(Q27933028)

1 December 2016

title

A complex of Pdi1p and the mannosidase Htm1p initiates clearance of unfolded glycoproteins from the endoplasmic reticulum (English)

1 reference

PubMed

1 December 2016

A Complex of Pdi1p and the Mannosidase Htm1p Initiates Clearance of Unfolded Glycoproteins from the Endoplasmic Reticulum (English)

1 reference

https://api.crossref.org/works/10.1016/J.MOLCEL.2011.04.027

mannosyl-oligosaccharide 1,2-alpha-mannosidase complex

5 December 2024

main subject

endoplasmic reticulum

0 references

1 reference

Gene Ontology release 2020-05-02

Gene Ontology ID

GO:0106055

Protein disulfide isomerase PDI1 YCL043C

1 reference

Alpha-1,2-mannosidase MNL1 YHR204W

GOA release 2020-03-11

1 reference

GOA release 2020-03-11

author

Markus Aebi

5

0 references

Pedro Carvalho

3

object named as

Pedro Carvalho

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A21700223

5 December 2024

author name string

Robert Gauss

1

0 references

Kazue Kanehara

2

0 references

Davis T. W. Ng

4

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A21700223

full work available at URL

5 December 2024

language of work or name

English

0 references

publication date

24 June 2011

0 references

http://www.cell.com/article/S109727651100373X/pdf

1 reference

Europe PubMed Central

https://www.ebi.ac.uk/europepmc/webservices/rest/search?resulttype=core&format=json&query=SRC%3AMED%20AND%20EXT_ID%3A21700223

https://api.elsevier.com/content/article/PII:S109727651100373X?httpAccept=text/xml

5 December 2024

1 reference

https://api.crossref.org/works/10.1016/J.MOLCEL.2011.04.027

https://api.elsevier.com/content/article/PII:S109727651100373X?httpAccept=text/plain

5 December 2024

1 reference

https://api.crossref.org/works/10.1016/J.MOLCEL.2011.04.027

5 December 2024

1 reference

N-glycan structures: recognition and processing in the ER.

1 December 2016

volume

42

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issue

6

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page(s)

782-93

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cites work

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Distinct ubiquitin-ligase complexes define convergent pathways for the degradation of ER proteins

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Retrotranslocation of a misfolded luminal ER protein by the ubiquitin-ligase Hrd1p

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

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

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Protein disulfide isomerase: a critical evaluation of its function in disulfide bond formation

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Roles of N-linked glycans in the endoplasmic reticulum

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The ubiquitylation machinery of the endoplasmic reticulum

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

5 December 2024

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

5 December 2024

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A versatile toolbox for PCR-based tagging of yeast genes: new fluorescent proteins, more markers and promoter substitution cassettes

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Modularity of the Hrd1 ERAD complex underlies its diverse client range

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Interplay of Substrate Retention and Export Signals in Endoplasmic Reticulum Quality Control

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The b' domain provides the principal peptide-binding site of protein disulfide isomerase but all domains contribute to binding of misfolded proteins

5 December 2024

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Epitope tagging of yeast genes using a PCR-based strategy: more tags and improved practical routines

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Three binding sites in protein-disulfide isomerase cooperate in collagen prolyl 4-hydroxylase tetramer assembly.

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Importance of carbohydrate positioning in the recognition of mutated CPY for ER-associated degradation

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Crystal structure of the bb' domains of the protein disulfide isomerase ERp57

5 December 2024

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Protein disulphide isomerase is required for signal peptide peptidase-mediated protein degradation

5 December 2024

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Protein quality control in the ER: the recognition of misfolded proteins

5 December 2024

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

5 December 2024

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5 December 2024

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5 December 2024

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Redox-dependent domain rearrangement of protein disulfide isomerase coupled with exposure of its substrate-binding hydrophobic surface

5 December 2024

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Chaperone-Like Activity of Protein Disulfide-Isomerase in the Refolding Of Rhodanese

5 December 2024

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Stress tolerance of misfolded carboxypeptidase Y requires maintenance of protein trafficking and degradative pathways

5 December 2024

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Single, context-specific glycans can target misfolded glycoproteins for ER-associated degradation

5 December 2024

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Endoplasmic reticulum associated protein degradation: a chaperone assisted journey to hell

5 December 2024

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

5 December 2024

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Protein Disulfide Isomerase Acts as a Redox-Dependent Chaperone to Unfold Cholera Toxin

5 December 2024

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

5 December 2024

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Distinct retrieval and retention mechanisms are required for the quality control of endoplasmic reticulum protein folding

5 December 2024

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Protein disulfide isomerase is both an enzyme and a chaperone

5 December 2024

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Intrinsic conformational determinants signal protein misfolding to the Hrd1/Htm1 endoplasmic reticulum-associated degradation system

5 December 2024

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5 December 2024

Identifiers

0 references

1 reference

PubMed