ArticleScientific reports2016
Smoothing a rugged protein folding landscape by sequence-based redesign.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 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
13 citing papers in PubMed, 29 citations in OpenAlex.
- Protein stability is determined by single-site bias rather than pairwise covariance.Nature chemical biology · 2026Article
- Deep Learning-Enabled Engineering of a Hyper-Stable and Soluble MPB70-83 Antigen for Sensitive Bovine Tuberculosis Surveillance.Microbial biotechnology · 2026Article
- Comparison of structures and inhibition activities of serine protease inhibitors of Trichinella spiralis and Trichinella pseudospiralis.Cell & bioscience · 2025Article
- The stability and dynamics of computationally designed proteins.Protein engineering, design & selection : PEDS · 2022Review
- Targeted SERPIN (TaSER): A dual-action antithrombotic agent that targets platelets for SERPIN delivery.Journal of thrombosis and haemostasis : JTH · 2022Article
- Therapeutic SERPINs: Improving on Nature.Frontiers in cardiovascular medicine · 2021Review
- Engineering the serpin αProtein science : a publication of the Protein Society · 2020Review
- 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
- Reactive centre loop dynamics and serpin specificity.Scientific reports · 2019Article
- Probing the folding pathway of a consensus serpin using single tryptophan mutants.Scientific reports · 2018Article
- Creating a Homeodomain with High Stability and DNA Binding Affinity by Sequence Averaging.Journal of the American Chemical Society · 2017Article
- Mutational and biophysical robustness in a prestabilized monobody.The Journal of biological chemistryArticle
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
18 authors at 5 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The rugged folding landscapes of functional proteins puts them at risk of misfolding and aggregation. Serine protease inhibitors, or serpins, are paradigms for this delicate balance between function and misfolding. Serpins exist in a metastable state that undergoes a major conformational change in order to inhibit proteases. However, conformational labiality of the native serpin fold renders them susceptible to misfolding, which underlies misfolding diseases such as α
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.