Publications by authors named "M Kral"

Background And Purpose: This study evaluates the early clinical performance of the new Artisse Intrasaccular Device (Artisse ISD), a self-expandable intrasaccular flow diverter, for treating wide-necked aneurysms (WNAs). We report initial safety and efficacy outcomes in the first cohort of patients treated with this novel device.

Methods: Prospective clinical and radiological data were collected for all patients treated with the Artisse ISD at three Austrian neurovascular centers from July 2023 to August 2024.

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The PB2 subunit of the influenza virus polymerase complex is essential for viral replication, primarily through a mechanism known as cap-snatching. In this process, PB2 binds to the 5' cap structure of host pre-mRNAs, enabling the viral polymerase to hijack the host transcriptional machinery. This binding facilitates the cleavage and integration of the capped RNA fragment into viral mRNA, thereby promoting efficient viral replication.

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Article Synopsis
  • Type 2 innate lymphoid cells (ILC2s) play crucial roles in inflammation, metabolism, and maintaining tissue balance, becoming key players in various diseases.
  • The review highlights how ILC2s adjust their metabolism depending on the physiological or pathological conditions to perform and survive effectively.
  • Recent omics research, including transcriptomic, proteomic, and metabolomic studies, has shed light on ILC2s' gene expression, protein interactions, and metabolic networks, enhancing our understanding of their functional diversity in metabolic disorders.
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Article Synopsis
  • The influenza RNA-dependent RNA polymerase has an endonuclease subunit that contains a site with two metal ions, crucial for its function.
  • Researchers developed a series of inhibitors, specifically designed to bind these metal ions and inhibit the enzyme's activity, using a chemoenzymatic process.
  • The most effective inhibitors had IC50 values around 0.35 μM, and X-ray crystallography revealed how one of these inhibitors interacts with the enzyme at the atomic level.
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