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| Verfasst von: | Hassan, A. Quamrul [VerfasserIn]  |
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| | Kirby, Christina A. [VerfasserIn] |
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| | Zhou, Wenlai [VerfasserIn] |
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| | Schuhmann, Tim [VerfasserIn] |
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| | Kityk, Roman [VerfasserIn] |
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| | Kipp, D. Randal [VerfasserIn] |
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| | Baird, Jason [VerfasserIn] |
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| | Chen, Jinyun [VerfasserIn] |
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| | Chen, Yaoyu [VerfasserIn] |
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| | Chung, Franklin [VerfasserIn] |
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| | Hoepfner, Dominic [VerfasserIn] |
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| | Movva, N. Rao [VerfasserIn] |
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| | Pagliarini, Raymond [VerfasserIn] |
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| | Petersen, Frank [VerfasserIn] |
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| | Quinn, Christopher [VerfasserIn] |
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| | Quinn, Douglas [VerfasserIn] |
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| | Riedl, Ralph [VerfasserIn] |
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| | Schmitt, Esther K. [VerfasserIn] |
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| | Schitter, Anne [VerfasserIn] |
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| | Stams, Travis [VerfasserIn] |
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| | Studer, Christian [VerfasserIn] |
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| | Fortin, Pascal D. [VerfasserIn] |
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| | Mayer, Matthias P. [VerfasserIn] |
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| | Sadlish, Heather [VerfasserIn] |
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| Titel: | The novolactone natural product disrupts the allosteric regulation of Hsp70 |
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| Verf.angabe: | A. Quamrul Hassan, Christina A. Kirby, Wenlai Zhou, Tim Schuhmann, Roman Kityk, D. Randal Kipp, Jason Baird, Jinyun Chen, Yaoyu Chen, Franklin Chung, Dominic Hoepfner, N. Rao Movva, Raymond Pagliarini, Frank Petersen, Christopher Quinn, Douglas Quinn, Ralph Riedl, Esther K. Schmitt, Anne Schitter, Travis Stams, Christian Studer, Pascal D. Fortin, Matthias P. Mayer, Heather Sadlish |
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| E-Jahr: | 2015 |
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| Jahr: | January 22, 2015 |
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| Umfang: | 11 S. |
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| Fussnoten: | Gesehen am 14.07.2020 |
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| Titel Quelle: | Enthalten in: Chemistry & biology |
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| Ort Quelle: | Amsterdam [u.a.] : Cell Press, 1994 |
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| Jahr Quelle: | 2015 |
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| Band/Heft Quelle: | 22(2015), 1, Seite 87-97 |
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| ISSN Quelle: | 1879-1301 |
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| Abstract: | The highly conserved 70 kDa heat shock proteins (Hsp70) play an integral role in proteostasis such that dysregulation has been implicated in numerous diseases. Elucidating the precise role of Hsp70 family members in the cellular context, however, has been hampered by the redundancy and intricate regulation of the chaperone network, and relatively few selective and potent tools. We have characterized a natural product, novolactone, that targets cytosolic and ER-localized isoforms of Hsp70 through a highly conserved covalent interaction at the interface between the substrate-binding and ATPase domains. Biochemical and structural analyses indicate that novolactone disrupts interdomain communication by allosterically inducing a conformational change in the Hsp70 protein to block ATP-induced substrate release and inhibit refolding activities. Thus, novolactone is a valuable tool for exploring the requirements of Hsp70 chaperones in diverse cellular contexts. |
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| DOI: | doi:10.1016/j.chembiol.2014.11.007 |
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| URL: | Bitte beachten Sie: Dies ist ein Bibliographieeintrag. Ein Volltextzugriff für Mitglieder der Universität besteht hier nur, falls für die entsprechende Zeitschrift/den entsprechenden Sammelband ein Abonnement besteht oder es sich um einen OpenAccess-Titel handelt.
Volltext: https://doi.org/10.1016/j.chembiol.2014.11.007 |
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| | Verlag: http://www.sciencedirect.com/science/article/pii/S1074552114004153 |
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| | DOI: https://doi.org/10.1016/j.chembiol.2014.11.007 |
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| Datenträger: | Online-Ressource |
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| Sprache: | eng |
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| K10plus-PPN: | 1724638742 |
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| Verknüpfungen: | → Zeitschrift |
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¬The¬ novolactone natural product disrupts the allosteric regulation of Hsp70 / Hassan, A. Quamrul [VerfasserIn]; January 22, 2015 (Online-Ressource)
