Zobrazeno 1 - 10
of 27
pro vyhledávání: '"Ibrahim A. Ilik"'
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:
İbrahim Avşar Ilik, Michal Malszycki, Anna Katharina Lübke, Claudia Schade, David Meierhofer, Tuğçe Aktaş
Publikováno v:
eLife, Vol 9 (2020)
Nuclear speckles (NS) are among the most prominent biomolecular condensates. Despite their prevalence, research on the function of NS is virtually restricted to colocalization analyses, since an organizing core, without which NS cannot form, remains
Externí odkaz:
https://doaj.org/article/2686ad69ff9f484ab363499b8693b19f
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-13 (2018)
RNA-binding proteins have important roles in gene expression and regulation. Here the authors develop uvCLAP to purify proteins and determine their binding sites without the use of radioactivity.
Externí odkaz:
https://doaj.org/article/28437366da674ac9985b0fd4e479430d
Autor:
Raha Weigert, Sara Hetzel, Nina Bailly, Chuck Haggerty, Ibrahim A. Ilik, Philip Yuk Kwong Yung, Carmen Navarro, Adriano Bolondi, Abhishek Sampath Kumar, Chiara Anania, Björn Brändl, David Meierhofer, Darío G. Lupiáñez, Franz-Josef Müller, Tugce Aktas, Simon J. Elsässer, Helene Kretzmer, Zachary D. Smith, Alexander Meissner
Publikováno v:
Nature Cell Biology
DNA and Histone 3 Lysine 27 methylation typically function as repressive modifications and operate within distinct genomic compartments. In mammals, the majority of the genome is kept in a DNA methylated state, whereas the Polycomb repressive complex
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d193c70d47a07e4ccd7fa7838357e2d0
https://hdl.handle.net/21.11116/0000-000D-1F8D-321.11116/0000-000D-1F8F-1
https://hdl.handle.net/21.11116/0000-000D-1F8D-321.11116/0000-000D-1F8F-1
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
Autor:
Tugce Aktas, Ibrahim Avsar Ilik
Publikováno v:
The FEBS Journal
Complex, multistep biochemical reactions that routinely take place in our cells require high concentrations of enzymes, substrates, and other structural components to proceed efficiently and typically require chemical environments that can inhibit ot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::06d697ee47ee8f0cf08eff1834a37394
https://hdl.handle.net/21.11116/0000-0009-00B1-E21.11116/0000-0009-00B3-C
https://hdl.handle.net/21.11116/0000-0009-00B1-E21.11116/0000-0009-00B3-C
Autor:
Claudia Schade, Tugce Aktas, Michal Malszycki, David Meierhofer, Ibrahim Avsar Ilik, Anna Katharina Lübke
Publikováno v:
eLife, Vol 9 (2020)
eLife
eLife
Nuclear speckles (NS) are among the most prominent biomolecular condensates. Despite their prevalence, research on the function of NS is virtually restricted to colocalization analyses, since an organizing core, without which NS cannot form, remains
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::72748273fc0eb7973e2716ade2fdc842
https://elifesciences.org/articles/60579
https://elifesciences.org/articles/60579