ER stress response: getting the UPR hand on misfolded proteins (Q33970911)

30 July 2017

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title

ER stress response: getting the UPR hand on misfolded proteins (English)

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30 July 2017

Hampton RY

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30 July 2017

language of work or name

English

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publication date

1 July 2000

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30 July 2017

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30 July 2017

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30 July 2017

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30 July 2017

page(s)

R518-21

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Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation

30 July 2017

cites work

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7 January 2021

The unfolded protein response regulates multiple aspects of secretory and membrane protein biogenesis and endoplasmic reticulum quality control

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Degradation of proteins from the ER of S. cerevisiae requires an intact unfolded protein response pathway

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Signal transduction from the endoplasmic reticulum to the cell nucleus

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The presence of malfolded proteins in the endoplasmic reticulum signals the induction of glucose-regulated proteins

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S. cerevisiae encodes an essential protein homologous in sequence and function to mammalian BiP.

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Transcriptional induction of genes encoding endoplasmic reticulum resident proteins requires a transmembrane protein kinase

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A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response

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A transmembrane protein with a cdc2+/CDC28-related kinase activity is required for signaling from the ER to the nucleus

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7 January 2021

The Transmembrane Kinase Ire1p Is a Site-Specific Endonuclease That Initiates mRNA Splicing in the Unfolded Protein Response

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tRNA ligase is required for regulated mRNA splicing in the unfolded protein response

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The unfolded protein response: an intracellular signalling pathway with many surprising features

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Splicing: HACking into the unfolded-protein response

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Oligomerization and phosphorylation of the Ire1p kinase during intracellular signaling from the endoplasmic reticulum to the nucleus

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Dynamic interaction of BiP and ER stress transducers in the unfolded-protein response

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A stress response pathway from the endoplasmic reticulum to the nucleus requires a novel bifunctional protein kinase/endoribonuclease (Ire1p) in mammalian cells

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A role for presenilin-1 in nuclear accumulation of Ire1 fragments and induction of the mammalian unfolded protein response

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Protein translation and folding are coupled by an endoplasmic-reticulum-resident kinase

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7 January 2021

Perk is essential for translational regulation and cell survival during the unfolded protein response

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7 January 2021

IRE1 encodes a putative protein kinase containing a membrane-spanning domain and is required for inositol phototrophy in Saccharomyces cerevisiae

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The unfolded protein response coordinates the production of endoplasmic reticulum protein and endoplasmic reticulum membrane

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Genome-wide expression monitoring in Saccharomyces cerevisiae

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Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein

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Ubiquitin-mediated regulation of 3-hydroxy-3-methylglutaryl-CoA reductase

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Ubiquitin and the control of protein fate in the secretory and endocytic pathways

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7 January 2021

ER protein quality control and proteasome-mediated protein degradation

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7 January 2021

The engagement of Sec61p in the ER dislocation process

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7 January 2021

10.1016/S0960-9822(00)00583-2

Identifiers

DOI

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30 July 2017

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