Dissecting the molecular organization of the translocon-associated protein complex

The translocon-associated protein complex (TRAP) is a crucial component of the endoplasmic reticulum protein translocon. Here the authors study native translocon structures from human disease patients and algae cells to determine the molecular organization of the TRAP complex.

Bibliographic Details
Main Authors: Stefan Pfeffer, Johanna Dudek, Miroslava Schaffer, Bobby G. Ng, Sahradha Albert, Jürgen M. Plitzko, Wolfgang Baumeister, Richard Zimmermann, Hudson H. Freeze, Benjamin D. Engel, Friedrich Förster
Format: Article
Language:English
Published: Nature Publishing Group 2017-02-01
Series:Nature Communications
Online Access:https://doi.org/10.1038/ncomms14516
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spelling doaj-023a7bda41494344bc4c30d1b798446d2021-05-11T07:45:07ZengNature Publishing GroupNature Communications2041-17232017-02-01811910.1038/ncomms14516Dissecting the molecular organization of the translocon-associated protein complexStefan Pfeffer0Johanna Dudek1Miroslava Schaffer2Bobby G. Ng3Sahradha Albert4Jürgen M. Plitzko5Wolfgang Baumeister6Richard Zimmermann7Hudson H. Freeze8Benjamin D. Engel9Friedrich Förster10Department of Molecular Structural Biology, Max-Planck Institute of BiochemistryDepartment of Medical Biochemistry and Molecular Biology, Saarland UniversityDepartment of Molecular Structural Biology, Max-Planck Institute of BiochemistryHuman Genetics Program, Sanford Burnham Prebys Medical Discovery InstituteDepartment of Molecular Structural Biology, Max-Planck Institute of BiochemistryDepartment of Molecular Structural Biology, Max-Planck Institute of BiochemistryDepartment of Molecular Structural Biology, Max-Planck Institute of BiochemistryDepartment of Medical Biochemistry and Molecular Biology, Saarland UniversityHuman Genetics Program, Sanford Burnham Prebys Medical Discovery InstituteDepartment of Molecular Structural Biology, Max-Planck Institute of BiochemistryDepartment of Molecular Structural Biology, Max-Planck Institute of BiochemistryThe translocon-associated protein complex (TRAP) is a crucial component of the endoplasmic reticulum protein translocon. Here the authors study native translocon structures from human disease patients and algae cells to determine the molecular organization of the TRAP complex.https://doi.org/10.1038/ncomms14516
collection DOAJ
language English
format Article
sources DOAJ
author Stefan Pfeffer
Johanna Dudek
Miroslava Schaffer
Bobby G. Ng
Sahradha Albert
Jürgen M. Plitzko
Wolfgang Baumeister
Richard Zimmermann
Hudson H. Freeze
Benjamin D. Engel
Friedrich Förster
spellingShingle Stefan Pfeffer
Johanna Dudek
Miroslava Schaffer
Bobby G. Ng
Sahradha Albert
Jürgen M. Plitzko
Wolfgang Baumeister
Richard Zimmermann
Hudson H. Freeze
Benjamin D. Engel
Friedrich Förster
Dissecting the molecular organization of the translocon-associated protein complex
Nature Communications
author_facet Stefan Pfeffer
Johanna Dudek
Miroslava Schaffer
Bobby G. Ng
Sahradha Albert
Jürgen M. Plitzko
Wolfgang Baumeister
Richard Zimmermann
Hudson H. Freeze
Benjamin D. Engel
Friedrich Förster
author_sort Stefan Pfeffer
title Dissecting the molecular organization of the translocon-associated protein complex
title_short Dissecting the molecular organization of the translocon-associated protein complex
title_full Dissecting the molecular organization of the translocon-associated protein complex
title_fullStr Dissecting the molecular organization of the translocon-associated protein complex
title_full_unstemmed Dissecting the molecular organization of the translocon-associated protein complex
title_sort dissecting the molecular organization of the translocon-associated protein complex
publisher Nature Publishing Group
series Nature Communications
issn 2041-1723
publishDate 2017-02-01
description The translocon-associated protein complex (TRAP) is a crucial component of the endoplasmic reticulum protein translocon. Here the authors study native translocon structures from human disease patients and algae cells to determine the molecular organization of the TRAP complex.
url https://doi.org/10.1038/ncomms14516
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