Roles of protein-disulfide isomerase-mediated disulfide bond formation of yeast Mnl1p in endoplasmic reticulum-associated degradation (Q27934273)

1 December 2016

title

Roles of protein-disulfide isomerase-mediated disulfide bond formation of yeast Mnl1p in endoplasmic reticulum-associated degradation (English)

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Alpha-1,2-mannosidase MNL1 YHR204W

1 December 2016

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endoplasmic reticulum

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1 reference

Journal of Biological Chemistry

GOA release 2020-03-11

author

Machiko Sakoh-Nakatogawa

series ordinal

1

object named as

Machiko Sakoh-Nakatogawa

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author name string

Shuh-Ichi Nishikawa

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Toshiya Endo

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language of work or name

English

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publication date

1 May 2009

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published in

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Htm1 protein generates the N-glycan signal for glycoprotein degradation in the endoplasmic reticulum

1 December 2016

volume

284

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issue

18

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page(s)

11815-25

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cites work

1 reference

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20 March 2017

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Domain architecture of protein-disulfide isomerase facilitates its dual role as an oxidase and an isomerase in Ero1p-mediated disulfide formation.

20 March 2017

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Yos9 protein is essential for degradation of misfolded glycoproteins and may function as lectin in ERAD.

20 March 2017

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Yos9p detects and targets misfolded glycoproteins for ER-associated degradation

20 March 2017

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Exploration of the topological requirements of ERAD identifies Yos9p as a lectin sensor of misfolded glycoproteins in the ER lumen

20 March 2017

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Possibility of cytoplasmic pre-tRNA splicing: the yeast tRNA splicing endonuclease mainly localizes on the mitochondria

20 March 2017

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Unfolded cholera toxin is transferred to the ER membrane and released from protein disulfide isomerase upon oxidation by Ero1

20 March 2017

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Molecular chaperones in the yeast endoplasmic reticulum maintain the solubility of proteins for retrotranslocation and degradation

20 March 2017

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Htm1p, a mannosidase-like protein, is involved in glycoprotein degradation in yeast

20 March 2017

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A novel ER alpha-mannosidase-like protein accelerates ER-associated degradation

20 March 2017

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Mnl1p, an alpha -mannosidase-like protein in yeast Saccharomyces cerevisiae, is required for endoplasmic reticulum-associated degradation of glycoproteins

20 March 2017

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20 March 2017

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

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The yeast JEM1p is a DnaJ-like protein of the endoplasmic reticulum membrane required for nuclear fusion

20 March 2017

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SEC11 is required for signal peptide processing and yeast cell growth

20 March 2017

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Protein sorting in Saccharomyces cerevisiae: isolation of mutants defective in the delivery and processing of multiple vacuolar hydrolases

20 March 2017

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EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin

20 March 2017

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A single polypeptide acts both as the beta subunit of prolyl 4-hydroxylase and as a protein disulfide-isomerase

20 March 2017

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ERdj5 is required as a disulfide reductase for degradation of misfolded proteins in the ER

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EDEM3, a soluble EDEM homolog, enhances glycoprotein endoplasmic reticulum-associated degradation and mannose trimming

20 March 2017

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20 March 2017

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7 April 2017

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The recognition and retrotranslocation of misfolded proteins from the endoplasmic reticulum

29 September 2017

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29 September 2017

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29 September 2017

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29 September 2017

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EDEM1 regulates ER-associated degradation by accelerating de-mannosylation of folding-defective polypeptides and by inhibiting their covalent aggregation.

29 September 2017

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29 September 2017

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Export of a cysteine-free misfolded secretory protein from the endoplasmic reticulum for degradation requires interaction with protein disulfide isomerase

29 September 2017

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Assembly of ER-associated protein degradation in vitro: dependence on cytosol, calnexin, and ATP.

29 September 2017

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The essential function of yeast protein disulfide isomerase does not reside in its isomerase activity

29 September 2017

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Mechanisms and catalysts of disulfide bond formation in proteins

29 September 2017

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Protein disulfide isomerase and assisted protein folding

29 September 2017

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Active site mutations in yeast protein disulfide isomerase cause dithiothreitol sensitivity and a reduced rate of protein folding in the endoplasmic reticulum

2 June 2018

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Cloning of the Candida glabrata TRP1 and HIS3 genes, and construction of their disruptant strains by sequential integrative transformation

2 June 2018

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Crossref

https://api.crossref.org/works/10.1074%2FJBC.M900813200

Glycoproteins form mixed disulphides with oxidoreductases during folding in living cells

21 January 2018

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Crossref

https://api.crossref.org/works/10.1074%2FJBC.M900813200

RHO gene products, putative small GTP-binding proteins, are important for activation of the CAL1/CDC43 gene product, a protein geranylgeranyltransferase in Saccharomyces cerevisiae

21 January 2018

1 reference

https://pubmed.ncbi.nlm.nih.gov/19279007

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum

1 reference

https://pubmed.ncbi.nlm.nih.gov/19279007

inferred from PubMed ID database lookup

12 December 2020

based on heuristic

Identifiers

DOI

10.1074/JBC.M900813200

0 references

PMC publication ID

2673250

0 references

1 reference