ArticleNucleic acids research2016
Start2Fold: a database of hydrogen/deuterium exchange data on protein folding and stability.
Article in Nucleic acids research, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Protein Language Models Identify Early Folding Residues as Critical Hotspots for Pathogenic Variants and Cancer Prognosis.International journal of molecular sciences · 2026Article
- Article
- MAVISp: A modular structure-based framework for protein variant effects.Protein science : a publication of the Protein Society · 2026Article
- Unavailability of experimental 3D structural data on protein folding dynamics and necessity for a new generation of structure prediction methods in this context.Bioinformatics (Oxford, England) · 2026Article
- Site-resolved energetic information from HX-MS experiments.Nature chemical biology · 2026Article
- Inferring protein-folding mechanisms from natural sequence diversity.Biophysical journal · 2025Article
- Reassessing the exon-foldon correspondence using frustration analysis.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- FoldPAthreader: predicting protein folding pathway using a novel folding force field model derived from known protein universe.Genome biology · 2024Article
- Recent Advances in Protein Folding Pathway Prediction through Computational Methods.Current medicinal chemistry · 2024Review
- Pathfinder: Protein folding pathway prediction based on conformational sampling.PLoS computational biology · 2023Article
- Evolutionary adaptation of the protein folding pathway for secretability.The EMBO journal · 2022Article
- Protein Structure Prediction with Mass Spectrometry Data.Annual review of physical chemistry · 2022Review
- Computational Structure Prediction for Antibody-Antigen Complexes From Hydrogen-Deuterium Exchange Mass Spectrometry: Challenges and Outlook.Frontiers in immunology · 2022Review
- Interpreting a black box predictor to gain insights into early folding mechanisms.Computational and structural biotechnology journal · 2021Article
- ThermoScan: Semi-automatic Identification of Protein Stability Data From PubMed.Frontiers in molecular biosciences · 2021Review
- StructureDistiller: Structural relevance scoring identifies the most informative entries of a contact map.Scientific reports · 2019Article
- Auto-encoding NMR chemical shifts from their native vector space to a residue-level biophysical index.Nature communications · 2019Article
- Application of an interpretable classification model on Early Folding Residues during protein folding.BioData mining · 2019Article
- A General Method for Predicting Amino Acid Residues Experiencing Hydrogen Exchange.... IEEE-EMBS International Conference on Biomedical and Health Informatics. IEEE-EMBS International Conference on Biomedical and Health Informatics · 2018Article
- Article
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4 authors.
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Abstract
Proteins fulfil a wide range of tasks in cells; understanding how they fold into complex three-dimensional (3D) structures and how these structures remain stable while retaining sufficient dynamics for functionality is essential for the interpretation of overall protein behaviour. Since the 1950's, solvent exchange-based methods have been the most powerful experimental means to obtain information on the folding and stability of proteins. Considerable expertise and care were required to obtain the resulting datasets, which, despite their importance and intrinsic value, have never been collected, curated and classified. Start2Fold is an openly accessible database (http://start2fold.eu) of carefully curated hydrogen/deuterium exchange (HDX) data extracted from the literature that is open for new submissions from the community. The database entries contain (i) information on the proteins investigated and the underlying experimental procedures and (ii) the classification of the residues based on their exchange protection levels, also allowing for the instant visualization of the relevant residue groups on the 3D structures of the corresponding proteins. By providing a clear hierarchical framework for the easy sharing, comparison and (re-)interpretation of HDX data, Start2Fold intends to promote a better understanding of how the protein sequence encodes folding and structure as well as the development of new computational methods predicting protein folding and stability.
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