Related Experiment Video
Updated: Jul 13, 2026

09:51
Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
Published on: July 16, 2017
15.6K
bia-binder: a web-native cloud compute service for the bioimage analysis community.
Craig T Russell1, Jean-Marie Burel2, Awais Athar1
1European Molecular Biology Laboratory, European Bioinformatics Institute (EMBL-EBI), Cambridge CB10 1SD, United Kingdom.
Bioinformatics (Oxford, England)
|July 22, 2025
Summary
BioImage Archive Binder (bia-binder) offers a free, web-based coding environment for bioimage analysis. This open-source tool enhances research accessibility and reproducibility by providing direct access to biological image databases.
Area of Science:
- Bioimage analysis
- Computational biology
- Scientific computing
Background:
- Bioimage analysis requires significant computational resources and specialized software.
- Unequal access to these resources hinders scientific progress and collaboration.
- Existing platforms may lack integration with major bioimage data repositories.
Purpose of the Study:
- To introduce BioImage Archive Binder (bia-binder), a novel, accessible coding environment.
- To facilitate bioimage analysis through cloud-based Jupyter Notebooks.
- To promote equitable access to computational tools and biological image data.
Main Methods:
- Development of an open-source, cloud-architectured, web-based platform (bia-binder).
- Integration with EMBL-EBI's Embassy Cloud for substantial computational power.
- Deployment using helmsman and helm, accessible via standard web browsers.
Main Results:
- bia-binder provides free, easy-to-use Jupyter Notebook environments.
- Direct and fast access to images from BioImage Archive, Image Data Resource, and BioStudies.
- The platform is open-source and publicly available for deployment.
Conclusions:
- bia-binder democratizes bioimage analysis by offering a free, cloud-hosted solution.
- The service mitigates inequalities in scientific resource access.
- Permanent links to coding environments will foster exploratory research and community use.
Related Concept Videos
Conserved Binding Sites
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 analyses the...
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 analyses the...
Conserved Binding Sites
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 analyses the...
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 analyses the...
Bioavailability: Overview
Bioavailability refers to the proportion of an unaltered drug that, after administration, enters the systemic circulation and can be distributed to the desired action site. Factors such as gastrointestinal (GI) absorption and liver biotransformation influence the bioavailability of a drug when it is administered orally. When a drug is administered intravenously, it enters the systemic circulation directly; by definition, its bioavailability is assumed to be 100%. The bioavailability of an...

