Lectin-deficient calnexin is capable of binding class I histocompatibility molecules in vivo and preventing their degradation (Q38346469)

2 September 2017

Lectin-deficient calnexin is capable of binding class I histocompatibility molecules in vivo and preventing their degradation (English)

1 reference

2 September 2017

Michael R Leach

1

1 reference

PubMed ID

14699098

2 September 2017

David B Williams

series ordinal

2

1 reference

PubMed ID

14699098

2 September 2017

language of work or name

English

0 references

publication date

29 December 2003

1 reference

Journal of Biological Chemistry

2 September 2017

1 reference

2 September 2017

279

1 reference

2 September 2017

10

1 reference

2 September 2017

9072-9079

1 reference

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

2 September 2017

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

The Structure of calnexin, an ER chaperone involved in quality control of protein folding

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

Localization of the lectin, ERp57 binding, and polypeptide binding sites of calnexin and calreticulin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

TROSY-NMR reveals interaction between ERp57 and the tip of the calreticulin P-domain

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

Role of N-oligosaccharide endoplasmic reticulum processing reactions in glycoprotein folding and degradation

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

ER quality control: towards an understanding at the molecular level

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

Functional relationship between calreticulin, calnexin, and the endoplasmic reticulum luminal domain of calnexin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

The putative chaperone calmegin is required for sperm fertility

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

Calnexin-dependent enhancement of nicotinic acetylcholine receptor assembly and surface expression

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

Regulation of MHC class I transport by the molecular chaperone, calnexin (p88, IP90).

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

Calnexin retains unassembled major histocompatibility complex class I free heavy chains in the endoplasmic reticulum

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

EDEM as an acceptor of terminally misfolded glycoproteins released from calnexin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

Role of EDEM in the release of misfolded glycoproteins from the calnexin cycle

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

Role of N-linked oligosaccharide recognition, glucose trimming, and calnexin in glycoprotein folding and quality control

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

Calnexin discriminates between protein conformational states and functions as a molecular chaperone in vitro

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

Conformational requirements for glycoprotein reglucosylation in the endoplasmic reticulum

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

The lectin chaperone calnexin utilizes polypeptide-based interactions to associate with many of its substrates in vivo

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

Calreticulin functions in vitro as a molecular chaperone for both glycosylated and non-glycosylated proteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

Relationship between calnexin and BiP in suppressing aggregation and promoting refolding of protein and glycoprotein substrates

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

Oligosaccharide binding characteristics of the molecular chaperones calnexin and calreticulin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

Characterization and use of the Drosophila metallothionein promoter in cultured Drosophila melanogaster cells

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

Peptide influences the folding and intracellular transport of free major histocompatibility complex class I heavy chains

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

Nucleotide sequence of aDrosophila melanogastergene encoding a calreticulin homologue

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

Nucleotide sequence of a Drosophila melanogaster cDNA encoding a calnexin homologue.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

Role of calnexin, calreticulin, and endoplasmic reticulum mannosidase I in apolipoprotein(a) intracellular targeting

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

Role of calnexin in the glycan-independent quality control of proteolipid protein

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

Mutational studies of the amino acid residues in the combining site of Erythrina corallodendron lectin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

Identification of N-acetylglucosamine binding residues in Griffonia simplicifolia lectin II.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

ERGIC-53 is a functional mannose-selective and calcium-dependent human homologue of leguminous lectins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

Structure of a legume lectin with an ordered N-linked carbohydrate in complex with lactose

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

Calreticulin recognizes misfolded HLA-A2 heavy chains

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

Kinetics and the mechanism of interaction of the endoplasmic reticulum chaperone, calreticulin, with monoglucosylated (Glc1Man9GlcNAc2) substrate

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

Fractionation and structural assessment of oligosaccharides and glycopeptides by use of immobilized lectins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

Promotion of tyrosinase folding in COS 7 cells by calnexin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

Trypanosoma cruzi calreticulin is a lectin that binds monoglucosylated oligosaccharides but not protein moieties of glycoproteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

Calreticulin functions as a molecular chaperone in the biosynthesis of myeloperoxidase

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

Retention of unassembled components of integral membrane proteins by calnexin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

Calnexin associates exclusively with individual CD3 delta and T cell antigen receptor (TCR) alpha proteins containing incompletely trimmed glycans that are not assembled into multisubunit TCR complexes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

Calnexin interaction with N-glycosylation mutants of a polytopic membrane glycoprotein, the human erythrocyte anion exchanger 1 (band 3).

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

P-glycoprotein. Associations between domains and between domains and molecular chaperones

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

Calreticulin interacts with newly synthesized human immunodeficiency virus type 1 envelope glycoprotein, suggesting a chaperone function similar to that of calnexin

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

Transient, lectin-like association of calreticulin with folding intermediates of cellular and viral glycoproteins

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

Calnexin fails to associate with substrate proteins in glucosidase-deficient cell lines

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

Enhanced Catalysis of Ribonuclease B Folding by the Interaction of Calnexin or Calreticulin with ERp57

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.M310788200

21 January 2018

Identifiers

DOI

10.1074/JBC.M310788200

1 reference

2 September 2017

1 reference

PubMed ID

14699098