ArticlePloS one2012
Deciphering the preference and predicting the viability of circular permutations in proteins.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
16 citing papers in PubMed, 29 citations in OpenAlex.
- SARST2 high-throughput and resource-efficient protein structure alignment against massive databases.Nature communications · 2025Article
- Optimizing Ligand Valency to Maximize Tendon Accumulation of Peptide-Targeted Nanoparticles.ACS applied materials & interfaces · 2024Article
- 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
- Design of stable circular permutants of the GroEL chaperone apical domain.Cell communication and signaling : CCS · 2024Article
- Conformational Variation in Enzyme Catalysis: A Structural Study on Catalytic Residues.Journal of molecular biology · 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
- A secondary structure-based position-specific scoring matrix applied to the improvement in protein secondary structure prediction.PloS one · 2021Article
- The influence of dataset homology and a rigorous evaluation strategy on 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
- The Structure of a Thermophilic Kinase Shapes Fitness upon Random Circular Permutation.ACS synthetic biology · 2016Article
- Protein switch engineering by domain insertion.Methods in enzymology · 2013Article
- CPred: a web server for predicting viable circular permutations in proteins.Nucleic acids research · 2012Article
- Article
- Folding circular permutants of IL-1β: route selection driven by functional frustration.PloS one · 2012Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Circular permutation (CP) refers to situations in which the termini of a protein are relocated to other positions in the structure. CP occurs naturally and has been artificially created to study protein function, stability and folding. Recently CP is increasingly applied to engineer enzyme structure and function, and to create bifunctional fusion proteins unachievable by tandem fusion. CP is a complicated and expensive technique. An intrinsic difficulty in its application lies in the fact that not every position in a protein is amenable for creating a viable permutant. To examine the preferences of CP and develop CP viability prediction methods, we carried out comprehensive analyses of the sequence, structural, and dynamical properties of known CP sites using a variety of statistics and simulation methods, such as the bootstrap aggregating, permutation test and molecular dynamics simulations. CP particularly favors Gly, Pro, Asp and Asn. Positions preferred by CP lie within coils, loops, turns, and at residues that are exposed to solvent, weakly hydrogen-bonded, environmentally unpacked, or flexible. Disfavored positions include Cys, bulky hydrophobic residues, and residues located within helices or near the protein's core. These results fostered the development of an effective viable CP site prediction system, which combined four machine learning methods, e.g., artificial neural networks, the support vector machine, a random forest, and a hierarchical feature integration procedure developed in this work. As assessed by using the hydrofolate reductase dataset as the independent evaluation dataset, this prediction system achieved an AUC of 0.9. Large-scale predictions have been performed for nine thousand representative protein structures; several new potential applications of CP were thus identified. Many unreported preferences of CP are revealed in this study. The developed system is the best CP viability prediction method currently available. This work will facilitate the application of CP in research and biotechnology.
Indexed as
Identifiers
What OpenQuestion holds
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.