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Christopher J. Schwalen

Researcher at University of Illinois at Urbana–Champaign

Publications -  10
Citations -  1731

Christopher J. Schwalen is an academic researcher from University of Illinois at Urbana–Champaign. The author has contributed to research in topics: Peptide Biosynthesis & Folding (chemistry). The author has an hindex of 7, co-authored 9 publications receiving 1382 citations. Previous affiliations of Christopher J. Schwalen include Novartis.

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antiSMASH 4.0-improvements in chemistry prediction and gene cluster boundary identification.

TL;DR: The thoroughly updated antiSMASH version 4 is presented, which adds several novel features, including prediction of gene cluster boundaries using the ClusterFinder method or the newly integrated CASSIS algorithm, improved substrate specificity prediction for non-ribosomal peptide synthetase adenylation domains based on the new SANDPUMA algorithm, and several usability features have been updated and improved.
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A new genome-mining tool redefines the lasso peptide biosynthetic landscape

TL;DR: RODEO (Rapid ORF Description and Evaluation Online), which combines hidden Markov model-based analysis, heuristic scoring, and machine learning to identify biosynthetic gene clusters and predict RiPP precursor peptides to provide a framework for future genome-mining efforts.
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YcaO-Dependent Posttranslational Amide Activation: Biosynthesis, Structure, and Function

TL;DR: The formerly enigmatic YcaO superfamily (DUF181), has been found to catalyze a unique phosphorylation of a ribosomal peptide backbone amide upon attack by different nucleophiles.
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Bioinformatic Expansion and Discovery of Thiopeptide Antibiotics.

TL;DR: A combination of whole-genome sequencing, comparative genomics, and heterologous expression experiments confirmed that the thioamide moiety of saalfelduracin is installed post-translationally by the joint action of two proteins, TfuA and YcaO, reconciling the previously unknown origin of the thaiamide in two long-known thiopeptides.
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Bioinformatic Mapping of Radical S-Adenosylmethionine-Dependent Ribosomally Synthesized and Post-Translationally Modified Peptides Identifies New Cα, Cβ, and Cγ-Linked Thioether-Containing Peptides

TL;DR: This work bioinformatically mapped the sactipeptide RiPP class via the radical S-adenosylmethionine (SAM) enzymes that form the characteristic sactionine-to-α carbon cross-links between cysteine and acceptor residues and proposed the renaming of the SCIFF family as radical non-α thioether peptides (ranthipeptides) to better distinguish them from the saCTipeptid and lanthipePTide