The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase
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Summary
The results indicate that PDI1 and EUG1 encode functionally related proteins that are likely to be involved in interacting with nascent polypeptides in the yeast endoplasmic reticulum.
- Type
- article
- Published
- 1992-10-01
- Cited by
- 147
- References
- 66
- Access
- Open access
- OpenAlex
- https://openalex.org/W1914964702
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:22946974
Keywords
Endoplasmic reticulum, Protein disulfide-isomerase, Biology, Saccharomyces cerevisiae, STIM1
References
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- In vitro mutagenesis and plasmid shuffling: from cloned gene to mutant yeast.
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- Expression and site-directed mutagenesis of human protein disulfide isomerase in Escherichia coli. This multifunctional polypeptide has two independently acting catalytic sites for the isomerase activity.
- Protein disulfide isomerase is a component of the microsomal triglyceride transfer protein complex.
- The stress response in Chinese hamster ovary cells. Regulation of ERp72 and protein disulfide isomerase expression and secretion.
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- Methods for studying the yeast vacuole.
- Analysis of glycoproteins from Saccharomyces cerevisiae.
- The reactivities and ionization properties of the active-site dithiol groups of mammalian protein disulphide-isomerase.
- Role of vacuolar acidification in protein sorting and zymogen activation: a genetic analysis of the yeast vacuolar proton-translocating ATPase
- Sequences that regulate the divergent GAL1-GAL10 promoter in Saccharomyces cerevisiae
- Structural and functional dissection of Sec62p, a membrane-bound component of the yeast endoplasmic reticulum protein import machinery
- Glycosylation site binding protein, a component of oligosaccharyl transferase, is highly similar to three other 57 kd luminal proteins of the ER.
- Transformation of intact yeast cells treated with alkali cations.
Cited by
- The cellular response to unfolded proteins: intercompartmental signaling.
- Molecular Characterization of a Pancreas-Specific Protein Disulfide Isomerase, PDIp
- CHARACTERIZATION OF FACTORS THAT IMPACT APOLIPOPROTEIN BSECRETION AND ENDOPLASMIC RETICULUM ASSOCIATED DEGRADATION
- Protein disulfide isomerase: a multifunctional protein of the endoplasmic reticulum.
- The CXXC motif: imperatives for the formation of native disulfide bonds in the cell.
- The Contribution Of Molecular Chaperones To The ER-Associated Degradation Of Apolipoprotein B In Both Yeast And Mammalian Systems
- Fate of Mammalian Golgi Sialyltransferases in Yeast
- The unfolded protein response and HLA-B27 misfolding : implications for ankylosing spondylitis.
- Collagen hydroxylases and the protein disulfide isomerase subunit of prolyl 4-hydroxylases.
- Directed evolution of a stable scaffold for T-cell receptor engineering
- Unterschiedliche Funktionen der Ionenpumpe Pmr1
- Structural and functional interrogation of Anterior Gradient-2
- Identification and regulation of genes involved in anaerobic growth of Saccharomyces cerevisiae
- Functional analysis of the yeast "Saccharomyces cerevisiae" Gpi8 protein and characterization of the purified GPI-transamidase complex
- Endoplasmic reticulum associated protein degradation (ERAD): the function of Dfm1 and other novel components of the pathway
- Functional genomic approaches to understanding molecular chaperones and stress responses.
- Protein disulfide isomerase : function and mechanism in oxidative protein folding
- The folding catalyst protein disulfide isomerase is constructed of active and inactive thioredoxin modules.
- Diversity of the protein disulfide isomerase family: identification of breast tumor induced Hag2 and Hag3 as novel members of the protein family.
- Reductive depolymerization of bovine thyroglobulin multimersvia enzymatic reduction of protein disulfide and glutathionylated mixed disulfide linkages
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