2011
DOI: 10.1074/jbc.m111.224469
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Introduction of N-Linked Glycans in the Lectin Domain of Surfactant Protein D

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Cited by 22 publications
(23 citation statements)
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“…For this purpose, we applied the HEK293 expression system that was previously used successfully for the production of full-length wild-type pSP-D, wild-type hSP-D, and various h/pSP-D derivatives (26). Biochemical characterization showed that both RpNCRD and RpNCRD-dNG were expressed as trimeric proteins, and N-glycanase digestions confirmed the absence of N-linked glycans in the RpNCRD-dNG preparation.…”
Section: Discussionmentioning
confidence: 99%
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“…For this purpose, we applied the HEK293 expression system that was previously used successfully for the production of full-length wild-type pSP-D, wild-type hSP-D, and various h/pSP-D derivatives (26). Biochemical characterization showed that both RpNCRD and RpNCRD-dNG were expressed as trimeric proteins, and N-glycanase digestions confirmed the absence of N-linked glycans in the RpNCRD-dNG preparation.…”
Section: Discussionmentioning
confidence: 99%
“…Chemical crosslinking of RpNCRD and RpNCRD-dNG was achieved with a BS3 cross-linker as described previously (26).…”
Section: Methodsmentioning
confidence: 99%
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“…It is speculated that the SGA‐loop region is involved in generating enhanced binding properties of the CRD of pSP‐D to viral glycans. In addition, site‐directed mutagenesis studies with recombinant human SP‐D have also indicated that this porcine‐specific SGA‐loop is likely to be involved in mediating the antiviral activity of the N‐linked glycan in the CRD of pSP‐D [65].…”
Section: Collectinsmentioning
confidence: 99%