Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Ruth Kunze"'
Autor:
Bebiana Sá-Moura, Markus Kornprobst, Satyavati Kharde, Yasar Luqman Ahmed, Gunter Stier, Ruth Kunze, Irmgard Sinning, Ed Hurt
Publikováno v:
PLoS ONE, Vol 15, Iss 6, p e0234932 (2020)
[This corrects the article DOI: 10.1371/journal.pone.0183272.].
Externí odkaz:
https://doaj.org/article/9d5d4cacd600456c9e73b7606f982251
Publikováno v:
International Journal of Molecular Sciences, Vol 21, Iss 23, p 9108 (2020)
The ribosome assembly factor Nsa2 is part of the Rea1-Rsa4-Nsa2 interconnected relay on nuclear pre-60S particles that is essential for 60S ribosome biogenesis. Cryo-EM structures depict Nsa2 docked via its C-terminal β-barrel domain to nuclear pre-
Externí odkaz:
https://doaj.org/article/8c17172b141340d8afff238bde9a436a
Autor:
Bebiana Sá-Moura, Markus Kornprobst, Satyavati Kharde, Yasar Luqman Ahmed, Gunter Stier, Ruth Kunze, Irmgard Sinning, Ed Hurt
Publikováno v:
PLoS ONE, Vol 12, Iss 8, p e0183272 (2017)
In eukaryotes, ribosome assembly is a highly complex process that involves more than 200 assembly factors that ensure the folding, modification and processing of the different rRNA species as well as the timely association of ribosomal proteins. One
Externí odkaz:
https://doaj.org/article/cc1b9f4e13af49aabcf07f564b9ae8c6
Publikováno v:
International Journal of Molecular Sciences, Vol 21, Iss 9108, p 9108 (2020)
International Journal of Molecular Sciences
Volume 21
Issue 23
International Journal of Molecular Sciences
Volume 21
Issue 23
The ribosome assembly factor Nsa2 is part of the Rea1-Rsa4-Nsa2 interconnected relay on nuclear pre-60S particles that is essential for 60S ribosome biogenesis. Cryo-EM structures depict Nsa2 docked via its C-terminal &beta
barrel domain to nucl
barrel domain to nucl
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fa436351c501d9e9e0cf3066ea34d591
https://www.mdpi.com/1422-0067/21/23/9108
https://www.mdpi.com/1422-0067/21/23/9108
Autor:
Gunter Stier, Bebiana Sá-Moura, Ed Hurt, Satyavati Kharde, Yasar Luqman Ahmed, Irmgard Sinning, Ruth Kunze, Markus Kornprobst
Publikováno v:
PLoS ONE, Vol 15, Iss 6, p e0234932 (2020)
[This corrects the article DOI: 10.1371/journal.pone.0183272.].
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::edda7473882fbb92a0826e9dc1ee51ef
https://doaj.org/article/9d5d4cacd600456c9e73b7606f982251
https://doaj.org/article/9d5d4cacd600456c9e73b7606f982251
Autor:
Ruth Kunze, Sabine Griesel, Paulina Fischer, Otto Berninghausen, Roland Beckmann, Nikola Kellner, Benjamin Lau, Jingdong Cheng, Ed Hurt, Daniela Strauss, Martina Kallas, Jochen Baßler
Publikováno v:
Molecular Cell
The ‘birth’ of the eukaryotic ribosome is preceded by RNA folding and processing reactions that depend on assembly factors and snoRNAs. The 90S (SSU-processome) is the earliest pre-ribosome structurally analyzed, which was suggested to assemble s
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8159f1be09329bd6d62169c63592f558
Publikováno v:
Nature Structural & Molecular Biology. 22:774-781
Nuclear pore complexes (NPCs) mediate transport between the nucleus and cytoplasm. NPCs are composed of ∼30 nucleoporins (Nups), most of which are organized in stable subcomplexes. How these modules are interconnected within the large NPC framework
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::166938de1b0c5b4637980b26a70b1b2f
https://doi.org/10.1038/nsmb.3084
https://doi.org/10.1038/nsmb.3084
Autor:
Satyavati Kharde, Irmgard Sinning, Gunter Stier, Markus Kornprobst, Ed Hurt, Ruth Kunze, Bebiana Sá-Moura, Yasar Luqman Ahmed
Publikováno v:
PLOS ONE
PLoS ONE, Vol 12, Iss 8, p e0183272 (2017)
'PloS One ', vol: 12, pages: e0183272-1-e0183272-18 (2017)
PLoS ONE
PLoS ONE, Vol 12, Iss 8, p e0183272 (2017)
'PloS One ', vol: 12, pages: e0183272-1-e0183272-18 (2017)
PLoS ONE
In eukaryotes, ribosome assembly is a highly complex process that involves more than 200 assembly factors that ensure the folding, modification and processing of the different rRNA species as well as the timely association of ribosomal proteins. One
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::76a17abe741ab113b2ec8bd74c58da7c
Autor:
Manimozhiyan Arumugam, Phillip Sarges, Dirk Flemming, Vera van Noort, Ed Hurt, Stefan Amlacher, Damien P. Devos, Peer Bork, Ruth Kunze
Publikováno v:
Cell. 146(2):277-289
SummaryDespite decades of research, the structure and assembly of the nuclear pore complex (NPC), which is composed of ∼30 nucleoporins (Nups), remain elusive. Here, we report the genome of the thermophilic fungus Chaetomium thermophilum (ct) and i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::cc9b82d8ebfafb787465acafd50bc9e6
Publikováno v:
The Journal of Cell Biology
A new tool to probe the FG repeat network of the nuclear pore complex transport channel in vivo provides insight into the organization and functional features of the channel.
Unraveling the organization of the FG repeat meshwork that forms the a
Unraveling the organization of the FG repeat meshwork that forms the a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::63b533a68259ef33dfb88d2ad3a5e564
http://europepmc.org/articles/PMC3198172
http://europepmc.org/articles/PMC3198172