ArticleBioinformatics advances2022
Folding the unfoldable: using AlphaFold to explore spurious proteins.
Article in Bioinformatics advances, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed.
- Structural Diversity and Differential Natural Pairings of MAT1-1-1 and MAT1-2-1 Proteins Essential for Sexual Reproduction inInternational journal of molecular sciences · 2026Article
- Testing the reliability of AI-generated protein structures.bioRxiv : the preprint server for biology · 2026Article
- Microproteins in Human Physiology and Pathology.Biochemistry · 2026Review
- Uncovering evolutionarily remote and highly potent antimicrobial peptides with protein language models.Nature biomedical engineering · 2026Article
- Article
- Protein structure-informed bacteriophage genome annotation with Phold.Nucleic acids research · 2026Article
- Folding the unfoldable 2: using AlphaFold and ESMFold to explore spurious proteins.Bioinformatics advances · 2026Article
- Ten rules for a structural bioinformatic analysis.PLoS computational biology · 2025Article
- Investigating the role of long non-coding RNA in hypertrophic cardiomyopathy.bioRxiv : the preprint server for biology · 2025Article
- Fold first, ask later: structure-informed function annotation ofbioRxiv : the preprint server for biology · 2025Article
- Three-Dimensional Structural Heteromorphs of Mating-Type Proteins inJournal of fungi (Basel, Switzerland) · 2025Article
- BFVD-a large repository of predicted viral protein structures.Nucleic acids research · 2025Article
- AlphaFold 2, but not AlphaFold 3, predicts confident but unrealistic β-solenoid structures for repeat proteins.Computational and structural biotechnology journal · 2025Article
- Challenges in bridging the gap between protein structure prediction and functional interpretation.Proteins · 2025Article
- Multimeric protein interaction and complex prediction: Structure, dynamics and function.Computational and structural biotechnology journal · 2025Review
- Bilingual language model for protein sequence and structure.NAR genomics and bioinformatics · 2024Article
- Proteome-scale structural prediction of the giant Marseillevirus reveals conserved folds and putative homologs of the hypothetical proteins.Archives of virology · 2024Article
- Article
- Insights into docking in megasynthases from the investigation of the toblerolRSC chemical biology · 2024Article
- Protein remote homology detection and structural alignment using deep learning.Nature biotechnology · 2024Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Motivation: The release of AlphaFold 2.0 has revolutionized our ability to determine protein structures from sequences. This tool also inadvertently opens up many unanticipated opportunities. In this article, we investigate the AntiFam resource, which contains 250 protein sequence families that we believe to be spurious protein translations. We would not expect proteins belonging to these families to fold into well-ordered globular structures. To test this hypothesis, we have attempted to computationally determine the structure of a representative sequence from all AntiFam 6.0 families. Results: Although the large majority of families showed no evidence of globular structure, we have identified one example for which a globular structure is predicted. Proteins in this AntiFam entry indeed seem likely to be Availability and implementation: The AlphaFold predictions for representative sequences can be found at the following URL: https://drive.google.com/drive/folders/1u9OocRIAabGQn56GljoG1JTDAxjkY1ro. Supplementary information: Supplementary data are available at
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.