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Glycosylation influences the lectin activities of the macrophage mannose receptor

The Journal of Biological Chemistry

Jun 29, 2005

Yunpeng SuLuisa Martinez-Pomares

Abstract

The mannose receptor (MR) is a heavily glycosylated endocytic receptor that recognizes both mannosylated and sulfated ligands through its C-type lectin domains and cysteine-rich (CR) domain, respectively. Differential binding properties have been described for MR isolated from different...read more

Mentioned in this Paper

Flow Cytometry
Carbohydrate nutrients
CD206 antigen
Endocytosis
Hormone Receptors, Cell Surface
Tertiary Protein Structure
Sulfur
Chinese Hamster Ovary Cell
Mannose
Plasma Protein Binding Capacity
54
1
Paper Details
References
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  • Citations27
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  • References41
  • Citations27
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Glycosylation influences the lectin activities of the macrophage mannose receptor

The Journal of Biological Chemistry

Jun 29, 2005

Yunpeng SuLuisa Martinez-Pomares

PMID: 15983039

DOI: 10.1074/jbc.m503457200

Abstract

The mannose receptor (MR) is a heavily glycosylated endocytic receptor that recognizes both mannosylated and sulfated ligands through its C-type lectin domains and cysteine-rich (CR) domain, respectively. Differential binding properties have been described for MR isolated from different...read more

Mentioned in this Paper

Flow Cytometry
Carbohydrate nutrients
CD206 antigen
Endocytosis
Hormone Receptors, Cell Surface
Tertiary Protein Structure
Sulfur
Chinese Hamster Ovary Cell
Mannose
Plasma Protein Binding Capacity
54
1

Similar Papers Found In These Feeds

ASBMB Publications

The American Society for Biochemistry and Molecular Biology (ASBMB) includes the Journal of Biological Chemistry, Molecular & Cellular Proteomics, and the Journal of Lipid Research. Discover the latest research from ASBMB here.

Exocytosis & Endocytosis: Imaging

Dynamin GTPases are proteins that are responsible for endocytosis in cells, as well as division of organelles, cytokinesis, and pathogen resistance. Discover the latest research on dynamin GTPases here.

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Paper Details
References
  • References41
  • Citations27
12345
  • References41
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123
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