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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Nature Portfolio
2016
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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 |
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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 |
work_keys_str_mv |
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