Structure of the ribosome post-recycling complex probed by chemical cross-linking and mass spectrometry

Ribosome recycling orchestrated by ABCE1 connects translation termination and mRNA surveillance mechanisms with re-initiation. Using a cross-linking and mass spectrometry approach, Kiosze-Becker et al. provide new information on the large conformational rearrangements that occur during ribosome recy...

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Autores principales:	Kristin Kiosze-Becker, Alessandro Ori, Milan Gerovac, André Heuer, Elina Nürenberg-Goloub, Umar Jan Rashid, Thomas Becker, Roland Beckmann, Martin Beck, Robert Tampé
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2016
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/5a65ddf3ea894a958d14576a7a06d340
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spelling	oai:doaj.org-article:5a65ddf3ea894a958d14576a7a06d3402021-12-02T14:39:33ZStructure of the ribosome post-recycling complex probed by chemical cross-linking and mass spectrometry10.1038/ncomms132482041-1723https://doaj.org/article/5a65ddf3ea894a958d14576a7a06d3402016-11-01T00:00:00Zhttps://doi.org/10.1038/ncomms13248https://doaj.org/toc/2041-1723Ribosome recycling orchestrated by ABCE1 connects translation termination and mRNA surveillance mechanisms with re-initiation. Using a cross-linking and mass spectrometry approach, Kiosze-Becker et al. provide new information on the large conformational rearrangements that occur during ribosome recycling.Kristin Kiosze-BeckerAlessandro OriMilan GerovacAndré HeuerElina Nürenberg-GoloubUmar Jan RashidThomas BeckerRoland BeckmannMartin BeckRobert TampéNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-9 (2016)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Kristin Kiosze-Becker Alessandro Ori Milan Gerovac André Heuer Elina Nürenberg-Goloub Umar Jan Rashid Thomas Becker Roland Beckmann Martin Beck Robert Tampé Structure of the ribosome post-recycling complex probed by chemical cross-linking and mass spectrometry
description	Ribosome recycling orchestrated by ABCE1 connects translation termination and mRNA surveillance mechanisms with re-initiation. Using a cross-linking and mass spectrometry approach, Kiosze-Becker et al. provide new information on the large conformational rearrangements that occur during ribosome recycling.
format	article
author	Kristin Kiosze-Becker Alessandro Ori Milan Gerovac André Heuer Elina Nürenberg-Goloub Umar Jan Rashid Thomas Becker Roland Beckmann Martin Beck Robert Tampé
author_facet	Kristin Kiosze-Becker Alessandro Ori Milan Gerovac André Heuer Elina Nürenberg-Goloub Umar Jan Rashid Thomas Becker Roland Beckmann Martin Beck Robert Tampé
author_sort	Kristin Kiosze-Becker
title	Structure of the ribosome post-recycling complex probed by chemical cross-linking and mass spectrometry
title_short	Structure of the ribosome post-recycling complex probed by chemical cross-linking and mass spectrometry
title_full	Structure of the ribosome post-recycling complex probed by chemical cross-linking and mass spectrometry
title_fullStr	Structure of the ribosome post-recycling complex probed by chemical cross-linking and mass spectrometry
title_full_unstemmed	Structure of the ribosome post-recycling complex probed by chemical cross-linking and mass spectrometry
title_sort	structure of the ribosome post-recycling complex probed by chemical cross-linking and mass spectrometry
publisher	Nature Portfolio
publishDate	2016
url	https://doaj.org/article/5a65ddf3ea894a958d14576a7a06d340
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_version_	1718390590761074688

Structure of the ribosome post-recycling complex probed by chemical cross-linking and mass spectrometry

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