Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Marylena Dabrowski"'
Autor:
Timo Flügel, Magdalena Schacherl, Anett Unbehaun, Birgit Schroeer, Marylena Dabrowski, Jörg Bürger, Thorsten Mielke, Thiemo Sprink, Christoph A. Diebolder, Yollete V. Guillén Schlippe, Christian M. T. Spahn
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-15 (2024)
Abstract Structural studies of translating ribosomes traditionally rely on in vitro assembly and stalling of ribosomes in defined states. To comprehensively visualize bacterial translation, we reactivated ex vivo-derived E. coli polysomes in the PURE
Externí odkaz:
https://doaj.org/article/a8b8bb6841e3415faf91a35352ba940b
Autor:
Julia Flis, Mikael Holm, Emily J. Rundlet, Justus Loerke, Tarek Hilal, Marylena Dabrowski, Jörg Bürger, Thorsten Mielke, Scott C. Blanchard, Christian M.T. Spahn, Tatyana V. Budkevich
Publikováno v:
Cell Reports, Vol 25, Iss 10, Pp 2676-2688.e7 (2018)
Summary: Translocation moves the tRNA2⋅mRNA module directionally through the ribosome during the elongation phase of protein synthesis. Although translocation is known to entail large conformational changes within both the ribosome and tRNA substra
Externí odkaz:
https://doaj.org/article/2865020d75fd4c0b8a1c8de64eb95a4d
Autor:
Christian M. T. Spahn, Kaori Yamamoto, Marianne Collier, Thiemo Sprink, Patrick Scheerer, Hiroshi Yamamoto, Jörg Bürger, Peter W. Hildebrand, Marylena Dabrowski, Jochen Ismer, T. Hilal, Justus Loerke, Andrea Schmidt, Tanvir R. Shaikh, Thorsten Mielke
Publikováno v:
EMBO Journal
Internal ribosomal entry sites (IRESs) are structured cis ‐acting RNAs that drive an alternative, cap‐independent translation initiation pathway. They are used by many viruses to hijack the translational machinery of the host cell. IRESs facilita
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::66749e80b34dae02cfccda7a9a419064
https://doi.org/10.15252/embj.201592469
https://doi.org/10.15252/embj.201592469
Autor:
Christian M. T. Spahn, Martin Schüler, Eric Westhof, Pawel A. Penczek, Sean R. Connell, Birgit Schroeer, Marylena Dabrowski, Aurélie Lescoute, Thorsten Mielke, Jan Giesebrecht
Publikováno v:
Nature Structural and Molecular Biology
Nature Structural and Molecular Biology, Nature Publishing Group, 2006, 13 (12), pp.1092-6. ⟨10.1038/nsmb1177⟩
Nature Structural and Molecular Biology, Nature Publishing Group, 2006, 13 (12), pp.1092-6. ⟨10.1038/nsmb1177⟩
Internal ribosome entry sites (IRESs) facilitate an alternative, end-independent pathway of translation initiation. A particular family of dicistroviral IRESs can assemble elongation-competent 80S ribosomal complexes in the absence of canonical initi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ce382679e6ae02f5caa9c5fb68b58e9
https://doi.org/10.1038/nsmb1177
https://doi.org/10.1038/nsmb1177
Autor:
Sebastian Patzke, Markus A. Schäfer, Marylena Dabrowski, Edda Einfeldt, Gundo Diedrich, Ulrich Stelzl, Detlev Kamp, Knud H. Nierhaus, Christian M. T. Spahn, Viter Márquez, Gregor Blaha, Heinrich B. Stuhrmann, Regine Willumeit, Nils Burkhardt
This chapter provides a brief review of the reactions of the elongation cycle, and discusses recent data that clarify and explain some points of the divergent aspects of the current models of the elongation cycle. It shows that the location and the f
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::2c64119f502308778dd1d6860e4495c0
https://doi.org/10.1128/9781555818142.ch26
https://doi.org/10.1128/9781555818142.ch26
Autor:
Sebastian Patzke, Knud H. Nierhaus, Christian M. T. Spahn, Markus A. Schäfer, Marylena Dabrowski
Publikováno v:
Journal of Biological Chemistry. 273:32793-32800
The translocation reaction of two tRNAs on the ribosome during elongation of the nascent peptide chain is one of the most puzzling reactions of protein biosynthesis. We show here that the ribosomal contact patterns of the two tRNAs at A and P sites,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::807fa942081177a7f57ead8968a7cade
https://doi.org/10.1074/jbc.273.49.32793
https://doi.org/10.1074/jbc.273.49.32793
Autor:
Jörg-Uwe Bittner, Detlev Kamp, Dieter Beyer, Helga Voss, Jörg Wadzack, Knud H. Nierhaus, Markus A. Schäfer, Marylena Dabrowski, Nils Burkhardt, Heinrich B. Stuhrmann, Ralf Jünemann, Christian M. T. Spahn, Gundo Diedrich
Publikováno v:
Biochemistry and Cell Biology. 73:1011-1021
We determined the positions and arrangements of RNA ligands within the ribosome with a new neutron-scattering technique, the proton-spin contrast-variation. Two tRNAs were bound to the ribosome in the pre-translocational and the post-translocational
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::435ac70feb8cff7e01565497253ad024
https://doi.org/10.1139/o95-108
https://doi.org/10.1139/o95-108
Autor:
Maximilian Rost, Hongfei Wang, Martin Schüler, Marylena Dabrowski, Thorsten Mielke, Chie Takemoto, Takaho Terada, Daniel N. Wilson, Shigeyuki Yokoyama, Paola Fucini, Jan Giesebrecht, Kazutaka Murayama, Sean R. Connell, Mikako Shirouzu, Christian M. T. Spahn
Publikováno v:
Molecular cell. 25(5)
Summary Elongation factor G (EF-G) catalyzes tRNA translocation on the ribosome. Here a cryo-EM reconstruction of the 70S•EF-G ribosomal complex at 7.3 A resolution and the crystal structure of EF-G-2•GTP, an EF-G homolog, at 2.2 A resolution are
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d041a7d3d652b9eada32cd6d04ef090a
https://pubmed.ncbi.nlm.nih.gov/17349960
https://pubmed.ncbi.nlm.nih.gov/17349960
In vitro transcribed tRNA(Phe) analogues from Escherichia coli containing up to four randomly distributed A, G, U or C phosphorothioated nucleotides were used to investigate contact patterns with the ribosome in the A and P sites. The tRNAs were biol
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d80154299195bcb8565cef9b9a0da471
https://europepmc.org/articles/PMC394585/
https://europepmc.org/articles/PMC394585/