Indispensable role of the Ubiquitin-fold modifier 1-specific E3 ligase in maintaining intestinal homeostasis and controlling gut inflammation
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
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2056-5968
- Extent
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Online-Ressource
- Language
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Englisch
- Notes
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online resource.
- Bibliographic citation
-
Indispensable role of the Ubiquitin-fold modifier 1-specific E3 ligase in maintaining intestinal homeostasis and controlling gut inflammation ; volume:5 ; number:1 ; day:29 ; month:1 ; year:2019 ; pages:1-16 ; date:12.2019
Cell discovery ; 5, Heft 1 (29.1.2019), 1-16, 12.2019
- Creator
-
Cai, Yafei
Zhu, Guangxun
Liu, Siyang
Pan, Zezheng
Quintero, Michaela
Poole, Candace J.
Lu, Chunwan
Zhu, Huabin
Islam, Bianca
Riggelen, Jan van
Browning, Darren
Liu, Kebin
Blumberg, Richard
Singh, Nagendra
Li, Honglin
- Contributor
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SpringerLink (Online service)
- DOI
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10.1038/s41421-018-0070-x
- URN
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urn:nbn:de:101:1-2019021622093151935830
- Rights
-
Open Access; Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
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
- Cai, Yafei
- Zhu, Guangxun
- Liu, Siyang
- Pan, Zezheng
- Quintero, Michaela
- Poole, Candace J.
- Lu, Chunwan
- Zhu, Huabin
- Islam, Bianca
- Riggelen, Jan van
- Browning, Darren
- Liu, Kebin
- Blumberg, Richard
- Singh, Nagendra
- Li, Honglin
- SpringerLink (Online service)
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Visualization of structural intermediates in an E3-E3 ligase ubiquitylation cascade via cryo-EM
Regulation mechanism of the quality control E3 ligase CHIP
Defining E3 ligase–substrate relationships through multiplex CRISPR screening
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A heterotypic assembly mechanism regulates CHIP E3 ligase activity
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Visualization of structural intermediates in an E3-E3 ligase ubiquitylation cascade via cryo-EM
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Radiosensibilisierung von Mammakarzinomzellen durch E3-Ubiquitin-Ligase SIAH1 in vitro