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pro vyhledávání: '"Alexandra Bergfort"'
Autor:
Alexandra Bergfort, Marco Preußner, Benno Kuropka, İbrahim Avşar Ilik, Tarek Hilal, Gert Weber, Christian Freund, Tuğçe Aktaş, Florian Heyd, Markus C. Wahl
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-16 (2022)
Bergfort et al. use biochemistry, cryoEM, structure-guided mutagenesis, transcriptomics and proteomics to reveal how the intrinsically unstructured C9ORF78 protein binds BRR2 and PRPF8, regulating cassette exons and alternative 3’-splice sites.
Externí odkaz:
https://doaj.org/article/9cdd9c825b2e49b8b316d5d1c8d55312
Autor:
Alexandra Bergfort, Tarek Hilal, Benno Kuropka, İbrahim Avşar Ilik, Gert Weber, Tuğçe Aktaş, Christian Freund, Markus C Wahl
Publikováno v:
Nucleic Acids Research (London)
Biogenesis of spliceosomal small nuclear ribonucleoproteins (snRNPs) and their recycling after splicing require numerous assembly/recycling factors whose modes of action are often poorly understood. The intrinsically disordered TSSC4 protein has been
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0499513ffacd2dcbb3714aef9a0ddb56
Autor:
Markus C. Wahl, Gert Weber, Marco Preussner, Benno Kuropka, T. Hilal, Christian Freund, Florian Heyd, Tugce Aktas, Alexandra Bergfort, Ibrahim Avsar Ilik
The complete inventory of regulatory factors in human spliceosomes remains unknown, and many flexibly bound components are not revealed in present spliceosome structures. The intrinsically unstructured C9ORF78 protein was detected in C complex splice
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::5292da8790800b2533680d2315f234f5
https://doi.org/10.21203/rs.3.rs-639521/v1
https://doi.org/10.21203/rs.3.rs-639521/v1
Autor:
Alexandra, Bergfort, Marco, Preußner, Benno, Kuropka, İbrahim Avşar, Ilik, Tarek, Hilal, Gert, Weber, Christian, Freund, Tuğçe, Aktaş, Florian, Heyd, Markus C, Wahl
Publikováno v:
Nature communications. 13(1)
The intrinsically unstructured C9ORF78 protein was detected in spliceosomes but its role in splicing is presently unclear. We find that C9ORF78 tightly interacts with the spliceosome remodeling factor, BRR2, in vitro. Affinity purification/mass spect
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::2028a879792fd10ad6a518ed2b9684b9
https://pubmed.ncbi.nlm.nih.gov/35241646
https://pubmed.ncbi.nlm.nih.gov/35241646