Zobrazeno 1 - 10
of 10
pro vyhledávání: '"Stefan Amlacher"'
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
Autor:
Vladimir Rybin, Christiane Kotthoff, Andrew Bowman, Stefan Amlacher, Andreas G. Ladurner, Ed Hurt, Bianca Nijmeijer, Markus Hassler, Maria Hondele, Felix Halbach, Elisa T. Zhang, Tobias Stuwe
Publikováno v:
Nature. 499:111-114
Facilitates chromatin transcription (FACT) is a conserved histone chaperone that reorganizes nucleosomes and ensures chromatin integrity during DNA transcription, replication and repair. Key to the broad functions of FACT is its recognition of histon
Publikováno v:
Journal of Structural Biology. 177:99-105
Nuclear pore complexes (NPCs) embedded in the double nuclear membrane mediate the entire nucleocytoplasmic transport between the nucleus and cytoplasm. Each NPC is composed of about 30 different proteins (nucleoporins or Nups), which exist in multipl
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
Autor:
Goran Stjepanovic, Stefan Amlacher, Irmgard Sinning, Gert Bange, Fabio Vilardi, Vincenzo Favaloro, Karsten Rippe, Bernhard Dobberstein, Ed Hurt, Klemens Wild, Gunes Bozkurt
Publikováno v:
Proceedings of the National Academy of Sciences. 106:21131-21136
Tail-anchored (TA) membrane proteins are involved in a variety of important cellular functions, including membrane fusion, protein translocation, and apoptosis. The ATPase Get3 (Asna1, TRC40) was identified recently as the endoplasmic reticulum targe
Autor:
Torsten Heidenreich, Ulrich Mühlenhoff, Holger Webert, Angelo Gallo, Roland Lill, Uwe Linne, Stefan Amlacher, Ed Hurt, Sven-Andreas Freibert, Lucia Banci
Publikováno v:
Nature Communications
Maturation of iron-sulphur (Fe/S) proteins involves complex biosynthetic machinery. In vivo synthesis of [2Fe-2S] clusters on the mitochondrial scaffold protein Isu1 requires the cysteine desulphurase complex Nfs1-Isd11, frataxin, ferredoxin Yah1 and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1a1b40b2c438c7a5ca0abba62757d94e
http://hdl.handle.net/2318/1825758
http://hdl.handle.net/2318/1825758
Autor:
Gert Bange, Stefan Amlacher, Yoshihiro Yoneda, Irmgard Sinning, Bettina Bradatsch, Jun Katahira, Yutaka Ogawa, Dagmar Pratte, Dieter Kressler, Ed Hurt, Goran Stjepanovic, Daniela Strauß
Publikováno v:
Science (New York, N.Y.). 338(6107)
Symportin Synchrony Ribosomes, the macromolecular machines responsible for protein synthesis, function in the cytoplasm but are assembled in the nucleus. Ribosomal proteins must be imported into the nucleus, but how this is coordinated with assembly
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
Publikováno v:
FEBS letters. 584(8)
Tail-anchored proteins play important roles in protein translocation, membrane fusion and apoptosis. They are targeted to the endoplasmic reticulum membrane via the guided-entry of tail-anchored proteins (Get) pathway. We present the 2A crystal struc
Autor:
Sebastian Falk, Stefan Amlacher, Gert Bange, Manimozhiyan Arumugam, Daniel R. Mende, Peer Bork, Vera van Noort, Ed Hurt, Irmgard Sinning, Christopher J. Creevey, Bettina Bradatsch
Publikováno v:
'BMC Evolutionary Biology ', vol: 13, pages: 7-1-7-13 (2013)
BMC Evolutionary Biology, Vol 13, Iss 1, p 7 (2013)
BMC Evolutionary Biology
BMC Evolutionary Biology, Vol 13, Iss 1, p 7 (2013)
BMC Evolutionary Biology
Background Proteomes of thermophilic prokaryotes have been instrumental in structural biology and successfully exploited in biotechnology, however many proteins required for eukaryotic cell function are absent from bacteria or archaea. With Chaetomiu