Publications by authors named "R Fuchs"

This collaborative work by over 180 researchers from 40+ countries addresses the challenges posed by "phantom agents"-putative pathogenic agents named in literature without supporting data on their existence. Those agents remain on regulatory lists, creating barriers in trade and plant certification. Historically identified based solely on symptoms, these agents lack isolates or sequence data, making reliable detection or risk assessment impossible.

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Purpose: Mismatch repair deficient (dMMR) tumors have demonstrated favorable responses to immune checkpoint inhibition targeting PD-1. However, more in-depth identification of predictors of response could further refine patient selection for immunotherapy treatment.

Experimental Design: We undertook integrated evaluation performed on samples collected from 28 of 42 patients enrolled on the NCI-MATCH arm Z1D trial that evaluated PD-1 inhibition treatment with nivolumab in patients with non-colorectal dMMR tumors.

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Steroid hormones are C-C-sterane derivatives, featuring the typical 6-6-6-5 ring system. Here we report on a novel C-steroid ring system named batrachane with a contracted A-ring resulting in a 5-6-6-5 ring arrangement. The isolation, structural elucidation, and total synthesis of three members of the novel batrachopolyene family occurring in the tropical frog genus Odontobatrachus is reported.

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Ribosome structure and activity are challenged at high temperatures, often demanding modifications to ribosomal RNAs (rRNAs) to retain translation fidelity. LC-MS/MS, bisulfite-sequencing, and high-resolution cryo-EM structures of the archaeal ribosome identified an RNA modification, 4,4-dimethylcytidine (mC), at the universally conserved C918 in the 16S rRNA helix 31 loop. Here, we characterize and structurally resolve a class of RNA methyltransferase that generates mC whose function is critical for hyperthermophilic growth.

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Article Synopsis
  • The endoplasmic reticulum has organized regions rich in cholesterol and sphingomyelin, where rabbit CYP1A1 and CYP1A2 localize to disordered and ordered microdomains, respectively.
  • Researchers aimed to find specific amino acid residues that determine the microdomain localization of CYP1A enzymes by creating chimeras of the proteins and expressing them in cells.
  • The study identified three amino acids from CYP1A1 that influence localization patterns and suggests that the positive charges in the linker regions of CYP1A1 and CYP1A2 lead to differences in their membrane immersion, explaining their distinct microdomain distributions.
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