Cargando…
A BRET-based assay reveals collagen–Hsp47 interaction dynamics in the endoplasmic reticulum and small-molecule inhibition of this interaction
Molecular chaperones perform pivotal roles in proteostasis by engaging in protein–protein interactions (PPIs). The collagen-specific molecular chaperone Hsp47 (heat shock protein 47) interacts with procollagen in the endoplasmic reticulum (ER) and plays crucial roles in collagen synthesis. PPIs betw...
Autores principales: | Ito, Shinya, Saito, Masazumi, Yoshida, Masahito, Takeuchi, Koh, Doi, Takayuki, Nagata, Kazuhiro |
---|---|
Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American Society for Biochemistry and Molecular Biology
2019
|
Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6827286/ https://www.ncbi.nlm.nih.gov/pubmed/31492754 http://dx.doi.org/10.1074/jbc.RA119.010567 |
Ejemplares similares
-
Lowering the culture temperature corrects collagen abnormalities caused by HSP47 gene knockout
por: Fujii, Kazunori K., et al.
Publicado: (2019) -
Hsp47 promotes cancer metastasis by enhancing collagen-dependent cancer cell-platelet interaction
por: Xiong, Gaofeng, et al.
Publicado: (2020) -
Involvement of the stress protein HSP47 in procollagen processing in the endoplasmic reticulum
Publicado: (1992) -
NMR and Mutational Identification of the Collagen-Binding Site of the Chaperone Hsp47
por: Yagi-Utsumi, Maho, et al.
Publicado: (2012) -
cTAGE5 mediates collagen secretion through interaction with TANGO1 at endoplasmic reticulum exit sites
por: Saito, Kota, et al.
Publicado: (2011)