- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Deutsch
- Bibliographic citation
-
In: BIOspektrum ; 26 (2020), 5. - S. 471-474. - Springer. - ISSN 0947-0867. - eISSN 1868-6249
- Keyword
-
Ubiquitin
Proteine
Proteasom
Affinitätschromatographie
Massenspektrometrie
Cytologie
Proteolyse
Forschung
Molekularbiologie
- Event
-
Veröffentlichung
- (where)
-
Konstanz
- (who)
-
KOPS Universität Konstanz
- (when)
-
2020
- Creator
- URN
-
urn:nbn:de:bsz:352-2-15njfj1d051i96
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
15.08.2025, 7:39 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
- Lutz, Joachim
- Höllmüller, Eva
- Scheffner, Martin
- Marx, Andreas
- Stengel, Florian
- KOPS Universität Konstanz
Time of origin
- 2020
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Die Länge spezifischer Ubiquitin-ketten beeinflusst ihre Erkennung
Die Länge einer Ubiquitinkette: ein genereller Faktor für die selektive Erkennung durch Ubiquitin‐bindende Proteine
The Length of a Ubiquitin Chain: A General Factor for Selective Recognition by Ubiquitin‐Binding Proteins
The length of a ubiquitin chain is a general determinant for selective recognition by ubiquitin-binding proteins
Identification of Proteins Interacting with Ubiquitin Chains
The Evolving Contribution of Mass Spectrometry to Integrative Structural Biology
The Evolving Contribution of Mass Spectrometry to Integrative Structural Biology
A Photo‐Caged Cross‐Linker for Identifying Protein‐Protein Interactions
Parkin is an E3 ligase for the ubiquitin-like modifier FAT10, which inhibits Parkin activation and mitophagy
A ubiquitin variant-based affinity approach selectively identifies substrates of the ubiquitin ligase E6AP in complex with HPV-11 E6 or HPV-16 E6
Interrogating protein-ligand interactions through structural mass spectrometry, computational simulations and biophysical techniques
Molecular basis of AKAP79 regulation by calmodulin
Die Länge spezifischer Ubiquitin-ketten beeinflusst ihre Erkennung
Die Länge einer Ubiquitinkette: ein genereller Faktor für die selektive Erkennung durch Ubiquitin‐bindende Proteine
The Length of a Ubiquitin Chain: A General Factor for Selective Recognition by Ubiquitin‐Binding Proteins
The length of a ubiquitin chain is a general determinant for selective recognition by ubiquitin-binding proteins
Identification of Proteins Interacting with Ubiquitin Chains
The Evolving Contribution of Mass Spectrometry to Integrative Structural Biology
The Evolving Contribution of Mass Spectrometry to Integrative Structural Biology
A Photo‐Caged Cross‐Linker for Identifying Protein‐Protein Interactions
Parkin is an E3 ligase for the ubiquitin-like modifier FAT10, which inhibits Parkin activation and mitophagy
A ubiquitin variant-based affinity approach selectively identifies substrates of the ubiquitin ligase E6AP in complex with HPV-11 E6 or HPV-16 E6
Interrogating protein-ligand interactions through structural mass spectrometry, computational simulations and biophysical techniques