ArticleNucleic acids research2012
CPred: a web server for predicting viable circular permutations in proteins.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed.
- SplitSeek-Pro: accurate prediction of splittable sites on protein structures.Nature communications · 2026Article
- Circular Permutation of theACS omega · 2026Article
- Exploration of Comprehensive Structural and Functional Potential of Recombinant Proteins Using Cutting-Edge Bioinformatics Tools.Applied biochemistry and biotechnology · 2025Review
- SARST2 high-throughput and resource-efficient protein structure alignment against massive databases.Nature communications · 2025Article
- Design and evaluation of a tripartite chemogenetic fluorescent reporter for visualizing ternary protein complexes.Nature communications · 2025Article
- Mitigating genetic instability caused by the excision activity of theApplied and environmental microbiology · 2025Article
- The importance of the location of the N-terminus in successful protein folding in vivo and in vitro.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- SeqCP: A sequence-based algorithm for searching circularly permuted proteins.Computational and structural biotechnology journal · 2023Article
- Engineering protein and DNA tools for creating DNA-dependent protein switches.Methods in enzymology · 2022Article
- Discovering the Ultimate Limits of Protein Secondary Structure Prediction.Biomolecules · 2021Article
- CirPred, the first structure modeling and linker design system for circularly permuted proteins.BMC bioinformatics · 2021Article
- Resources and Methods for Engineering "Designer" Glycan-Binding Proteins.Molecules (Basel, Switzerland) · 2021Review
- The influence of dataset homology and a rigorous evaluation strategy on protein secondary structure prediction.PloS one · 2021Article
- A secondary structure-based position-specific scoring matrix applied to the improvement in protein secondary structure prediction.PloS one · 2021Article
- A simple strategy to enhance the speed of protein secondary structure prediction without sacrificing accuracy.PloS one · 2020Article
- Tandem domain swapping: determinants of multidomain protein misfolding.Current opinion in structural biology · 2019Review
- Article
- The Structure of a Thermophilic Kinase Shapes Fitness upon Random Circular Permutation.ACS synthetic biology · 2016Article
- Structural Determinants of Misfolding in Multidomain Proteins.PLoS computational biology · 2016Article
- Article
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6 authors.
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Abstract
Circular permutation (CP) is a protein structural rearrangement phenomenon, through which nature allows structural homologs to have different locations of termini and thus varied activities, stabilities and functional properties. It can be applied in many fields of protein research and bioengineering. The limitation of applying CP lies in its technical complexity, high cost and uncertainty of the viability of the resulting protein variants. Not every position in a protein can be used to create a viable circular permutant, but there is still a lack of practical computational tools for evaluating the positional feasibility of CP before costly experiments are carried out. We have previously designed a comprehensive method for predicting viable CP cleavage sites in proteins. In this work, we implement that method into an efficient and user-friendly web server named CPred (CP site predictor), which is supposed to be helpful to promote fundamental researches and biotechnological applications of CP. The CPred is accessible at http://sarst.life.nthu.edu.tw/CPred.
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