ArticleThe journal of physical chemistry. B2020
Rosetta Machine Learning Models Accurately Classify Positional Effects of Thioamides on Proteolysis.
Article in The journal of physical chemistry. B, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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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.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Peptide vaccines get an OS update.Nature chemical biology · 2024Article
- Thioamide Analogues of MHC I Antigen Peptides.Journal of the American Chemical Society · 2023Article
- AggBERT: Best in Class Prediction of Hexapeptide Amyloidogenesis with a Semi-Supervised ProtBERT Model.Journal of chemical information and modeling · 2023Article
- Structural impact of thioamide incorporation into a β-hairpin.RSC chemical biology · 2022Article
- Structure determinants defining the specificity of papain-like cysteine proteases.Computational and structural biotechnology journal · 2022Review
- Developing a Hybrid Risk Assessment Tool for Familial Hypercholesterolemia: A Machine Learning Study of Chinese Arteriosclerotic Cardiovascular Disease Patients.Frontiers in cardiovascular medicine · 2022Article
- Biomolecular simulation based machine learning models accurately predict sites of tolerability to the unnatural amino acid acridonylalanine.Scientific reports · 2021Article
- Rational design of thioamide peptides as selective inhibitors of cysteine protease cathepsin L.Chemical science · 2021Article
- Incorporating thioamides into proteins by native chemical ligation.Methods in enzymology · 2021Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Thioamide substitutions of the peptide backbone have been shown to stabilize therapeutic and imaging peptides toward proteolysis. In order to rationally design thioamide modifications, we have developed a novel Rosetta custom score function to classify thioamide positional effects on proteolysis in substrates of serine and cysteine proteases. Peptides of interest were docked into proteases using the FlexPepDock application in Rosetta. Docked complexes were modified to contain thioamides parametrized through the creation of custom atom types in Rosetta based on
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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.