The low-density lipoprotein receptor-related protein associates with calnexin, calreticulin, and protein disulfide isomerase in receptor-associated-protein-deficient fibroblasts (Q44774255)

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scientific article published in March 2004

Language	Label	Description	Also known as
English	The low-density lipoprotein receptor-related protein associates with calnexin, calreticulin, and protein disulfide isomerase in receptor-associated-protein-deficient fibroblasts	scientific article published in March 2004

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scholarly article

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Europe PubMed Central

PubMed publication ID

6 December 2017

The low-density lipoprotein receptor-related protein associates with calnexin, calreticulin, and protein disulfide isomerase in receptor-associated-protein-deficient fibroblasts (English)

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Europe PubMed Central

PubMed publication ID

6 December 2017

author name string

Robert A Orlando

1

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Europe PubMed Central

PubMed publication ID

6 December 2017

language of work or name

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publication date

1 March 2004

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Europe PubMed Central

PubMed publication ID

6 December 2017

Experimental Cell Research

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Europe PubMed Central

PubMed publication ID

6 December 2017

294

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Europe PubMed Central

PubMed publication ID

6 December 2017

1

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Europe PubMed Central

PubMed publication ID

6 December 2017

244-253

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Europe PubMed Central

PubMed publication ID

6 December 2017

The mammalian low-density lipoprotein receptor family

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Cell surface APP751 forms complexes with protease nexin 2 ligands and is internalized via the low density lipoprotein receptor-related protein (LRP).

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Association of membrane-bound amyloid precursor protein APP with the apolipoprotein E receptor LRP.

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Demonstration by fluorescence resonance energy transfer of two sites of interaction between the low-density lipoprotein receptor-related protein and the amyloid precursor protein: role of the intracellular adapter protein Fe65.

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The cytoplasmic domain of the LDL receptor-related protein regulates multiple steps in APP processing

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The low density lipoprotein receptor-related protein complexes with cell surface heparan sulfate proteoglycans to regulate proteoglycan-mediated lipoprotein catabolism

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LRP: role in vascular wall integrity and protection from atherosclerosis

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Platelet-derived growth factor (PDGF)-induced tyrosine phosphorylation of the low density lipoprotein receptor-related protein (LRP). Evidence for integrated co-receptor function betwenn LRP and the PDGF.

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Surface location and high affinity for calcium of a 500-kd liver membrane protein closely related to the LDL-receptor suggest a physiological role as lipoprotein receptor

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Calcium coordination and pH dependence of the calcium affinity of ligand-binding repeat CR7 from the LRP. Comparison with related domains from the LRP and the LDL receptor

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Disulfide bridges of a cysteine-rich repeat of the LDL receptor ligand-binding domain

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39 kDa receptor-associated protein is an ER resident protein and molecular chaperone for LDL receptor-related protein

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Receptor-associated protein is a folding chaperone for low density lipoprotein receptor-related protein

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Functional expression of low density lipoprotein receptor-related protein is controlled by receptor-associated protein in vivo

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RAP, a specialized chaperone, prevents ligand-induced ER retention and degradation of LDL receptor-related endocytic receptors

1 reference

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Functional domains of the receptor-associated protein (RAP)

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Endocytic trafficking of megalin/RAP complexes: dissociation of the complexes in late endosomes

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Pathogenic antibodies inhibit the binding of apolipoproteins to megalin/gp330 in passive Heymann nephritis

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19 Receptor-mediated endocytosis of low-density lipoprotein in cultured cells

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Identification of a cell line that expresses a cell surface and a soluble form of the gp330/receptor-associated protein (RAP) Heymann nephritis antigenic complex

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Calnexin: a membrane-bound chaperone of the endoplasmic reticulum

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Association of folding intermediates of glycoproteins with calnexin during protein maturation

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

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Lectin control of protein folding and sorting in the secretory pathway

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The carboxyl-terminal domain of receptor-associated protein facilitates proper folding and trafficking of the very low density lipoprotein receptor by interaction with the three amino-terminal ligand-binding repeats of the receptor

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gp330 and RAP: the Heymann nephritis antigenic complex

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gp330 associates with a 44-kDa protein in the rat kidney to form the Heymann nephritis antigenic complex

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Three-dimensional structure of the LDL receptor-binding domain of human apolipoprotein E

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Structural studies of detergent-solubilized and vesicle-reconstituted low-density lipoprotein (LDL) receptor.

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Solution structure of the LDL receptor EGF-AB pair: a paradigm for the assembly of tandem calcium binding EGF domains

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Three-dimensional structure of a cysteine-rich repeat from the low-density lipoprotein receptor

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Protein oligomerization in the endoplasmic reticulum

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

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

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Trimming and readdition of glucose to N-linked oligosaccharides determines calnexin association of a substrate glycoprotein in living cells

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Expression and disulfide-bond connectivity of the second ligand-binding repeat of the human LDL receptor

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Tissue distribution of three members of the murine protein disulfide isomerase (PDI) family

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Analysis of the human LRPAP1 gene coding for the lipoprotein receptor-associated protein: identification of 22 polymorphisms and one mutation

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Variation in the lipoprotein receptor-related protein, alpha2-macroglobulin and lipoprotein receptor-associated protein genes in relation to plasma lipid levels and risk of early myocardial infarction

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Identifiers

10.1016/J.YEXCR.2003.11.004

1 reference

Europe PubMed Central

PubMed publication ID

6 December 2017

PubMed publication ID

1 reference

Europe PubMed Central

PubMed publication ID

6 December 2017

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