Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Protein-protein Interfaces02:04

Protein-protein Interfaces

15.0K
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...
15.0K
Protein Networks02:26

Protein Networks

4.7K
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.
These interactions can be represented through maps depicting protein-protein interaction networks, represented as nodes and edges. Nodes are circles that are representative of a protein,...
4.7K
Protein Folding Quality Check in the RER01:29

Protein Folding Quality Check in the RER

5.5K
ER is the primary site for the maturation and folding of soluble and transmembrane secretory proteins. The calnexin cycle is a specific chaperone system that folds and assesses the confirmation of N-glycosylated proteins before they can exit the ER lumen. The primary players of this quality check pipeline are the lectins, ER-resident chaperones, and a glucosyl transferase enzyme. In case the calnexin system in the lumen fails to salvage a misfolded protein, it is transported to the cytoplasm...
5.5K

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Liposomal Cancer Drug Database (LCDD): a comprehensive resource for liposome research in cancer therapy and diagnosis.

Database : the journal of biological databases and curation·2025
Same author

Large-scale examination of early-age sex differences in neurotypical toddlers and those with autism spectrum disorder or other developmental conditions.

Nature human behaviour·2025
Same author

Efficacy and safety of mechanical transvenous lead extraction: median follow-up analysis and development of an experimental model for predicting survival post-extraction.

The Egyptian heart journal : (EHJ) : official bulletin of the Egyptian Society of Cardiology·2025
Same author

Beyond the Spectrum: Subtype-Specific Molecular Insights into Autism Spectrum Disorder Via Multimodal Data Integration.

medRxiv : the preprint server for health sciences·2024
Same author

Differences in regional brain structure in toddlers with autism are related to future language outcomes.

Nature communications·2024
Same author

Transcriptomic Analysis of Cyclamen persicum to Identify Invovled Genes in Triterpene Secondary Metabolites Pathway.

Biochemical genetics·2024

Related Experiment Video

Updated: Mar 21, 2026

Visualization of Protein-protein Interaction in Nuclear and Cytoplasmic Fractions by Co-immunoprecipitation and In Situ Proximity Ligation Assay
10:05

Visualization of Protein-protein Interaction in Nuclear and Cytoplasmic Fractions by Co-immunoprecipitation and In Situ Proximity Ligation Assay

Published on: January 16, 2017

13.5K

rpiCOOL: A tool for In Silico RNA-protein interaction detection using random forest.

Mohammad Akbaripour-Elahabad1, Javad Zahiri2, Reza Rafeh1

  • 1Department of Computer Engineering, Arak University, Arak, Iran.

Journal of Theoretical Biology
|May 3, 2016
PubMed
Summary

This study introduces rpiCOOL, a machine learning tool for predicting RNA-protein interactions (RPIs) using sequence data. It offers improved accuracy for RPI detection, aiding gene regulation and disease research.

Keywords:
Machine learningMotifRNA–protein interactionRPIRandom forest

More Related Videos

Sample Preparation for Mass Spectrometry-based Identification of RNA-binding Regions
10:52

Sample Preparation for Mass Spectrometry-based Identification of RNA-binding Regions

Published on: September 28, 2017

8.6K
Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions
08:07

Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions

Published on: August 2, 2015

8.5K

Related Experiment Videos

Last Updated: Mar 21, 2026

Visualization of Protein-protein Interaction in Nuclear and Cytoplasmic Fractions by Co-immunoprecipitation and In Situ Proximity Ligation Assay
10:05

Visualization of Protein-protein Interaction in Nuclear and Cytoplasmic Fractions by Co-immunoprecipitation and In Situ Proximity Ligation Assay

Published on: January 16, 2017

13.5K
Sample Preparation for Mass Spectrometry-based Identification of RNA-binding Regions
10:52

Sample Preparation for Mass Spectrometry-based Identification of RNA-binding Regions

Published on: September 28, 2017

8.6K
Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions
08:07

Probing High-density Functional Protein Microarrays to Detect Protein-protein Interactions

Published on: August 2, 2015

8.5K

Area of Science:

  • Bioinformatics
  • Computational Biology
  • Molecular Biology

Background:

  • RNA-protein interactions (RPIs) are crucial for post-transcriptional gene regulation and understanding complex diseases.
  • Experimental determination of RPIs is challenging, necessitating computational prediction methods.

Purpose of the Study:

  • To develop a novel machine learning method for predicting RPIs based on sequence information.
  • To identify informative sequence-derived features for accurate RPI prediction.

Main Methods:

  • A random forest classifier was employed using sequence composition, motif information, and repetitive patterns as descriptors.
  • Feature selection methods identified informative features, with sequence motifs and nucleotide composition proving effective.
  • The proposed method, rpiCOOL, was evaluated using 10-fold cross-validation on benchmark datasets.

Main Results:

  • The rpiCOOL method demonstrated superior performance compared to existing state-of-the-art methods across various metrics.
  • Sequence motifs and nucleotide composition were identified as significant contributors to RPI prediction accuracy.
  • Prediction accuracy varied significantly across different organisms, highlighting the need for organism-specific models.

Conclusions:

  • The developed machine learning approach effectively predicts RNA-protein interactions using sequence-based features.
  • rpiCOOL provides a valuable, user-friendly tool for researchers to predict RPIs, advancing gene regulation and disease studies.
  • The findings underscore the importance of sequence features and organism context in RPI prediction.