ArticleProceedings of the National Academy of Sciences of the United States of America1994
Functional domains of the receptor-associated protein (RAP).
Article in Proceedings of the National Academy of Sciences of the United States of America, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
18 citing papers in PubMed, 65 citations in OpenAlex.
- Trial
- Article
- Role of Specific B-Cell Receptor Antigens in Lymphomagenesis.Frontiers in oncology · 2020Review
- Article
- Receptor-associated protein (RAP) has two high-affinity binding sites for the low-density lipoprotein receptor-related protein (LRP): consequences for the chaperone functions of RAP.The Biochemical journal · 2009Article
- Article
- Syndecan-1 mediates internalization of apoE-VLDL through a low density lipoprotein receptor-related protein (LRP)-independent, non-clathrin-mediated pathway.Lipids in health and disease · 2006Article
- Cationic sites on granzyme B contribute to cytotoxicity by promoting its uptake into target cells.Molecular and cellular biology · 2005Article
- Cell surface heparan sulfate proteoglycans contribute to intracellular lipid accumulation in adipocytes.Lipids in health and disease · 2005Article
- Direct binding of occupied urokinase receptor (uPAR) to LDL receptor-related protein is required for endocytosis of uPAR and regulation of cell surface urokinase activity.Molecular biology of the cell · 2001Article
- MIR16, a putative membrane glycerophosphodiester phosphodiesterase, interacts with RGS16.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
- Pathogenic antibodies inhibit the binding of apolipoproteins to megalin/gp330 in passive Heymann nephritis.The Journal of clinical investigation · 1997Article
- The solution structure of the N-terminal domain of alpha2-macroglobulin receptor-associated protein.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- Role of basic residues in the subgroup-determining region of the subgroup A avian sarcoma and leukosis virus envelope in receptor binding and infection.Journal of virology · 1997Article
- Identification of the second cluster of ligand-binding repeats in megalin as a site for receptor-ligand interactions.Proceedings of the National Academy of Sciences of the United States of America · 1997Article
- Endocytic trafficking of megalin/RAP complexes: dissociation of the complexes in late endosomes.Molecular biology of the cell · 1997Article
- Megalin-mediated endocytosis of transcobalamin-vitamin-B12 complexes suggests a role of the receptor in vitamin-B12 homeostasis.Proceedings of the National Academy of Sciences of the United States of America · 1996Article
- Molecular analysis of the pathological autoimmune antigens of Heymann nephritis.The American journal of pathology · 1996Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The receptor-associated protein (RAP) specifically associates with gp330 and the low density lipoprotein (LDL) receptor-related protein (LRP), the two newest members of the LDL receptor gene family. Results obtained by ligand blotting, affinity chromatography, and density-gradient sedimentation demonstrate that RAP binds to both receptors with high affinity and that the binding is Ca2+ dependent. RAP also binds heparin and is identical to a mouse heparin binding protein (HBP-44) identified in a teratocarcinoma cell line (F9). While biochemical studies have shown that RAP is present on the cell surface and is an effective inhibitor of ligand binding to gp330 and LRP, immunocytochemical findings indicate that RAP is most abundant in the endoplasmic reticulum lumen and may function in receptor folding and/or trafficking. To facilitate the characterization of RAP's function(s) we have mapped its gp330 and heparin binding sites by performing direct binding studies on fusion proteins representing overlapping domains of RAP. gp330 was found to bind to two separate sites on RAP--i.e., between amino acids 85-148 and 178-248. Binding studies with radiolabeled heparin indicate that the heparin binding site is between amino acids 261 and 323, which is consistent with our previously proposed site (residues 287-306) based on the amphipathic nature of the C terminus of RAP. These data demonstrate that the gp330 and heparin binding sites and the Heymann nephritis pathogenic epitope (amino acids 1-86) demonstrated earlier are represented by distinct domains of the RAP polypeptide.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.