Immuno- and constitutive proteasomes do not differ in their abilities to degrade ubiquitinated proteins
- Language
-
Englisch
- Identifier
-
1152946927
Subject
Physiologische Chemie
Contributor
Nathan, James A.
Spinnenhirn, Valentina
Schmidtke, Gunter
Basler, Michael
Groettrup, Marcus
Goldberg, Alfred L.
Spinnenhirn, Valentina
Schmidtke, Gunter
Basler, Michael
Groettrup, Marcus
Goldberg, Alfred L.
- URN
- Rights
-
Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
-
26.01.2023, 1:55 PM CET
Associated
- Nathan, James A.
- Spinnenhirn, Valentina
- Schmidtke, Gunter
- Basler, Michael
- Groettrup, Marcus
- Goldberg, Alfred L.
Other Objects (12)
The ubiquitin-like modifier FAT10 decorates autophagy-targeted Salmonella and contributes to Salmonella resistance in mice
Newly translated proteins are substrates for ubiquitin, ISG15, and FAT10
The proteomic analysis of endogenous FAT10 substrates identifies p62/SQSTM1 as a substrate of FAT10ylation
The ubiquitin-like protein FAT10 forms covalent conjugates and induces apoptosis
NEDD8 Ultimate Buster-1L Interacts with the Ubiquitin-like Protein FAT10 and Accelerates Its Degradation
FAT10ylation as a signal for proteasomal degradation
The ubiquitin-like modifier FAT10 interacts with HDAC6 and localizes to aggresomes under proteasome inhibition
Degradation of FAT10 by the 26S proteasome is independent of ubiquitylation but relies on NUB1L
Interferon-γ inducible exchanges of 20S proteasome active site subunits : why?
Activating the ubiquitin family : UBA6 challenges the field
Evidence for the existence of a non-catalytic modifier site of peptide hydrolysis by the 20 S proteasome
FAT10 and NUB1L bind to the VWA domain of Rpn10 and Rpn1 to enable proteasome-mediated proteolysis
The ubiquitin-like modifier FAT10 decorates autophagy-targeted Salmonella and contributes to Salmonella resistance in mice
Newly translated proteins are substrates for ubiquitin, ISG15, and FAT10
The proteomic analysis of endogenous FAT10 substrates identifies p62/SQSTM1 as a substrate of FAT10ylation
The ubiquitin-like protein FAT10 forms covalent conjugates and induces apoptosis
NEDD8 Ultimate Buster-1L Interacts with the Ubiquitin-like Protein FAT10 and Accelerates Its Degradation
FAT10ylation as a signal for proteasomal degradation
The ubiquitin-like modifier FAT10 interacts with HDAC6 and localizes to aggresomes under proteasome inhibition
Degradation of FAT10 by the 26S proteasome is independent of ubiquitylation but relies on NUB1L
Interferon-γ inducible exchanges of 20S proteasome active site subunits : why?
Activating the ubiquitin family : UBA6 challenges the field
Evidence for the existence of a non-catalytic modifier site of peptide hydrolysis by the 20 S proteasome
FAT10 and NUB1L bind to the VWA domain of Rpn10 and Rpn1 to enable proteasome-mediated proteolysis
The ubiquitin-like modifier FAT10 decorates autophagy-targeted Salmonella and contributes to Salmonella resistance in mice
Newly translated proteins are substrates for ubiquitin, ISG15, and FAT10
The proteomic analysis of endogenous FAT10 substrates identifies p62/SQSTM1 as a substrate of FAT10ylation
The ubiquitin-like protein FAT10 forms covalent conjugates and induces apoptosis
NEDD8 Ultimate Buster-1L Interacts with the Ubiquitin-like Protein FAT10 and Accelerates Its Degradation
FAT10ylation as a signal for proteasomal degradation
The ubiquitin-like modifier FAT10 interacts with HDAC6 and localizes to aggresomes under proteasome inhibition
Degradation of FAT10 by the 26S proteasome is independent of ubiquitylation but relies on NUB1L
Interferon-γ inducible exchanges of 20S proteasome active site subunits : why?
Activating the ubiquitin family : UBA6 challenges the field
Evidence for the existence of a non-catalytic modifier site of peptide hydrolysis by the 20 S proteasome