Cargando…
The ER folding sensor UGGT1 acts on TAPBPR-chaperoned peptide-free MHC I
Adaptive immune responses are triggered by antigenic peptides presented on major histocompatibility complex class I (MHC I) at the surface of pathogen-infected or cancerous cells. Formation of stable peptide-MHC I complexes is facilitated by tapasin and TAPBPR, two related MHC I-specific chaperones...
Autores principales: | Sagert, Lina, Winter, Christian, Ruppert, Ina, Zehetmaier, Maximilian, Thomas, Christoph, Tampé, Robert |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
eLife Sciences Publications, Ltd
2023
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10325711/ https://www.ncbi.nlm.nih.gov/pubmed/37345806 http://dx.doi.org/10.7554/eLife.85432 |
Ejemplares similares
-
A loop structure allows TAPBPR to exert its dual function as MHC I chaperone and peptide editor
por: Sagert, Lina, et al.
Publicado: (2020) -
Visualisation of a flexible modular structure of the ER folding-sensor enzyme UGGT
por: Satoh, Tadashi, et al.
Publicado: (2017) -
Chaperone function in antigen presentation by MHC class I molecules—tapasin in the PLC and TAPBPR beyond
por: Margulies, David H., et al.
Publicado: (2023) -
HspB8 prevents aberrant phase transitions of FUS by chaperoning its folded RNA-binding domain
por: Boczek, Edgar E, et al.
Publicado: (2021) -
Cell-based HTS identifies a chemical chaperone for preventing ER protein aggregation and proteotoxicity
por: Kitakaze, Keisuke, et al.
Publicado: (2019)