ArticleDatabase : the journal of biological databases and curation2016
CoDNaS 2.0: a comprehensive database of protein conformational diversity in the native state.
Article in Database : the journal of biological databases and curation, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
- Generation of Pathway Signatures by Combining Normal Modes with Weighted Ensemble Simulations.bioRxiv : the preprint server for biology · 2026Article
- Disentangling coevolutionary constraints for modeling protein conformational heterogeneity.Communications chemistry · 2026Article
- Beyond static structures: protein dynamic conformations modeling in the post-AlphaFold era.Briefings in bioinformatics · 2025Review
- AlphaFold2-Based Characterization of Apo and Holo Protein Structures and Conformational Ensembles Using Randomized Alanine Sequence Scanning Adaptation: Capturing Shared Signature Dynamics and Ligand-Induced Conformational Changes.International journal of molecular sciences · 2024Article
- Exploring protein functions from structural flexibility using CABS-flex modeling.Protein science : a publication of the Protein Society · 2024Review
- Data-driven probabilistic definition of the low energy conformational states of protein residues.NAR genomics and bioinformatics · 2024Article
- ThermoPCD: a database of molecular dynamics trajectories of antibody-antigen complexes at physiologic and fever-range temperatures.Database : the journal of biological databases and curation · 2024Article
- Searching for Frataxin Function: Exploring the Analogy with Nqo15, the Frataxin-like Protein of Respiratory Complex I fromInternational journal of molecular sciences · 2024Article
- Alternate conformations found in protein structures implies biological functions: A case study using cyclophilin A.Current research in structural biology · 2024Article
- CaviDB: a database of cavities and their features in the structural and conformational space of proteins.Database : the journal of biological databases and curation · 2023Article
- MobiDB: 10 years of intrinsically disordered proteins.Nucleic acids research · 2023Article
- Protein Function Analysis through Machine Learning.Biomolecules · 2022Review
- Machine learning/molecular dynamic protein structure prediction approach to investigate the protein conformational ensemble.Scientific reports · 2022Article
- D3PM: a comprehensive database for protein motions ranging from residue to domain.BMC bioinformatics · 2022Article
- Challenges in describing the conformation and dynamics of proteins with ambiguous behavior.Frontiers in molecular biosciences · 2022Article
- High throughput and quantitative enzymology in the genomic era.Current opinion in structural biology · 2021Review
- ModFlex: Towards Function Focused Protein Modeling.Journal of molecular biology · 2021Article
- Bioinformatic analysis of subfamily-specific regions in 3D-structures of homologs to study functional diversity and conformational plasticity in protein superfamilies.Computational and structural biotechnology journal · 2021Article
- Exploring Protein Intrinsic Disorder with MobiDB.Methods in molecular biology (Clifton, N.J.) · 2020Article
- Computational andFrontiers in cell and developmental biology · 2020Article
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4 authors.
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Abstract
CoDNaS (conformational diversity of the native state) is a protein conformational diversity database. Conformational diversity describes structural differences between conformers that define the native state of proteins. It is a key concept to understand protein function and biological processes related to protein functions. CoDNaS offers a well curated database that is experimentally driven, thoroughly linked, and annotated. CoDNaS facilitates the extraction of key information on small structural differences based on protein movements. CoDNaS enables users to easily relate the degree of conformational diversity with physical, chemical and biological properties derived from experiments on protein structure and biological characteristics. The new version of CoDNaS includes ∼70% of all available protein structures, and new tools have been added that run sequence searches, display structural flexibility profiles and allow users to browse the database for different structural classes. These tools facilitate the exploration of protein conformational diversity and its role in protein function. Database URL:http://ufq.unq.edu.ar/codnas.
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