Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Marcel J. Tauchert"'
Autor:
Carsten Boesler, Norbert Rigo, Maria M. Anokhina, Marcel J. Tauchert, Dmitry E. Agafonov, Berthold Kastner, Henning Urlaub, Ralf Ficner, Cindy L. Will, Reinhard Lührmann
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-12 (2016)
The assembly of the splicesome involves several distinct stages that require the sequential action of DExD/H-box RNA helicases. Here, the authors uncover a new intermediate, the pre-B complex, that accumulates in the presence of an inactive form of t
Externí odkaz:
https://doaj.org/article/e7d1d18e40824533a67b9650add6c83c
Publikováno v:
eLife, Vol 6 (2017)
The DEAH-box helicase Prp43 is a key player in pre-mRNA splicing as well as the maturation of rRNAs. The exact modus operandi of Prp43 and of all other spliceosomal DEAH-box RNA helicases is still elusive. Here, we report crystal structures of Prp43
Externí odkaz:
https://doaj.org/article/e2813cda8c5d4d2d9f6a71b02c3d7616
Autor:
Jean-Baptiste Fourmann, Olexandr Dybkov, Dmitry E Agafonov, Marcel J Tauchert, Henning Urlaub, Ralf Ficner, Patrizia Fabrizio, Reinhard Lührmann
Publikováno v:
eLife, Vol 5 (2016)
The DEAH-box NTPase Prp43 and its cofactors Ntr1 and Ntr2 form the NTR complex and are required for disassembling intron-lariat spliceosomes (ILS) and defective earlier spliceosomes. However, the Prp43 binding site in the spliceosome and its target(s
Externí odkaz:
https://doaj.org/article/77ca72ef612c484b8264a63da2c7c456
Autor:
Jean-Baptiste Fourmann, Ralf Ficner, Henning Christian, Marcel J. Tauchert, Reinhard Lührmann
Publikováno v:
Acta Crystallographica Section F
RNA helicases are indispensable for all organisms in each domain of life and have implications in numerous cellular processes. The DEAH-box RNA helicase Prp43 is involved in pre-mRNA splicing as well as rRNA maturation. Here, the crystal structure of
Publikováno v:
eLife, Vol 6 (2017)
eLife
eLife 6, e21510 (2017). doi:10.7554/eLife.21510
eLife
eLife 6, e21510 (2017). doi:10.7554/eLife.21510
The DEAH-box helicase Prp43 is a key player in pre-mRNA splicing as well as the maturation of rRNAs. The exact modus operandi of Prp43 and of all other spliceosomal DEAH-box RNA helicases is still elusive. Here, we report crystal structures of Prp43
Autor:
Patrizia Fabrizio, Reinhard Lührmann, Jean-Baptiste Fourmann, Ralf Ficner, Marcel J. Tauchert
Publikováno v:
Nucleic Acids Research
The DEAH-box NTPase Prp43 disassembles spliceosomes in co-operation with the cofactors Ntr1/Spp382 and Ntr2, forming the NTR complex. How Prp43 is regulated by its cofactors to discard selectively only intron-lariat spliceosomes (ILS) and defective s
Autor:
Ralf Ficner, Henning Urlaub, Marcel J. Tauchert, Olexandr Dybkov, Jean-Baptiste Fourmann, Reinhard Lührmann, Patrizia Fabrizio, Dmitry E. Agafonov
Publikováno v:
eLife
eLife, Vol 5 (2016)
eLife, Vol 5 (2016)
The DEAH-box NTPase Prp43 and its cofactors Ntr1 and Ntr2 form the NTR complex and are required for disassembling intron-lariat spliceosomes (ILS) and defective earlier spliceosomes. However, the Prp43 binding site in the spliceosome and its target(s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2dd091062df99a81f90e9348730e21f8
https://hdl.handle.net/11858/00-001M-0000-002A-DB05-B11858/00-001M-0000-002A-DB03-F11858/00-001M-0000-002A-DB06-9
https://hdl.handle.net/11858/00-001M-0000-002A-DB05-B11858/00-001M-0000-002A-DB03-F11858/00-001M-0000-002A-DB06-9
Autor:
Marcel J. Tauchert, Jean-Baptiste Fourmann, Olexandr Dybkov, Patrizia Fabrizio, Henning Urlaub, Reinhard Lührmann, Ralf Ficner, Dmitry E. Agafonov
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::518d6bf9122d90281afd1a110fefe20b
https://doi.org/10.7554/elife.15564.015
https://doi.org/10.7554/elife.15564.015
Autor:
Ralf Ficner, Marcel J. Tauchert
Publikováno v:
Acta crystallographica. Section F, Structural biology communications. 72(Pt 5)
Prp28 (pre-mRNA-splicing ATP-dependent RNA helicase 28) is a spliceosomal DEAD-box helicase which is involved in two steps of spliceosome assembly. It is required for the formation of commitment complex 2 in an ATP-independent manner as well as for t