Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Christoph Leidig"'
Autor:
Bettina Bradatsch, Bettina Böttcher, Sander Granneman, David Tollervey, Ed Hurt, Christoph Leidig, Roland Beckmann, Marén Gnädig
Publikováno v:
Nature structural & molecular biology
Bradatsch, B, Leidig, C, Granneman, S, Gnädig, M, Tollervey, D, Böttcher, B, Beckmann, R & Hurt, E 2012, ' Structure of the pre-60S ribosomal subunit with nuclear export factor Arx1 bound at the exit tunnel ', Nature Structural & Molecular Biology . https://doi.org/10.1038/nsmb.2438
Bradatsch, B, Leidig, C, Granneman, S, Gnädig, M, Tollervey, D, Böttcher, B, Beckmann, R & Hurt, E 2012, ' Structure of the pre-60S ribosomal subunit with nuclear export factor Arx1 bound at the exit tunnel ', Nature Structural & Molecular Biology . https://doi.org/10.1038/nsmb.2438
Pre-ribosomal particles evolve in the nucleus through transient interaction with biogenesis factors, before export to the cytoplasm. Here, we report the architecture of the late pre-60S particle purified from Saccharomyces cerevisiae through Arx1, a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dedb30b2e357ad4effa295a559293759
http://europepmc.org/articles/PMC3678077
http://europepmc.org/articles/PMC3678077
Publikováno v:
Acta Crystallographica Section F: Structural Biology and Crystallization Communications
The removal of flexible protein regions is generally used to promote crystallization, but advanced strategies to quickly remove multiple flexible regions from proteins or protein complexes are lacking. Here, it is shown how a protein heterodimer with
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::06d7b8b0c142cfe19d744e3b420752b2
https://doi.org/10.1107/s174430910800972x
https://doi.org/10.1107/s174430910800972x
Autor:
Gert Bange, Christoph Leidig, Roland Beckmann, Matthias Thoms, Bettina Bradatsch, Iris Holdermann, Ed Hurt, Irmgard Sinning, Otto Berninghausen
Publikováno v:
Nature communications. 5
During eukaryotic ribosome biogenesis, nascent ribosomal RNA (rRNA) forms pre-ribosomal particles containing ribosomal proteins and assembly factors. Subsequently, these immature rRNAs are processed and remodelled. Little is known about the premature
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b6c7aab959d039a398b59bf1e3c07105
https://pubmed.ncbi.nlm.nih.gov/24662372
https://pubmed.ncbi.nlm.nih.gov/24662372
Autor:
Roland Beckmann, Stephan Wickles, Christoph Leidig, Thomas Becker, Ramin Norousi, Volker Schmid, Achim Tresch
Cryo-electron microscopy (cryo-EM) studies using single particle reconstruction are extensively used to reveal structural information on macromolecular complexes. Aiming at the highest achievable resolution, state of the art electron microscopes auto
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8b0690f85a1eda581be805c3f6ddd5cd
http://arxiv.org/abs/1212.4871
http://arxiv.org/abs/1212.4871
Autor:
Irmgard Sinning, Christoph Leidig, Ed Hurt, Gregor Witte, Roland Beckmann, Stefan Amlacher, Stephan Wickles, Gert Bange, Ajay Aravind, Jürgen Kopp
Publikováno v:
Nature structuralmolecular biology. 20(1)
Ribosome-associated chaperones act in early folding events during protein synthesis. Structural information is available for prokaryotic chaperones (such as trigger factor), but structural understanding of these processes in eukaryotes lags far behin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::36b94a62e249dbed01f8940794824a5c
https://pubmed.ncbi.nlm.nih.gov/23202586
https://pubmed.ncbi.nlm.nih.gov/23202586