2 results match your criteria: "Bavarian NMR Center and Department of Bioscience[Affiliation]"
Dynamic interactions drive early spliceosome assembly.
Curr Opin Struct Biol
October 2024
Helmholtz Munich, Molecular Targets and Therapeutics Center, Institute of Structural Biology, Ingolstädter Landstrasse 1, 85764 Neuherberg, Germany; Technical University of Munich, TUM School of Natural Sciences, Bavarian NMR Center and Department of Bioscience, Lichtenbergstrasse 4, 85747 Garching, Germany. Electronic address:
Splicing is a critical processing step during pre-mRNA maturation in eukaryotes. The correct selection of splice sites during the early steps of spliceosome assembly is highly important and crucial for the regulation of alternative splicing. Splice site recognition and alternative splicing depend on cis-regulatory sequence elements in the RNA and trans-acting splicing factors that recognize these elements and crosstalk with the canonical splicing machinery.
View Article and Find Full Text PDFModulation of peroxisomal import by the PEX13 SH3 domain and a proximal FxxxF binding motif.
Nat Commun
April 2024
Technical University of Munich, TUM School of Natural Sciences, Bavarian NMR Center and Department of Bioscience, Lichtenbergstr. 4, 85747, Garching, Germany.
Article Synopsis
- The import of proteins into peroxisomes relies on specific proteins: PEX5, PEX13, and PEX14.
- The SH3 domain of PEX13 plays a crucial role in binding to peptide motifs found in PEX5, impacting how these proteins interact.
- Structural studies highlight that these interactions are evolutionarily conserved, and the binding dynamics of these proteins are essential for proper functioning of peroxisomal matrix import.