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  Proteintranslation und Prozessierung in physiologischer Umgebung abgebildet

Pfeffer, S., & Förster, F. (2015). Proteintranslation und Prozessierung in physiologischer Umgebung abgebildet. Biospektrum, 21(4), 385-387. doi: 10.1007/s12268-015-0590-y.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-AA05-8 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-AA06-6
Genre: Journal Article

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 Creators:
Pfeffer, Stefan1, Author              
Förster, Friedrich1, Author              
Affiliations:
1Förster, Friedrich / Modeling of Protein Complexes, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565148              

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 Abstract: Cryoelectron tomography allows 3D imaging of crowded pleiomorphic environments at molecular resolution and is consequently an excellent method for studying the structure and organization of large molecules in their natural context. Using this approach for the analysis of ribosomal complexes in different cellular compartments, we obtained detailed insights into the supramolecular organization of the cytosolic and mitochondrial translation machineries and their association to membranes for co-translational protein transport.

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Language(s): deu - German
 Dates: 2015-06
 Publication Status: Published in print
 Pages: 3
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1007/s12268-015-0590-y
 Degree: -

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Title: Biospektrum
Source Genre: Journal
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Publ. Info: Heidelberg, Germany : Spektrum Akademischer Verlag
Pages: - Volume / Issue: 21 (4) Sequence Number: - Start / End Page: 385 - 387 Identifier: ISSN: 0947-0867
CoNE: https://pure.mpg.de/cone/journals/resource/110978984077563