about
The myeloid receptor PILRβ mediates the balance of inflammatory responses through regulation of IL-27 productionInsertion mutations in herpes simplex virus 1 glycoprotein H reduce cell surface expression, slow the rate of cell fusion, or abrogate functions in cell fusion and viral entry.Evolutionarily conserved paired immunoglobulin-like receptor α (PILRα) domain mediates its interaction with diverse sialylated ligands.Herpes virus fusion and entry: a story with many characters.Host factor SAMHD1 restricts DNA viruses in non-dividing myeloid cellsFusing structure and function: a structural view of the herpesvirus entry machinery.Murine Corneal Inflammation and Nerve Damage After Infection With HSV-1 Are Promoted by HVEM and Ameliorated by Immune-Modifying Nanoparticle Therapy.Technologies for Proteome-Wide Discovery of Extracellular Host-Pathogen Interactions.Alphaherpesviruses and the cytoskeleton in neuronal infections.The tug-of-war between dendritic cells and human chronic viruses.
P2860
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P2860
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on June 2008
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
HSV-1 infection through inhibitory receptor, PILRalpha.
@en
HSV-1 infection through inhibitory receptor, PILRalpha.
@nl
type
label
HSV-1 infection through inhibitory receptor, PILRalpha.
@en
HSV-1 infection through inhibitory receptor, PILRalpha.
@nl
prefLabel
HSV-1 infection through inhibitory receptor, PILRalpha.
@en
HSV-1 infection through inhibitory receptor, PILRalpha.
@nl
P356
P1433
P1476
HSV-1 infection through inhibitory receptor, PILRalpha
@en
P2093
Takeshi Satoh
P356
10.2222/JSV.58.27
P577
2008-06-01T00:00:00Z