Quantitative interaction mapping reveals an extended UBX domain in ASPL that disrupts functional p97 hexamers

The AAA+ ATPase p97 is an essential hexameric protein with multiple protein interaction partners and cellular functions. Here, the authors use interaction mapping to examine partner proteins of this large complex, and assess the effects of these proteins on the disassembly of the p97 complex.

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Autores principales: Anup Arumughan, Yvette Roske, Carolin Barth, Laura Lleras Forero, Kenny Bravo-Rodriguez, Alexandra Redel, Simona Kostova, Erik McShane, Robert Opitz, Katja Faelber, Kirstin Rau, Thorsten Mielke, Oliver Daumke, Matthias Selbach, Elsa Sanchez-Garcia, Oliver Rocks, Daniela Panáková, Udo Heinemann, Erich E. Wanker
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Publicado: Nature Portfolio 2016
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Acceso en línea:https://doaj.org/article/c05c3467f02d4df0b4320632445b06fa
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spelling oai:doaj.org-article:c05c3467f02d4df0b4320632445b06fa2021-12-02T16:56:45ZQuantitative interaction mapping reveals an extended UBX domain in ASPL that disrupts functional p97 hexamers10.1038/ncomms130472041-1723https://doaj.org/article/c05c3467f02d4df0b4320632445b06fa2016-10-01T00:00:00Zhttps://doi.org/10.1038/ncomms13047https://doaj.org/toc/2041-1723The AAA+ ATPase p97 is an essential hexameric protein with multiple protein interaction partners and cellular functions. Here, the authors use interaction mapping to examine partner proteins of this large complex, and assess the effects of these proteins on the disassembly of the p97 complex.Anup ArumughanYvette RoskeCarolin BarthLaura Lleras ForeroKenny Bravo-RodriguezAlexandra RedelSimona KostovaErik McShaneRobert OpitzKatja FaelberKirstin RauThorsten MielkeOliver DaumkeMatthias SelbachElsa Sanchez-GarciaOliver RocksDaniela PanákováUdo HeinemannErich E. WankerNature PortfolioarticleScienceQENNature Communications, Vol 7, Iss 1, Pp 1-13 (2016)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Anup Arumughan
Yvette Roske
Carolin Barth
Laura Lleras Forero
Kenny Bravo-Rodriguez
Alexandra Redel
Simona Kostova
Erik McShane
Robert Opitz
Katja Faelber
Kirstin Rau
Thorsten Mielke
Oliver Daumke
Matthias Selbach
Elsa Sanchez-Garcia
Oliver Rocks
Daniela Panáková
Udo Heinemann
Erich E. Wanker
Quantitative interaction mapping reveals an extended UBX domain in ASPL that disrupts functional p97 hexamers
description The AAA+ ATPase p97 is an essential hexameric protein with multiple protein interaction partners and cellular functions. Here, the authors use interaction mapping to examine partner proteins of this large complex, and assess the effects of these proteins on the disassembly of the p97 complex.
format article
author Anup Arumughan
Yvette Roske
Carolin Barth
Laura Lleras Forero
Kenny Bravo-Rodriguez
Alexandra Redel
Simona Kostova
Erik McShane
Robert Opitz
Katja Faelber
Kirstin Rau
Thorsten Mielke
Oliver Daumke
Matthias Selbach
Elsa Sanchez-Garcia
Oliver Rocks
Daniela Panáková
Udo Heinemann
Erich E. Wanker
author_facet Anup Arumughan
Yvette Roske
Carolin Barth
Laura Lleras Forero
Kenny Bravo-Rodriguez
Alexandra Redel
Simona Kostova
Erik McShane
Robert Opitz
Katja Faelber
Kirstin Rau
Thorsten Mielke
Oliver Daumke
Matthias Selbach
Elsa Sanchez-Garcia
Oliver Rocks
Daniela Panáková
Udo Heinemann
Erich E. Wanker
author_sort Anup Arumughan
title Quantitative interaction mapping reveals an extended UBX domain in ASPL that disrupts functional p97 hexamers
title_short Quantitative interaction mapping reveals an extended UBX domain in ASPL that disrupts functional p97 hexamers
title_full Quantitative interaction mapping reveals an extended UBX domain in ASPL that disrupts functional p97 hexamers
title_fullStr Quantitative interaction mapping reveals an extended UBX domain in ASPL that disrupts functional p97 hexamers
title_full_unstemmed Quantitative interaction mapping reveals an extended UBX domain in ASPL that disrupts functional p97 hexamers
title_sort quantitative interaction mapping reveals an extended ubx domain in aspl that disrupts functional p97 hexamers
publisher Nature Portfolio
publishDate 2016
url https://doaj.org/article/c05c3467f02d4df0b4320632445b06fa
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