Hochschulschrift
Microgravity- and shear stress-mediated regulation of E3 ligase NEDD4 and its substrate Cx43 in endothelial cells
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Dimensions
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30 cm
- Extent
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98 Bl.
- Language
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Englisch
- Notes
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Ill., graph. Darst.
Berlin, Freie Univ., Diss., 2012 (Nicht für den Austausch)
- Classification
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Medizin, Gesundheit
- Creator
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Fiedorowicz, Katarzyna
- Table of contents
- Rights
-
Bei diesem Objekt liegt nur das Inhaltsverzeichnis digital vor. Der Zugriff darauf ist unbeschränkt möglich.
- Last update
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11.06.2025, 1:41 PM 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.
Object type
- Hochschulschrift
Associated
- Fiedorowicz, Katarzyna
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Microgravity- and shear stress-mediated regulation of E3 ligase NEDD4 and its substrate Cx43 in endothelial cells
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Microgravity- and shear stress-mediated regulation of E3 ligase NEDD4 and its substrate Cx43 in endothelial cells
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
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S100A4 als Zielprotein der E3-Ligase Asb2β
A representation and deep learning model for annotating ubiquitylation sentences stating E3 ligase - substrate interaction
Visualization of structural intermediates in an E3-E3 ligase ubiquitylation cascade via cryo-EM
Regulation mechanism of the quality control E3 ligase CHIP
The circadian E3 ligase complex SCFFBXL3+CRY targets TLK2
Microgravity- and shear stress-mediated regulation of E3 ligase NEDD4 and its substrate Cx43 in endothelial cells
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
Prospective discovery of small molecule enhancers of an E3 ligase-substrate interaction
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S100A4 als Zielprotein der E3-Ligase Asb2β
A representation and deep learning model for annotating ubiquitylation sentences stating E3 ligase - substrate interaction
Visualization of structural intermediates in an E3-E3 ligase ubiquitylation cascade via cryo-EM
Regulation mechanism of the quality control E3 ligase CHIP