- Location
-
Deutsche Nationalbibliothek Frankfurt am Main
- Extent
-
Online-Ressource
- Language
-
Englisch
- Bibliographic citation
-
In: Biomolecules ; 10 (2020), 6. - 951. - MDPI. - eISSN 2218-273X
- Event
-
Veröffentlichung
- (where)
-
Konstanz
- (who)
-
KOPS Universität Konstanz
- (when)
-
2020
- Creator
- URN
-
urn:nbn:de:bsz:352-2-utj1o6komg682
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
25.03.2025, 1:45 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
- Mah, Mei Min
- Roverato, Nicola
- Groettrup, Marcus
- KOPS Universität Konstanz
Time of origin
- 2020
Other Objects (12)
The ubiquitin-like modifier FAT10 in cancer development
The ubiquitin-like modifier FAT10 : much more than a proteasome-targeting signal
The ubiquitin-like modifier FAT10 in antigen processing and antimicrobial defense
Conjugation of the Ubiquitin Activating Enzyme UBE1 with the Ubiquitin-Like Modifier FAT10 Targets It for Proteasomal Degradation
The ubiquitin-like modifier FAT10 interacts with HDAC6 and localizes to aggresomes under proteasome inhibition
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 stimulates the activity of the deubiquitylating enzyme OTUB1
The ubiquitin-like modifier FAT10 interferes with SUMO activation
A Cytomegalovirus Inhibitor of Gamma Interferon Signaling Controls Immunoproteasome Induction
The ubiquitin-like modifier FAT10 decorates autophagy-targeted Salmonella and contributes to Salmonella resistance in mice
The ubiquitin-like modifier FAT10 inhibits retinal PDE6 activity and mediates its proteasomal degradation
The ubiquitin-like modifier FAT10 in cancer development
The ubiquitin-like modifier FAT10 : much more than a proteasome-targeting signal
The ubiquitin-like modifier FAT10 in antigen processing and antimicrobial defense
Conjugation of the Ubiquitin Activating Enzyme UBE1 with the Ubiquitin-Like Modifier FAT10 Targets It for Proteasomal Degradation
The ubiquitin-like modifier FAT10 interacts with HDAC6 and localizes to aggresomes under proteasome inhibition
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 stimulates the activity of the deubiquitylating enzyme OTUB1
The ubiquitin-like modifier FAT10 interferes with SUMO activation
A Cytomegalovirus Inhibitor of Gamma Interferon Signaling Controls Immunoproteasome Induction
The ubiquitin-like modifier FAT10 decorates autophagy-targeted Salmonella and contributes to Salmonella resistance in mice
The ubiquitin-like modifier FAT10 inhibits retinal PDE6 activity and mediates its proteasomal degradation
The ubiquitin-like modifier FAT10 in cancer development
The ubiquitin-like modifier FAT10 : much more than a proteasome-targeting signal
The ubiquitin-like modifier FAT10 in antigen processing and antimicrobial defense
Conjugation of the Ubiquitin Activating Enzyme UBE1 with the Ubiquitin-Like Modifier FAT10 Targets It for Proteasomal Degradation
The ubiquitin-like modifier FAT10 interacts with HDAC6 and localizes to aggresomes under proteasome inhibition
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 stimulates the activity of the deubiquitylating enzyme OTUB1
The ubiquitin-like modifier FAT10 interferes with SUMO activation
A Cytomegalovirus Inhibitor of Gamma Interferon Signaling Controls Immunoproteasome Induction
The ubiquitin-like modifier FAT10 decorates autophagy-targeted Salmonella and contributes to Salmonella resistance in mice