NEDD8 Ultimate Buster-1L Interacts with the Ubiquitin-like Protein FAT10 and Accelerates Its Degradation
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- Extent
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Online-Ressource
- Language
-
Englisch
- Bibliographic citation
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In: Journal of Biological Chemistry ; 279 (2004), 16. - S. 16503-16510. - ISSN 0021-9258. - eISSN 1083-351X
- Classification
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Biowissenschaften, Biologie
- Event
-
Veröffentlichung
- (where)
-
Konstanz
- (who)
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Bibliothek der Universität Konstanz
- (when)
-
2004
- Creator
- URN
-
urn:nbn:de:bsz:352-221338
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
25.03.2025, 1:47 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
- Raasi, Shahri
- Groettrup, Marcus
- Schmidtke, Gunter
- Bibliothek der Universität Konstanz
Time of origin
- 2004
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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
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
FAT10, a ubiquitin-independent signal for proteasomal degradation
Evidence for an involvement of the ubiquitin-like modifier ISG15 in MHC class I antigen presentation
Evidence for an involvement of the ubiquitin‐like modifier ISG15 in MHC class I antigen presentation
The ubiquitin-like modifier FAT10 in cancer development
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
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
FAT10, a ubiquitin-independent signal for proteasomal degradation
Evidence for an involvement of the ubiquitin-like modifier ISG15 in MHC class I antigen presentation
Evidence for an involvement of the ubiquitin‐like modifier ISG15 in MHC class I antigen presentation
The ubiquitin-like modifier FAT10 in cancer development
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
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
FAT10, a ubiquitin-independent signal for proteasomal degradation
Evidence for an involvement of the ubiquitin-like modifier ISG15 in MHC class I antigen presentation