Functional and genomic analyses reveal an essential coordination between the unfolded protein response and ER-associated degradation (Q28131669)

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C K Patil

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L Wodicka

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D J Lockhart

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J S Weissman

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P Walter

Role of Cue1p in ubiquitination and degradation at the ER surface

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language of work or name

English

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publication date

28 April 2000

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published in

Cell

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volume

101

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page(s)

249-58

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issue

3

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cites work

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

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

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

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

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Regulation of the dolichol pathway in human fibroblasts by the endoplasmic reticulum unfolded protein response

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The medial-Golgi ion pump Pmr1 supplies the yeast secretory pathway with Ca2+ and Mn2+ required for glycosylation, sorting, and endoplasmic reticulum-associated protein degradation

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Degradation of misfolded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure

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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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Identifiers

DOI

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Consolidated OpenCitations Corpus – April 2017

114870

114870

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Consolidated OpenCitations Corpus – April 2017

Consolidated OpenCitations Corpus – April 2017

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