Key residues at the membrane-distal surface of KACL, but not glycosylation, determine the functional interaction of the keratinocyte-specific C-type lectin-like receptor KACL with its high-affinity receptor NKp65.
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The Activating C-type Lectin-like Receptor NKp65 Signals through a Hemi-immunoreceptor Tyrosine-based Activation Motif (hemITAM) and Spleen Tyrosine Kinase (Syk).Clr-a: A Novel Immune-Related C-Type Lectin-like Molecule Exclusively Expressed by Mouse Gut Epithelium.Transcriptomic analysis of skin in a case of ichthyosis Curth-Macklin caused by a KRT1 mutation.
P2860
Key residues at the membrane-distal surface of KACL, but not glycosylation, determine the functional interaction of the keratinocyte-specific C-type lectin-like receptor KACL with its high-affinity receptor NKp65.
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Key residues at the membrane-d ...... high-affinity receptor NKp65.
@en
Key residues at the membrane-d ...... high-affinity receptor NKp65.
@nl
type
label
Key residues at the membrane-d ...... high-affinity receptor NKp65.
@en
Key residues at the membrane-d ...... high-affinity receptor NKp65.
@nl
prefLabel
Key residues at the membrane-d ...... high-affinity receptor NKp65.
@en
Key residues at the membrane-d ...... high-affinity receptor NKp65.
@nl
P2093
P2860
P356
P1433
P1476
Key residues at the membrane-d ...... high-affinity receptor NKp65.
@en
P2093
Björn Bauer
Christina Rohe
Isabel Vogler
Jessica Spreu
P2860
P304
P356
10.1111/IMM.12432
P577
2015-05-01T00:00:00Z