Active site mutations in yeast protein disulfide isomerase cause dithiothreitol sensitivity and a reduced rate of protein folding in the endoplasmic reticulum.
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Role of ubiquilin associated with protein-disulfide isomerase in the endoplasmic reticulum in stress-induced apoptotic cell deathTwo pairs of conserved cysteines are required for the oxidative activity of Ero1p in protein disulfide bond formation in the endoplasmic reticulumThe CXXCXXC motif determines the folding, structure and stability of human Ero1-LalphaUnfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Ero1Oxidative protein folding in eukaryotes: mechanisms and consequencesThe Catalytic Activity of Protein-disulfide Isomerase Requires a Conformationally Flexible MoleculeDomain architecture of protein-disulfide isomerase facilitates its dual role as an oxidase and an isomerase in Ero1p-mediated disulfide formation.Roles of protein-disulfide isomerase-mediated disulfide bond formation of yeast Mnl1p in endoplasmic reticulum-associated degradationGrx5 is a mitochondrial glutaredoxin required for the activity of iron/sulfur enzymes.The coatomer-interacting protein Dsl1p is required for Golgi-to-endoplasmic reticulum retrieval in yeast.The contributions of protein disulfide isomerase and its homologues to oxidative protein folding in the yeast endoplasmic reticulum.Functional differences in yeast protein disulfide isomerases.A flavoprotein oxidase defines a new endoplasmic reticulum pathway for biosynthetic disulphide bond formation.Mutation of yeast Eug1p CXXS active sites to CXXC results in a dramatic increase in protein disulphide isomerase activityMTH1745, a protein disulfide isomerase-like protein from thermophilic archaea, Methanothermobacter thermoautotrophicum involving in stress responseThe protein disulphide-isomerase family: unravelling a string of folds.Oxidative activity of yeast Ero1p on protein disulfide isomerase and related oxidoreductases of the endoplasmic reticulumGlycoprotein folding in the endoplasmic reticulum.The pathogenic human Torsin A in Drosophila activates the unfolded protein response and increases susceptibility to oxidative stress.Protein disulfide isomerases contribute differentially to the endoplasmic reticulum-associated degradation of apolipoprotein B and other substratesExport of a cysteine-free misfolded secretory protein from the endoplasmic reticulum for degradation requires interaction with protein disulfide isomerase.Genomic-scale comparison of sequence- and structure-based methods of function prediction: does structure provide additional insight?Redox regulation of multidrug resistance in cancer chemotherapy: molecular mechanisms and therapeutic opportunitiesProtein disulfide isomerase-2 of Arabidopsis mediates protein folding and localizes to both the secretory pathway and nucleus, where it interacts with maternal effect embryo arrest factor.Endoplasmic reticulum protein quality control and its relationship to environmental stress responses in plants.Description of the topographical changes associated to the different stages of the DsbA catalytic cycle.Randomization of the entire active-site helix alpha 1 of the thiol-disulfide oxidoreductase DsbA from Escherichia coli.Retrotranslocation of a viral A/B toxin from the yeast endoplasmic reticulum is independent of ubiquitination and ERAD.Characterization of Escherichia coli thioredoxin variants mimicking the active-sites of other thiol/disulfide oxidoreductases.The CXC motif: a functional mimic of protein disulfide isomerase.Complementation of DsbA deficiency with secreted thioredoxin variants reveals the crucial role of an efficient dithiol oxidant for catalyzed protein folding in the bacterial periplasm.Secretion of human serum albumin by Kluyveromyces lactis overexpressing KlPDI1 and KlERO1.Combinations of protein-disulfide isomerase domains show that there is little correlation between isomerase activity and wild-type growth.Sulfhydryl oxidation, not disulfide isomerization, is the principal function of protein disulfide isomerase in yeast Saccharomyces cerevisiae.Glutathione is required to regulate the formation of native disulfide bonds within proteins entering the secretory pathway.Mutational analysis of the oxidoreductase ERp57 reveals the importance of the two central residues in the redox motif.The membrane tethered transcription factor EcbZIP17 from finger millet promotes plant growth and enhances tolerance to abiotic stresses.In Vitro Nitrosation of Insulin A- and B-Chains
P2860
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P2860
Active site mutations in yeast protein disulfide isomerase cause dithiothreitol sensitivity and a reduced rate of protein folding in the endoplasmic reticulum.
description
1997 nî lūn-bûn
@nan
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
1997年论文
@zh
1997年论文
@zh-cn
name
Active site mutations in yeast ...... in the endoplasmic reticulum.
@en
Active site mutations in yeast ...... in the endoplasmic reticulum.
@nl
type
label
Active site mutations in yeast ...... in the endoplasmic reticulum.
@en
Active site mutations in yeast ...... in the endoplasmic reticulum.
@nl
prefLabel
Active site mutations in yeast ...... in the endoplasmic reticulum.
@en
Active site mutations in yeast ...... in the endoplasmic reticulum.
@nl
P2093
P2860
P356
P1476
Active site mutations in yeast ...... in the endoplasmic reticulum.
@en
P2093
P2860
P304
P356
10.1083/JCB.138.6.1229
P407
P577
1997-09-01T00:00:00Z