Food proteins may be modified during processing and storage through reactions with reducing sugars (Maillard reaction, glycation) or by reactive oxygen species (protein oxidation). Little is known about particular reactions at the interface of glycation and oxidation. In the present study, the glycated amino acid pyrraline (6-(2-formyl-5-hydroxymethyl-1-pyrrolyl)-l-norleucine) and the proteinogenic amino acids tyrosine and tryptophan were subjected to different types of oxidation.
View Article and Find Full Text PDFBackground: Alternative polyadenylation (APA) affects most human genes and is recurrently dysregulated in all studied cancers. However, the mechanistic origins of this dysregulation are incompletely understood.
Results: We describe an unbiased analysis of molecular regulators of poly(A) site selection across The Cancer Genome Atlas and identify that colorectal adenocarcinoma is an outlier relative to all other cancer subtypes.
Many of the most highly conserved elements in the human genome are "poison exons," alternatively spliced exons that contain premature termination codons and permit post-transcriptional regulation of mRNA abundance through induction of nonsense-mediated mRNA decay (NMD). Poison exons are widely assumed to be highly conserved due to their presumed importance for organismal fitness, but this functional importance has never been tested in the context of a whole organism. Here, we report that a poison exon in Smndc1 is conserved across mammals and plants and plays a molecular autoregulatory function in both kingdoms.
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