The transmembrane kinase Ire1p is a site-specific endonuclease that initiates mRNA splicing in the unfolded protein response.
about
Prion switching in response to environmental stressMammalian transcription factor ATF6 is synthesized as a transmembrane protein and activated by proteolysis in response to endoplasmic reticulum stressLHS1 and SIL1 provide a lumenal function that is essential for protein translocation into the endoplasmic reticulumStructure of the Ire1 autophosphorylation complex and implications for the unfolded protein responseA synthetic biology approach identifies the mammalian UPR RNA ligase RtcBPARP16 is a tail-anchored endoplasmic reticulum protein required for the PERK- and IRE1α-mediated unfolded protein responseSUMO modification regulates the transcriptional activity of XBP1A ubiquitin ligase HRD1 promotes the degradation of Pael receptor, a substrate of ParkinA stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cellsUnusual features of fibrillarin cDNA and gene structure in Euglena gracilis: evolutionary conservation of core proteins and structural predictions for methylation-guide box C/D snoRNPs throughout the domain Eucarya.Activation of hepatitis B virus S promoter by a cell type-restricted IRE1-dependent pathway induced by endoplasmic reticulum stressAnalysis of 2'-phosphotransferase (Tpt1p) from Saccharomyces cerevisiae: evidence for a conserved two-step reaction mechanism.Basis for regulated RNA cleavage by functional analysis of RNase L and Ire1pAlternative function of a protein kinase homology domain in 2', 5'-oligoadenylate dependent RNase LThe inner nuclear membrane: simple, or very complex?New insights into the role of RNase L in innate immunityIdentification of Toyocamycin, an agent cytotoxic for multiple myeloma cells, as a potent inhibitor of ER stress-induced XBP1 mRNA splicingPotent and selective inhibitors of the inositol-requiring enzyme 1 endoribonucleaseEndoplasmic reticulum stress and the inflammatory basis of metabolic diseaseConserved RNA structures in the non-canonical Hac1/Xbp1 intronDiverse functions of RNase L and implications in pathologyCellular interplay between neurons and glia: toward a comprehensive mechanism for excitotoxic neuronal loss in neurodegenerationIRE1-mediated unconventional mRNA splicing and S2P-mediated ATF6 cleavage merge to regulate XBP1 in signaling the unfolded protein responseA scientific journey through the 2-5A/RNase L systemSCFCdc4-mediated degradation of the Hac1p transcription factor regulates the unfolded protein response in Saccharomyces cerevisiaeGene recruitment of the activated INO1 locus to the nuclear membraneIRE1-independent gain control of the unfolded protein responseGcn4p and novel upstream activating sequences regulate targets of the unfolded protein responseA highly specific phosphatase that acts on ADP-ribose 1''-phosphate, a metabolite of tRNA splicing in Saccharomyces cerevisiaeA molecular portrait of the response to unfolded proteinsGenome-scale approaches for discovering novel nonconventional splicing substrates of the Ire1 nucleaseThe unfolded protein response: the dawn of a new fieldThe unfolded protein response in neurodegenerative diseases: a neuropathological perspectiveInnate immunity at mucosal surfaces: the IRE1-RIDD-RIG-I pathwayEndoplasmic reticulum stress and diabetic cardiomyopathyProtein tyrosine phosphatase 1B deficiency potentiates PERK/eIF2α signaling in brown adipocytesA Genome Scale Screen for Mutants with Delayed Exit from Mitosis: Ire1-Independent Induction of Autophagy Integrates ER Homeostasis into Mitotic LifespanUnique evolution of the UPR pathway with a novel bZIP transcription factor, Hxl1, for controlling pathogenicity of Cryptococcus neoformansStructure and mechanism of action of the hydroxy–aryl–aldehyde class of IRE1 endoribonuclease inhibitorsStructure of the Dual Enzyme Ire1 Reveals the Basis for Catalysis and Regulation in Nonconventional RNA Splicing
P2860
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P2860
The transmembrane kinase Ire1p is a site-specific endonuclease that initiates mRNA splicing in the unfolded protein response.
description
1997 nî lūn-bûn
@nan
1997 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年論文
@yue
1997年論文
@zh-hant
1997年論文
@zh-hk
1997年論文
@zh-mo
1997年論文
@zh-tw
1997年论文
@wuu
name
The transmembrane kinase Ire1p ...... the unfolded protein response.
@ast
The transmembrane kinase Ire1p ...... the unfolded protein response.
@en
The transmembrane kinase Ire1p ...... the unfolded protein response.
@nl
type
label
The transmembrane kinase Ire1p ...... the unfolded protein response.
@ast
The transmembrane kinase Ire1p ...... the unfolded protein response.
@en
The transmembrane kinase Ire1p ...... the unfolded protein response.
@nl
prefLabel
The transmembrane kinase Ire1p ...... the unfolded protein response.
@ast
The transmembrane kinase Ire1p ...... the unfolded protein response.
@en
The transmembrane kinase Ire1p ...... the unfolded protein response.
@nl
P3181
P1433
P1476
The transmembrane kinase Ire1p ...... the unfolded protein response.
@en
P2093
P304
P3181
P356
10.1016/S0092-8674(00)80369-4
P407
P577
1997-09-19T00:00:00Z