Misfolding of glycoproteins is a prerequisite for peptide: N-glycanase mediated deglycosylation (Q45238415)

11 December 2017

title

Misfolding of glycoproteins is a prerequisite for peptide: N-glycanase mediated deglycosylation. (English)

1 reference

11 December 2017

Shivanjali Joshi

1 reference

11 December 2017

Samiksha Katiyar

series ordinal

1 reference

11 December 2017

William J Lennarz

series ordinal

1 reference

11 December 2017

language of work or name

English

0 references

publication date

1 January 2005

1 reference

11 December 2017

1 reference

11 December 2017

volume

579

1 reference

11 December 2017

1 reference

11 December 2017

page(s)

823-826

1 reference

ER-associated degradation in protein quality control and cellular regulation

11 December 2017

cites work

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2004.12.060

Quality Control and Protein Folding in the Secretory Pathway

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2004.12.060

PNG1, a yeast gene encoding a highly conserved peptide:N-glycanase

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2004.12.060

A role for N-glycanase in the cytosolic turnover of glycoproteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2004.12.060

A glycosylated type I membrane protein becomes cytosolic when peptide: N-glycanase is compromised

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2004.12.060

Yeast N-glycanase distinguishes between native and non-native glycoproteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2004.12.060

BiP/Kar2p serves as a molecular chaperone during carboxypeptidase Y folding in yeast

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2004.12.060

The unfolded protein response regulates multiple aspects of secretory and membrane protein biogenesis and endoplasmic reticulum quality control

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2004.12.060

ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2004.12.060

Site-directed mutagenesis study of yeast peptide:N-glycanase. Insight into the reaction mechanism of deglycosylation

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2004.12.060

Cytoplasmic peptide:N-glycanase (PNGase) in eukaryotic cells: occurrence, primary structure, and potential functions

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2004.12.060

Peptides glycosylated in the endoplasmic reticulum of yeast are subsequently deglycosylated by a soluble peptide: N-glycanase activity

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2004.12.060

Rad23 provides a link between the Png1 deglycosylating enzyme and the 26 S proteasome in yeast.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2004.12.060

Identification of proteins that interact with mammalian peptide:N-glycanase and implicate this hydrolase in the proteasome-dependent pathway for protein degradation

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2004.12.060

A complex between peptide:N-glycanase and two proteasome-linked proteins suggests a mechanism for the degradation of misfolded glycoproteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2004.12.060

Temperature control for kinetic refolding of heat‐denatured ovalbumin

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2FJ.FEBSLET.2004.12.060

10.1016/J.FEBSLET.2004.12.060

21 January 2018

Identifiers

DOI

1 reference

11 December 2017

1 reference