Prospective discovery of small molecule enhancers of an E3 ligase-substrate interaction
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
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2041-1723
- Extent
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Online-Ressource
- Language
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Englisch
- Notes
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online resource.
- Bibliographic citation
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Prospective discovery of small molecule enhancers of an E3 ligase-substrate interaction ; volume:10 ; number:1 ; day:29 ; month:3 ; year:2019 ; pages:1-12 ; date:12.2019
Nature Communications ; 10, Heft 1 (29.3.2019), 1-12, 12.2019
- Creator
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Simonetta, Kyle R.
Taygerly, Joshua
Boyle, Kathleen
Basham, Stephen E.
Padovani, Chris
Lou, Yan
Cummins, Thomas J.
Yung, Stephanie L.
Soly, Szerenke Kiss von
Kayser, Frank
Kuriyan, John
Rape, Michael
Cardozo, Mario
Gallop, Mark A.
Bence, Neil F.
Barsanti, Paul A.
Saha, Anjanabha
- Contributor
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SpringerLink (Online service)
- DOI
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10.1038/s41467-019-09358-9
- URN
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urn:nbn:de:101:1-2019041620182508399005
- Rights
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Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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14.08.2025, 11:01 AM CEST
Data provider
This object is provided by:
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Deutsche Nationalbibliothek. If you have any questions about the object, please contact the data provider.
Associated
- Simonetta, Kyle R.
- Taygerly, Joshua
- Boyle, Kathleen
- Basham, Stephen E.
- Padovani, Chris
- Lou, Yan
- Cummins, Thomas J.
- Yung, Stephanie L.
- Soly, Szerenke Kiss von
- Kayser, Frank
- Kuriyan, John
- Rape, Michael
- Cardozo, Mario
- Gallop, Mark A.
- Bence, Neil F.
- Barsanti, Paul A.
- Saha, Anjanabha
- SpringerLink (Online service)
Other Objects (12)
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From substrate to function : deciphering substrate specificity of the SCFFbxw5 ubiquitin E3 ligase complex
Author Correction: Defining E3 ligase–substrate relationships through multiplex CRISPR screening
Structural insights into substrate recognition by the SOCS2 E3 ubiquitin ligase
Targeting TRAF6 E3 ligase activity with a small-molecule inhibitor combats autoimmunity
Profiling cellular E3 ubiquitin ligase networks
S100A4 als Zielprotein der E3-Ligase Asb2β
A representation and deep learning model for annotating ubiquitylation sentences stating E3 ligase - substrate interaction
Hemmung der Myc-Funktion durch niedermolekulare Inhibitoren der E3-Ubiquitin-Ligase HuweI=Inhibition of Myc function using small molecule inhibitors of the E3 ubiquitin ligase HuweI
Microgravity- and shear stress-mediated regulation of E3 ligase NEDD4 and its substrate Cx43 in endothelial cells
Microgravity- and shear stress-mediated regulation of E3 ligase NEDD4 and its substrate Cx43 in endothelial cells
Visualization of structural intermediates in an E3-E3 ligase ubiquitylation cascade via cryo-EM
Defining E3 ligase–substrate relationships through multiplex CRISPR screening
From substrate to function : deciphering substrate specificity of the SCFFbxw5 ubiquitin E3 ligase complex
Author Correction: Defining E3 ligase–substrate relationships through multiplex CRISPR screening
Structural insights into substrate recognition by the SOCS2 E3 ubiquitin ligase
Targeting TRAF6 E3 ligase activity with a small-molecule inhibitor combats autoimmunity
Profiling cellular E3 ubiquitin ligase networks
S100A4 als Zielprotein der E3-Ligase Asb2β
A representation and deep learning model for annotating ubiquitylation sentences stating E3 ligase - substrate interaction
Hemmung der Myc-Funktion durch niedermolekulare Inhibitoren der E3-Ubiquitin-Ligase HuweI=Inhibition of Myc function using small molecule inhibitors of the E3 ubiquitin ligase HuweI
Microgravity- and shear stress-mediated regulation of E3 ligase NEDD4 and its substrate Cx43 in endothelial cells
Microgravity- and shear stress-mediated regulation of E3 ligase NEDD4 and its substrate Cx43 in endothelial cells
Visualization of structural intermediates in an E3-E3 ligase ubiquitylation cascade via cryo-EM
Defining E3 ligase–substrate relationships through multiplex CRISPR screening
From substrate to function : deciphering substrate specificity of the SCFFbxw5 ubiquitin E3 ligase complex
Author Correction: Defining E3 ligase–substrate relationships through multiplex CRISPR screening
Structural insights into substrate recognition by the SOCS2 E3 ubiquitin ligase
Targeting TRAF6 E3 ligase activity with a small-molecule inhibitor combats autoimmunity
Profiling cellular E3 ubiquitin ligase networks
S100A4 als Zielprotein der E3-Ligase Asb2β
A representation and deep learning model for annotating ubiquitylation sentences stating E3 ligase - substrate interaction
Hemmung der Myc-Funktion durch niedermolekulare Inhibitoren der E3-Ubiquitin-Ligase HuweI=Inhibition of Myc function using small molecule inhibitors of the E3 ubiquitin ligase HuweI
Microgravity- and shear stress-mediated regulation of E3 ligase NEDD4 and its substrate Cx43 in endothelial cells
Microgravity- and shear stress-mediated regulation of E3 ligase NEDD4 and its substrate Cx43 in endothelial cells