analyses, including sequence binding motifs and attribution maps.

Conclusions:

  • diPaRIS accurately predicts dynamic protein-RNA interactions and enhances interpretability.
  • The method provides insights into conserved binding patterns and functional interpretation of genetic variants.
  • Findings facilitate understanding of gene-disease associations in complex diseases.