Publications by authors named "Jann-Patrick Pelz"

Background: Nirmatrelvir/ritonavir is authorized for the treatment of COVID-19 but has several contraindications and potential drug-drug interactions (pDDIs) due to ritonavir-induced irreversible inhibition of cytochrome P450 3A4. We aimed to assess the prevalence of individuals with one or more risk factors for severe COVID-19 along with contraindications and pDDIs due to ritonavir-containing COVID-19 therapy.

Methods: Retrospective observational study of individuals with one or more risk factors according to Robert Koch Institute criteria for severe COVID-19 according to German statutory health insurance (SHI) claims data from the pre-pandemic years 2018-2019 based on the German Analysis Database for Evaluation and Health Services Research.

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Eukaryotic cells determine the protein output of their genetic program by regulating mRNA transcription, localization, translation and turnover rates. This regulation is accomplished by an ensemble of RNA-binding proteins (RBPs) that bind to any given mRNA, thus forming mRNPs. Poly(A) binding proteins (PABPs) are prominent members of virtually all mRNPs that possess poly(A) tails.

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The small nuclear ribonucleoproteins (snRNPs) U1, U2, U4/6 and U5 are major constituents of the pre-mRNA processing spliceosome. They contain a common RNP core that is formed by the ordered binding of Sm proteins onto the single-stranded Sm site of the snRNA. Although spontaneous in vitro, assembly of the Sm core requires assistance from the PRMT5 and SMN complexes in vivo.

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Article Synopsis
  • Small nuclear ribonucleoproteins (snRNPs) are essential components of spliceosomes, formed by Sm proteins and snRNA, and their assembly involves various stages facilitated by specific proteins like pICln.* -
  • The pICln protein helps stabilize Sm proteins by forming a pentameric unit known as the 6S complex, which eventually binds to the SMN complex to transfer proteins onto snRNA.* -
  • Structural analyses using X-ray crystallography and electron microscopy revealed that pICln acts as a mimic of Sm proteins, aiding in their organization, and provided insights into the mechanisms of pICln removal and activation of Sn proteins for RNA binding.*
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