ArticleJournal of the American Chemical Society2017
Creating a Homeodomain with High Stability and DNA Binding Affinity by Sequence Averaging.
Article in Journal of the American Chemical Society, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Protein stability is determined by single-site bias rather than pairwise covariance.Nature chemical biology · 2026Article
- Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026Review
- Missense variants in human forkhead transcription factors reveal determinants of forkhead DNA bispecificity.Cell reports · 2025Article
- GArNet: A Genetic Algorithm-Based Protein Redesign Approach to Optimize Mutation Combinations Informed by Network Theory.Journal of chemical information and modeling · 2025Article
- Missense variants in human forkhead transcription factors reveal determinants of forkhead DNA bispecificity.bioRxiv : the preprint server for biology · 2025Article
- DNA binding analysis of rare variants in homeodomains reveals homeodomain specificity-determining residues.Nature communications · 2024Article
- Derivation of a novel antimicrobial peptide from the Red Sea Brine Pools modified to enhance its anticancer activity against U2OS cells.BMC biotechnology · 2024Article
- High-Accuracy Prediction of Stabilizing Surface Mutations to the Three-Helix Bundle, UBA(1), with EmCAST.Journal of the American Chemical Society · 2023Article
- Singular value decomposition of protein sequences as a method to visualize sequence and residue space.Protein science : a publication of the Protein Society · 2022Article
- The stability and dynamics of computationally designed proteins.Protein engineering, design & selection : PEDS · 2022Review
- Surface residues and nonadditive interactions stabilize a consensus homeodomain protein.Biophysical journal · 2021Article
- Data-driven computational protein design.Current opinion in structural biology · 2021Review
- The use of consensus sequence information to engineer stability and activity in proteins.Methods in enzymology · 2020Article
- Consensus sequence design as a general strategy to create hyperstable, biologically active proteins.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- A Dynamic Hydrophobic Core and Surface Salt Bridges Thermostabilize a Designed Three-Helix Bundle.Biophysical journal · 2019Article
- TGIF1 homeodomain interacts with Smad MH1 domain and represses TGF-β signaling.Nucleic acids research · 2018Article
- Extreme stability in de novo-designed repeat arrays is determined by unusually stable short-range interactions.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
There is considerable interest in generating proteins with both high stability and high activity for biomedical and industrial purposes. One approach that has been used successfully to increase the stability of linear repeat proteins is consensus design. It is unclear the extent over which the consensus design approach can be used to produce folded and hyperstable proteins, and importantly, whether such stabilized proteins would retain function. Here we extend the consensus strategy to design a globular protein. We show that a consensus-designed homeodomain (HD) sequence adopts a cooperatively folded homeodomain structure. The unfolding free energy of the consensus-HD is 5 kcal·mol
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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.