Title : Porcine arterivirus attachment to the macrophage-specific receptor sialoadhesin is dependent on the sialic acid-binding activity of the N-terminal immunoglobulin domain of sialoadhesin.

Pub. Date : 2007 Sep

PMID : 17567703






3 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Porcine arterivirus attachment to the macrophage-specific receptor sialoadhesin is dependent on the sialic acid-binding activity of the N-terminal immunoglobulin domain of sialoadhesin. N-Acetylneuraminic Acid sialic acid binding Ig like lectin 1 Homo sapiens
2 Porcine arterivirus attachment to the macrophage-specific receptor sialoadhesin is dependent on the sialic acid-binding activity of the N-terminal immunoglobulin domain of sialoadhesin. N-Acetylneuraminic Acid sialic acid binding Ig like lectin 1 Homo sapiens
3 The sialic acid-binding lectin sialoadhesin (Sn) is a macrophage-restricted receptor for porcine reproductive and respiratory syndrome virus (PRRSV). N-Acetylneuraminic Acid sialic acid binding Ig like lectin 1 Homo sapiens