ArticleInternational journal of molecular sciences2010
Retro-MoRFs: identifying protein binding sites by normal and reverse alignment and intrinsic disorder prediction.
Article in International journal of molecular sciences, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed.
- Predicting molecular recognition features in protein sequences with MoRFchibi 2.0.BMC bioinformatics · 2026Article
- Intrinsically disordered regions in the yeast transcriptional regulator Ixr1 support prion-like behavior.Scientific reports · 2026Article
- Computational Prediction of Linear Interacting Peptides.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Advanced computational approaches to understand protein aggregation.Biophysics reviews · 2024Review
- Biophysical and Integrative Characterization of Protein Intrinsic Disorder as a Prime Target for Drug Discovery.Biomolecules · 2023Review
- Computational prediction of disordered binding regions.Computational and structural biotechnology journal · 2023Review
- Intrinsically disordered proteins play diverse roles in cell signaling.Cell communication and signaling : CCS · 2022Review
- Prediction of protein-protein interaction sites in intrinsically disordered proteins.Frontiers in molecular biosciences · 2022Review
- Predicting Protein Conformational Disorder and Disordered Binding Sites.Methods in molecular biology (Clifton, N.J.) · 2022Article
- LRRC8A homohexameric channels poorly recapitulate VRAC regulation and pharmacology.American journal of physiology. Cell physiology · 2021Article
- New technologies to analyse protein function: an intrinsic disorder perspective.F1000Research · 2020Review
- Dishevelled-3 conformation dynamics analyzed by FRET-based biosensors reveals a key role of casein kinase 1.Nature communications · 2019Article
- A 30-year journey from volume-regulated anion currents to molecular structure of the LRRC8 channel.The Journal of general physiology · 2019Review
- Computational Prediction of MoRFs, Short Disorder-to-order Transitioning Protein Binding Regions.Computational and structural biotechnology journal · 2019Review
- Intracellular and extracellular loops of LRRC8 are essential for volume-regulated anion channel function.The Journal of general physiology · 2018Article
- Comprehensive review of methods for prediction of intrinsic disorder and its molecular functions.Cellular and molecular life sciences : CMLS · 2017Review
- MoRFchibi SYSTEM: software tools for the identification of MoRFs in protein sequences.Nucleic acids research · 2016Article
- Identifying Similar Patterns of Structural Flexibility in Proteins by Disorder Prediction and Dynamic Programming.International journal of molecular sciences · 2015Article
- Computational identification of MoRFs in protein sequences.Bioinformatics (Oxford, England) · 2015Article
- DBC1/CCAR2 and CCAR1 Are Largely Disordered Proteins that Have Evolved from One Common Ancestor.BioMed research international · 2014Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
Many cell functions in all living organisms rely on protein-based molecular recognition involving disorder-to-order transitions upon binding by molecular recognition features (MoRFs). A well accepted computational tool for identifying likely protein-protein interactions is sequence alignment. In this paper, we propose the combination of sequence alignment and disorder prediction as a tool to improve the confidence of identifying MoRF-based protein-protein interactions. The method of reverse sequence alignment is also rationalized here as a novel approach for finding additional interaction regions, leading to the concept of a retro-MoRF, which has the reversed sequence of an identified MoRF. The set of retro-MoRF binding partners likely overlap the partner-sets of the originally identified MoRFs. The high abundance of MoRF-containing intrinsically disordered proteins in nature suggests the possibility that the number of retro-MoRFs could likewise be very high. This hypothesis provides new grounds for exploring the mysteries of protein-protein interaction networks at the genome level.
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Registered trials
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