TY  - JOUR
AU  - Orsi, Andrea
AU  - van Anken, Eelco
AU  - Vitale, Milena
AU  - Zamai, Moreno
AU  - Caiolfa, Valeria R
AU  - Sitia, Roberto
AU  - Bakunts, Anush
PY  - 2024
DO  - 10.26508/lsa.202302562
UR  - http://hdl.handle.net/20.500.12105/20212
AB  - The unfolded protein response can switch from a pro-survival to a maladaptive, pro-apoptotic mode. During ER stress, IRE1α sensors dimerize, become phosphorylated, and activate XBP1 splicing, increasing folding capacity in the ER protein factory. The...
LA  - eng
PB  - eLife Sciences Publications
KW  - Endoribonucleases
KW  - Protein Serine-Threonine Kinases
KW  - Endoplasmic Reticulum Stress
KW  - Phosphorylation
KW  - Humans
KW  - Protein Multimerization
KW  - Unfolded Protein Response
KW  - Endoplasmic Reticulum
KW  - Ribonucleases
TI  - Congress of multiple dimers is needed for cross-phosphorylation of IRE1α and its RNase activity.
TY  - journal article
ER  -