Results 1 to 10 of about 19,138 (225)
Structural and functional basis for RNA cleavage by Ire1 [PDF]
Background The unfolded protein response (UPR) controls the protein folding capacity of the endoplasmic reticulum (ER). Central to this signaling pathway is the ER-resident bifunctional transmembrane kinase/endoribonuclease Ire1.
Stroud Robert M +7 more
doaj +12 more sources
Pharmacological Targeting of IRE1 in Cancer [PDF]
IRE1α (inositol requiring enzyme 1 alpha) is one of the main transducers of the unfolded protein response (UPR). IRE1α plays instrumental protumoral roles in several cancers, and high IRE1α activity has been associated with poorer prognoses. In this context, IRE1α has been identified as a potentially relevant therapeutic target.
Leif A Eriksson +2 more
exaly +5 more sources
Signal sequence-triage is activated by translocon obstruction sensed by an ER stress sensor IRE1α
Secretory pathway proteins are cotranslationally translocated into the endoplasmic reticulum (ER) of metazoan cells through the protein channel, translocon.
Ashuei Sogawa +8 more
doaj +1 more source
Mechanism of Hsp70 specialized interactions in protein translocation and the unfolded protein response [PDF]
Hsp70 chaperones interact with substrate proteins in a coordinated fashion that is regulated by nucleotides and enhanced by assisting cochaperones.
Natacha Larburu +4 more
doaj +1 more source
Context Icariin (ICA), a flavonol glycoside extracted from Epimedium brevicornum Maxim (Berberidaceae), has been proven to inhibit inflammatory response in ischaemic rats in our laboratory's previous work.
Zhen-Tao Mo, Jie Zheng, Yu-ling Liao
doaj +1 more source
Endoplasmic reticulum stress (ERS)-mediated autophagy is indispensable for modulation of replication and pathogenesis of numerous mammalian viruses. We have previously shown that classical swine fever virus (CSFV) infection induces ERS-mediated autophagy
Erpeng Zhu +14 more
doaj +1 more source
Quaternary structure analysis of IRE1
IRE1 belongs to a type I transmembrane protein family harboring two functional domains, cytoplasmic domain with kinase and RNAse catalytic activity, and the luminal domain, which is involved in the sensing of unfolded proteins. IRE1 molecule undergoes dimerization in the lumenal domain, which functionally activates the catalytic C-terminal domain. IRE1
Bashir, Samirul +4 more
openaire +2 more sources
Fat body Ire1 regulates lipid homeostasis through the Xbp1s-FoxO axis in Drosophila
Summary: The endoplasmic reticulum (ER)-resident transmembrane protein kinase/RNase Ire1 is a conserved sensor of the cellular unfolded protein response and has been implicated in lipid homeostasis, including lipid synthesis and transport, across species.
Peng Zhao +15 more
doaj +1 more source
Upon endoplasmic-reticulum (ER) stress, the ER-located transmembrane protein, Ire1, is autophosphorylated and acts as an endoribonuclease to trigger the unfolded protein response (UPR).
Quynh Giang Le +5 more
doaj +1 more source
Protein folding homeostasis in the endoplasmic reticulum (ER) is regulated by a signaling network, termed the unfolded protein response (UPR). Inositol-requiring enzyme 1 (IRE1) is an ER membrane-resident kinase/RNase that mediates signal transmission in
Vladislav Belyy +4 more
doaj +1 more source

