(Q40793481)

English

N-glycan structure of a short-lived variant of ribophorin I expressed in the MadIA214 glycosylation-defective cell line reveals the role of a mannosidase that is not ER mannosidase I in the process of glycoprotein degradation

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scholarly article

1 reference

Europe PubMed Central

23 September 2017

N-glycan structure of a short-lived variant of ribophorin I expressed in the MadIA214 glycosylation-defective cell line reveals the role of a mannosidase that is not ER mannosidase I in the process of glycoprotein degradation (English)

1 reference

Europe PubMed Central

23 September 2017

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author name string

Ermonval M

1

1 reference

Europe PubMed Central

23 September 2017

Kitzmüller C

2

1 reference

Europe PubMed Central

23 September 2017

Mir AM

3

1 reference

Europe PubMed Central

23 September 2017

Cacan R

4

1 reference

Europe PubMed Central

23 September 2017

Ivessa NE

5

1 reference

Europe PubMed Central

23 September 2017

publication date

1 July 2001

1 reference

Europe PubMed Central

23 September 2017

1 reference

Europe PubMed Central

23 September 2017

11

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Europe PubMed Central

23 September 2017

7

1 reference

Europe PubMed Central

23 September 2017

565-576

1 reference

Europe PubMed Central

23 September 2017

Co-translational excision of alpha-glucose and alpha-mannose in nascent vesicular stomatitis virus G protein

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Molecular cloning and primary structure of Man9-mannosidase from human kidney

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Mammalian alpha-mannosidases--multiple forms but a common purpose?

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Degradation of a short-lived glycoprotein from the lumen of the endoplasmic reticulum: the role of N-linked glycans and the unfolded protein response

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Ubiquitination is required for the retro-translocation of a short-lived luminal endoplasmic reticulum glycoprotein to the cytosol for degradation by the proteasome

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Reciprocal relationship between alpha1,2 mannosidase processing and reglucosylation in the rough endoplasmic reticulum of Man-P-Dol deficient cells

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Hepatitis C virus glycoprotein complex localization in the endoplasmic reticulum involves a determinant for retention and not retrieval.

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Setting the standards: quality control in the secretory pathway

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Truncated N-glycans affect protein folding in the ER of CHO-derived mutant cell lines without preventing calnexin binding

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The role of N-glycans in the secretory pathway.

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Purification of a RAS-responsive adenylyl cyclase complex from Saccharomyces cerevisiae by use of an epitope addition method

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Quality control in the secretory pathway

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How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum

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Importance of glycosidases in mammalian glycoprotein biosynthesis

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Topography of glycosylation in the rough endoplasmic reticulum and Golgi apparatus

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Misfolded major histocompatibility complex class I heavy chains are translocated into the cytoplasm and degraded by the proteasome

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O-glycosylation of intact and truncated ribophorins in brefeldin A-treated cells: newly synthesized intact ribophorins are only transiently accessible to the relocated glycosyltransferases

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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 translocon: a dynamic gateway at the ER membrane

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Processing of viral envelope glycoprotein by the endomannosidase pathway: evaluation of host cell specificity

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Protein degradation in the endoplasmic reticulum

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3-Hydroxy-3-methylglutaryl-CoA reductase: a transmembrane glycoprotein of the endoplasmic reticulum with N-linked "high-mannose" oligosaccharides

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Intracellular disposal of incompletely folded human alpha1-antitrypsin involves release from calnexin and post-translational trimming of asparagine-linked oligosaccharides

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Oligosaccharide modification in the early secretory pathway directs the selection of a misfolded glycoprotein for degradation by the proteasome

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Segregation of the polypeptide translocation apparatus to regions of the endoplasmic reticulum containing ribophorins and ribosomes. II. Rat liver microsomal subfractions contain equimolar amounts of ribophorins and ribosomes

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BiP acts as a molecular ratchet during posttranslational transport of prepro-alpha factor across the ER membrane

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Glycosidases of the asparagine-linked oligosaccharide processing pathway

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Mannose-dependent endoplasmic reticulum (ER)-Golgi intermediate compartment-53-mediated ER to Golgi trafficking of coagulation factors V and VIII.

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Retrograde protein translocation: ERADication of secretory proteins in health and disease

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Biosynthesis and processing of ribophorins in the endoplasmic reticulum

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Definition of the lectin-like properties of the molecular chaperone, calreticulin, and demonstration of its copurification with endomannosidase from rat liver Golgi

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Cloning and expression of a specific human alpha 1,2-mannosidase that trims Man9GlcNAc2 to Man8GlcNAc2 isomer B during N-glycan biosynthesis

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Molecular cloning, chromosomal mapping and tissue-specific expression of a novel human alpha1,2-mannosidase gene involved in N-glycan maturation

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Lectins as chaperones in glycoprotein folding

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Carboxy terminally truncated forms of ribophorin I are degraded in pre-Golgi compartments by a calcium-dependent process

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Crystal structure of a class I α1,2-mannosidase involved in N-glycan processing and endoplasmic reticulum quality control

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Biological roles of oligosaccharides: all of the theories are correct

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Trafficking of oligomannosides released during N-glycosylation: a clearing mechanism of the rough endoplasmic reticulum

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Degradation of CFTR by the ubiquitin-proteasome pathway

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The molecular chaperone calnexin binds Glc1Man9GlcNAc2 oligosaccharide as an initial step in recognizing unfolded glycoproteins

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Endoplasmic reticulum kifunensine-resistant alpha-mannosidase is enzymatically and immunologically related to the cytosolic alpha-mannosidase

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Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction

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Pivotal role of calnexin and mannose trimming in regulating the endoplasmic reticulum-associated degradation of major histocompatibility complex class I heavy chain.

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Identifiers

10.1093/GLYCOB/11.7.565

1 reference

Europe PubMed Central

23 September 2017

1 reference

Europe PubMed Central

23 September 2017

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