
Alanna Schepartz
Articles
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Jan 6, 2025 |
nature.com | Alanna Schepartz
AbstractAminoacyl-tRNA synthetases (aaRSs) provide an essential functional link between an mRNA sequence and the protein it encodes. aaRS enzymes catalyze a two-step chemical reaction that acylates specific tRNAs with a cognate α-amino acid. In addition to their role in translation, acylated tRNAs contribute to non-ribosomal natural product biosynthesis and are implicated in multiple human diseases.
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Sep 28, 2024 |
biorxiv.org | Teresia Chen |diego rodriguez |Diego Rodríguez |Madeline A. Zoltek |Alanna Schepartz
AbstractThere is enormous interest in strategies to efficiently traffic biologics-proteins, nucleic acids, and complexes thereof-into the mammalian cell cytosol and internal organelles. Not only must these materials reach the appropriate cellular locale fully intact and in therapeutically relevant concentrations, they must also retain activity upon arrival.
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Jul 29, 2024 |
biorxiv.org | Joshua Davisson |Evan Kalb |Isaac Knudson |Alanna Schepartz
AbstractLife as we know it depends on the homochirality of nucleic acids and proteins. However, there is no widely accepted explanation for why life uses only D-sugars for nucleic acids and L-amino acids for proteins. Here we demonstrate a prebiotically plausible method of nonenzymatic aminoacylation in a water ice-eutectic phase. These reactions produce high yields of aminoacyl-tRNAs, which are active in translation.
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Nov 8, 2023 |
biorxiv.org | Noah Xue Hamlish |Ara M. Abramyan |Alanna Schepartz
AbstractSequence-defined biomaterials whose monomer backbones diverge from canonical alpha-amino acids represents the next frontier in protein and biomaterial evolution with the potential to yield better biological therapeutics, bioremediation tools, and biodegradable plastic-like materials. One monomer family of particular interest for biomaterials are beta-hydroxy acids.
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Oct 3, 2023 |
biorxiv.org | Alanna Schepartz |Leah Roe |Carly K. Schissel |Taylor L. Dover
AbstractProteins and polypeptides containing extended backbone monomers embody highly desirable structures and functions, but they cannot yet be biosynthesized in cells. There are two challenges at work. First is the ribosome, whose ability to promote rapid bond-forming reactions to and from anything other than an α-amino acid or α-hydroxy acid is unknown. The second challenge is the absence of orthogonal enzymes that acylate tRNA with extended backbone monomers.
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