- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Bibliographic citation
-
In: Molecular and Cellular Biology ; 25 (2005), 9. - S. 3483-3491. - ISSN 0270-7306
- Classification
-
Biowissenschaften, Biologie
- Event
-
Veröffentlichung
- (where)
-
Konstanz
- (who)
-
Bibliothek der Universität Konstanz
- (when)
-
2005
- Creator
- URN
-
urn:nbn:de:bsz:352-166793
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
25.03.2025, 1:52 PM CET
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
- Hipp, Mark Steffen
- Kalveram, Birte
- Raasi, Shahri
- Groettrup, Marcus
- Schmidtke, Gunter
- Bibliothek der Universität Konstanz
Time of origin
- 2005
Other Objects (12)
The ubiquitin-like modifier FAT10 : much more than a proteasome-targeting signal
Conjugation of the Ubiquitin Activating Enzyme UBE1 with the Ubiquitin-Like Modifier FAT10 Targets It for Proteasomal Degradation
FAT10ylation as a signal for proteasomal degradation
The ubiquitin-like modifier FAT10 in cancer development
Degradation of FAT10 by the 26S proteasome is independent of ubiquitylation but relies on NUB1L
NEDD8 Ultimate Buster-1L Interacts with the Ubiquitin-like Protein FAT10 and Accelerates Its Degradation
Regulation of Interferon Induction by the Ubiquitin-Like Modifier FAT10
The ubiquitin-like protein FAT10 forms covalent conjugates and induces apoptosis
The ubiquitin-like modifier FAT10 in antigen processing and antimicrobial defense
The ubiquitin-like modifier FAT10 interacts with HDAC6 and localizes to aggresomes under proteasome inhibition
Activating the ubiquitin family : UBA6 challenges the field
Newly translated proteins are substrates for ubiquitin, ISG15, and FAT10
The ubiquitin-like modifier FAT10 : much more than a proteasome-targeting signal
Conjugation of the Ubiquitin Activating Enzyme UBE1 with the Ubiquitin-Like Modifier FAT10 Targets It for Proteasomal Degradation
FAT10ylation as a signal for proteasomal degradation
The ubiquitin-like modifier FAT10 in cancer development
Degradation of FAT10 by the 26S proteasome is independent of ubiquitylation but relies on NUB1L
NEDD8 Ultimate Buster-1L Interacts with the Ubiquitin-like Protein FAT10 and Accelerates Its Degradation
Regulation of Interferon Induction by the Ubiquitin-Like Modifier FAT10
The ubiquitin-like protein FAT10 forms covalent conjugates and induces apoptosis
The ubiquitin-like modifier FAT10 in antigen processing and antimicrobial defense
The ubiquitin-like modifier FAT10 interacts with HDAC6 and localizes to aggresomes under proteasome inhibition
Activating the ubiquitin family : UBA6 challenges the field
Newly translated proteins are substrates for ubiquitin, ISG15, and FAT10
The ubiquitin-like modifier FAT10 : much more than a proteasome-targeting signal
Conjugation of the Ubiquitin Activating Enzyme UBE1 with the Ubiquitin-Like Modifier FAT10 Targets It for Proteasomal Degradation
FAT10ylation as a signal for proteasomal degradation
The ubiquitin-like modifier FAT10 in cancer development
Degradation of FAT10 by the 26S proteasome is independent of ubiquitylation but relies on NUB1L
NEDD8 Ultimate Buster-1L Interacts with the Ubiquitin-like Protein FAT10 and Accelerates Its Degradation
Regulation of Interferon Induction by the Ubiquitin-Like Modifier FAT10
The ubiquitin-like protein FAT10 forms covalent conjugates and induces apoptosis
The ubiquitin-like modifier FAT10 in antigen processing and antimicrobial defense
The ubiquitin-like modifier FAT10 interacts with HDAC6 and localizes to aggresomes under proteasome inhibition
Activating the ubiquitin family : UBA6 challenges the field