ArticleProtein science : a publication of the Protein Society2018
Cytosolic expression, solution structures, and molecular dynamics simulation of genetically encodable disulfide-rich de novo designed peptides.
Article in Protein science : a publication of the Protein Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Chickpea NCR13 disulfide cross-linking variants exhibit profound differences in antifungal activity and modes of action.PLoS pathogens · 2024Article
- Directed evolution identifies high-affinity cystine-knot peptide agonists and antagonists of Wnt/β-catenin signaling.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- De novo designed protein inhibitors of amyloid aggregation and seeding.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Ex silico engineering of cystine-dense peptides yielding a potent bispecific T cell engager.Science translational medicine · 2022Article
- Toward complete rational control over protein structure and function through computational design.Current opinion in structural biology · 2021Review
- Antifungal symbiotic peptide NCR044 exhibits unique structure and multifaceted mechanisms of action that confer plant protection.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Structural diversity in the Mycobacteria DUF3349 superfamily.Protein science : a publication of the Protein Society · 2020Article
- Integration of the Rosetta suite with the python software stack via reproducible packaging and core programming interfaces for distributed simulation.Protein science : a publication of the Protein Society · 2020Article
- In Silico Insights towards the Identification of NLRP3 Druggable Hot Spots.International journal of molecular sciences · 2019Article
Corrections and comments
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Authors and funding
10 authors.
Funding
Abstract
Disulfide-rich peptides represent an important protein family with broad pharmacological potential. Recent advances in computational methods have made it possible to design new peptides which adopt a stable conformation de novo. Here, we describe a system to produce disulfide-rich de novo peptides using Escherichia coli as the expression host. The advantage of this system is that it enables production of uniformly
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Registered trials
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