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A. Link

As seen in: Nature, Wiley Online Library, Bild, ZDF, ACS Publications, Analytical Chemistry, Royal Society of Chemistry
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Articles

Probing Thrombosis Initiation with Lasso Peptide Variants as Inhibitors to the von Willebrand Protein-Collagen Interaction

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By Danielle A. Guarracino, Drew Carson, Toby Johnson, A. Link
| Wiley Online Library
Conflict of Interest The authors declare no conflict of interest. Supporting Information Filename Description cbic202500188-sup-0001-SuppData-S1.pdf514.9 KB Supplementary Material References 1, , , , Chem. Biol. Drug Des. 2013, 81, 136. 2, , , J. Med. Chem. 2018, 61, 1382. 3The website Cyclic Peptides: Current Status & Future Prospects Biopharma PEG: https://www.biochempeg.com/article/369.html, accessed: February 28 2025. 4, , J. Med. Chem. 2011, 54, 1961. 5, , , , Nat. Rev. Drug Discovery 2008, 7, 608.
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Functional and structural characterization of AtAbf43C: An exo-1,5-α-L-arabinofuranosidase from Acetivibrio thermocellus DSM1313

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By Philip Jeffrey, Angela Zhu, A. Link, Joey L Galindo
| biorxiv.org
Abstract The Acetivibrio thermocellus DSM1313 genome codes for seven predicted glycoside hydrolase family 43 (GH43) enzymes, four of which remain uncharacterized. This study describes the function and structure of one such enzyme, AtAbf43C, from GH43 subfamily 26 (GH43_26) which acts as an α-L-arabinofuranosidase (EC 3.2.1.55). AtAbf43C is active on para-nitrophenol-α-L-arabinofuranoside (pNPAra), with optimal activity observed at pH 5.5 and 65 ℃.
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Cysimiditides: RiPPs with a Zn-tetracysteine motif and aspartimidylation

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By Angela Zhu, Li Cao, Truc Do, A. Link
| biorxiv.org
Abstract Aspartimidylation is a post-translational modification found in multiple families of ribosomally synthesized and post-translationally modified peptides (RiPPs). We recently reported on the imiditides, a new RiPP family in which aspartimidylation is the class-defining modification. Imiditide biosynthetic gene clusters encode a precursor protein and a methyltransferase that methylates a specific Asp residue, converting it to aspartimide.
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