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Article

Glycosylation influences the lectin activities of the macrophage mannose receptor.

The Journal of biological chemistry - 23 Sept 2005

Su Yunpeng, Bakker Talitha, Harris James, Tsang Clarence, Brown Gordon D, Wormald Mark R, Gordon Siamon, Dwek Raymond A, Rudd Pauline M, Martinez-Pomares Luisa

Abstract excerpt

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 sources, and we hypothesized that this could be due to altered glycosylation. Using MR transductants and purified MR, we...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

Identifiers

PMID: 15983039
DOI: 10.1074/jbc.M503457200

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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