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

14.3K
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...
14.3K
Protein Networks02:26

Protein Networks

4.4K
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,...
4.4K
Conserved Binding Sites01:49

Conserved Binding Sites

4.9K
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.
Binding sites are often located in large pockets, and if their location on a protein’s surface is unknown, it can be predicted using various approaches. The energetic method computationally...
4.9K
Protein Complex Assembly02:41

Protein Complex Assembly

16.3K
Proteins can form homomeric complexes with another unit of the same protein or heteromeric complexes with different types.  Most protein complexes self-assemble spontaneously via ordered pathways, while some proteins need assembly factors that guide their proper assembly. Despite the crowded intracellular environment, proteins usually interact with their correct partners and form functional complexes.
Many viruses self-assemble into a fully functional unit using the infected host cell to...
16.3K

You might also read

Related Articles

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

Sort by
Same author

The predictive value of fresh embryo transfer pregnancy results on frozen embryo transfer outcomes: a cohort study.

Frontiers in endocrinology·2026
Same author

Case Report: early regression and bladder-intact survival after limited-course immunotherapy-based systemic therapy in two patients with clinically staged bulky muscle-invasive bladder cancer.

Frontiers in immunology·2026
Same author

Global mining has undermined forest conservation within and beyond protected areas.

Nature communications·2026
Same author

ASMem: Anchor sparse memory for multi-domain knowledge editing of large language models.

Neural networks : the official journal of the International Neural Network Society·2026
Same author

FOXK1: a multifaceted regulator in metabolic reprogramming and disease progression.

Biology direct·2026
Same author

An ultrasensitive aptamer-based fluorescent biosensor for luteinizing hormone with mutually orthogonal DNAzyme and self-replication CHA amplification.

Analytical and bioanalytical chemistry·2026
Same journal

circ2DGNN: circRNA-Disease Association Prediction via Transformer-Based Graph Neural Network.

IEEE/ACM transactions on computational biology and bioinformatics·2024
Same journal

Hierarchical Hypergraph Learning in Association- Weighted Heterogeneous Network for miRNA- Disease Association Identification.

IEEE/ACM transactions on computational biology and bioinformatics·2024
Same journal

Discriminative Domain Adaption Network for Simultaneously Removing Batch Effects and Annotating Cell Types in Single-Cell RNA-Seq.

IEEE/ACM transactions on computational biology and bioinformatics·2024
Same journal

MLW-BFECF: A Multi-Weighted Dynamic Cascade Forest Based on Bilinear Feature Extraction for Predicting the Stage of Kidney Renal Clear Cell Carcinoma on Multi-Modal Gene Data.

IEEE/ACM transactions on computational biology and bioinformatics·2024
Same journal

An End-to-End Knowledge Graph Fused Graph Neural Network for Accurate Protein-Protein Interactions Prediction.

IEEE/ACM transactions on computational biology and bioinformatics·2024
Same journal

Generative Biomedical Event Extraction With Constrained Decoding Strategy.

IEEE/ACM transactions on computational biology and bioinformatics·2024
See all related articles

Related Experiment Video

Updated: Dec 13, 2025

A Comparative Approach to Characterize the Landscape of Host-Pathogen Protein-Protein Interactions
13:56

A Comparative Approach to Characterize the Landscape of Host-Pathogen Protein-Protein Interactions

Published on: July 18, 2013

11.5K

Seq-BEL: Sequence-Based Ensemble Learning for Predicting Virus-Human Protein-Protein Interaction.

Yingjun Ma, Tingting He, Yuting Tan

    IEEE/ACM Transactions on Computational Biology and Bioinformatics
    |August 6, 2020
    PubMed
    Summary
    This summary is machine-generated.

    This study introduces a novel Sequence-Based Ensemble Learning (Seq-BEL) method to predict virus-human protein-protein interactions (PPIs). Seq-BEL effectively identifies potential interactions, outperforming existing methods and showing strong generalization for new proteins.

    More Related Videos

    Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
    06:50

    Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

    Published on: January 26, 2024

    2.4K
    In Vivo Functional Study of Disease-associated Rare Human Variants Using Drosophila
    06:41

    In Vivo Functional Study of Disease-associated Rare Human Variants Using Drosophila

    Published on: August 20, 2019

    14.1K

    Related Experiment Videos

    Last Updated: Dec 13, 2025

    A Comparative Approach to Characterize the Landscape of Host-Pathogen Protein-Protein Interactions
    13:56

    A Comparative Approach to Characterize the Landscape of Host-Pathogen Protein-Protein Interactions

    Published on: July 18, 2013

    11.5K
    Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
    06:50

    Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

    Published on: January 26, 2024

    2.4K
    In Vivo Functional Study of Disease-associated Rare Human Variants Using Drosophila
    06:41

    In Vivo Functional Study of Disease-associated Rare Human Variants Using Drosophila

    Published on: August 20, 2019

    14.1K

    Area of Science:

    • Virology
    • Bioinformatics
    • Computational Biology

    Background:

    • Infectious diseases pose a significant global health challenge, necessitating a deeper understanding of viral infection mechanisms.
    • Predicting virus-human protein-protein interactions (PPIs) is crucial for controlling highly infectious viral diseases.
    • Existing prediction methods struggle with data imbalances, lack of non-interactive protein pairs, and poor generalization for viral proteins.

    Purpose of the Study:

    • To develop an effective computational method for predicting potential virus-human PPIs.
    • To address the limitations of traditional supervised learning and ensemble methods in PPI prediction.
    • To enhance the understanding of viral pathogenesis through accurate interaction prediction.

    Main Methods:

    • A Sequence-Based Ensemble Learning (Seq-BEL) method was proposed, utilizing amino acid sequences of human and viral proteins.
    • Seq-BEL calculates protein features and similarities based on known virus-human PPI networks.
    • A scoring system combines these features and similarities to predict potential PPIs.

    Main Results:

    • Seq-BEL demonstrated high success in predicting potential virus-human PPIs.
    • The method outperformed current state-of-the-art techniques in prediction accuracy.
    • Seq-BEL exhibited robust performance for novel human and viral proteins, indicating good generalization ability.

    Conclusions:

    • The Seq-BEL method is a robust and effective tool for predicting virus-human PPIs.
    • Its strong generalization capability makes it valuable for identifying interactions involving new proteins.
    • This approach contributes to understanding viral infection mechanisms and developing control strategies.